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Information on EC 3.1.3.48 - protein-tyrosine-phosphatase and Organism(s) Homo sapiens and UniProt Accession P26045

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.48 protein-tyrosine-phosphatase
IUBMB Comments
Dephosphorylates O-phosphotyrosine groups in phosphoproteins, such as the products of EC 2.7.10.2, non-specific protein-tyrosine kinase.
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P26045
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
ptp1b, protein tyrosine phosphatase, shp-1, shp-2, tyrosine phosphatase, protein phosphatase 2a, acid phosphatase activity, mkp-1, cdc25a, ptpn22, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
protein tyrosine phosphatase
-
protein tyrosine phosphatase N3
-
70Z-SHP
-
-
-
-
alpha-PTP-PEST
-
-
Brain-derived phosphatase
-
-
-
-
BVP
-
-
-
-
CD148
-
-
CD148 antigen
-
-
-
-
CD45 antigen
-
-
-
-
CD45 protein tyrosine phosphatase
-
-
Cdc25 phosphatase
-
-
Cdc25-like protein
-
-
-
-
Cdc25A
Cdc25B
Cdc25B phosphatase
Cdc25C
CDK2-associated dual specificity phosphatase
-
-
-
-
Ch-1PTPase
CPTP1
-
-
-
-
cysteine-dependent protein tyrosine phosphatase
-
-
DEP-1
DLAR
-
-
-
-
DSP18
-
-
dual specificity phosphatase
Dual specificity phosphatase Cdc25A
-
-
-
-
Dual specificity phosphatase Cdc25B
-
-
-
-
Dual specificity phosphatase Cdc25C
-
-
-
-
dual specificity protein phosphatase
-
dual specificity protein phosphatase 23
UniProt
dual specificity protein phosphatase 3
UniProt
Dual specificity protein phosphatase hVH1
-
-
-
-
Dual specificity protein phosphatase hVH2
-
-
-
-
Dual specificity protein phosphatase hVH3
-
-
-
-
Dual specificity protein phosphatase PYST1
-
-
-
-
Dual specificity protein phosphatase PYST2
-
-
-
-
Dual specificity protein phosphatase VHR
-
-
-
-
dual-specificity (Thr/Tyr) MAPK protein phosphatase
-
-
dual-specificity phosphatase
-
dual-specificity protein tyrosine phosphatase 18
-
-
Dual-specificity tyrosine phosphatase TS-DSP6
-
-
-
-
Dual-specificity tyrosine phosphatase YVH1
-
-
-
-
ES cell phosphatase
-
-
-
-
FAP-1
-
-
HCP
-
-
-
-
HD-PTP
Hematopoietic cell protein-tyrosine phosphatase
-
-
-
-
Hematopoietic cell protein-tyrosine phosphatase 70Z-PEP
-
-
-
-
Hematopoietic protein-tyrosine phosphatase
-
-
-
-
hematopoietic tyrosine phosphatase
-
HEPTP
His domain protein tyrosine phosphatase
-
histidine domain-protein tyrosine phosphatase
-
-
HPTP beta-like tyrosine phosphatase
-
-
-
-
HPTP eta
-
-
-
-
HPTPbeta
-
-
HPTPbeta-CD
-
hPTPE1
-
-
-
-
ICAAR
-
-
-
-
insulinoma associated protein tyrosine phosphatase 2
-
islet cell antigen-related PTP
-
-
Islet cell autoantigen related protein
-
-
-
-
kinase associated phosphatase
-
-
-
-
kinase interaction motif phosphatase
-
L-CA
-
-
-
-
Late protein H1
-
-
-
-
LCA
-
-
-
-
LCA-related phosphatase
-
-
-
-
LDP-3
UniProt
leucocyte common antigen-related protein tyrosine phosphatase
-
-
Leukocyte antigen related
-
-
-
-
leukocyte common antigen-related
-
-
LMW-PTP
low molecular mass dual specificity phosphatase 3
UniProt
Low molecular weight cytosolic acid phosphatase
-
-
-
-
low molecular weight protein tyrosine phosphatase
-
low molecular weight-PTP
-
-
LRP
-
-
-
-
Lymphoid phosphatase
-
-
-
-
lymphoid-specific tyrosine phosphatase
-
-
M1851
-
-
-
-
MAP kinase phosphatase
-
MAP-kinase phosphatase CPG21
-
-
-
-
MAPK-specific tyrosine phosphatase
-
MEG
-
-
-
-
mitogen-activated protein kinase phosphatase
-
mitogen-activated protein kinase phosphatase-1
-
-
mitogen-activated protein kinase-specific tyrosine phosphatase
-
Mitosis initiation protein
-
-
-
-
Mitosis initiation protein MIH1
-
-
-
-
Mitotic inducer homolog
-
-
-
-
MKP-1
-
trivial names CL100, erp, 3CH134, hVH1
MKP-1 like protein tyrosine phosphatase
-
-
-
-
MKP-2
-
trivial names Typ1, Sty8, hVH2
MKP-3
MKP-4
MKP-5
MKP-7
-
-
MKP-X
-
trivial names Pyst2, B59
MKP1
-
a dual-specificity phosphatase
MKP5-C
catalytic domain of MKP5
MPTP
-
-
-
-
MPTP-PEST
-
-
-
-
NC-PTPCOM1
Neural-specific protein-tyrosine phosphatase
-
-
-
-
non-receptor protein tyrosine phosphatase
-
-
ORF5
-
-
-
-
OST-PTP
osteoclastic protein-tyrosine phosphatase
-
P19-PTP
-
-
-
-
p52shc
-
-
p66shc
-
-
P80
-
-
-
-
PC12-PTP1
-
-
-
-
PCPTP1
UniProt
PEST
-
-
Phogrin
-
-
-
-
Phosphacan
-
-
-
-
phosphatase of regenerating liver-3
-
-
phosphatase, phosphoprotein (phosphotyrosine)
-
-
-
-
phosphatase, phosphotyrosine
-
-
-
-
phosphoprotein phosphatase (phosphotyrosine)
-
-
-
-
phosphotyrosine histone phosphatase
-
-
-
-
phosphotyrosine phosphatase
-
-
-
-
Phosphotyrosine phosphatase 13
-
-
-
-
phosphotyrosine phosphatase 1B
-
-
phosphotyrosine protein phosphatase
-
-
-
-
phosphotyrosine-specific PP
-
-
phosphotyrosylprotein phosphatase
-
-
-
-
PP2A
-
-
Protein phosphatase 1B
-
protein phosphatase 2A
-
-
protein phosphotyrosine phosphatase
-
-
-
-
protein tyrosine phosphatase
protein tyrosine phosphatase 1B
protein tyrosine phosphatase beta
-
protein tyrosine phosphatase epsilon
-
protein tyrosine phosphatase N12
-
Protein tyrosine phosphatase receptor-type T
-
-
protein tyrosine phosphatase SHP-1
-
-
protein tyrosine phosphatase, non-receptor type 1
-
protein tyrosine phosphatase, receptor-type, Z polypeptide 1
-
-
protein tyrosine phosphatase-1B
protein tyrosine phosphatase-2
-
-
protein tyrosine phosphatase-BL
-
-
Protein tyrosine phosphatase-NP
-
-
-
-
Protein-protein-tyrosine phosphatase HA2
-
-
-
-
protein-tyrosine phosphatase
Protein-tyrosine phosphatase 1B
Protein-tyrosine phosphatase 1C
-
-
-
-
Protein-tyrosine phosphatase 1E
-
-
-
-
Protein-tyrosine phosphatase 2C
-
-
-
-
Protein-tyrosine phosphatase 2E
-
-
-
-
Protein-tyrosine phosphatase 3CH134
-
-
-
-
Protein-tyrosine phosphatase CL100
-
-
-
-
Protein-tyrosine phosphatase D1
Protein-tyrosine phosphatase ERP
-
-
-
-
Protein-tyrosine phosphatase G1
-
-
-
-
Protein-tyrosine phosphatase H1
-
-
-
-
Protein-tyrosine phosphatase LC-PTP
-
-
-
-
Protein-tyrosine phosphatase MEG1
-
-
-
-
Protein-tyrosine phosphatase MEG2
-
-
-
-
Protein-tyrosine phosphatase P19
-
-
-
-
Protein-tyrosine phosphatase PCPTP1
-
-
-
-
Protein-tyrosine phosphatase pez
-
-
-
-
Protein-tyrosine phosphatase PTP-RL10
-
-
-
-
Protein-tyrosine phosphatase PTP36
-
-
-
-
Protein-tyrosine phosphatase PTPL1
-
-
-
-
Protein-tyrosine phosphatase striatum-enriched
-
-
-
-
Protein-tyrosine phosphatase SYP
-
-
-
-
Protein-tyrosine-phosphatase SL
-
-
-
-
Protein-tyrosine-phosphate phosphohydrolase
-
-
-
-
PTEN
-
-
PTEN phosphoprotein phosphatase
-
-
PTP IA-2beta
-
-
-
-
PTP-1B
PTP-1C
-
-
-
-
PTP-1D
-
-
-
-
PTP-2C
-
-
-
-
PTP-BAS
PTP-BL
-
-
PTP-E1
-
-
-
-
PTP-eta
-
-
PTP-H1
-
-
-
-
PTP-HA2
-
-
-
-
PTP-MEG2
-
-
PTP-NP
-
-
-
-
PTP-PEST
PTP-phosphatase
-
-
PTP-SH2beta
-
-
-
-
PTP1
-
-
PTP1B
PTP1C
-
-
-
-
PTP1D
-
-
-
-
PTP1e
-
-
PTP2C
-
-
-
-
PTPalpha
PTPase YVH1
-
-
-
-
PTPase-MEG1
PTPase-MEG2
PTPB1
PTPbeta
PTPD1
PTPepsilon
-
PTPG1
-
-
-
-
PTPgamma
-
-
PTPL1
-
-
PTPMEG
-
-
PTPN11
PTPN14
PTPN20 variant 15
-
PTPN22
PTPN23
PTPN5
PTPN6
PTPN7
PTPNE6
-
-
-
-
PTPP
-
-
PTPRdelta
-
PTPRJ
PTPRomega
-
PTPRQ
PTPRR
PTPRT
PTPRV
-
-
PTPRZ1
-
-
PY protein phosphatase
-
-
-
-
R-PTP-alpha
-
-
-
-
R-PTP-beta
-
-
-
-
R-PTP-delta
-
-
-
-
R-PTP-epsilon
-
-
-
-
R-PTP-eta
-
-
-
-
R-PTP-gamma
-
-
-
-
R-PTP-kappa
-
-
-
-
R-PTP-mu
-
-
-
-
R-PTP-zeta
-
-
-
-
receptor protein tyrosine phosphatase isoform delta
-
receptor protein tyrosine phosphatase isoform omega
-
receptor protein tyrosine phosphatase T
-
-
receptor protein tyrosine phosphatase {kappa}
-
-
receptor PTPepsilon
-
Receptor-linked protein-tyrosine phosphatase 10D
-
-
-
-
Receptor-linked protein-tyrosine phosphatase 99A
-
-
-
-
receptor-type protein tyrosine phosphatase J
-
-
Receptor-type protein-tyrosine phosphatase-kappa
-
-
receptor-type tyrosine-protein phosphatase R
UniProt
RNA/RNP complex-intereracting phosphatase
-
-
-
-
ROL B protein
-
-
-
-
RPTPalpha
RPTPdelta
-
RPTPgamma
-
RPTPkappa
RPTPlambda
-
RPTPsigma
-
Scr homology 2-containing tyrosine phosphatase
-
-
selective striatal enriched protein phosphatase
-
SH-PTP1
-
-
-
-
SH-PTP2
-
-
-
-
SH-PTP3
-
-
-
-
SH2 domain-containing tyrosine phosphatase-1
-
-
SH2 domain-containing tyrosine phosphatase-2
-
-
SHP
-
-
-
-
SHP-1
SHP-2
Small tyrosine phosphatase
-
-
-
-
Small, acidic phosphotyrosine protein phosphatase
-
-
-
-
SPH-1
-
-
SPH-2
-
-
Src homology region 2 domain-containing phosphatase 1
-
-
Src homology-2 domain containing protein tyrosine phosphatase-1
-
-
Src homology-2 domain containing protein tyrosine phosphatase-2
-
-
striatal-enriched PTP
-
-
String protein
-
-
-
-
Syp
-
-
-
-
T cell protein tyrosine phosphatase
-
-
T-cell protein tyrosine phosphatase
-
-
T-cell protein-tyrosine phosphatase
-
-
-
-
T-cell PTP
T-DSP11
-
-
-
-
T200
-
-
-
-
TC PTP
-
-
TC48
isoform
TCPTP
testis- and skeletal-muscle-specific DSP
-
-
testis- and skeletal-muscle-specific dual specificity protein phosphatase
-
-
Testis-and skeletal-muscle-specific DSP
-
-
-
-
TMDP
-
-
tyrosine O-phosphate phosphatase
-
-
-
-
tyrosine phosphatase
Tyrosine phosphatase CBPTP
-
-
-
-
tyrosine phosphatase IA-2
-
tyrosine phosphatase-1B
-
tyrosine-protein phosphatase non-receptor type 5
UniProt
tyrosylprotein phosphatase
-
-
-
-
vaccinia H1-related PTP
-
[phosphotyrosine]protein phosphatase
-
-
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
protein-tyrosine-phosphate phosphohydrolase
Dephosphorylates O-phosphotyrosine groups in phosphoproteins, such as the products of EC 2.7.10.2, non-specific protein-tyrosine kinase.
CAS REGISTRY NUMBER
COMMENTARY hide
79747-53-8
-
97162-86-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
show the reaction diagram
[Eps15 peptide846-854 P850V]-tyrosine phosphate + H2O
[Eps15 peptide846-854 P850V]-tyrosine + phosphate
show the reaction diagram
-
-
-
?
[Eps15 peptide846-854]-tyrosine phosphate + H2O
[Eps15 peptide846-854]-tyrosine + phosphate
show the reaction diagram
-
-
-
?
[Eps15 peptide]-tyrosine phosphate + H2O
[Eps15 peptide]-tyrosine + phosphate
show the reaction diagram
3,6-fluorescein diphosphate + H2O
? + phosphate
show the reaction diagram
-
-
-
?
3-nitrobenzyl phosphate + H2O
3-nitrobenzyl alcohol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
4-nitrophenylphosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
6,8-difluoro-4-methylumbelliferyl phosphate + H2O
6,8-difluoro-4-methylumbelliferol + phosphate
show the reaction diagram
6,8-difluoro-4-methylumbelliferyl phosphate + H2O
6,8-difluoro-4-methylumbelliferone + phosphate
show the reaction diagram
AAAAApYEEVH + H2O
AAAAAYEEVH + phosphate
show the reaction diagram
-
substrate of RPTPalpha
-
-
?
AAAAApYRHRR + H2O
AAAAAYRHRR + phosphate
show the reaction diagram
-
substrate of RPTPalpha
-
-
?
Ac-AAAApYAAAA-NH2 + H2O
Ac-AAAAYAAAA-NH2 + phosphate
show the reaction diagram
-
-
-
-
?
Ac-AAAEpYAAAA-NH2 + H2O
Ac-AAAEYAAAA-NH2 + phosphate
show the reaction diagram
-
-
-
-
?
Ac-AAAQpYAAAA-NH2 + H2O
Ac-AAAQYAAAA-NH2 + phosphate
show the reaction diagram
-
-
-
-
?
Ac-DGEEpYDDPF-NH2 + H2O
Ac-DGEEYDDPF-NH2 + phosphate
show the reaction diagram
-
SKAP-HOM Tyr75 peptide
-
-
?
Ac-ENDEpYTARE-NH2 + H2O
Ac-ENDEYTARE-NH2 + phosphate
show the reaction diagram
-
Lck Tyr394 peptide
-
-
?
Ac-TEPQpYQPGE-NH2 + H2O
Ac-TEPQYQPGE-NH2 + phosphate
show the reaction diagram
-
Lck Tyr505 peptide
-
-
?
Ac-YGEEpYDDLY-NH2 + H2O
Ac-YGEEYDDLY-NH2 + phosphate
show the reaction diagram
-
consensus peptide 1
-
-
?
Ac-YGYEpYDDEY-NH2 + H2O
Ac-YGYEYDDEY-NH2 + phosphate
show the reaction diagram
-
consensus peptide 2
-
-
?
acetyl-DADEpY-NH2 + H2O
acetyl-DADEY-NH2 + phosphate
show the reaction diagram
-
-
-
?
acetyl-DADEpYL-NH2 + H2O
acetyl-DADEYL-NH2 + phosphate
show the reaction diagram
-
-
?
ADEDFpYAA + H2O
ADEDFYAA + phosphate
show the reaction diagram
-
substrate of SHP-2
-
-
?
AKFEDTpYAA + H2O
AKFEDTYAA + phosphate
show the reaction diagram
-
substrate of SHP-1
-
-
?
angiotensin I + H2O
? + phosphate
show the reaction diagram
-
-
-
-
?
ARKRIpYAA + H2O
ARKRIYAA + phosphate
show the reaction diagram
-
substrate of RPTPalpha
-
-
?
ASSDDpYAA + H2O
ASSDDYAA + phosphate
show the reaction diagram
-
substrate of RPTPalpha
-
-
?
AVWEFpYpYAA + H2O
? + phosphate
show the reaction diagram
-
substrate of SHP-1
-
-
?
AWSpYADpYAA + H2O
? + phosphate
show the reaction diagram
-
substrate of SHP-1
-
-
?
AYTEpYTpYAA + H2O
? + phosphate
show the reaction diagram
-
substrate of SHP-1
-
-
?
bis(4-nitrophenyl) phosphate + H2O
?
show the reaction diagram
-
-
-
?
bis-(p-phosphophenyl) methane + H2O
?
show the reaction diagram
synthetic high-affinity low-molecular weight nonpeptide substrate
-
-
?
bovine serum albumin + H2O
? + phosphate
show the reaction diagram
carrier protein-Cdc2-phosphotyrosine + H2O
carrier protein-Cdc2-tyrosine + phosphate
show the reaction diagram
-
-
-
-
?
carrier protein-Y3-phosphotyrosine + H2O
carrier protein-Y3-tyrosine + phosphate
show the reaction diagram
-
-
-
-
?
carrier protein-Y5-phosphotyrosine + H2O
carrier protein-Y5-tyrosine + phosphate
show the reaction diagram
-
-
-
-
?
Cdk2-pTpY + H2O
Cdk2-TpY + phosphate
show the reaction diagram
-
dephosphorylates Cdk/cyclins on pThr14 and/or pTyr15 residues
-
-
?
Cdk2-pTpY/CycA + H2O
Cdk2-pTY/CycA + phosphate
show the reaction diagram
-
-
-
-
?
DADE(pY)LIPQQG + H2O
DADEYLIPQQG + phosphate
show the reaction diagram
DADEpYIPQQG + H2O
DADEYIPQQG + phosphate
show the reaction diagram
-
specific substrate for PTP1B
-
-
?
DADEpYLIPQQG + H2O
DADEYLIPQQG + phosphate
show the reaction diagram
DAEDFpYAA + H2O
DAEDFYAA + phosphate
show the reaction diagram
-
substrate of SHP-2
-
-
?
DDT-(3,5-difluoro)YDpYAA + H2O
DDT-(3,5-difluoro)YDYAA + phosphate
show the reaction diagram
-
-
-
-
?
DDTYDpYAA + H2O
DDTYDYAA + phosphate
show the reaction diagram
-
-
-
-
?
DFEDFpYAA + H2O
DFEDFYAA + phosphate
show the reaction diagram
-
substrate of SHP-2
-
-
?
difluoromethylumbelliferyl phosphate + H2O
difluoromethylumbelliferone + phosphate
show the reaction diagram
-
-
-
?
DNL-(3,5-difluoro)YpYWD + H2O
DNL-(3,5-difluoro)YYWD + phosphate
show the reaction diagram
-
-
-
-
?
DNLYpYWD + H2O
DNLYYWD + phosphate
show the reaction diagram
-
-
-
-
?
DWEDFpYAA + H2O
DWEDFYAA + phosphate
show the reaction diagram
-
substrate of SHP-2
-
-
?
EADTApYAA + H2O
EADTAYAA + phosphate
show the reaction diagram
-
substrate of RPTPalpha
-
-
?
EIFDFpYAA + H2O
EIFDFYAA + phosphate
show the reaction diagram
-
substrate of SHP-1 and SHP-2
-
-
?
ENDpYINASL + H2O
ENDYINASL + phosphate
show the reaction diagram
-
-
-
-
?
ENPE(pY)LGLD + H2O
ENPEYLGLD + phosphate
show the reaction diagram
dephosphorylation at Tyr1248
-
-
?
ENPE(pY)LTPQ + H2O
ENPEYLTPQ + phosphate
show the reaction diagram
dephosphorylation at Tyr1196
-
-
?
EphA3-phosphotyrosine + H2O
EphA3-tyrosine + phosphate
show the reaction diagram
-
-
-
-
?
epidermal growth factor + H2O
? + phosphate
show the reaction diagram
-
-
-
-
?
epidermal growth factor receptor + H2O
? + phosphate
show the reaction diagram
-
with phosphotyrosine Tyr992
-
-
?
FDEDFpYAA + H2O
FDEDFYAA + phosphate
show the reaction diagram
-
substrate of SHP-2
-
-
?
FDIDIpYAA + H2O
FDIDIYAA + phosphate
show the reaction diagram
-
substrate of SHP-1 and SHP-2
-
-
?
FDNL(pY)2WDQD + H2O
FDNLYYWDQD + 2 phosphate
show the reaction diagram
dephosphorylation at Tyr1221/1222
-
-
?
fluorescein diphosphate + H2O
?
show the reaction diagram
-
-
-
-
?
fluorescein diphosphate + H2O
fluorescein phosphate + phosphate
show the reaction diagram
-
-
-
?
FYDIDpYAA + H2O
FYDIDYAA + phosphate
show the reaction diagram
-
substrate of SHP-1 and SHP-2
-
-
?
Gab1 tyrosine phosphate + H2O
Gab1 tyrosine + phosphate
show the reaction diagram
-
-
-
-
?
GESDGGpYMDMSKD + H2O
GESDGGYMDMSKD + phosphate
show the reaction diagram
-
this peptide corresponds to the sequence containing Tyr740 of the human platelet-derived growth factor receptor
-
-
?
GNGDpYMPMSPKS + H2O
GNGDYMPMSPKS + phosphate
show the reaction diagram
-
-
-
-
?
human A431 membrane protein + H2O
? + phosphate
show the reaction diagram
-
-
-
-
?
insulin receptor phosphopeptide + H2O
insulin receptor peptide + phosphate
show the reaction diagram
-
-
-
-
?
insulin-like growth factor-1 + H2O
? + phosphate
show the reaction diagram
-
-
-
-
?
LDEpYVATR + H2O
LDEYVATR + phosphate
show the reaction diagram
-
-
-
?
LIEDNEpYTARQGA + H2O
LIEDNEYTARQGA + phosphate
show the reaction diagram
-
substrate of RPTPalpha
-
-
?
lysozyme + H2O
? + phosphate
show the reaction diagram
-
reduced, carboxymethylated and maleylated
-
-
?
membrane protein 3 + H2O
? + phosphate
show the reaction diagram
-
-
-
-
?
myelin basic protein + H2O
? + phosphate
show the reaction diagram
-
-
-
-
?
myosin P-light chain + H2O
? + phosphate
show the reaction diagram
-
-
-
-
?
n-nitrophenyl phosphate + H2O
n-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
O-phospho-L-tyrosine + H2O
tyrosine + phosphate
show the reaction diagram
-
-
-
?
p-nitrophenyl phosphate
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
p38 + H2O
?
show the reaction diagram
paxilin tyrosine phosphate + H2O
paxilin tyrosine + phosphate
show the reaction diagram
PGSAAP-pY-LKTKFI + H2O
PGSAAPYLKTKFI + phosphate
show the reaction diagram
STAT3 peptide
-
-
?
phosphocaveolin-1 + H2O
caveolin-1 + phosphate
show the reaction diagram
-
phosphorylated at Y14
-
-
?
phosphorylated actin + H2O
actin + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated adenomatous Polyposis coli-protein + H2O
adenomatous Polyposis coli-protein + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated alpha-actinin + H2O
alpha-actinin + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated BCR-Abl + H2O
BCR-Abl + phosphate
show the reaction diagram
-
-
-
?
phosphorylated c-MET + H2O
c-MET + phosphate
show the reaction diagram
phosphorylated CD3 epsilon + H2O
CD3 epsilon + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated Cdk2-pTpY/CycA protein + H2O
Cdk2-pTpY/CycA protein + phosphate
show the reaction diagram
-
-
-
?
phosphorylated EphA2 receptor + H2O
EphA2 receptor + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated EphA5 + H2O
EphA5 + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated epidermal growth factor receptor + H2O
epidermal growth factor receptor + phosphate
show the reaction diagram
phosphorylated ErbB1 + H2O
ErbB1 + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated ErbB2 + H2O
ErbB2 + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated ERK1 + H2O
ERK1 + phosphate
show the reaction diagram
-
-
-
?
phosphorylated ERK2 + H2O
ERK2 + phosphate
show the reaction diagram
HePTP binds the phosphorylated tyrosine of the Erk2 peptide (pY185), Erk2 residue T183, which is phosphorylated in maximally activated Erk2, is not essential for substrate recognition and binding by HePTP
-
-
?
phosphorylated extracellular signal regulated kinase + H2O
extracellular signal regulated kinase + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated Ezrin + H2O
Ezrin + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated focal adhesion kinase + H2O
focal adhesion kinase + phosphate
show the reaction diagram
-
dephosphorylation occurs at Tyr-397, PTPD1 activity is required for focal adhesion kinase autophosphorylation and adhesion plaque stability
-
-
?
phosphorylated IGF-I receptor + H2O
IGF-I receptor + phosphate
show the reaction diagram
-
isozyme p52shc
-
-
?
phosphorylated insulin receptor + H2O
insulin receptor + phosphate
show the reaction diagram
phosphorylated JAK2 + H2O
JAK2 + phosphate
show the reaction diagram
-
SHP2 dephosphorylates the Tyr1007 site, preventing the formation of the JAK2-Socs1 complex
-
-
?
phosphorylated Janus kinase 2 + H2O
Janus kinase 2 + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated JNK + H2O
JNK + phosphate
show the reaction diagram
-
-
-
?
phosphorylated Jun amino-terminal kinase + H2O
Jun amino-terminal kinase + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated Lck + H2O
Lck + phosphate
show the reaction diagram
-
component of the T cell receptor signaling pathway
-
-
?
phosphorylated Munc18c + H2O
Munc18c + phosphate
show the reaction diagram
-
dephosphorylation at Tyr218/219 and Tyr521
-
-
?
phosphorylated p130 Crk-associated substrate + H2O
p130 Crk-associated substrate + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated p38 mitogen-activated protein kinase + H2O
p38 mitogen-activated protein kinase + phosphate
show the reaction diagram
phosphorylated phospholipase Cgamma + H2O
phospholipase Cgamma + phosphate
show the reaction diagram
-
dephosphorylation occurs at Tyr-783
-
-
?
phosphorylated platelet-derived growth factor receptor + H2O
platelet-derived growth factor receptor + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated protein kinase-like endoplasmic reticulum kinase + H2O
protein kinase-like endoplasmic reticulum kinase + phosphate
show the reaction diagram
-
dephosphorylation at Tyr615
-
-
?
phosphorylated protein p85
protein p85 + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated pyruvate kinase M2 + H2O
pyruvate kinase M2 + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated RET(C634R) oncoprotein + H2O
RET(C634R) oncoprotein + phosphate
show the reaction diagram
-
dephosphorylation at Tyr905 and Tyr1062
-
-
?
phosphorylated RET-MEN2A oncoprotein + H2O
RET-MEN2A oncoprotein + phosphate
show the reaction diagram
-
dephosphorylation at Tyr905 and Tyr1062
-
-
?
phosphorylated RET/PTC1 oncoprotein + H2O
RET/PTC1 oncoprotein + phosphate
show the reaction diagram
-
dephosphorylation at Tyr905 and Tyr1062
-
-
?
phosphorylated signal transducer and activator of transcription 3 + H2O
signal transducer and activator of transcription 3 + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated Src + H2O
Src + phosphate
show the reaction diagram
phosphorylated Src protein + H2O
Src protein + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated Src tyrosine kinase + H2O
Src tyrosine kinase + phosphate
show the reaction diagram
-
PTPD1 associates with and activates Src tyrosine kinase
-
-
?
phosphorylated STAT1 + H2O
STAT1 + phosphate
show the reaction diagram
phosphorylated STAT3 + H2O
STAT3 + phosphate
show the reaction diagram
phosphorylated STAT5 + H2O
STAT5 + phosphate
show the reaction diagram
-
purified SHP2 protein directly dephosphorylates STAT5 or tyrosine-phosphorylated peptides derived from STAT5
-
-
?
phosphorylated T cell antigen receptor zeta + H2O
T cell antigen receptor zeta + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated valosin containing protein + H2O
valosin containing protein + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated vascular endothelial growth factor receptor 2 + H2O
vascular endothelial growth factor receptor 2 + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated Vav + H2O
Vav + phosphate
show the reaction diagram
-
component of the T cell receptor signaling pathway
-
-
?
phosphorylated ZAP-70 + H2O
ZAP-70 + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated Zap70 + H2O
Zap70 + phosphate
show the reaction diagram
-
protein-tyrosine kinase
-
-
?
phosphothreonine + H2O
threonine + phosphate
show the reaction diagram
-
-
-
-
?
phosphotyrosine + H2O
tyrosine + phosphate
show the reaction diagram
phosphotyrosine serum albumin + H2O
? + phosphate
show the reaction diagram
-
-
-
-
?
phosphotyrosyl bovine serum albumin + H2O
tyrosyl-bovine serum albumin + phosphate
show the reaction diagram
-
-
-
-
?
phosphotyrosyl-casein + H2O
? + phosphate
show the reaction diagram
-
-
-
-
?
phosphotyrosyl-STAT3 + H2O
STAT3 + phosphate
show the reaction diagram
platelet-derived growth factor receptor + H2O
? + phosphate
show the reaction diagram
PLC-gamma1 tyrosine phosphate + H2O
PLC-gamma1 tyrosine + phosphate
show the reaction diagram
-
-
-
-
?
PLQR(pY)SEDP + H2O
PLQRYSEDP + phosphate
show the reaction diagram
dephosphorylation at Tyr1112
-
-
?
poly(Glu,Tyr) + H2O
? + phosphate
show the reaction diagram
-
-
-
-
?
PQDKEY-pY-KVKEPG + H2O
PQDKEYYKVKEPG + phosphate
show the reaction diagram
JAK2 peptide
-
-
?
protein FAK + H2O
?
show the reaction diagram
-
-
-
-
?
protein Shc + H2O
?
show the reaction diagram
-
-
-
-
?
RE-(3,5-difluoro)YEFpYAA + H2O
RE-(3,5-difluoro)YEFYAA + phosphate
show the reaction diagram
-
-
-
-
?
REYEFpYAA + H2O
REYEFYAA + phosphate
show the reaction diagram
-
-
-
-
?
RKGSGD-pY-MPMSPK + H2O
RKGSGDYMPMSPK + phosphate
show the reaction diagram
IRS1 peptide
-
-
?
RRISTpYAA + H2O
RRISTYAA + phosphate
show the reaction diagram
-
substrate of RPTPalpha
-
-
?
RRLIEDAEpYAARG + H2O
RRLIEDAEYAARG + phosphate
show the reaction diagram
-
-
-
-
?
SASASpYDWEF + H2O
SASASYDWEF + phosphate
show the reaction diagram
-
substrate of SHP-1 and SHP-2
-
-
?
SASASpYSASA + H2O
SASASYSASA + phosphate
show the reaction diagram
SKAP-HOM + H2O
?
show the reaction diagram
-
a cytosolic adaptor protein required for proper activation of the immune system, a bona fide Lyp substrate
-
-
?
soluble N-ethylmaleimide-sensitive factor attachment protein receptor + H2O
soluble N-ethylmaleimide-sensitive factor attachment protein receptor + phosphate
show the reaction diagram
-
-
-
-
?
TATEPQpYQPGEN + H2O
TATEPQYQPGEN + phosphate
show the reaction diagram
-
substrate of RPTPalpha
-
-
?
TATEPQpYQPGENL + H2O
TATEPQYQPGENL + phosphate
show the reaction diagram
-
substrate of RPTPalpha
-
-
?
TGFLTELpYVATRWY + H2O
TGFLTELYVATRWY + phosphate
show the reaction diagram
-
this peptide corresponds to the sequence containing Tyr204 of the human extracellular signal-regulated kinase
-
-
?
TSTEPQpYQPGENL + H2O
TSTEPQYQPGENL + phosphate
show the reaction diagram
tyrosin kinase + H2O
? + phosphate
show the reaction diagram
-
-
-
-
?
WAGDDpYAA + H2O
WAGDDYAA + phosphate
show the reaction diagram
-
substrate of SHP-1 and SHP-2
-
-
?
WDEDFpYAA + H2O
WDEDFYAA + phosphate
show the reaction diagram
-
substrate of SHP-2
-
-
?
WDEDFpYDWEF + H2O
WDEDFYDWEF + phosphate
show the reaction diagram
-
substrate of SHP-1 and SHP-2
-
-
?
WDEDFpYRWKF + H2O
WDEDFYRWKF + phosphate
show the reaction diagram
-
substrate of SHP-1 and SHP-2
-
-
?
WDEDFpYSASA + H2O
WDEDFYSASA + phosphate
show the reaction diagram
WRKRFpYDWEF + H2O
WRKRFYDWEF + phosphate
show the reaction diagram
-
substrate of SHP-1 and SHP-2
-
-
?
Y527-phosphorylated Src + H2O
Src + phosphate
show the reaction diagram
-
-
-
-
?
YCRPESQEHPEADPGAAPpYLK + H2O
YCRPESQEHPEADPGAAYLK + phosphate
show the reaction diagram
-
YCRPESQEHPEADPGAApYLK is signal transducer and activator of transcription 3, is dephosphorylated at Y705
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
show the reaction diagram
[epidermal growth factor receptor 2]-tyrosine phosphate + H2O
[epidermal growth factor receptor 2]-tyrosine + phosphate
show the reaction diagram
dephosphorylation of epidermal growth factor receptor 2 (HER2)-pY1196 site
-
-
?
[epidermal growth factor receptor]-tyrosine phosphate + H2O
[epidermal growth factor receptor]-tyrosine + phosphate
show the reaction diagram
-
-
-
?
[Eps15 peptide846-854]-tyrosine phosphate + H2O
[Eps15 peptide846-854]-tyrosine + phosphate
show the reaction diagram
[FAK]-tyrosine phosphate + H2O
[FAK]-tyrosine + phosphate
show the reaction diagram
dephosphorylation at Tyr397
-
-
?
[FYN kinase]-tyrosine phosphate + H2O
[FYN kinase]-tyrosine + phosphate
show the reaction diagram
-
-
-
?
[HER2]-tyrosine phosphate + H2O
[HER2]-tyrosine + phosphate
show the reaction diagram
dephosphorylation at Tyr1112, Tyr1196, Tyr1221, Tyr1222, and Tyr1248
-
-
?
[insulin receptor kinase]-tyrosine phosphate + H2O
[insulin receptor kinase]-tyrosine + phosphate
show the reaction diagram
-
-
-
?
[p130Cas]-tyrosine phosphate + H2O
[p130Cas]-tyrosine + phosphate
show the reaction diagram
dephosphorylation at Tyr165
-
-
?
[p190RhoGAP]-tyrosine phosphate + H2O
[p190RhoGAP]-tyrosine + phosphate
show the reaction diagram
dephosphorylation at Tyr1105
-
-
?
[paxillin]-tyrosine phosphate + H2O
[paxillin]-tyrosine + phosphate
show the reaction diagram
dephosphorylation at Tyr118
-
-
?
[SRC]-tyrosine phosphate + H2O
[SRC]-tyrosine + phosphate
show the reaction diagram
dephosphorylation at Tyr416
-
-
?
[VAV2]-tyrosine phosphate + H2O
[VAV2]-tyrosine + phosphate
show the reaction diagram
dephosphorylation at Tyr172
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
show the reaction diagram
[Eps15 peptide]-tyrosine phosphate + H2O
[Eps15 peptide]-tyrosine + phosphate
show the reaction diagram
DADE(pY)LIPQQG + H2O
DADEYLIPQQG + phosphate
show the reaction diagram
a physiological phosphopeptide substrate of enzyme PTP1B
-
-
?
paxilin tyrosine phosphate + H2O
paxilin tyrosine + phosphate
show the reaction diagram
-
PTPRT specifically regulates paxillin phosphorylation at Tyr88 in colorectal cancer cells
-
-
?
phosphocaveolin-1 + H2O
caveolin-1 + phosphate
show the reaction diagram
-
phosphorylated at Y14
-
-
?
phosphorylated alpha-actinin + H2O
alpha-actinin + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated CD3 epsilon + H2O
CD3 epsilon + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated epidermal growth factor receptor + H2O
epidermal growth factor receptor + phosphate
show the reaction diagram
-
inactivation of EGFR
-
-
?
phosphorylated IGF-I receptor + H2O
IGF-I receptor + phosphate
show the reaction diagram
-
isozyme p52shc
-
-
?
phosphorylated Lck + H2O
Lck + phosphate
show the reaction diagram
-
component of the T cell receptor signaling pathway
-
-
?
phosphorylated p130 Crk-associated substrate + H2O
p130 Crk-associated substrate + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated T cell antigen receptor zeta + H2O
T cell antigen receptor zeta + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated valosin containing protein + H2O
valosin containing protein + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated Vav + H2O
Vav + phosphate
show the reaction diagram
-
component of the T cell receptor signaling pathway
-
-
?
phosphorylated Zap70 + H2O
Zap70 + phosphate
show the reaction diagram
-
protein-tyrosine kinase
-
-
?
phosphotyrosyl-STAT3 + H2O
STAT3 + phosphate
show the reaction diagram
-
signal transducers and activator of transcription 3, STAT3, is a transcription factor that is associated with survival, proliferation, chemoresistance, and angiogenesis of tumor cells
-
-
?
Y527-phosphorylated Src + H2O
Src + phosphate
show the reaction diagram
-
-
-
-
?
[a protein]-tyrosine phosphate + H2O
[a protein]-tyrosine + phosphate
show the reaction diagram
[epidermal growth factor receptor 2]-tyrosine phosphate + H2O
[epidermal growth factor receptor 2]-tyrosine + phosphate
show the reaction diagram
dephosphorylation of epidermal growth factor receptor 2 (HER2)-pY1196 site
-
-
?
[FYN kinase]-tyrosine phosphate + H2O
[FYN kinase]-tyrosine + phosphate
show the reaction diagram
-
-
-
?
[insulin receptor kinase]-tyrosine phosphate + H2O
[insulin receptor kinase]-tyrosine + phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NaF
-
activation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
((1E)-2-nitroprop-1-en-1-yl)benzene
-
50% inhibition at 0.023 mM in absence of 2-mercaptoethanol, at 0.515 mM in presence of 1 mM 2-mercaptoethanol
((2-bromo-4-((((2E)-3-phenylprop-2-en-1-yl)sulfanyl)methyl)phenyl)carbonyl)phosphonate
50% inhibition at 810 nM for wild-type, at 1290 nM for mutant S295F
((2-bromo-4-(((4-chlorobenzyl)thio)methyl)phenyl)(difluoro)methyl)phosphonate
50% inhibition at 285 nM for wild-type, at 1644 nM for mutant S295F
((2-phenyl-2-(phenylcarbonyl)propane-1,3-diyl)bis(benzene-4,1-diyl(difluoromethanediyl)))bis(phosphonate)
50% inhibition at 82 nM for wild-type, at 399 nM for mutant S295F
((4-((((3'-(acetylsulfamoyl)biphenyl-4-yl)methyl)sulfanyl)methyl)-2-bromophenyl)(difluoro)methyl)phosphonate
50% inhibition at 2.2 nM for wild-type, at 11 nM for mutant S295F
((4-((4E)-2-(1,3-benzothiazol-2-yl)-2-(1H-benzotriazol-1-yl)-5-phenylpent-4-en-1-yl)phenyl)(difluoro)methyl)phosphonate
50% inhibition at 47 nM for wild-type, at 260 nM for mutant S295F
((4-((4E)-2-(1,3-benzothiazol-2-yl)-2-(1H-benzotriazol-1-yl)-5-phenylpent-4-en-1-yl)phenyl)(fluoro)methyl)phosphonate
50% inhibition at 570 nM for wild-type, at 830 nM for mutant S295F
((4-((4E)-2-(1H-benzotriazol-1-yl)-2,5-diphenylpent-4-en-1-yl)phenyl)(difluoro)methyl)phosphonic acid
-
50% inhibition at 109 nM for isoform PTP-1B, at 95 nM for isoform TCPTP
((E)-2-nitrovinyl)benzene
-
i.e. trans-beta-nitrostyrene, slow-binding inhibitor, acting as a pY mimetic and binding to the enzyme active site to form an initial noncovalent E*I complex, followed by nucleophilic attack on the nitrostyrene nitro group by C215 of enzyme to form a reversible, covalent adduct. 50% inhibition at 0.0025 mM in absence of 2-mercaptoethanol, at 0.4 mM in presence of 1 mM 2-mercaptoethanol
(1-benzyl-3-methyl-2,3-dihydro-1H-imidazol-2-yl)(chloro)gold
-
i.e. [(BzMeIm)AuICl]
(1R,3aS,3bS,10aR,10bS,12aR)-1-[(2R)-4-carboxybutan-2-yl]-6,6,10a,12a-tetramethyl-1,2,3,3a,3b,4,6,7,10,10a,10b,11,12,12a-tetradecahydrocyclopenta[5,6]naphtho[1,2-f]indazole-9-carboxylic acid
-
-
(1R,5S,6S,6aR,7S,10S,10aS,11S)-10-(acetyloxy)-7-hydroxy-7,10a-dimethyl-4-methylidene-6-[(2-methylpropanoyl)oxy]-3-oxodecahydro-1H-1,5-methano-2-benzoxocin-11-yl 2-methylprop-2-enoate
no inhibition at 0.021 mM
(1S,3aR,8S,8aS,8bR)-4-henicosyl-1,8-dimethyl-3a-[(1E)-tricos-1-en-1-yl]-1,3a,5a,8,8a,8b-hexahydrobenzo[1,2-c:3,4-c']difuran-3,6-dione
-
-
(1S,3aS,4R,8S,8aS,8bR)-4-icosyl-1,8-dimethyl-3a-[(1E)-tricos-1-en-1-yl]-1,3a,4,8,8a,8b-hexahydrobenzo[1,2-c:3,4-c']difuran-3,6-dione
-
-
(2alpha,3alpha)-2,3-dihydroxyolean-12-en-28-oic acid
-
-
(2aS,3R,6aR,7aS,7bR,7cS)-2a-(hydroxymethyl)-3-icosyl-6a,7a-dimethyl-2a,3,6a,7a,7b,7c-hexahydrodifuro[2,3,4-cd:4',3',2'-hi][2]benzofuran-2,5-dione
-
-
(2aS,3R,6aR,7aS,7bR,7cS)-3-icosyl-6a,7a-dimethyl-2,5-dioxo-3,5,6a,7a,7b,7c-hexahydrodifuro[2,3,4-cd:4',3',2'-hi][2]benzofuran-2a(2H)-carbaldehyde
-
-
(2beta,3beta)-2,3-dihydroxyolean-12-en-28-oic acid
-
-
(2E)-1-(2,4-dihydroxyphenyl)-3-(4-hydroxyphenyl)prop-2-en-1-one
-
isolated from the CH2Cl2 extract of Glycyrrhiza inflata
(2E)-1-(3-aminophenyl)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)prop-2-en-1-one
-
-
(2E)-1-(4-aminophenyl)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)prop-2-en-1-one
-
-
(2E)-1-[3-(benzyloxy)phenyl]-3-(5-bromo-4-hydroxy-2-methoxyphenyl)prop-2-en-1-one
-
-
(2E)-3-(4-hydroxy-2-methoxyphenyl)-1-(4-hydroxyphenyl)prop-2-en-1-one
-
isolated from the CH2Cl2 extract of Glycyrrhiza inflata
(2E)-3-(5-bromo-2,4-dihydroxyphenyl)-1-[4-methoxy-3-(3-methylbut-3-en-2-yl)phenyl]prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-(3-methoxyphenyl)prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-(3-[[(methoxycarbonyl)sulfanyl]amino]phenyl)prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-(4-butoxyphenyl)prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-(4-hydroxyphenyl)prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-(4-methoxyphenyl)prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[2-(dimethylamino)phenyl]prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[2-(piperidin-1-yl)phenyl]prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[2-[di(prop-2-en-1-yl)amino]phenyl]prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[3-(3-methylbut-3-en-2-yl)-4-[(3-methylbut-2-en-1-yl)oxy]phenyl]prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[3-(dimethylamino)phenyl]prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[3-(piperidin-1-yl)phenyl]prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[3-[di(prop-2-en-1-yl)amino]phenyl]prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-(1H-pyrazol-1-yl)phenyl]prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-(dimethylamino)phenyl]prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-(methylsulfonyl)phenyl]prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-(morpholin-4-yl)phenyl]prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-(piperidin-1-yl)phenyl]prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-hydroxy-3-(3-methylbut-2-en-1-yl)phenyl]prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-hydroxy-3-(3-methylbut-3-en-2-yl)phenyl]prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-hydroxy-3-(prop-2-en-1-yl)phenyl]prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-methoxy-3-(3-methylbut-2-en-1-yl)phenyl]prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-methoxy-3-(3-methylbut-3-en-2-yl)phenyl]prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-methoxy-3-(prop-2-en-1-yl)phenyl]prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-[(3-methylbut-2-en-1-yl)oxy]phenyl]prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-[(4-methylphenyl)sulfonyl]phenyl]prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-[di(prop-2-en-1-yl)amino]phenyl]prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[6-(dimethylamino)-1,3-benzodioxol-5-yl]prop-2-en-1-one
-
-
(2E)-3-[2,4-dimethoxy-5-(2-methylbut-3-en-2-yl)phenyl]-1-(4-hydroxyphenyl)prop-2-en-1-one
-
a semisynthetic licochalcone A derivative
(2E)-3-[2,4-dimethoxy-5-(2-methylbut-3-en-2-yl)phenyl]-1-(4-methoxyphenyl)prop-2-en-1-one
-
a semisynthetic licochalcone A derivative
(2E)-3-[4-hydroxy-2-methoxy-3-(3-methylbut-2-en-1-yl)phenyl]-1-(4-hydroxyphenyl)prop-2-en-1-one
-
isolated from the CH2Cl2 extract of Glycyrrhiza inflata
(2E)-3-[4-hydroxy-2-methoxy-5-(2-methylbut-3-en-2-yl)phenyl]-1-(4-hydroxyphenyl)prop-2-en-1-one
-
isolated from the CH2Cl2 extract of Glycyrrhiza inflata
(2E)-3-[4-hydroxy-2-methoxy-5-(2-methylbut-3-en-2-yl)phenyl]-1-(4-methoxyphenyl)prop-2-en-1-one
-
a semisynthetic licochalcone A derivative
(2E)-3-[4-hydroxy-2-methoxy-5-(3-methylbut-3-en-2-yl)phenyl]-1-(4-hydroxyphenyl)prop-2-en-1-one
-
isolated from the CH2Cl2 extract of Glycyrrhiza inflata
(2E)-3-[5-bromo-2-hydroxy-4-(tetrahydro-2H-pyran-2-yloxy)phenyl]-1-[4-methoxy-3-(3-methylbut-3-en-2-yl)phenyl]prop-2-en-1-one
-
-
(2E)-3-[5-bromo-2-methoxy-4-(tetrahydro-2H-pyran-2-yloxy)phenyl]-1-[4-hydroxy-3-(3-methylbut-3-en-2-yl)phenyl]prop-2-en-1-one
-
-
(2R)-2-benzyl-3-[2,6-dibromo-4-(6-bromo-5a,11a-dihydrobenzo[b]naphtho[2,3-d]furan-11-yl)phenyl]propanoic acid
-
(2Z)-2-([5-[4-(1H-tetrazol-1-yl)phenyl]furan-2-yl]methylidene)[1,3]thiazolo[3,2-a]benzimidazol-3(2H)-one
-
(2Z)-2-[[5-(2-methyl-5-nitrophenyl)furan-2-yl]methylidene][1,3]thiazolo[3,2-a]benzimidazol-3(2H)-one
-
(3alpha,5beta,8alpha,9beta,10alpha,13alpha)-3-[[(2E)-4-phenylbut-2-enoyl]oxy]kaur-16-en-18-oic acid
-
(3aR,4R,4aR,5R,8R,8aR,9S,9aR)-8-(acetyloxy)-5-hydroxy-5,8a-dimethyl-3-methylidene-4-[(2-methylpropanoyl)oxy]-2-oxododecahydronaphtho[2,3-b]furan-9-yl 3-methylbutanoate
no inhibition at 0.020 mM
(3aR,4R,4aR,5R,8R,8aS,9S,9aR)-8-(acetyloxy)-5,9-dihydroxy-5,8a-dimethyl-3-methylidene-2-oxododecahydronaphtho[2,3-b]furan-4-yl 2-methylprop-2-enoate
no inhibition at 0.025 mM
(3aR,4R,4aR,5R,8R,8aS,9S,9aR)-8-(acetyloxy)-5,9-dihydroxy-5,8a-dimethyl-3-methylidene-2-oxododecahydronaphtho[2,3-b]furan-4-yl 2-methylpropanoate
no inhibition at 0.024 mM
(3beta)-3-(acetyloxy)olean-12-en-28-oic acid
-
-
(3beta)-3-hydroxyolean-12-en-28-oic acid
-
-
(3beta)-3-hydroxyoleana-11,13(18)-dien-28-oic acid
-
-
(3S,3aR,4S,5R,7aR)-4-acetyl-7-henicosyl-3-methyl-1-oxo-7a-[(1E)-tricos-1-en-1-yl]-1,3,3a,4,5,7a-hexahydro-2-benzofuran-5-carboxylic acid
-
-
(3S,3aR,4S,7R,7aS)-4-acetyl-7-icosyl-3-methyl-1-oxo-7a-[(1E)-tricos-1-en-1-yl]-1,3,3a,4,7,7a-hexahydro-2-benzofuran-5-carboxylic acid
-
-
(4-((4E)-2-(1,3-benzothiazol-2-yl)-2-(1H-benzotriazol-1-yl)-5-phenylpent-4-en-1-yl)benzyl)phosphonate
50% inhibition at 3260 nM for wild-type, at 5030 nM for mutant S295F
(4aR,6aR,6bS,8aR,12aS,14aR,14bR)-8a-hydroxy-4,4,6a,6b,11,11,14b-heptamethyl-1,4a,5,6,6a,6b,7,8a,9,10,11,12,12a,14,14a,14b-hexadecahydropicene-3,8(2H,4H)-dione
-
-
(4aR,6aS,6bR,8aR,10S,12aR,12bR,14bS)-4a,10-dihydroxy-2,2,6a,6b,9,9,12a-heptamethyl-2,3,4,4a,6,6a,6b,7,8,8a,9,10,11,12,12a,12b,13,14b-octadecahydropicen-5(1H)-one
-
-
(4aS,6aS,6bR,13aR)-10-acetyl-2,2,6a,6b,9,9,13a-heptamethyl-1,2,3,4,5,6,6a,6b,7,8,8a,9,10,13,13a,13b,14,15b-octadecahydro-4aH-chryseno[1,2-f]indazole-4a-carboxylic acid
-
-
(4aS,6aS,6bR,13aR)-10-hexanoyl-2,2,6a,6b,9,9,13a-heptamethyl-1,2,3,4,5,6,6a,6b,7,8,8a,9,10,13,13a,13b,14,15b-octadecahydro-4aH-chryseno[1,2-f]indazole-4a-carboxylic acid
-
-
(4aS,6aS,6bR,13aR)-11-amino-2,2,6a,6b,9,9,13a-heptamethyl-1,3,4,5,6,6a,6b,7,8,8a,9,13,13a,13b,14,15b-hexadecahydropiceno[3,2-d][1,3]thiazole-4a(2H)-carboxylic acid
-
-
(4aS,6aS,6bR,13aR)-2,2,6a,6b,9,9,13a-heptamethyl-1,2,3,4,5,6,6a,6b,7,8,8a,9,10,13,13a,13b,14,15b-octadecahydro-4aH-chryseno[1,2-f]indazole-4a-carboxylic acid
-
-
(4aS,6aS,6bR,13aR)-2,2,6a,6b,9,9,13a-heptamethyl-1,3,4,5,6,6a,6b,7,8,8a,9,13,13a,13b,14,15b-hexadecahydropiceno[2,3-d][1,2]oxazole-4a(2H)-carboxylic acid
-
-
(4aS,6aS,6bR,13aR)-2,2,6a,6b,9,9,13a-heptamethyl-10-(pyridin-3-ylcarbonyl)-1,2,3,4,5,6,6a,6b,7,8,8a,9,10,13,13a,13b,14,15b-octadecahydro-4aH-chryseno[1,2-f]indazole-4a-carboxylic acid
-
-
(4aS,6aS,6bR,13aR)-2,2,6a,6b,9,9,13a-heptamethyl-10-(pyridin-4-ylcarbonyl)-1,2,3,4,5,6,6a,6b,7,8,8a,9,10,13,13a,13b,14,15b-octadecahydro-4aH-chryseno[1,2-f]indazole-4a-carboxylic acid
-
-
(4aS,6aS,6bR,13aR)-2,2,6a,6b,9,9,13a-heptamethyl-10-phenyl-1,2,3,4,5,6,6a,6b,7,8,8a,9,10,13,13a,13b,14,15b-octadecahydro-4aH-chryseno[1,2-f]indazole-4a-carboxylic acid
-
-
(4aS,6aS,6bR,14aR)-11-amino-2,2,6a,6b,9,9,14a-heptamethyl-1,3,4,5,6,6a,6b,7,8,8a,9,14,14a,14b,15,16b-hexadecahydrochryseno[1,2-g]quinazoline-4a(2H)-carboxylic acid
-
-
(4aS,6aS,6bR,14aR)-2,2,6a,6b,9,9,11,14a-octamethyl-1,3,4,5,6,6a,6b,7,8,8a,9,14,14a,14b,15,16b-hexadecahydrochryseno[1,2-g]quinazoline-4a(2H)-carboxylic acid
-
-
(4aS,6aS,6bR,14aR)-2,2,6a,6b,9,9,14a-heptamethyl-1,3,4,5,6,6a,6b,7,8,8a,9,14,14a,14b,15,16b-hexadecahydrochryseno[1,2-g]quinazoline-4a(2H)-carboxylic acid
(4aS,6aS,6bR,14aR)-2,2,6a,6b,9,9,14a-heptamethyl-1,3,4,5,6,6a,6b,7,8,8a,9,14,14a,14b,15,16b-hexadecahydrochryseno[1,2-g]quinoxaline-4a(2H)-carboxylic acid
-
-
(4aS,6aS,6bR,14aR)-2,2,6a,6b,9,9,14a-heptamethyl-11-(methylamino)-1,3,4,5,6,6a,6b,7,8,8a,9,14,14a,14b,15,16b-hexadecahydrochryseno[1,2-g]quinazoline-4a(2H)-carboxylic acid
-
-
(4aS,6aS,6bR,15aR)-2,2,6a,6b,9,9,15a-heptamethyl-1,2,3,4,5,6,6a,6b,7,8,8a,9,10,15,15a,15b,16,17b-octadecahydro-4aH-chryseno[2,1-b]carbazole-4a-carboxylic acid
-
-
(4aS,6aS,6bR,16aR)-2,2,6a,6b,9,9,16a-heptamethyl-1,3,4,5,6,6a,6b,7,8,8a,9,16,16a,16b,17,18b-hexadecahydrochryseno[1,2-b]phenazine-4a(2H)-carboxylic acid
-
-
(4R)-4-[(1R,3aS,3bS,10aR,10bS,12aR)-6,6,10a,12a-tetramethyl-1,2,3,3a,3b,4,6,6a,7,9a,10,10a,10b,11,12,12a-hexadecahydrocyclopenta[5,6]naphtho[1,2-f]indazol-1-yl]pentanoic acid
-
-
(4R)-4-[(1R,3aS,3bS,10aR,10bS,12aR)-6,6,10a,12a-tetramethyl-2,3,3a,3b,4,6,10,10a,10b,11,12,12a-dodecahydro-1H-cyclopenta[7,8]phenanthro[2,3-d][1,2,3]thiadiazol-1-yl]pentanoic acid
-
-
(4R)-4-[(1R,3aS,3bS,10aR,10bS,12aR)-6,6,10a,12a-tetramethyl-2,3,3a,3b,4,6,6a,9a,10,10a,10b,11,12,12a-tetradecahydro-1H-cyclopenta[7,8]phenanthro[3,2-d][1,2]oxazol-1-yl]pentanoic acid
-
-
(4R)-4-[(1R,3aS,3bS,10aR,10bS,12aR)-6,6,10a,12a-tetramethyl-7-phenyl-1,2,3,3a,3b,4,6,6a,7,9a,10,10a,10b,11,12,12a-hexadecahydrocyclopenta[5,6]naphtho[1,2-f]indazol-1-yl]pentanoic acid
-
competitive PTP1B inhibitor
(4R)-4-[(1R,3aS,3bS,10aR,10bS,12aR)-8-amino-6,6,10a,12a-tetramethyl-2,3,3a,3b,4,6,10,10a,10b,11,12,12a-dodecahydro-1H-cyclopenta[7,8]phenanthro[2,3-d][1,3]thiazol-1-yl]pentanoic acid
-
-
(4R)-4-[(1R,3aS,3bS,11aR,11bS,13aR)-6,6,11a,13a-tetramethyl-2,3,3a,3b,4,6,11,11a,11b,12,13,13a-dodecahydro-1H-cyclopenta[5,6]naphtho[1,2-g]quinazolin-1-yl]pentanoic acid
-
-
(4R)-4-[(1R,3aS,3bS,11aR,11bS,13aR)-6,6,11a,13a-tetramethyl-2,3,3a,3b,4,6,11,11a,11b,12,13,13a-dodecahydro-1H-cyclopenta[5,6]naphtho[1,2-g]quinoxalin-1-yl]pentanoic acid
-
-
(4R)-4-[(1R,3aS,3bS,11aR,11bS,13aR)-6,6,8,11a,13a-pentamethyl-2,3,3a,3b,4,6,11,11a,11b,12,13,13a-dodecahydro-1H-cyclopenta[5,6]naphtho[1,2-g]quinazolin-1-yl]pentanoic acid
-
-
(4R)-4-[(1R,3aS,3bS,11aR,11bS,13aR)-8-amino-6,6,11a,13a-tetramethyl-2,3,3a,3b,4,6,11,11a,11b,12,13,13a-dodecahydro-1H-cyclopenta[5,6]naphtho[1,2-g]quinazolin-1-yl]pentanoic acid
-
-
(5beta,8alpha,9beta,10alpha,13alpha)-kaur-16-en-18-oic acid
-
(5R)-2-((carboxycarbonyl)amino)-5-((1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl)-4,7-dihydro-5H-thieno(2,3-c)pyran-3-carboxylic acid
-
(5S)-2-((carboxycarbonyl)amino)-5-((1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl)-4,7-dihydro-5H-thieno(2,3-c)pyran-3-carboxylic acid
-
(5Z)-3-benzyl-5-(5-bromo-4-butoxy-2-methoxybenzylidene)-1,3-thiazolidine-2,4-dione
-
(5Z)-3-benzyl-5-[2-methoxy-5-(prop-2-en-1-yl)-4-(tetrahydro-2H-pyran-2-yloxy)benzylidene]-1,3-thiazolidine-2,4-dione
-
(5Z)-3-benzyl-5-[4-hydroxy-2-methoxy-5-(prop-2-en-1-yl)benzylidene]-1,3-thiazolidine-2,4-dione
-
(5Z)-3-butyl-5-[2-methoxy-5-(prop-2-en-1-yl)-4-(tetrahydro-2H-pyran-2-yloxy)benzylidene]-1,3-thiazolidine-2,4-dione
-
(5Z)-3-butyl-5-[4-hydroxy-2-methoxy-5-(prop-2-en-1-yl)benzylidene]-1,3-thiazolidine-2,4-dione
-
(5Z)-5-(4-hydroxy-2-methoxybenzylidene)-1,3-thiazolidine-2,4-dione
-
(5Z)-5-(5-bromo-2,4-dimethoxybenzylidene)-1,3-thiazolidine-2,4-dione
-
(5Z)-5-(5-bromo-2,4-dimethoxybenzylidene)-3-(4-methylpent-3-en-1-yl)-1,3-thiazolidine-2,4-dione
-
(5Z)-5-(5-bromo-2,4-dimethoxybenzylidene)-3-butyl-1,3-thiazolidine-2,4-dione
-
(5Z)-5-(5-bromo-2,4-dimethoxybenzylidene)-3-methyl-1,3-thiazolidine-2,4-dione
-
(5Z)-5-(5-bromo-4-butoxy-2-methoxybenzylidene)-1,3-thiazolidine-2,4-dione
-
(5Z)-5-(5-bromo-4-butoxy-2-methoxybenzylidene)-3-(4-methylpent-3-en-1-yl)-1,3-thiazolidine-2,4-dione
-
(5Z)-5-(5-bromo-4-butoxy-2-methoxybenzylidene)-3-butyl-1,3-thiazolidine-2,4-dione
-
(5Z)-5-(5-bromo-4-hydroxy-2-methoxybenzylidene)-1,3-thiazolidine-2,4-dione
-
(5Z)-5-[2-methoxy-5-(prop-2-en-1-yl)-4-(tetrahydro-2H-pyran-2-yloxy)benzylidene]-1,3-thiazolidine-2,4-dione
-
(5Z)-5-[2-methoxy-5-(prop-2-en-1-yl)-4-(tetrahydro-2H-pyran-2-yloxy)benzylidene]-3-(3-methylbut-2-en-1-yl)-1,3-thiazolidine-2,4-dione
-
(5Z)-5-[2-methoxy-5-(prop-2-en-1-yl)-4-(tetrahydro-2H-pyran-2-yloxy)benzylidene]-3-(prop-2-en-1-yl)-1,3-thiazolidine-2,4-dione
-
(5Z)-5-[2-methoxy-5-(prop-2-en-1-yl)-4-(tetrahydro-2H-pyran-2-yloxy)benzylidene]-3-(propan-2-yl)-1,3-thiazolidine-2,4-dione
-
(5Z)-5-[2-methoxy-5-(prop-2-en-1-yl)-4-(tetrahydro-2H-pyran-2-yloxy)benzylidene]-3-methyl-1,3-thiazolidine-2,4-dione
-
(5Z)-5-[4-(benzyloxy)-5-bromo-2-methoxybenzylidene]-1,3-thiazolidine-2,4-dione
-
(5Z)-5-[4-(benzyloxy)-5-bromo-2-methoxybenzylidene]-3-(4-methylpent-3-en-1-yl)-1,3-thiazolidine-2,4-dione
-
(5Z)-5-[4-(benzyloxy)-5-bromo-2-methoxybenzylidene]-3-methyl-1,3-thiazolidine-2,4-dione
-
(5Z)-5-[4-hydroxy-2-methoxy-5-(prop-2-en-1-yl)benzylidene]-1,3-thiazolidine-2,4-dione
-
(5Z)-5-[4-hydroxy-2-methoxy-5-(prop-2-en-1-yl)benzylidene]-3-(3-methylbut-2-en-1-yl)-1,3-thiazolidine-2,4-dione
-
(5Z)-5-[4-hydroxy-2-methoxy-5-(prop-2-en-1-yl)benzylidene]-3-(prop-2-en-1-yl)-1,3-thiazolidine-2,4-dione
-
(5Z)-5-[4-hydroxy-2-methoxy-5-(prop-2-en-1-yl)benzylidene]-3-(propan-2-yl)-1,3-thiazolidine-2,4-dione
-
(5Z)-5-[4-hydroxy-2-methoxy-5-(prop-2-en-1-yl)benzylidene]-3-methyl-1,3-thiazolidine-2,4-dione
-
(5Z)-5-[5-bromo-2-methoxy-4-(prop-2-en-1-yloxy)benzylidene]-1,3-thiazolidine-2,4-dione
-
(5Z)-5-[5-bromo-2-methoxy-4-(prop-2-en-1-yloxy)benzylidene]-3-(4-methylpent-3-en-1-yl)-1,3-thiazolidine-2,4-dione
-
(5Z)-5-[5-bromo-2-methoxy-4-(prop-2-en-1-yloxy)benzylidene]-3-butyl-1,3-thiazolidine-2,4-dione
-
(5Z)-5-[5-bromo-2-methoxy-4-(propan-2-yloxy)benzylidene]-3-(4-methylpent-3-en-1-yl)-1,3-thiazolidine-2,4-dione
-
(5Z)-5-[5-bromo-2-methoxy-4-(propan-2-yloxy)benzylidene]-3-butyl-1,3-thiazolidine-2,4-dione
-
(5Z)-5-[5-bromo-2-methoxy-4-[(3-methylbut-2-en-1-yl)oxy]benzylidene]-1,3-thiazolidine-2,4-dione
-
(5Z)-5-[5-bromo-2-methoxy-4-[(4-methylpent-3-en-1-yl)oxy]benzylidene]-3-(4-methylpent-3-en-1-yl)-1,3-thiazolidine-2,4-dione
-
(6aS,6bR,8aR,10S,12aS,12bR)-10-hydroxy-2,2,6a,6b,9,9,12a-heptamethyl-2,3,4,4a,6,6a,6b,7,8,8a,9,10,11,12,12a,12b-hexadecahydropicen-5(1H)-one
-
-
(7bS,9R,13bR,15R)-7-amino-9-(hydroxymethyl)-10,13-dioxo-2,3,3a,3b,4,5,6,7,7a,7b,9,10,13,13b-tetradecahydro-1H-6,8-methanobenzo[h]imidazo[1,2-a]pyrido[3,2-c][1,5]naphthyridine-15-carbonitrile
inhibits Cdc25B modestly
(7bS,9R,13bR,15S)-7-amino-15-hydroxy-9-(hydroxymethyl)-2,3,3a,3b,4,5,6,7,7a,7b,9,13b-dodecahydro-1H-6,8-methanobenzo[h]imidazo[1,2-a]pyrido[3,2-c][1,5]naphthyridine-10,13-dione
-
(difluoro(4-((4E)-2-((4-fluorophenyl)carbonyl)-2-(4-(3-methyl-1,2,4-oxadiazol-5-yl)phenyl)-5-phenylpent-4-en-1-yl)phenyl)methyl)phosphonic acid
-
50% inhibition at 163 nM for PTP-1B wild-type, at 1903 nM for PTP-1B mutant L119V, and at 1600 nM for isoform TCPTP wild-type and 138 nM for TCPTP mutant V121L
(E)-N-(4,5-diphenyl-1,3-thiazol-2-yl)-2-naphthalen-2-ylethenesulfonamide
-
(E)-N-[4-(4-chlorophenyl)-5-propyl-1,3-thiazol-2-yl]-2-(3,4-dichlorophenyl)ethenesulfonamide
-
(Z)-1-(3-(3-carboxy-3-hydroxyacryloyl)benzyl)-6-iodo-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
-
IC50 of 2.4 mg/ml
(Z)-1-(3-(4-ethoxy-3-hydroxy-4-oxobut-2-enoyl)benzyl)-6-iodo-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
-
IC50 of 3.1 mg/ml
(Z)-2-(2-(5-(N-(4-chloro-3-(trifluoromethyl)benzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
-
-
(Z)-3-(2-(2-carboxyphenyl)hydrazono)-2-oxoindoline-5-carboxylic acid
-
-
(Z)-3-(2-(2-nitrophenyl)hydrazono)-2-oxoindoline-5-sulfonic acid
-
NSC-117199
(Z)-3-(2-(3-carboxyphenyl)hydrazono)-2-oxoindoline-5-carboxylic acid
-
-
(Z)-3-(2-(5-(4-chlorobenzylcarbamoyl)-2-oxoindolin-3-ylidene)-hydrazinyl)benzoic acid
-
-
(Z)-3-(2-(5-(N-(2,4-dichlorophenethyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
-
-
(Z)-3-(2-(5-(N-(2-chlorobenzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
-
-
(Z)-3-(2-(5-(N-(3-chloro-4-fluorobenzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
-
-
(Z)-3-(2-(5-(N-(3-chlorobenzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
-
-
(Z)-3-(2-(5-(N-(4-chloro-3-(trifluoromethyl)benzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
-
-
(Z)-3-(2-(5-(N-(4-chlorobenzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
-
-
(Z)-3-(2-(5-(N-(4-fluorobenzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
-
-
(Z)-3-(2-(5-(N-(4-methylbenzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
-
-
(Z)-4-(2-(5-(N-(2-chlorobenzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
-
-
(Z)-4-(2-(5-(N-(4-chloro-3-(trifluoromethyl)benzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
-
-
(Z)-4-(2-(5-(N-(4-chlorobenzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
-
-
(Z)-4-(2-(5-(N-(4-fluorobenzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
-
-
(Z)-4-(2-(5-(N-benzylsulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl) benzoic acid
-
-
([2-bromo-4-(3-oxo-2,3-diphenylpropyl)phenyl](difluoro)methyl)phosphonic acid
-
1,1'-(piperazine-1,4-diyl)bis(4-(3-(dibenzylamino)phenyl)butane-1,2,4-trione)
-
-
1,3-difluoro-2-[(E)-2-nitroethenyl]benzene
-
50% inhibition at 0.0048 mM in absence of 2-mercaptoethanol, at 0.34 mM in presence of 1 mM 2-mercaptoethanol
1,6-dibenzyl-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
-
15.1% inhibition at 0.02 mg/ml
1-(1,3-benzodioxol-5-yl)-2-([1-(4-hydroxyphenyl)-1H-1,2,3,4-tetraazol-5-yl]sulfanyl)-1-ethanone
88% inhibition at 0.2 mM
1-(2,6-dihydroxy-4-methoxy-3-methylphenyl)ethanone
-
isolated from a methanol extract of the Antarctic lichen Stereocaulon alpinum
1-(4-fluorobenzyl)-6-nitro-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
-
36.2% inhibition at 0.02 mg/ml
1-(4-hydroxy-3-(methoxycarbonyl)benzyl)-6-iodo-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
-
IC50 of 8.1 mg/ml
1-benzyl-6-fluoro-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
-
15.1% inhibition at 0.02 mg/ml
1-benzyl-6-iodo-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
-
3.1% inhibition at 0.02 mg/ml
1-benzyl-7-fluoro-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
-
0.7% inhibition at 0.02 mg/ml
1-cyclopropyl-6-fluoro-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
-
0.8% inhibition at 0.02 mg/ml
1-cyclopropyl-6-iodo-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
-
3.5% inhibition at 0.02 mg/ml
1-cyclopropyl-N-(4-fluorobenzyl)-6-iodo-4-oxo-1,4-dihydroquinoline-3-carboxamide
-
3.3% inhibition at 0.02 mg/ml
1-ethyl-6-methyl-3-phenyl-1H-pyrimido(5,4-e)(1,2,4)triazine-5,7-dione
-
covalent mode of action
1-methoxy-4-((E)-2-nitrovinyl)benzene
-
50% inhibition at 0.0045 mM in absence of 2-mercaptoethanol, at 0.27 mM in presence of 1 mM 2-mercaptoethanol
1-methyl-4-((E)-2-nitrovinyl)benzene
-
50% inhibition at 0.003 mM in absence of 2-mercaptoethanol, at 0.225 mM in presence of 1 mM 2-mercaptoethanol
15-hydroxykaur-9(11),16-dien-19-oic acid
-
16alphaH,17-isovaleryloxy-ent-kauran-19-oic acid
-
diterpenoid isolated from Acanthopanax koreanum, 50% inhibition at 0.007 mM, noncompetitive
19alpha,24-dihydroxyurs-12-en-3-on-28-oic acid
-
-
2',4'-dihydroxy-1,1'-biphenyl
-
2,2'-[benzene-1,4-diylbis(methanediyloxybenzene-4,1-diyl)]bis(oxoacetic acid)
-
-
2,2-dioxo-2,3-dihydro-2-OMEGA-16-benzo (1,2,3)oxathiazole-6-carboxylic acid (5-phenylsulfanyl-1H-benzoimidazol-2-ylmethyl)-amide
-
competitive, noncovalent mode of action
2,4-dihydroxy-6-methylbenzoic acid
-
45% inhibition of PTPB1 at 0.178 mM
2,4-dimethoxy-1-((E)-2-nitrovinyl)benzene
-
50% inhibition at 0.028 mM in absence of 2-mercaptoethanol, at 0.390 mM in presence of 1 mM 2-mercaptoethanol
2,5-dihydroxy-3-[7-(2-methylbenzyl)-1H-indol-3-yl]cyclohexa-2,5-diene-1,4-dione
-
2,5-dihydroxy-3-[7-(3-methylbut-2-en-1-yl)-1H-indol-3-yl]cyclohexa-2,5-diene-1,4-dione
-
2-((carboxycarbonyl)amino)-4,7-dihydro-5H-thieno(2,3-c)pyran-3-carboxylic acid
i.e. OATP
2-((carboxycarbonyl)amino)-5-((1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl)-4,7-dihydro-5H-thieno(2,3-c)pyran-3-carboxylic acid
-
2-((carboxycarbonyl)amino)-5-((4-fluoro-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl)-4,7-dihydro-5H-thieno(2,3-c)pyran-3-carboxylic acid
-
2-((carboxycarbonyl)amino)-5-((4-hydroxy-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl)-4,7-dihydro-5H-thieno(2,3-c)pyran-3-carboxylic acid
-
2-((carboxycarbonyl)amino)-5-((5-hydroxy-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl)-4,7-dihydro-5H-thieno(2,3-c)pyran-3-carboxylic acid
-
2-(2,5-dimethyl-1H-pyrrol-1-yl)-5-hydroxybenzoic acid
2-(4-hydroxyphenyl)-3-[(3,4-dihydroxy-1,1'-biphenyl-4-yl)methyl]-4H-1-benzopyran-4-one
-
2-(4-hydroxyphenyl)-3-[(4-carboxy-3-hydroxy-1,1'-biphenyl-4-yl)methyl]-4H-1-benzopyran-4-one
-
2-(oxalyl-amino)-4,5,6,7-tetrahydro-thieno[2,3-c]pyridine-3-carboxylic acid
-
2-(oxalyl-amino)-4,5,6,7-tetrahydrobenzo[b]thiophene-3-carboxylic acid
-
2-(oxalyl-amino)-4,7-dihydro-5H-thieno[2,3-c]thiopyran-3-carboxylic acid
-
-
2-carboperoxybenzoate
-
complete inhibition at 150 mM
2-chloro-4-(2,5-dimethyl-1H-pyrrol-1-yl) benzoic acid
2-chloro-5-(2,5-dimethyl-1H-pyrrol-1-yl) benzoic acid
2-hydroperoxytetrahydrofuran
-
inactivation by 2-hydroperoxytetrahydrofuran (0.05 mM, 10 min) is reversed upon reaction of the enzyme with dithiothreitol (54% return of activity, following treatment with 100 mM dthiothreitol for 1 h)
2-[(carboxycarbonyl)amino]-4,5,6,7-tetrahydro-thieno[2,3-c]-pyridine-3-carboxylic acid
i.e. TCS401, binds to the active site
2-[4,5-bis(1,3,2-dithiarsolan-2-yl)-6-hydroxy-3-oxo-3H-xanthen-9-yl]benzoic acid
i.e. FlAsH
2-[6-chloro-5-(1-naphthalyloxy)-1H-benzimidazol-2-yl]thio-N-(thiazol-2-yl)acetamide
mixed-type inhibition, 99% inhibition at 0.2 mM
24-hydroxyursolic acid
-
-
28-(10-decanoic)-oleanolic acid
-
28-(12-dodecanoic)-oleanolic acid
-
28-(2-acetic)-oleanolic acid
-
28-(4-butyric)-oleanolic acid
-
28-(6-hexanoic)-oleanolic acid
-
28-(8-octanoic)-oleanolic acid
-
28-(glycine)-oleanolic acid amide
-
28-(L-glutamic acid)-oleanolic acid amide
-
28-(L-phenylalanine)-oleanolic acid amide
-
28-(p-carboxyphenyl)-oleanolic acid amide
-
28-[4-butyric((R)-1-carboxy-phenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric((S)-1-carboxy-3-indole-ethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric((S)-1-carboxy-5-imidazole-ethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric((S)-1-carboxy-methylthioethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric((S)-1-carboxy-phenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-2,3-dimethoxyphenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-3,4-dimethoxyphenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-3,4-oxymethyleneoxyphenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-3,5-dimethoxyphenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-m-chlorophenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-m-methoxyphenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-o-chlorophenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-o-methoxyphenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-o-methylphenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-p-chlorophenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-p-fluorophenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-p-methoxyphenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-p-methylphenylethyl)-amide]-DELTA12-oleanene
-
28-[4-butyric(1-carboxy-p-nitrophenylethyl)-amide]-DELTA12-oleanene
-
2alpha,3alpha,19alpha,23-tetrahydroxyurs-12-en-28-oic acid
-
50% inhibition at 0.0421 mM
2beta,3beta-2,3-dihydroxyolean-12-en-28-oic acid
-
-
3',4'-dihydroxy-1,1'-biphenyl
no inhibition of LMW-PTP isozymes, but 5% inhibition of PTP-B1 at 0.02 mM
3,16-dioxo-olean-12(13),17(18)-diene
-
-
3-((3,5-dibromo-4-hydroxyphenyl)carbonyl)-2-ethyl-N-(4-(1,3-thiazol-2-ylsulfamoyl)phenyl)-1-benzofuran-6-sulfonamide
50% inhibition of PTP1B at 0.008 mM, noncompetitive noncompetitive allosteric inhibitor, prevents formation of the active form of the enzyme by blocking the mobility of the catalytic loop
3-((3,5-dibromo-4-hydroxyphenyl)carbonyl)-2-ethyl-N-(4-sulfamoylphenyl)-1-benzofuran-6-sulfonamide
50% inhibition of PTP1B at 0.022 mM, noncompetitive allosteric inhibitor, prevents formation of the active form of the enzyme by blocking the mobility of the catalytic loop
3-(1-carboxy-ethoxy)-6-chloro-benzo(b)-thiophene-2-carboxylic acid
-
-
3-(2,2'-dimethyl-carboxypropanoyloxy)-oleanolic acid
-
3-(2,5-dimethyl-1H-pyrrol-1-yl)-4-hydroxybenzoic acid
3-(2-carboxy-benzyloxy)-oleanolic acid
-
3-(2-carboxybenzoyloxy)-oleanolic acid
-
3-(3,5-dibromo-4-hydroxybenzoyl)-2-ethyl-N,N-dimethyl-1-benzofuran-6-sulfonamide
50% inhibition of PTP1B at 0.35 mM
3-(3,5-dibromo-4-hydroxybenzoyl)-2-ethyl-N-[4-(1,3-thiazol-2-ylsulfamoyl)phenyl]-1-benzofuran-6-sulfonamide
-
3-(3,5-dibromo-4-hydroxybenzoyl)-2-ethylbenzofuran-6-sulfonic acid-[4-(thiazol-2-ylsulfamyl)phenyl]-amide
i.e. BBR
3-(3-carboxy-benzyloxy)-oleanolic acid
-
3-(4-carboxy-benzyloxy)-28-[4-butyric((s)-1-carboxyphenylethyl)-amide]-DELTA12-oleanene
-
3-(4-carboxy-benzyloxy)-oleanolic acid
-
3-(biphenyl-4-ylmethyl)-6-hydroxy-2-(4-hydroxybenzyl)-4H-chromen-4-one
-
3-(carboxy-fluoro-methoxy)-6-chloro-benzo(b)thiophene-2-carboxylic acid
-
-
3-(carboxymethoxy)-2-naphthoic acid
-
-
3-(carboxymethoxy)-5-((cyclohexylmethyl)-amino)thieno(3,2-b)(1)benzothiophene-2-carboxylic acid
-
-
3-(carboxymethoxy)-5-(cyclohexylamino)-thieno(3,2-b)(1)benzothiophene-2-carboxylic acid
-
-
3-(carboxymethoxy)-5-chlorothieno(3,2-b)(1)benzothiophene-2-carboxylic acid
-
-
3-(carboxymethoxy)-6-((1-(ethylsulfonyl)-piperidin-4-yl)amino)thieno(3,2-b)(1)benzothiophene-2-carboxylic acid
-
-
3-(carboxymethoxy)-6-((cyclohexylmethyl)-amino)thieno(3,2-b)(1)benzothiophene-2-carboxylic acid
-
-
3-(carboxymethoxy)-6-(cyclohexylamino)-thieno(3,2-b)(1)benzothiophene-2-carboxylic acid
-
-
3-(carboxymethoxy)-6-(tetrahydro-2H-pyran-4-ylamino)thieno(3,2-b)(1)benzothiophene-2-carboxylic acid
-
-
3-(carboxymethoxy)-6-chlorothieno(3,2-b)(1)benzothiophene-2-carboxylic acid
-
-
3-(carboxymethoxy)-6-methylthieno(3,2-c)pyridine-2-carboxylic acid
-
-
3-(carboxymethoxy)benzo(b)thiophene-2-carboxylic acid
-
-
3-(carboxymethoxy)furo(2,3-b)pyridine-2-carboxylic acid
-
-
3-(carboxymethoxy)thieno(2,3-b)pyridine-2-carboxylic acid
-
reversible, competitive
3-(carboxymethoxy)thieno(3,2-b)(1)benzo-thiophene-2-carboxylic acid
-
-
3-(carboxymethoxy)thieno(3,2-b)pyridine-2-carboxylic acid
-
-
3-(carboxymethoxy)thieno(3,2-b)thiophene-2-carboxylic acid
-
-
3-([2-chloro-6-methoxy-4-[(E)-(3-oxo[1,3]thiazolo[3,2-a]benzimidazol-2(3H)-ylidene)methyl]phenoxy]methyl)benzoic acid
-
3-benzyl-7-hydroxy-2-(4-hydroxybenzyl)-4H-chromen-4-one
10% inhibition of LMW-PTP isozymes 1 and 2,no inhibition of PTP-B1, at 0.015 mM
3-benzyloxy-oleanolic acid
-
3-butyl-7-(2,4-dihydroxy-6-pentylphenoxy)-3,5-dimethoxy-2-benzofuran-1(3H)-one
-
a pseudodepsidone-type compound, isolated from a methanol extract of the Antarctic lichen Stereocaulon alpinum
3-carboxymethoxy-6-(4-hydroxyphenyl)-benzo(b)-thiophene-2-carboxylic acid
-
-
3-carboxymethoxy-6-(5-methyl-1-phenyl-1H-pyrazol-3-ylcarbamoyl)-benzo(b)thiophene-2-carboxylic acid
-
-
3-carboxymethoxy-6-chloro-benzo(b)-thiophene-2-carboxylic acid
-
-
3-carboxymethoxy-6-phenylbenzo(b)-thiophene-2-carboxylic acid
-
-
3-carboxymethoxy-6-thiophen-2-yl-benzo(b)-thiophene-2-carboxylic acid
-
-
3-carboxymethoxy-7-chloro-benzo(b)-thiophene-2-carboxylic acid
-
-
3-carboxymethoxy-7-methyl-benzo(b)-thiophene-2-carboxylic acid
-
-
3-carboxymethoxy-naphtho(1,2-b)thiophene-2-carboxylic acid
-
-
3-carboxymethoxy-thieno(3,2-c)quinoline-2-carboxylic acid
-
-
3-carboxypropanoyloxy-oleanolic acid
-
3-chlorobenzenecarboperoxoic acid
-
complete inhibition at 150 mM
3-dehydroxy-oleanolic acid
-
3-ethyl oxalyl-oleanolic acid
-
3-hydroxy-4-(methoxycarbonyl)-2,5-dimethylphenyl 3-acetyl-2,4-dihydroxy-6-methylbenzoate
-
isolated from a methanol extract of the Antarctic lichen Stereocaulon alpinum
3-hydroxy-4-(methoxycarbonyl)-5-methylphenyl 4-(beta-D-galactopyranosyloxy)-2-hydroxy-6-pentadecylbenzoate
-
-
3-methyl-2-butenal
-
95% remaining activity at 0.5 mM
3-methylene-oleanolic acid
-
3-oxalyl-oleanolic acid
-
3-oxo-oleanolic acid
-
3-[(1-butyl-1,6-dimethoxy-3-oxo-1,3-dihydro-2-benzofuran-4-yl)oxy]-4,6-dihydroxy-2-pentylbenzoic acid
-
a pseudodepsidone-type compound, isolated from a methanol extract of the Antarctic lichen Stereocaulon alpinum
3-[(2-nitrophenyl)hydrazono]-2-oxo-2,3-dihydro-1H-indole-5-sulfonamide
-
-
3-[(2-nitrophenyl)hydrazono]-2-oxo-2,3-dihydro-1H-indole-5-sulfonic acid 4-chlorobenzylamide
-
-
3-[(3-[(E)-[3-(4-carboxybenzyl)-2,4-dioxo-1,3-thiazolidin-5-ylidene]methyl]phenoxy)methyl]benzoic acid
-
3-[(4-[(Z)-[3-(4-carboxybenzyl)-2,4-dioxo-1,3-thiazolidin-5-ylidene]methyl]phenoxy)methyl]benzoic acid
-
3-[(E)-(3-oxo[1,3]thiazolo[3,2-a]benzimidazol-2(3H)-ylidene)methyl]benzoic acid
-
3-[2,5-dimethyl-3-[(3-oxo-2,3-dihydro[1,3]thiazolo[3,2-a]benzimidazol-2-yl)methyl]-1H-pyrrol-1-yl]benzoic acid
irreversible inhibition, detailed kinetic analysis of the interaction between E4 and the catalytic domain of enzyme STEP, overview. kinact is 0.068/s
3-[3-(2,4-dichlorophenyl)propanoyl]-2-hydroxycyclohepta-2,4,6-trien-1-one
-
3-[N'-(5-isopropylsulfamoyl-2-oxo-1,2-dihydroindol-3-ylidene)-hydrazino]benzoic acid
-
-
3-[oxalyl-amino]naphthalene-2-carboxylic acid
-
3a,4,5,9b-tetrahydro-3H-cyclopenta[c]quinoline-4,6-dicarboxylic acid
3a,4,5,9b-tetrahydro-3H-cyclopenta[c]quinoline-4,8-dicarboxylic acid
3a,4,5,9b-tetrahydro-3H-cyclopenta[c]quinoline-4-carboxylic acid
3alpha-angeloyloxypterokaurene L3
18% inhibition at 0.024 mM
3alpha-cinnamoyloxypterokaurene L3
-
3alpha-oleanolic acid
-
3alpha-tigloyloxypterokaurene L3
no inhibition at 0.024 mM
3beta,16a,17-trihydroxy-olean-12-ene
-
-
3beta-acetoxy-17beta-hydroxy-28-norolean-12-ene
-
-
3beta-acetoxy-28-hydroxyolean-12-ene
-
-
3beta-acetoxyolean-12-en-28-acid
-
-
3beta-acetoxyolean-12-en-28-aldehyde
-
-
3beta-hydroxyolean-12-en-28-oic acid
-
-
4'-carboxy-3'-hydroxy-1,1'-biphenyl
no inhibition of LMW-PTP isozymes, but 10% inhibition of PTP-B1 at 0.02 mM
4'-[(2-butyl-1-benzofuran-3-yl)methyl]biphenyl-4-ol
-
4'-[2-(4-hydroxybutyl)-1-benzofuran-3-yl]biphenyl-4-ol
-
4,4'-[benzene-1,4-diylbis(methanediyloxy)]dibenzoic acid
-
4,6-bis(1,3,2-dithiarsolan-2-yl)-7-hydroxy-3H-phenoxazin-3-one
i.e. ReAsH
4-(((5Z)-2-(4-fluorophenylimino)-4-oxo-5-[(3-phenoxyphenyl)methylidene]thiazolidin-3-yl)methyl)benzoic acid
-
4-(((5Z)-2-(4-fluorophenylimino)-4-oxo-5-[(3-phenylmethoxyphenyl)methylidene]thiazolidin-3-yl)methyl)benzoic acid
-
4-(((5Z)-2-(4-fluorophenylimino)-4-oxo-5-[(4-phenoxyphenyl)methylidene]thiazolidin-3-yl) methyl)benzoic acid
-
4-(((5Z)-2-(4-fluorophenylimino)-4-oxo-5-[(4-phenylmethoxyphenyl)methylidene]thiazolidin-3-yl)methyl)benzoic acid
-
4-(((5Z)-4-oxo-5-[(3-phenoxyphenyl)methylidene]-2-thioxothiazolidin-3-yl)methyl)benzoic acid
-
4-(((5Z)-4-oxo-5-[(3-phenylmethoxyphenyl)methylidene]-2-thioxothiazolidin-3-yl)methyl)benzoic acid
-
4-(((5Z)-4-oxo-5-[(4-phenoxyphenyl)methylidene]-2-thioxothiazolidin-3-yl)methyl)benzoic acid
-
4-(((5Z)-4-oxo-5-[(4-phenylmethoxyphenyl)methylidene]-2-thioxothiazolidin-3-yl)methyl)benzoic acid
-
4-((3E)-1-(1H-benzotriazol-1-yl)-1-(4-(difluoro(phosphono)methyl)benzyl)-4-phenylbut-3-en-1-yl)benzoic acid
-
50% inhibition at 39 nM for wild-type PTP-1B, at 39 nM for mutant V113I, at 45 nM for mutant M114V, at 29 nM for mutant V113I/M114V, at 32 nM for mutant G117E, at 142 nM for mutant L119V, and at 87 nM for isoform TCPTP wild-type and 24 nM for isoform TCPTP mutant V121L
4-((E)-2-nitrovinyl)benzoic acid
-
50% inhibition at 0.0027 mM in absence of 2-mercaptoethanol, at 0.425 mM in presence of 1 mM 2-mercaptoethanol
4-(2,5-dimethyl-1H-pyrrol-1-yl) benzoic acid
4-(2,5-dimethyl-1H-pyrrol-1-yl)-3-hydroxybenzoic acid
4-(2,5-dimethyl-1H-pyrrol-1-yl)phthalic acid
4-(3-(dibenzylamino)phenyl)-2,4-dioxobutanoic acid
-
-
4-(5-bromo-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-2-hydroxybenzoic acid
-
4-(5-[5-(3,5-dichlorophenoxy)-2-furyl]-1,2,4-oxadiazol-3-yl)phenyl-N,N-dimethylsulfamate
85% inhibition at 0.2 mM
4-(beta-D-galactopyranosyloxy)-2-hydroxy-6-pentadecylbenzoic acid
-
-
4-(difluoro(phosphono)methyl)-N-pentadecanoyl-L-phenylalanyl-L-a-aspartyl-4-(difluoro(phosphono)methyl)-L-phenylalaninamide
-
-
4-(difluoro(phosphono)methyl)-N-pentadecanoyl-L-phenylalanyl-L-alpha-aspartyl-4-(difluoro(phosphono)methyl)-L-phenylalaninamide
-
dose-dependent increase in Y527 phosphorylation of Src
4-([(2E,5Z)-2-[(4-methoxyphenyl)imino]-4-oxo-5-[(3-phenoxyphenyl)methylidene]-1,3-thiazolidin-3-yl]methyl)benzoic acid
-
4-([(2E,5Z)-2-[(4-methoxyphenyl)imino]-4-oxo-5-[(4-phenoxyphenyl)methylidene]-1,3-thiazolidin-3-yl]methyl)benzoic acid
-
4-([(2E,5Z)-2-[(4-tert-butylphenyl)imino]-4-oxo-5-[(3-phenoxyphenyl)methylidene]-1,3-thiazolidin-3-yl]methyl)benzoic acid
-
4-([(2E,5Z)-2-[(4-tert-butylphenyl)imino]-4-oxo-5-[(4-phenoxyphenyl)methylidene]-1,3-thiazolidin-3-yl]methyl)benzoic acid
-
4-([(2E,5Z)-5-[[3-(benzyloxy)phenyl]methylidene]-2-[(4-methoxyphenyl)imino]-4-oxo-1,3-thiazolidin-3-yl]methyl)benzoic acid
-
4-([(2E,5Z)-5-[[3-(benzyloxy)phenyl]methylidene]-2-[(4-tert-butylphenyl)imino]-4-oxo-1,3-thiazolidin-3-yl]methyl)benzoic acid
-
4-([(2E,5Z)-5-[[4-(benzyloxy)phenyl]methylidene]-2-[(4-methoxyphenyl)imino]-4-oxo-1,3-thiazolidin-3-yl]methyl)benzoic acid
-
4-([(2E,5Z)-5-[[4-(benzyloxy)phenyl]methylidene]-2-[(4-tert-butylphenyl)imino]-4-oxo-1,3-thiazolidin-3-yl]methyl)benzoic acid
-
4-([(5E)-5-[3-(benzyloxy)benzylidene]-2,4-dioxo-1,3-thiazolidin-3-yl]methyl)benzoic acid
-
4-([(5Z)-2,4-dioxo-5-[(3-phenoxyphenyl)methylidene]-1,3-thiazolidin-3-yl]methyl)benzoic acid
-
4-([(5Z)-2,4-dioxo-5-[(4-phenoxyphenyl)methylidene]-1,3-thiazolidin-3-yl]methyl)benzoic acid
-
4-([(5Z)-2-(4-fluorophenylimino)-4-oxo-5-([3-(2-phenylethoxy)phenyl]methylidene)thiazolidin-3-yl]methyl)benzoic acid
-
4-([(5Z)-2-(4-fluorophenylimino)-4-oxo-5-([4-(2-phenylethoxy)phenyl]methylidene)thiazolidin-3-yl]methyl)benzoic acid
-
4-([(5Z)-4-oxo-5-[[3-(2-phenylethoxy)phenyl]methylidene)-2-thioxothiazolidin-3-yl]methyl]benzoic acid
-
4-([(5Z)-4-oxo-5-[[4-(2-phenylethoxy)phenyl]methylidene)-2-thioxothiazolidin-3-yl]methyl]benzoic acid
-
4-([(5Z)-5-[4-(benzyloxy)benzylidene]-2,4-dioxo-1,3-thiazolidin-3-yl]methyl)benzoic acid
-
4-fluorobenzyl-1-cyclopropyl-6-(4-fluorobenzyl)-4-oxo-1,4-dihydroquinoline-3-carboxylate
-
73% inhibition at 0.02 mg/ml
4-isoavenaciolide
potent irreversible inhibitor of VHR
4-methoxy-3-(5-methoxy-1-benzofuran-6-yl)-5-(4-methoxyphenyl)isoxazole
-
4-methoxy-3-(5-methoxy-1-benzofuran-6-yl)-5-phenylisoxazole
-
4-nitrophenyl phosphate
substrate inhibition at higher concentrations
4-oxo-4H-chromene-3-carbaldehyde
50% inhibition at 0.073 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases
4-oxo-6,8-diphenyl-4H-chromene-3-carbaldehyde
50% inhibition at 0.0033 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases, 50% inhibition of isoform LAR above 1 mM
4-oxo-6-(2-phenyl-1-benzothien-3-yl)-4H-chromene-3-carbaldehyde
50% inhibition at 0.0062 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases
4-oxo-6-phenyl-4H-chromene-3-carbaldehyde
50% inhibition at 0.014 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases
4-oxo-8-(phenylsulfanyl)-1,4-dihydro-1,7-naphthyridine-3-carboxylic acid
-
4-oxo-8-phenyl-4H-chromene-3-carbaldehyde
50% inhibition at 0.016 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases
4-[(1E)-3-(4-hydroxyphenyl)-3-oxoprop-1-en-1-yl]-5-methoxy-2-(2-methylbut-3-en-2-yl)phenyl acetate
-
a semisynthetic licochalcone A derivative
4-[(2,4-dihydroxy-6-pentadecylbenzoyl)oxy]-2-hydroxy-6-methylbenzoic acid
-
-
4-[(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)prop-2-enoyl]phenyl 4-bromobenzoate
-
-
4-[(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)prop-2-enoyl]phenyl 4-tert-butylbenzoate
-
-
4-[(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)prop-2-enoyl]phenyl benzoate
-
-
4-[(2E)-3-[2,4-dimethoxy-5-(2-methylbut-3-en-2-yl)phenyl]prop-2-enoyl]phenyl acetate
-
a semisynthetic licochalcone A derivative
4-[(2E)-3-[4-(acetyloxy)-2-methoxy-5-(2-methylbut-3-en-2-yl)phenyl]prop-2-enoyl]phenyl acetate
-
a semisynthetic licochalcone A derivative
4-[(2E)-3-[4-hydroxy-2-methoxy-5-(2-methylbut-3-en-2-yl)phenyl]prop-2-enoyl]phenyl acetate
-
a semisynthetic licochalcone A derivative
4-[(3-[(E)-[(2Z)-3-(4-carboxybenzyl)-4-oxo-2-(phenylimino)-1,3-thiazolidin-5-ylidene]methyl]phenoxy)methyl]benzoic acid
-
4-[(3-[(E)-[3-(4-carboxybenzyl)-2,4-dioxo-1,3-thiazolidin-5-ylidene]methyl]phenoxy)methyl]benzoic acid
-
4-[(4-[(Z)-[(2Z)-3-(4-carboxybenzyl)-4-oxo-2-(phenylimino)-1,3-thiazolidin-5-ylidene]methyl]phenoxy)methyl]benzoic acid
-
4-[(4-[(Z)-[3-(4-carboxybenzyl)-2,4-dioxo-1,3-thiazolidin-5-ylidene]methyl]phenoxy)methyl]benzoic acid
-
4-[2-[(5-chloro-1,3-benzoxazol-2-yl)sulfanyl]acetamido]benzoic acid
-
4-[4-[(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)prop-2-enoyl]phenoxy]butanoic acid
-
-
4-[N'-(5-isopropylsulfamoyl-2-oxo-1,2-dihydroindol-3-ylidene)-hydrazino]benzoic acid
-
-
4-[[(2E,5Z)-2-[(4-methoxyphenyl)imino]-4-oxo-5-[[3-(2-phenylethoxy)phenyl]methylidene]-1,3-thiazolidin-3-yl]methyl]benzoic acid
-
4-[[(2E,5Z)-2-[(4-methoxyphenyl)imino]-4-oxo-5-[[4-(2-phenylethoxy)phenyl]methylidene]-1,3-thiazolidin-3-yl]methyl]benzoic acid
-
4-[[(2E,5Z)-2-[(4-tert-butylphenyl)imino]-4-oxo-5-[[3-(2-phenylethoxy)phenyl]methylidene]-1,3-thiazolidin-3-yl]methyl]benzoic acid
-
4-[[(2E,5Z)-2-[(4-tert-butylphenyl)imino]-4-oxo-5-[[4-(2-phenylethoxy)phenyl]methylidene]-1,3-thiazolidin-3-yl]methyl]benzoic acid
-
4-[[(2E,5Z)-4-oxo-5-[(3-phenoxyphenyl)methylidene]-2-(phenylimino)-1,3-thiazolidin-3-yl]methyl]benzoic acid
-
4-[[(2E,5Z)-4-oxo-5-[(4-phenoxyphenyl)methylidene]-2-(phenylimino)-1,3-thiazolidin-3-yl]methyl]benzoic acid
-
4-[[(2E,5Z)-4-oxo-5-[[3-(2-phenylethoxy)phenyl]methylidene]-2-(phenylimino)-1,3-thiazolidin-3-yl]methyl]benzoic acid
-
4-[[(2E,5Z)-4-oxo-5-[[4-(2-phenylethoxy)phenyl]methylidene]-2-(phenylimino)-1,3-thiazolidin-3-yl]methyl]benzoic acid
-
4-[[(2E,5Z)-5-[[3-(benzyloxy)phenyl]methylidene]-4-oxo-2-(phenylimino)-1,3-thiazolidin-3-yl]methyl]benzoic acid
-
4-[[(2E,5Z)-5-[[4-(benzyloxy)phenyl]methylidene]-4-oxo-2-(phenylimino)-1,3-thiazolidin-3-yl]methyl]benzoic acid
-
4-[[(2Z,5E)-5-(3-[[4-(hydroxymethyl)benzyl]oxy]benzylidene)-4-oxo-2-(phenylimino)-1,3-thiazolidin-3-yl]methyl]benzoic acid
-
4-[[(2Z,5E)-5-[3-(benzyloxy)benzylidene]-4-oxo-2-(phenylimino)-1,3-thiazolidin-3-yl]methyl]benzoic acid
-
4-[[(2Z,5Z)-5-(4-[[4-(hydroxymethyl)benzyl]oxy]benzylidene)-4-oxo-2-(phenylimino)-1,3-thiazolidin-3-yl]methyl]benzoic acid
-
4-[[(2Z,5Z)-5-[4-(benzyloxy)benzylidene]-4-oxo-2-(phenylimino)-1,3-thiazolidin-3-yl]methyl]benzoic acid
-
4-[[(5E)-5-(3-[[4-(hydroxymethyl)benzyl]oxy]benzylidene)-2,4-dioxo-1,3-thiazolidin-3-yl]methyl]benzoic acid
-
4-[[(5Z)-2,4-dioxo-5-[[3-(2-phenylethoxy)phenyl]methylidene]-1,3-thiazolidin-3-yl]methyl]benzoic acid
-
4-[[(5Z)-2,4-dioxo-5-[[4-(2-phenylethoxy)phenyl]methylidene]-1,3-thiazolidin-3-yl]methyl]benzoic acid
-
4-[[(5Z)-5-(4-[[4-(hydroxymethyl)benzyl]oxy]benzylidene)-2,4-dioxo-1,3-thiazolidin-3-yl]methyl]benzoic acid
-
4-[[(5Z)-5-[[3-(benzyloxy)phenyl]methylidene]-2,4-dioxo-1,3-thiazolidin-3-yl]methyl]benzoic acid
-
4-[[(5Z)-5-[[4-(benzyloxy)phenyl]methylidene]-2,4-dioxo-1,3-thiazolidin-3-yl]methyl]benzoic acid
-
5-(1,3,2-dithiarsolan-2-yl)-2-[(1E,3E)-3-[5-(1,3,2-dithiarsolan-2-yl)-3,3-dimethyl-1-(4-sulfobutyl)-1,3-dihydro-2H-indol-2-ylidene]prop-1-en-1-yl]-3,3-dimethyl-1-(4-sulfobutyl)-3H-indol-1-ium
i.e. AsCy3, 70% inhibition at 250 nM AsCy3, AsCy3 is capable of specifically and potently inhibiting mutant enzyme asPTP1B in the presence of a complex proteome, while AsCy3 does not inhibit wild-type PTP1B activity in a cell lysate
5-(1,3,2-dithiarsolan-2-yl)-2-[(1E,3E,5E)-5-[5-(1,3,2-dithiarsolan-2-yl)-3,3-dimethyl-1-(4-sulfobutyl)-1,3-dihydro-2H-indol-2-ylidene]penta-1,3-dien-1-yl]-3,3-dimethyl-1-(4-sulfobutyl)-3H-indol-1-ium
i.e. AsCy5
5-(2-fluoro-5-((1E)-3-[3-hydroxy-2-(methoxycarbonyl)phenoxy]prop-1-en-1-yl)phenyl)isoxazole-3-carboxylic acid
-
5-acetylamino-2-(2,5-dimethyl-1H-pyrrol-1-yl) benzoic acid
5-chloro-2-[methyl(methylidene)-lambda4-sulfanyl]-6-[(naphthalen-2-yl)oxy]-1H-benzimidazole
65% inhibition at 0.2 mM
5-chloro-N-[6-chloro-5-(2,3-dichlorophenoxy)-1H-benzimidazol-2-yl]-1-methyl-2-(methylthio)-1H-benz-imidazole-6-carboxamide
mixed-type inhibition, complete inhibition at 0.2 mM
5-methoxy-4-[(1E)-3-(4-methoxyphenyl)-3-oxoprop-1-en-1-yl]-2-(2-methylbut-3-en-2-yl)phenyl acetate
-
a semisynthetic licochalcone A derivative
6,7-dihydroxy-2-(4-hydroxyphenyl)-3-[(1,1-biphenyl-4-yl)methyl]-4H-1-benzopyran-4-one
-
6,8-dibenzyl-4-oxo-4H-chromene-3-carbaldehyde
50% inhibition at 0.013 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases
6-((1-(benzylsulfonyl)piperidin-4-yl)amino)-3-(carboxymethoxy)thieno(3,2-b)(1)benzothiophene-2-carboxylic acid
-
-
6-((2-benzyl-1-benzothien-3-yl)methyl)-4-oxo-4H-chromene-3-carbaldehyde
50% inhibition at 0.0032 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases, 50% inhibition of isoform LAR above 1 mM
6-((E)-1,2-diphenylvinyl)-4-oxo-4H-chromene-3-carbaldehyde
50% inhibition at 0.0097 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases
6-(1-benzothien-2-ylmethyl)-4-oxo-4H-chromene-3-carbaldehyde
50% inhibition at 0.006 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases
6-(1-benzothien-3-yl)-4-oxo-4H-chromene-3-carbaldehyde
50% inhibition at 0.0077 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases
6-(1-benzothien-3-ylmethyl)-4-oxo-4H-chromene-3-carbaldehyde
50% inhibition at 0.06 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases
6-(10-bromo-9-anthryl)-4-oxo-4H-chromene-3-carbaldehyde
50% inhibition at 0.0025 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases, 50% inhibition of isoform LAR at 0.57 mM
6-(4-((2-benzyl-1-benzothiophen-3-yl)methyl)phenyl)-4-oxo-4H-chromene-3-carbaldehyde
50% inhibition at 0.0011 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases, 50% inhibition of isoform LAR above 1 mM
6-(4-((2-benzyl-1-benzothiophen-3-yl)methyl)phenyl)-4-oxo-8-phenyl-4H-chromene-3-carbaldehyde
50% inhibition at 0.001 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases, 50% inhibition of isoform LAR at 0.52 mM
6-(4-(3-(3-(benzyloxy)-2-(methoxycarbonyl)phenoxy)propyl)piperazin-1-yl)-1-cyclopropyl-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
-
IC50 of 45.2 mg/ml
6-(4-benzylpiperazin-1-yl)-1-cyclopropyl-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
-
62.3% inhibition at 0.02 mg/ml
6-(9-anthryl)-4-oxo-4H-chromene-3-carbaldehyde
50% inhibition at 0.0071 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases
6-amino-1-(4-fluorobenzyl)-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
-
12.4% inhibition at 0.02 mg/ml
6-benzyl-1-cyclopropyl-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
-
87.5% inhibition at 0.02 mg/ml
6-benzyl-4-oxo-4H-chromene-3-carbaldehyde
50% inhibition at 0.036 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases
6-biphenyl-4-yl-4-oxo-4H-chromene-3-carbaldehyde
50% inhibition at 0.0043 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases
6-biphenyl-4-yl-4-oxo-8-phenyl-4H-chromene-3-carbaldehyde
50% inhibition at 0.002 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases, 50% inhibition of isoform LAR above 1 mM
6-bromo-3-carboxymethoxy-benzo(b)-thiophene-2-carboxylic acid
-
-
6-bromo-4-oxo-4H-chromene-3-carbaldehyde
50% inhibition at 0.020 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases
6-chloro-7-(2,3-dihydro-1H-inden-1-ylamino)quinoline-5,8-dione
-
6-chloro-7-[(2-morpholin-4-ylethyl)amino]quinoline-5,8-dione
-
6-dibenzo(b,d)thien-1-yl-4-oxo-4H-chromene-3-carbaldehyde
50% inhibition at 0.0076 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases
6-dibenzo(b,d)thien-4-yl-4-oxo-4H-chromene-3-carbaldehyde
50% inhibition at 0.011 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases
6-fluoro-3a,4,5,9b-tetrahydro-3H-cyclopenta[c]quinoline-4-carboxylic acid
6-hydroxy-2-(4-hydroxybenzyl)-3-[(1,1-biphenyl-4-yl)methyl]-4H-1-benzopyran-4-one
6-hydroxy-3-[1-[4-(naphthalen-1-ylamino)-4-oxobutyl]-1H-1,2,3-triazol-4-yl]-2-phenyl-1-benzofuran-5-carboxylic acid
-
-
6-hydroxy-3a,4,5,9b-tetrahydro-3H-cyclopenta[c]quinoline-4-carboxylate
-
80% residual activity at 0.1 mM
6-hydroxy-3a,4,5,9b-tetrahydro-3H-cyclopenta[c]quinoline-4-carboxylic acid
6-iodo-1-(4-methoxy-3-(methoxycarbonyl)benzyl)-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
-
IC50 of more than 20 mg/ml
6-oxo-6H-cyclohepta[b]furan-5,7-dicarboxylic acid
-
7-(2-((1H-imidazol-2-yl)thio)ethoxy)-2-phenyl-4H-chromen-4-one
-
7-(2-(1H-1,2,4-triazol-1-yl)ethoxy)-2-phenyl-4H-chromen-4-one
the inhibitor is significantly selective for enzyme protein tyrosine phosphatase 1B (PTP1B) versus other phosphatases, i.e. T-cell protein tyrosine phosphatase (TCPTP), megakaryocyte protein tyrosine phosphatase (PTP-MEG2), and src homology phosphatase 2
7-(2-(2-methyl-5-nitro-1H-imidazol-1-yl)ethoxy)-2-phenyl-4H-chromen-4-one
-
7-(2-(4-nitro-1H-imidazol-1-yl)ethoxy)-2-phenyl-4H-chromen-4-one
-
7-(2-(5-methyl-1H-tetrazol-1-yl)ethoxy)-2-phenyl-4H-chromen-4-one
-
7-(2-bromoethoxy)-2-phenyl-4H-1-benzopyran-4-one
-
7-(3-(4-nitro-1H-imidazol-1-yl)propoxy)-2-phenyl-4H-chromen-4-one
-
7-(4-((1H-imidazol-2-yl)thio)butoxy)-2-phenyl-4H-chromen-4-one
-
7-(4-(1H-1,2,4-triazol-1-yl)butoxy)-2-phenyl-4H-chromen-4-one
-
7-(4-(2-methyl-5-nitro-1H-imidazol-1-yl)butoxy)-2-phenyl-4H-chromen-4-one
-
7-(4-(5-methyl-1H-tetrazol-1-yl)butoxy)-2-phenyl-4H-chromen-4-one
-
7-(4-bromobutoxy)-2-phenyl-4H-1-benzopyran-4-one
-
7-bromo-6-difluoromethylphosphonate 3-naphthalenenitrile
50% inhibition at 230 nM for wild-type, at 886 nM for mutant S295F
7-chloro-6-[(2-morpholin-4-ylethyl)amino]quinoline-5,8-dione
-
7-hydroxy-2-(4'-hydroxyphenyl)-3-[(1,1'-biphenyl-4-yl)methyl]-4H-1-benzopyran-4-one
-
7-hydroxy-2-(4'-hydroxyphenyl)-3-[(3'',4''-dihydroxy-1,1'-biphenyl-4-yl)methyl]-4H-1-benzopyran-4-one
-
7-hydroxy-2-(4'-hydroxyphenyl)-3-[(3''-carboxy-1,1'-biphenyl-4-yl)methyl]-4H-1-benzopyran-4-one
-
7-hydroxy-2-(4'-hydroxyphenyl)-3-[(4''-carboxy-3''-hydroxy-1,1'-biphenyl-4-yl)methyl]-4H-1-benzopyran-4-one
-
7-hydroxy-2-(4'-hydroxyphenyl)-3-[(4''-hydroxy-1,1'-biphenyl-4-yl)methyl]-4H-1-benzopyran-4-one
-
7-hydroxy-2-(4-hydroxybenzyl)-4H-chromen-4-one
10% inhibition of LMW-PTP isozymes 1 and 2,no inhibition of PTP-B1, at 0.015 mM
7-hydroxy-2-(4-hydroxyphenyl)-2,3-dihydro-4H-chromen-4-one
-
isolated from the CH2Cl2 extract of Glycyrrhiza inflata
7-hydroxy-2-(4-hydroxyphenyl)-3-[(3',4'-dihydroxy-1,1-biphenyl-3-yl)methyl]-4H-1-benzopyran-4-one
60% inhibition of LMW-PTP isozyme 2, 25% inhibition of LMW-PTP 1, and 50% inhibition of PTP-B1, at 0.02 mM
7-hydroxy-2-(4-hydroxyphenyl)-3-[(4'-carboxy-3'-hydroxy-1,1-biphenyl-3-yl)methyl]-4H-1-benzopyran-4-one
5% inhibition of LMW-PTP isozyme 2, 10% inhibition of LMW-PTP 1, and 59% inhibition of PTP-B1, at 0.02 mM
7-hydroxy-2-(4-hydroxyphenylethyl)-3-[(1,1-biphenyl-4-yl)methyl]-4H-1-benzopyran-4-one
7-hydroxy-2-(4-hydroxyphenylmethyl)-3-[(1,1'-biphenyl-4-yl)methyl]-4H-1-benzopyran-4-one
7-hydroxy-2-(4-hydroxyphenylpropyl)-3-[(1,1'-biphenyl-4-yl)methyl]-4H-1-benzopyran-4-one
10% inhibition of LMW-PTP isozymes 1 and 2,no inhibition of PTP-B1, at 0.015 mM
8-acetyl-3a,4,5,9b-tetrahydro-3H-cyclopenta[c]quinoline-4-carboxylic acid
8-benzyl-4-oxo-4H-chromene-3-carbaldehyde
50% inhibition at 0.018 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases
8-bromo-3a,4,5,9b-tetrahydro-3H-cyclopenta[c]quinoline-4-carboxylic acid
8-bromo-4-oxo-6-(2-phenyl-1-benzothien-3-yl)-4H-chromene-3-carbaldehyde
50% inhibition at 0.0078 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases
8-bromo-6-(10-bromo-9-anthryl)-4-oxo-4H-chromene-3-carbaldehyde
50% inhibition at 0.011 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases
8-bromo-6-(2-bromo-1-benzothien-3-yl)-4-oxo-4H-chromene-3-carbaldehyde
50% inhibition at 0.0082 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases
8-bromo-6-dibenzo(b,d)thien-1-yl-4-oxo-4H-chromene-3-carbaldehyde
50% inhibition at 0.010 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases
8-bromo-6-dibenzo(b,d)thien-4-yl-4-oxo-4H-chromene-3-carbaldehyde
50% inhibition at 0.016 mM, irreversible, selective for isoform PTP1B over other human protein tyrosine phosphatases
8-hydroxy-3-methoxy-11-oxo-1-pentanoyl-6-pentyl-11H-dibenzo[b,e][1,4]dioxepine-7-carboxylic acid
-
isolated from a methanol extract of the Antarctic lichen Stereocaulon alpinum
abietic acid
a nonpolar inhibitor and weak mixed-type inhibitor of PTP1B, inhibits the enzyme by binding to its active site in a nonsubstrate-like manner that stabilizes the catalytically essential WPD loop in an inactive conformation, modelling of enzyme binding. Upon binding to the active site, abietic acid forms a hydrogen bond with R221 that weakens a bond between R221 and E115 and prevents the formation of a hydrogen bond between W179 and R221 that forms when the WPD loop closes
acanthoic acid
-
diterpenoid isolated from Acanthopanax koreanum, 50% inhibition at 0.024 mM
acetaldehyde
-
more than 95% remaining activity at 0.5 mM
acid
-
-
-
acrolein
-
4% remaining activity at 0.5 mM, potent irreversible time-dependent inhibitor, addition of 1 mM vanadate slows inactivation of PTP1B by 0.5 mM acrolein
aquastatin A
-
derived from marine fungus Cosmospora sp. SF-5060, competitive inhibition
auranofin
-
inhibition of cysteine-dependent protein tyrosine phosphatases
benzyl 1,6-dibenzyl-4-oxo-1,4-dihydroquinoline-3-carboxylate
-
0.1% inhibition at 0.02 mg/ml
benzyl 1-cyclopropyl-6-iodo-4-oxo-1,4-dihydroquinoline-3-carboxylate
-
80.5% inhibition at 0.02 mg/ml
benzyl oleanolic acid amide
-
benzyl oleanolic acid ester
-
Berberine
binding structure, molecular modeling, overview
betulinic acid
-
95.1% PTP1B inhibitory activity with 0.0007 mg/ml
betulinic acid methyl ester
-
89.4% PTP1B inhibitory activity with 0.00093 mg/ml
biphenyl-3,4-diol
25% inhibition of LMW-PTP isozyme 2, and 10% inhibition of LMW-PTP 1 and PTP-B1 at 0.02 mM
bis(2-ethyl-maltolato)oxidovanadium(IV)
noncompetitive inhibition of hydrolysis of 4-nitrophenyl phosphate and of phosphorylated undecapeptide substrate EGFR988-998 in the presence of bis(2-ethyl-maltolato)oxidovanadium(IV)
bis(2-methyl-maltolato)oxidovanadium(IV)
-
bis(3-hydroxy-2-methyl-4(1H)pyridinonato)oxidovanadium(IV)
-
bis(acetylacetonato)oxidovanadium(IV)
acts as an uncompetitive inhibitor of PTP1B with DADEpYLIPQQG as the substrate, but this VO2+-chelate exhibits only apparent competitive inhibition of 4-nitrophenyl phosphate hydrolysis when catalyzed by PTP1B, differing from that observed in the hydrolysis of the phosphotyrosine-containing undecapeptide DADEpYLIPQQG mimicking residues 988-998 of the epidermal growth factor receptor (EGFR). Addition of 4-nitrophenyl phosphate after addition of saturating amounts of bis(acetylacetonato)oxidovanadium(IV) to PTP1B causes complete loss of catalytic activity
BzN-EJJ-amide
calopocarpin
-
-
chloro(1,3-dimethyl-1,3-dihydro-2H-imidazol-2-ylidene)gold
-
i.e. [(p-MeMeIm)AuICl]
chloro(1-methyl-1,3-dihydro-2H-imidazol-2-ylidene)gold
-
i.e. [(MeIm)AuICl]
chloro[1-methyl-3-(4-methylbenzyl)-2,3-dihydro-1H-imidazol-2-yl]gold
-
i.e. [(p-MeBzMeIm)AuICl]
CinnGel 2ME
continentalic acid
modelling of enzyme binding
corosolic acid
-
50% inhibition at 0.0072mM, mixed-type inhibition
Cr(VI)
-
as Na2CrO4, induces clonogenic lethality
crotonaldehyde
-
85% remaining activity at 0.5 mM
cyclopropyl-6-(4-fluorobenzyl)-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
-
71.1% inhibition at 0.02 mg/ml
dehydroabietic acid
modelling of enzyme binding
dehydrocostuslactone
-
86.2% PTP1B inhibitory activity with 0.00651 mg/ml
dihydroabietic acid
modelling of enzyme binding
diphosphate
-
-
disodium 4-(((4-methyl-3-(((3-(((3-((2-methyl-5-((4-sulfonatophenyl)carbamoyl)phenyl)carbamoyl)phenyl)carbamoyl)amino)phenyl)carbonyl)amino)phenyl)carbonyl)amino)benzenesulfonate
-
suramin-derivative, 50% inhibition of PTP1B at 0.010 mM, reversible and competitive. Not inhibitory to PTPalpha or LAR
disodium hydrogen (3-(((4-(((4-((3-(hydroxyphosphinato)phenyl)carbamoyl)phenyl)carbamoyl)amino)phenyl)carbonyl)amino)phenyl)phosphonate
-
suramin-derivative, 50% inhibition of PTP1B at 0.0096 mM, reversible and competitive. Not inhibitory to PTPalpha or LAR
dysidiolide
inhibits Cdc25A
ent-17-hydroxykaur-15-en-19-oic acid
40% inhibition at 0.033 mM
ent-3beta-angeloyloxykaur-16-en-19-oic acid
-
ent-3beta-tigloyloxykaur-16-en-19-oic acid
-
ent-kaur-16-en-19-oic acid
-
diterpenoid isolated from Acanthopanax koreanum, 50% inhibition at 0.020 mM
ent-kaur-9(11),16-dien-19-oic acid
29% inhibition at 0.033 mM
erybraedin A
-
-
erylysins A
-
i.e. 3''-hydroxy-2',2'-dimethylpyrano[6',5':3,4]-2'',2''-dimethyldihydropyrano[6'',5'':9,10]pterocarpan, a pterocarpan isolated from stem bark of Erythrina lysistemon, inhibits PTPB1
erylysins B
-
i.e. furano[5',4':3,4]-9-hydroxy-10-prenylpterocarpan, a pterocarpan isolated from stem bark of Erythrina lysistemon, inhibits PTPB1
erysubin D
-
-
eryvarin D
-
-
ethyl (4R)-4-[(1R,3aS,3bS,10aR,10bS,12aR)-6,6,10a,12a-tetramethyl-1,2,3,3a,3b,4,6,6a,7,9a,10,10a,10b,11,12,12a-hexadecahydrocyclopenta[5,6]naphtho[1,2-f]indazol-1-yl]pentanoate
-
-
ethyl (4R)-4-[(1R,3aS,3bS,11aR,11bS,13aR)-8-amino-6,6,11a,13a-tetramethyl-2,3,3a,3b,4,6,11,11a,11b,12,13,13a-dodecahydro-1H-cyclopenta[5,6]naphtho[1,2-g]quinazolin-1-yl]pentanoate
-
-
ethyl 4-[4-[(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)prop-2-enoyl]phenoxy]butanoate
-
-
ethyl [4-[(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)prop-2-enoyl]phenoxy]acetate
-
-
ethyl-3,4-dephostatin
-
FlAsH
the small molecule biarsenical fluorescein derivative, FlAsH, is no inhibitor of the wild-type enzyme but of the engineered WPD insertion mutant enzyme that displays FlAsH-binding cysteine residues. Inhibition of the FlAsH-sensitized TCPTP mutants is rapid and specific, and strong FlAsH sensitivity is observed in mutants that contain as few as two cysteine point mutations in their engineered WPD loops, minimization of FlAsH-binding determinants, overview
fluorescein arsenical hairpin binder
fluorescein arsenical hairpin binder does not inhibit any wild type PTP, but insertion of a fluorescein arsenical hairpin binder-binding peptide (CCPGCC) at a conserved position in the PTP catalytic-domain's WPD loop confers fluorescein arsenical hairpin binder sensitivity upon divergent PTPs
-
glycyrrhetic acid
-
-
Glyoxal
-
93% remaining activity at 0.5 mM
glyoxalbis(N(4)-methylthiosemicarbazonato)Cu(II)
-
inhibition of protein tyrosine phosphatase activity is the prerequisite for activation of epidermal growth factor receptor by the compound, overview
H3VO4
heparin
hexadecanoyl-5-hydroxymethyl tetronic acid
potent irreversible inhibitor of VHR
hexasodium 8,8'-(((2E)-1,4-dioxobut-2-ene-1,4-diyl)bis(iminobenzene-3,1-diylcarbonylimino(4-methylbenzene-3,1-diyl)carbonylimino))dinaphthalene-1,3,5-trisulfonate
-
suramin-derivative, 50% inhibition of PTP1B at 0.005 mM, reversible and competitive. Not inhibitory to PTPalpha or LAR
hexasodium 8,8'-(benzene-1,3-diylbis(carbonyliminobenzene-3,1-diylcarbonylimino(4-methylbenzene-3,1-diyl)carbonylimino))dinaphthalene-1,3,5-trisulfonate
-
suramin-derivative, 50% inhibition of PTP1B at 0.0023 mM, reversible and competitive. Not inhibitory to PTPalpha or LAR
hexasodium 8-(((2'-(((3'-((4,6,8-trisulfonatonaphthalen-1-yl)carbamoyl)biphenyl-2-yl)carbamoyl)amino)biphenyl-4-yl)carbonyl)amino)naphthalene-1,3,5-trisulfonate
-
suramin-derivative, 50% inhibition of PTP1B at 0.070 mM, reversible and competitive. Not inhibitory to PTPalpha or LAR
hexasodium 8-(((3-methyl-4-(((3-(((3-((2-methyl-4-((4,6,8-trisulfonatonaphthalen-1-yl)carbamoyl)phenyl)carbamoyl)phenyl)carbamoyl)amino)phenyl)carbonyl)amino)phenyl)carbonyl)amino)naphthalene-1,3,5-trisulfonate
-
suramin-derivative, 50% inhibition of PTP1B at 0.0037 mM, reversible and competitive. Not inhibitory to PTPalpha or LAR
hexasodium 8-(((3-methyl-4-(((4-(((4-((4-((4,6,8-trisulfonatonaphthalen-1-yl)carbamoyl)phenyl)carbamoyl)phenyl)carbamoyl)amino)phenyl)carbonyl)amino)phenyl)carbonyl)amino)naphthalene-1,3,5-trisulfonate
-
suramin-derivative, 50% inhibition of PTP1B at 0.0021 mM, reversible and competitive. Not inhibitory to PTPalpha or LAR
hexasodium 8-(((4-(((3-(((3-((4-((4,6,8-trisulfonatonaphthalen-1-yl)carbamoyl)phenyl)carbamoyl)phenyl)carbamoyl)amino)phenyl)carbonyl)amino)phenyl)carbonyl)amino)naphthalene-1,3,5-trisulfonate
-
suramin-derivative, 50% inhibition of PTP1B at 0.0016 mM, reversible and competitive. Not inhibitory to PTPalpha or LAR
hexasodium 8-(((4-(1-methylethyl)-3-(((3-(((3-((2-(1-methylethyl)-5-((4,5,8-trisulfonatonaphthalen-1-yl)carbamoyl)phenyl)carbamoyl)phenyl)carbamoyl)amino)phenyl)carbonyl)amino)phenyl)carbonyl)amino)naphthalene-1,4,5-trisulfonate
-
suramin-derivative, 50% inhibition of PTP1B at 0.009 mM, reversible and competitive. Not inhibitory to PTPalpha or LAR
hexasodium 8-(((4-ethyl-3-(((3-(((3-((2-ethyl-5-((4,5,8-trisulfonatonaphthalen-1-yl)carbamoyl)phenyl)carbamoyl)phenyl)carbamoyl)amino)phenyl)carbonyl)amino)phenyl)carbonyl)amino)naphthalene-1,4,5-trisulfonate
-
suramin-derivative, 50% inhibition of PTP1B at 0.009 mM, reversible and competitive. Not inhibitory to PTPalpha or LAR
hexasodium 8-(((4-tert-butyl-3-(((3-(((3-((2-tert-butyl-5-((4,5,8-trisulfonatonaphthalen-1-yl)carbamoyl)phenyl)carbamoyl)phenyl)carbamoyl)amino)phenyl)carbonyl)amino)phenyl)carbonyl)amino)naphthalene-1,4,5-trisulfonate
-
suramin-derivative, 50% inhibition of PTP1B at 0.007 mM, reversible and competitive. Not inhibitory to PTPalpha or LAR
hexasodium 8-([[2-(3-[[(3-[5-[(4,6,8-trisulfonatonaphthalen-1-yl)carbamoyl]-1H-benzimidazol-2-yl]phenyl)carbamoyl]amino]phenyl)-1H-benzimidazol-5-yl]carbonyl]amino)naphthalene-1,3,5-trisulfonate
-
suramin-derivative, 50% inhibition of PTP1B at 0.00049 mM, reversible and competitive. Not inhibitory to PTPalpha or LAR
isoneorautenol
-
-
isopimaric acid
modelling of enzyme binding
JTT-551
-
i.e. monosodium (([5-(1,1-dimethylethyl)thiazol-2-yl]methyl)([(4-(4-[4-(1-propylbutyl)phenoxy]methyl)phenyl)thiazol-2-yl]methyl)amino)acetate, a specific protein tyrosine phosphatase 1B inhibitor in vitro and in vivo, mixed-type inhibition mode versus PTPB1, overview
L-Tartrate
-
weak
licochalcone E
-
lithocholic acid
-
natural inhibitor against PTP1B
lobaric acid
-
a depsidone-type compound, isolated from a methanol extract of the Antarctic lichen Stereocaulon alpinum
lupenone
-
isolated from Sorbus commixta stem bark, inhibits PTP1B in a selective and noncompetitive manner
lupeol
-
isolated from Sorbus commixta stem bark, inhibits PTP1B in a selective and noncompetitive manner
maslinic acid
menadione
inhibits Cdc25B irreversibly
methyl (4R)-4-[(1R,3aS,3bS,10aR,10bS,12aR)-8-amino-6,6,10a,12a-tetramethyl-2,3,3a,3b,4,6,10,10a,10b,11,12,12a-dodecahydro-1H-cyclopenta[7,8]phenanthro[2,3-d][1,3]thiazol-1-yl]pentanoate
-
-
methyl (4R)-4-[(1R,3aS,3bS,11aR,11bS,13aR)-6,6,11a,13a-tetramethyl-2,3,3a,3b,4,6,11,11a,11b,12,13,13a-dodecahydro-1H-cyclopenta[5,6]naphtho[1,2-g]quinoxalin-1-yl]pentanoate
-
-
methyl 2,4-dihydroxy-6-methylbenzoate
-
isolated from a methanol extract of the Antarctic lichen Stereocaulon alpinum
methyl 2-(3-(1-(4-fluorobenzyl)-6-nitro-4-oxo-1,4-dihydroquinoline-3-carboxamido)propoxy)-6-hydroxybenzoate
-
IC50 of 6.5 mg/ml
methyl 2-(3-(1-benzyl-7-fluoro-4-oxo-1,4-dihydroquinoline-3-carboxamido)propoxy)-6-hydroxybenzoate
-
IC50 of 9.4 mg/ml
methyl 2-[4-[(4-[[ethoxy(oxo)acetyl][2-(methoxycarbonyl)phenyl]amino]-3-ethylphenylalanyl)amino]butoxy]-6-hydroxybenzoate
-
methyl 3,8-dimethoxy-11-oxo-1-pentanoyl-6-pentyl-11H-dibenzo[b,e][1,4]dioxepine-7-carboxylate
-
isolated from a methanol extract of the Antarctic lichen Stereocaulon alpinum
methyl 3-formyl-2,4-dihydroxy-6-methylbenzoate
-
isolated from a methanol extract of the Antarctic lichen Stereocaulon alpinum
methyl 4,4-dimethyl-3-oxochol-5-en-24-oate
-
-
methyl 5-amino-6-(7-amino-6-methoxy-5,8-dioxo-5,8-dihydroquinolin-2-yl)-4-(2-hydroxy-3,4-dimethoxyphenyl)-3-methylpyridine-2-carboxylate
-
methyl 8-hydroxy-3-methoxy-11-oxo-1-pentanoyl-6-pentyl-11H-dibenzo[b,e][1,4]dioxepine-7-carboxylate
-
isolated from a methanol extract of the Antarctic lichen Stereocaulon alpinum
methyl oleanolic acid amide
-
methyl oleanolic acid ester
-
methyl-5-((3-(benzylcarbamoyl)-6-iodo-4-oxoquinolin-1(4H)-yl)methyl)-2-methoxybenzoate
-
IC50 of more than 20 mg/ml
mokko lactone
-
93.1% PTP1B inhibitory activity with 0.00141 mg/ml
molybdate
mpV(pic)
-
potent and selective PTP inhibitor, inhibits SPH-1 in a dose-dependent manner
MSI-1436
small molecule inhibitor MSI-1436 binds to the disordered C-terminal domain of PTP1B, C-terminal to the catalytic domain, MSI-1436 functions using an allosteric mechanism to direct the enzymatic activity of PTP1B
N,1-dibenzyl-6-fluoro-4-oxo-1,4-dihydroquinoline-3-carboxamide
-
41.4% inhibition at 0.02 mg/ml
N,1-dibenzyl-6-iodo-4-oxo-1,4-dihydroquinoline-3-carboxamide
-
61.8% inhibition at 0.02 mg/ml
N,N'-[benzene-1,4-diylbis(propane-2,2-diylbenzene-4,1-diyl)]bis(1,1,1-trifluoromethanesulfonamide)
-
-
N-((4-((E)-2-nitroethenyl)phenyl)carbonyl)glycyl-L-alpha-glutamyl-L-glutamic acid
-
50% inhibition at 0.0014 mM in absence of 2-mercaptoethanol, at 0.275 mM in presence of 1 mM 2-mercaptoethanol
N-((4-(difluoro(phosphono)methyl)phenyl)acetyl)-L-a-aspartyl-4-(difluoro(phosphono)methyl)-L-phenylalaninamide
-
inhibition of enzyme increases caveolin-1 phosphorylation
N-((4-(difluoro(phosphono)methyl)phenyl)acetyl)-L-alpha-aspartyl-4-(difluoro(phosphono)methyl)-L-phenylalaninamide
-
-
N-(1,4-dioxo-1,4-dihydronaphthalen-2-yl)-N-(4-methylphenyl)acetamide
-
N-(3-chloro-4-fluorophenyl)-2-[(6,7-dimethoxy-4-oxo-3-phenyl-3,4-dihydro-2-quinazolinyl)sulfanyl]acetamide
80% inhibition at 0.2 mM
N-(3-formylphenyl)-3-(((3-((3-formylphenyl)carbamoyl)phenyl)carbamoyl)amino)benzamide
-
suramin-derivative, 50% inhibition of PTP1B above 0.1 mM, reversible and competitive. Not inhibitory to PTPalpha, CD45 or LAR
N-(3-[(3,5-difluorobenzyl)oxy]pyridin-2-yl)-4-pentylbenzenesulfonamide
74% inhibition at 0.2 mM
N-(3-[(4-chlorophenyl)sulfanyl]-1,4-dioxo-1,4-dihydronaphthalen-2-yl)acetamide
-
N-([4-[difluoro(phosphono)methyl]phenyl]acetyl)-a-aspartyl-4-[difluoro(phosphono)methyl]phenylalaninamide
-
-
N-1-(2-[(2-oxo-4-propyl-2H-chromen-7-yl)oxy]propanoyl)-3-(trifluoromethyl)benzene-1-sulfonohydrazide
84% inhibition at 0.2 mM
N-benzoyl-L-glutamyl-[4-phosphono(difluoromethyl)]-L-phenylalanineamide
-
i.e. BzN-EJJ-amide, 50% inhibition at 4 nM
N-benzyl-1-cyclopropyl-6-fluoro-4-oxo-1,4-dihydroquinoline-3-carboxamide
N-benzyl-1-cyclopropyl-6-iodo-4-oxo-1,4-dihydroquinoline-3-carboxamide
-
6.1% inhibition at 0.02 mg/ml
N-[4-[(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)prop-2-enoyl]phenyl]-4-tert-butylbenzamide
-
-
N-[5-(dimethylamino)-2-hydroxy-3-methoxybenzyl]-N-methyl-2-(4-nitrophenyl)ethanaminium
-
N-[6-chloro-5-(2,3-dichlorophenoxy)-1-methyl-1H-benzimidazol-2-yl]acetamide
70% inhibition at 0.2 mM
N-[6-chloro-5-(2,3-dichlorophenoxy)-1H-benzimidazol-2-yl]-2,2,2-trifluoroacetamide
mixed-type inhibition, 92% inhibition at 0.2 mM
N2-(2-((2-((N-((4-(difluoro(phosphono)methyl)phenyl)acetyl)-L-alpha-aspartyl-4-(difluoro(phosphono)methyl)-L-phenylalanyl)amino)ethyl)disulfanyl)ethyl)-D-arginyl-D-arginyl-D-arginyl-D-arginyl-D-arginyl-D-arginyl-D-arginyl-D-argininamide
-
in presence of 5-50 nM, 11-35% decrease in cell spreading, 24% decrease in number of migratory cells, dose-dependent increase in Y527 phosphorylation of Src
Na3VO4
-
-
NAT6-297775
-
-
NO
-
inactivation, phosphate protects
nocardione A
inhibits Cdc25B
nocardione B
inhibits Cdc25B
NSC-87877
-
potent Shp2 and Shp1 inhibitor
oleanolic acid
oleanolic acid amide
-
oleanolic alcohol
-
oleanonic acid
-
-
orientanol C
-
-
orthovanadate
papaverine
binding structure, molecular modeling, overview
paracaseolide A
-
-
peracetic acid
-
a potent, time-dependent inactivator of the catalytic subunit of PTP1B, treatment of the enzyme with 0.015 mM for 15 sec inactivates 88% of the enzyme, inactivation of PTP1B by peracetic acid can be reversed by treatment of the enzyme with thiols
phaseollin
-
-
Phenylarsine oxide
phenylhydrazonopyrazolone sulfonate 1
-
potent, active site-directed small molecule inhibitor which is specific for Shp2 over the closely related tyrosine phosphatases Shp1 and PTP1B
phenylhydrazonopyrazolone sulfonate 4
-
the most potent inhibitor of Shp2 which shows a specificity profile similar to phenylhydrazonopyrazolone sulfonate 1
phosphate
PO43-
-
treatment of the enzyme with 0.05 mM PO43- for 15 sec inactivates 49% of the enzyme
poly(Glu-Tyr)
-
-
pomolic acid
-
-
potassium bisperoxo(1,10-phenanthroline)oxovanadate
propanal
-
93% remaining activity at 0.5 mM
pterokaurene L3
no inhibition at 0.031 mM
rilobolide-6-O-methacrylate
no inhibition at 0.026 mM
RK-682
rotungenic acid
-
-
small t antigen
-
small t antigen of DNA tumor virus SV40 inhibits the phosphatase activity of the PP2A core enzyme
-
sodium orthovanadate
sodium pervanadate
-
broad-acting tyrosine phosphatase inhibitor
Sodium vanadate
spathodic acid
-
-
spermidine
-
-
spermine
-
2.0-20 mM
stevastelin
inhibits VHR
stigmasterol
-
-
sulfircin
inhibits Cdc25A
suramin
taraxerol
-
-
tetrachyrin
-
tetrasodium 2-(((2-(3-(((3-(5-((2,5-disulfonatophenyl)carbamoyl)-1H-benzimidazol-2-yl)phenyl)carbamoyl)amino)phenyl)-1H-benzimidazol-5-yl)carbonyl)amino)benzene-1,4-disulfonate
-
suramin-derivative, 50% inhibition of PTP1B at 0.00025 mM, reversible and competitive. Not inhibitory to PTPalpha or LAR
tetrasodium 4,4'-(benzene-1,3-diylbis(carbonylimino))dinaphthalene-2,6-disulfonate
-
suramin-derivative, 50% inhibition of PTP1B above 0.1 mM, reversible and competitive. Not inhibitory to PTPalpha, CD45 or LAR
tetrasodium 4,4'-(benzene-1,3-diylbis(carbonyliminobenzene-4,1-diylcarbonylimino))dinaphthalene-2,6-disulfonate
-
suramin-derivative, 50% inhibition of PTP1B at 0.08 mM, reversible and competitive. Not inhibitory to PTPalpha or LAR
tetrasodium 4-(((3-(((3,5-bis((4-sulfonatophenyl)carbamoyl)phenyl)carbamoyl)amino)-5-((4-sulfonatophenyl)carbamoyl)phenyl)carbonyl)amino)benzenesulfonate
-
suramin-derivative, 50% inhibition of PTP1B at 0.0045 mM, reversible and competitive. Not inhibitory to PTPalpha or LAR
tetrasodium 4-(((3-(((5-((4,8-disulfonatonaphthalen-1-yl)carbamoyl)-2-methylphenyl)carbamoyl)amino)-4-methylphenyl)carbonyl)amino)naphthalene-1,5-disulfonate
-
suramin-derivative, 50% inhibition of PTP1B at 0.070 mM, reversible and competitive. Not inhibitory to PTPalpha or LAR
trilobolide-6-O-isobutyrate
no inhibition at 0.026 mM
tungstate
ursolic acid
uvaol
-
-
vanadate
VO3N3
-
oxovanadium(IV) is coordinated with one nitrogen and two oxygen atoms from the Schiff base and two nitrogen atoms from the bidentate planar ligands, in a distorted octahedral geometry, VO3N3
wedelolide D
32% inhibition at 0.020 mM
wedelolide H
no inhibition at 0.023 mM
wedelolide I
no inhibition at 0.021 mM
wedelolide J
no inhibition at 0.021 mM
[(4-[(4E)-2-(1H-benzotriazol-1-yl)-2-[4-(methoxycarbonyl)phenyl]-5-phenylpent-4-en-1-yl]phenyl)(difluoro)methyl]phosphonic acid
-
[2-bromo-4-[(E)-(7,8-dimethyl-3-oxo[1,3]thiazolo[3,2-a]benzimidazol-2(3H)-ylidene)methyl]-6-ethoxyphenoxy]acetic acid
irreversible inhibition
[4-[(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)prop-2-enoyl]phenoxy]acetic acid
-
-
[[1-(4-chlorophenyl)-2-methyl-1H-indol-5-yl]oxy]acetic acid
-
[[4'-(2-butyl-1-benzofuran-3-yl)biphenyl-4-yl]oxy]acetic acid
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-epoxy-3-(p-nitrophenoxy)propane
C215D mutant, not wild type
2,3-diphosphoglycerate
-
activation
2-mercaptoethanol
-
activation
2-mercaptoethylamine
-
activation
ADP
-
activation
dithiothreitol
-
activation
DTT
activates
EDTA
-
activation
glutathione
-
activation
IGF-I
-
IGF-I stimulates p52shc phosphorylation, with a significantly greater increase in p52shc phosphorylation in the p66shc knockdown cells compared to control cells. Overexpression of p66shc impairs IGF-I-stimulated p52shc tyrosine phosphorylation
-
NaCl
-
activity against phosphotyrosine, optimal at 0.1 M
phorbol 12-myristate 13-acetate
-
enzyme gene is among the 10 genes with the largest increased in expression upon phorbol 12-myristate 13-acetate stimulation
spermidine
-
activation
spermine
sulfhydryl compounds
-
-
suramin
-
0.01 mM, about 30% increase in activity of isoforms PTPalpha, LAR
tetrasodium 2-(((2-(3-(((3-(5-((2,5-disulfonatophenyl)carbamoyl)-1H-benzimidazol-2-yl)phenyl)carbamoyl)amino)phenyl)-1H-benzimidazol-5-yl)carbonyl)amino)benzene-1,4-disulfonate
-
0.01 mM, up to 4.5 activation of isoform PTPalpha wild-type
Triton X-100
-
0.1%, 25-30% activation
UpA
-
uPA regulates SHP-2 phosphorylation, stimulates its catalytic activity and association with PDGFR-beta and with lipid rafts
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0215
[Eps15 peptide846-854 P850V]-tyrosine phosphate
recombinant wild-type enzyme, pH and temperature not specified in the publication
-
0.0438
[Eps15 peptide846-854]-tyrosine phosphate
recombinant wild-type enzyme, pH and temperature not specified in the publication
-
15 - 19
3,6-fluorescein diphosphate
0.02 - 0.156
4,6,8-trimethyl-2-oxo-2H-chromen-7-yl dihydrogen phosphate
0.08 - 148
4-nitrophenyl phosphate
0.0039 - 0.0795
6,8-difluoro-4-methylumbelliferyl phosphate
2.6
AAAAApYRHRR
-
pH 7.4, temperature not specified in the publication, RPTPalpha
0.0228 - 0.219
acetyl-DADEpY-NH2
1.1 - 97.5
acetyl-DADEpYL-NH2
0.034
ADEDFpYAA
-
pH 7.4, temperature not specified in the publication, SHP-2
0.058
AKFEDTpYAA
-
pH 7.4, temperature not specified in the publication, SHP-1
0.49
ARKRIpYAA
-
pH 7.4, temperature not specified in the publication, RPTPalpha
0.075
AVWEFpYpYAA
-
pH 7.4, temperature not specified in the publication, SHP-1
0.022
AWSpYADpYAA
-
pH 7.4, temperature not specified in the publication, SHP-1
0.091
AYTEpYTpYAA
-
pH 7.4, temperature not specified in the publication, SHP-1
37
bis(4-nitrophenyl) phosphate
pH 7.3, 22°C, recombinant enzyme
0.00011 - 0.00026
bovine serum albumin
-
0.0005
Cdk2-pTpY/CycA
-
in 50 mM Tris, 50 mM Bis-Tris, 100 mM Na acetate, pH 6.0-6.5, at 5-25°C
-
0.00035 - 0.1
DADEpYLIPQQG
0.028
DAEDFpYAA
-
pH 7.4, temperature not specified in the publication, SHP-2
0.013
DDT-(3,5-difluoro)YDpYAA
-
pH 7.4
0.014
DDTYDpYAA
-
pH 7.4
0.023
DFEDFpYAA
-
pH 7.4, temperature not specified in the publication, SHP-2
5.2 - 11.1
difluoromethylumbelliferyl phosphate
0.0036
DNL-(3,5-difluoro)YpYWD
-
pH 7.4
0.0058
DNLYpYWD
-
pH 7.4
0.017
DWEDFpYAA
-
pH 7.4, temperature not specified in the publication, SHP-2
1.4
EADTApYAA
-
pH 7.4, temperature not specified in the publication, RPTPalpha
0.027 - 0.054
EIFDFpYAA
0.031
FDEDFpYAA
-
pH 7.4, temperature not specified in the publication, SHP-2
0.013 - 0.039
FDIDIpYAA
0.015
fluorescein diphosphate
-
22°C, pH 5.5
0.028 - 0.066
FYDIDpYAA
0.175
GESDGGpYMDMSKD
-
-
0.0096 - 0.0191
GNGDpYMPMSPKS
0.0029
insulin receptor phosphopeptide
-
isoform PTP1B, 37°C, pH 6.9
-
0.77
LIEDNEpYTARQGA
-
pH 7.4, temperature not specified in the publication, RPTPalpha
0.00028 - 0.012
lysozyme
-
0.00014 - 0.0126
myelin basic protein
-
0.0024 - 10
p-nitrophenyl phosphate
0.127
PGSAAP-pY-LKTKFI
pH 6.4, 25°C, recombinant PTPepsilon D1 domain, substrate is a STAT3 peptide
1.6 - 8.5
phosphotyrosine
0.015
phosphotyrosyl bovine serum albumin
-
-
-
0.059 - 0.789
platelet-derived growth factor receptor
value varies with the point of tyrosine phosphorylation, values for truncated enzyme reduced relative to wild-type form
-
0.119
PQDKEY-pY-KVKEPG
pH 6.4, 25°C, recombinant PTPepsilon D1 domain, substrate is a JAK2 peptide
0.014
RE-(3,5-difluoro)YEFpYAA
-
pH 7.4
0.006
REYEFpYAA
-
pH 7.4
0.124
RKGSGD-pY-MPMSPK
pH 6.4, 25°C, recombinant PTPepsilon D1 domain, substrate is a IRS1 peptide
1.2
RRISTpYAA
-
pH 7.4, temperature not specified in the publication, RPTPalpha
0.048 - 0.18
SASASpYDWEF
0.53 - 2.3
SASASpYSASA
1.07
TATEPQpYQPGEN
-
pH 7.4, temperature not specified in the publication, RPTPalpha
0.33
TGFLTELpYVATRWY
-
-
0.142 - 1.16
TSTEPQpYQPGENL
0.045 - 0.068
WAGDDpYAA
0.043
WDEDFpYAA
-
pH 7.4, temperature not specified in the publication, SHP-2
0.0032 - 0.0063
WDEDFpYDWEF
0.15 - 0.21
WDEDFpYRWKF
0.046 - 0.053
WDEDFpYSASA
0.56 - 0.78
WRKRFpYDWEF
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13.4
[Eps15 peptide846-854 P850V]-tyrosine phosphate
recombinant wild-type enzyme, pH and temperature not specified in the publication
-
17.3
[Eps15 peptide846-854]-tyrosine phosphate
recombinant wild-type enzyme, pH and temperature not specified in the publication
-
2 - 71.6
4,6,8-trimethyl-2-oxo-2H-chromen-7-yl dihydrogen phosphate
0.01 - 27.5
4-nitrophenyl phosphate
0.00016 - 8.66
6,8-difluoro-4-methylumbelliferyl phosphate
30
AAAAApYRHRR
-
pH 7.4, temperature not specified in the publication, RPTPalpha
2 - 8
ADEDFpYAA
-
pH 7.4, temperature not specified in the publication, SHP-2
19
AKFEDTpYAA
-
pH 7.4, temperature not specified in the publication, SHP-1
39
ARKRIpYAA
-
pH 7.4, temperature not specified in the publication, RPTPalpha
24
AVWEFpYpYAA
-
pH 7.4, temperature not specified in the publication, SHP-1
13
AWSpYADpYAA
-
pH 7.4, temperature not specified in the publication, SHP-1
17
AYTEpYTpYAA
-
pH 7.4, temperature not specified in the publication, SHP-1
0.033
bis(4-nitrophenyl) phosphate
pH 7.3, 22°C, recombinant enzyme
30
DAEDFpYAA
-
pH 7.4, temperature not specified in the publication, SHP-2
3 - 6
DDT-(3,5-difluoro)YDpYAA
-
pH 7.4
33
DDTYDpYAA
-
pH 7.4
37
DFEDFpYAA
-
pH 7.4, temperature not specified in the publication, SHP-2
3 - 6
DNL-(3,5-difluoro)YpYWD
-
pH 7.4
32
DNLYpYWD
-
pH 7.4
30
DWEDFpYAA
-
pH 7.4, temperature not specified in the publication, SHP-2
26
EADTApYAA
-
pH 7.4, temperature not specified in the publication, RPTPalpha
26 - 32
EIFDFpYAA
30
FDEDFpYAA
-
pH 7.4, temperature not specified in the publication, SHP-2
30 - 33
FDIDIpYAA
50 - 66
FYDIDpYAA
200
GESDGGpYMDMSKD
-
-
7.7 - 18.4
GNGDpYMPMSPKS
61.5
insulin receptor phosphopeptide
-
isoform PTP1B, 37°C, pH 6.9
-
8.3
LIEDNEpYTARQGA
-
pH 7.4, temperature not specified in the publication, RPTPalpha
0.11 - 0.35
lysozyme
-
0.37 - 3.1
p-nitrophenyl phosphate
3.6
PGSAAP-pY-LKTKFI
pH 6.4, 25°C, recombinant PTPepsilon D1 domain, substrate is a STAT3 peptide
0.66 - 7.2
platelet-derived growth factor receptor
value varies with the point ot tyrosine phosphorylation, values for truncated enzyme increased relative to wild-type form
-
3.1
PQDKEY-pY-KVKEPG
pH 6.4, 25°C, recombinant PTPepsilon D1 domain, substrate is a JAK2 peptide
44
RE-(3,5-difluoro)YEFpYAA
-
pH 7.4
33
REYEFpYAA
-
pH 7.4
3.2
RKGSGD-pY-MPMSPK
pH 6.4, 25°C, recombinant PTPepsilon D1 domain, substrate is a IRS1 peptide
49
RRISTpYAA
-
pH 7.4, temperature not specified in the publication, RPTPalpha
12 - 35
SASASpYDWEF
23 - 42
SASASpYSASA
9.7
TATEPQpYQPGEN
-
pH 7.4, temperature not specified in the publication, RPTPalpha
177
TGFLTELpYVATRWY
-
-
8.9 - 258
TSTEPQpYQPGENL
3 - 57
WAGDDpYAA
48
WDEDFpYAA
-
pH 7.4, temperature not specified in the publication, SHP-2
43 - 75
WDEDFpYDWEF
42 - 73
WDEDFpYRWKF
37 - 50
WDEDFpYSASA
1.3 - 1.7
WRKRFpYDWEF
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
623.3
[Eps15 peptide846-854 P850V]-tyrosine phosphate
recombinant wild-type enzyme, pH and temperature not specified in the publication
-
395
[Eps15 peptide846-854]-tyrosine phosphate
recombinant wild-type enzyme, pH and temperature not specified in the publication
-
0.024 - 18
4-nitrophenyl phosphate
39
AAAAApYEEVH
-
pH 7.4, temperature not specified in the publication, RPTPalpha
12
AAAAApYRHRR
-
pH 7.4, temperature not specified in the publication, RPTPalpha
0.00005
Ac-AAAApYAAAA-NH2
-
pH 7.0, 25°C
0.0016
Ac-AAAEpYAAAA-NH2
-
pH 7.0, 25°C
0.0003
Ac-AAAQpYAAAA-NH2
-
pH 7.0, 25°C
0.04
Ac-DGEEpYDDPF-NH2
-
pH 7.0, 25°C
0.0062
Ac-ENDEpYTARE-NH2
-
pH 7.0, 25°C
0.0006
Ac-TEPQpYQPGE-NH2
-
pH 7.0, 25°C
0.046
Ac-YGEEpYDDLY-NH2
-
pH 7.0, 25°C
0.021
Ac-YGYEpYDDEY-NH2
-
pH 7.0, 25°C
0.82
ADEDFpYAA
-
pH 7.4, temperature not specified in the publication, SHP-2
0.34
AKFEDTpYAA
-
pH 7.4, temperature not specified in the publication, SHP-1
81
ARKRIpYAA
-
pH 7.4, temperature not specified in the publication, RPTPalpha
13
ASSDDpYAA
-
pH 7.4, temperature not specified in the publication, RPTPalpha
3.3
AVWEFpYpYAA
-
pH 7.4, temperature not specified in the publication, SHP-1
0.58
AWSpYADpYAA
-
pH 7.4, temperature not specified in the publication, SHP-1
1.9
AYTEpYTpYAA
-
pH 7.4, temperature not specified in the publication, SHP-1
0.0009
bis(4-nitrophenyl) phosphate
pH 7.3, 22°C, recombinant enzyme
1.1
DAEDFpYAA
-
pH 7.4, temperature not specified in the publication, SHP-2
1.6
DFEDFpYAA
-
pH 7.4, temperature not specified in the publication, SHP-2
1.7
DWEDFpYAA
-
pH 7.4, temperature not specified in the publication, SHP-2
19
EADTApYAA
-
pH 7.4, temperature not specified in the publication, RPTPalpha
0.48 - 1.2
EIFDFpYAA
0.00112 - 0.00269
ENPE(pY)LGLD
0.00115 - 0.00271
ENPE(pY)LTPQ
1
FDEDFpYAA
-
pH 7.4, temperature not specified in the publication, SHP-2
0.77 - 2.5
FDIDIpYAA
0.00187 - 0.00397
FDNL(pY)2WDQD
0.75 - 2.4
FYDIDpYAA
11
LIEDNEpYTARQGA
-
pH 7.4, temperature not specified in the publication, RPTPalpha
28.35
PGSAAP-pY-LKTKFI
pH 6.4, 25°C, recombinant PTPepsilon D1 domain, substrate is a STAT3 peptide
0.00052 - 0.00142
PLQR(pY)SEDP
26.05
PQDKEY-pY-KVKEPG
pH 6.4, 25°C, recombinant PTPepsilon D1 domain, substrate is a JAK2 peptide
25.81
RKGSGD-pY-MPMSPK
pH 6.4, 25°C, recombinant PTPepsilon D1 domain, substrate is a IRS1 peptide
41
RRISTpYAA
-
pH 7.4, temperature not specified in the publication, RPTPalpha
0.19 - 0.25
SASASpYDWEF
0.013 - 43
SASASpYSASA
9.1
TATEPQpYQPGEN
-
pH 7.4, temperature not specified in the publication, RPTPalpha
7.7
TSTEPQpYQPGENL
-
pH 7.4, temperature not specified in the publication, RPTPalpha
0.53 - 1.3
WAGDDpYAA
1.1
WDEDFpYAA
-
pH 7.4, temperature not specified in the publication, SHP-2
6.8 - 23
WDEDFpYDWEF
0.28 - 0.34
WDEDFpYRWKF
0.7 - 69
WDEDFpYSASA
0.0022 - 0.0023
WRKRFpYDWEF
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0068
(2E)-1-(3-aminophenyl)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0062
(2E)-1-(4-aminophenyl)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0029
(2E)-1-[3-(benzyloxy)phenyl]-3-(5-bromo-4-hydroxy-2-methoxyphenyl)prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0026
(2E)-3-(5-bromo-2,4-dihydroxyphenyl)-1-[4-methoxy-3-(3-methylbut-3-en-2-yl)phenyl]prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0111
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-(3-methoxyphenyl)prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0113
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-(3-[[(methoxycarbonyl)sulfanyl]amino]phenyl)prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0042
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-(4-butoxyphenyl)prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0137
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-(4-hydroxyphenyl)prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0099
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-(4-methoxyphenyl)prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0139
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[2-(dimethylamino)phenyl]prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0068
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[2-(piperidin-1-yl)phenyl]prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0035
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[2-[di(prop-2-en-1-yl)amino]phenyl]prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.007
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[3-(3-methylbut-3-en-2-yl)-4-[(3-methylbut-2-en-1-yl)oxy]phenyl]prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0264
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[3-(dimethylamino)phenyl]prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0049
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[3-(piperidin-1-yl)phenyl]prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0045
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[3-[di(prop-2-en-1-yl)amino]phenyl]prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.006
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-(1H-pyrazol-1-yl)phenyl]prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.03
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-(dimethylamino)phenyl]prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0184
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-(methylsulfonyl)phenyl]prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.008
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-(morpholin-4-yl)phenyl]prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0026
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-(piperidin-1-yl)phenyl]prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0044
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-hydroxy-3-(3-methylbut-2-en-1-yl)phenyl]prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0053
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-hydroxy-3-(3-methylbut-3-en-2-yl)phenyl]prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0044
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-hydroxy-3-(prop-2-en-1-yl)phenyl]prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0029
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-methoxy-3-(3-methylbut-2-en-1-yl)phenyl]prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0019
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-methoxy-3-(3-methylbut-3-en-2-yl)phenyl]prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0053
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-methoxy-3-(prop-2-en-1-yl)phenyl]prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0035
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-[(3-methylbut-2-en-1-yl)oxy]phenyl]prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0027
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-[(4-methylphenyl)sulfonyl]phenyl]prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0034
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-[di(prop-2-en-1-yl)amino]phenyl]prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0063
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[6-(dimethylamino)-1,3-benzodioxol-5-yl]prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0029
(2E)-3-[5-bromo-2-hydroxy-4-(tetrahydro-2H-pyran-2-yloxy)phenyl]-1-[4-methoxy-3-(3-methylbut-3-en-2-yl)phenyl]prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.0103
(2E)-3-[5-bromo-2-methoxy-4-(tetrahydro-2H-pyran-2-yloxy)phenyl]-1-[4-hydroxy-3-(3-methylbut-3-en-2-yl)phenyl]prop-2-en-1-one
-
pH not specified in the publication, temperature not specified in the publication
0.023 - 0.1
(5R)-2-((carboxycarbonyl)amino)-5-((1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl)-4,7-dihydro-5H-thieno(2,3-c)pyran-3-carboxylic acid
0.0003 - 0.113
(5S)-2-((carboxycarbonyl)amino)-5-((1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl)-4,7-dihydro-5H-thieno(2,3-c)pyran-3-carboxylic acid
0.01
16alphaH,17-isovaleryloxy-ent-kauran-19-oic acid
-
pH 6.0, 30°C
0.019 - 0.109
2-((carboxycarbonyl)amino)-4,7-dihydro-5H-thieno(2,3-c)pyran-3-carboxylic acid
0.00091 - 0.115
2-((carboxycarbonyl)amino)-5-((1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl)-4,7-dihydro-5H-thieno(2,3-c)pyran-3-carboxylic acid
0.00061 - 0.147
2-((carboxycarbonyl)amino)-5-((4-fluoro-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl)-4,7-dihydro-5H-thieno(2,3-c)pyran-3-carboxylic acid
0.00019 - 0.0038
2-((carboxycarbonyl)amino)-5-((4-hydroxy-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl)-4,7-dihydro-5H-thieno(2,3-c)pyran-3-carboxylic acid
0.00017 - 0.088
2-((carboxycarbonyl)amino)-5-((5-hydroxy-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl)-4,7-dihydro-5H-thieno(2,3-c)pyran-3-carboxylic acid
2 - 81
2-(oxalyl-amino)-4,7-dihydro-5H-thieno[2,3-c]thiopyran-3-carboxylic acid
0.0042
2-[6-chloro-5-(1-naphthalyloxy)-1H-benzimidazol-2-yl]thio-N-(thiazol-2-yl)acetamide
pH 7.0, 37°C
2.5
3-(1-carboxy-ethoxy)-6-chloro-benzo(b)-thiophene-2-carboxylic acid
-
pH 7.0, 22°C
0.052
3-(carboxy-fluoro-methoxy)-6-chloro-benzo(b)thiophene-2-carboxylic acid
-
pH 7.0, 22°C
0.86
3-(carboxymethoxy)-2-naphthoic acid
-
pH 7.0, 22°C
0.00092
3-(carboxymethoxy)-5-((cyclohexylmethyl)-amino)thieno(3,2-b)(1)benzothiophene-2-carboxylic acid
-
pH 7.0, 22°C
0.0017
3-(carboxymethoxy)-5-(cyclohexylamino)-thieno(3,2-b)(1)benzothiophene-2-carboxylic acid
-
pH 7.0, 22°C
0.01
3-(carboxymethoxy)-5-chlorothieno(3,2-b)(1)benzothiophene-2-carboxylic acid
-
pH 7.0, 22°C
0.0016
3-(carboxymethoxy)-6-((1-(ethylsulfonyl)-piperidin-4-yl)amino)thieno(3,2-b)(1)benzo-thiophene-2-carboxylic acid
-
pH 7.0, 22°C
0.00068
3-(carboxymethoxy)-6-((cyclohexylmethyl)-amino)thieno(3,2-b)(1)benzothiophene-2-carboxylic acid
-
pH 7.0, 22°C
0.00074
3-(carboxymethoxy)-6-(cyclohexylamino)-thieno(3,2-b)(1)benzothiophene-2-carboxylic acid
-
pH 7.0, 22°C
0.0024
3-(carboxymethoxy)-6-(tetrahydro-2H-pyran-4-ylamino)thieno(3,2-b)(1)benzothiophene-2-carboxylic acid
-
pH 7.0, 22°C
0.035
3-(carboxymethoxy)-6-chlorothieno(3,2-b)(1)benzothiophene-2-carboxylic acid
-
pH 7.0, 22°C
2.5
3-(carboxymethoxy)-6-methylthieno(3,2-c)pyridine-2-carboxylic acid
-
pH 7.0, 22°C
0.16
3-(carboxymethoxy)benzo(b)thiophene-2-carboxylic acid
-
pH 7.0, 22°C
2.5
3-(carboxymethoxy)furo(2,3-b)pyridine-2-carboxylic acid
-
pH 7.0, 22°C
0.2 - 0.23
3-(carboxymethoxy)thieno(2,3-b)pyridine-2-carboxylic acid
0.0092
3-(carboxymethoxy)thieno(3,2-b)(1)benzo-thiophene-2-carboxylic acid
-
pH 7.0, 22°C
0.077
3-(carboxymethoxy)thieno(3,2-b)pyridine-2-carboxylic acid
-
pH 7.0, 22°C
0.28
3-(carboxymethoxy)thieno(3,2-b)thiophene-2-carboxylic acid
-
pH 7.0, 22°C
0.026
3-carboxymethoxy-6-(4-hydroxyphenyl)-benzo(b)-thiophene-2-carboxylic acid
-
pH 7.0, 22°C
0.02
3-carboxymethoxy-6-(5-methyl-1-phenyl-1H-pyrazol-3-ylcarbamoyl)-benzo(b)thiophene-2-carboxylic acid
-
pH 7.0, 22°C
0.061
3-carboxymethoxy-6-chloro-benzo(b)-thiophene-2-carboxylic acid
-
pH 7.0, 22°C
0.128
3-carboxymethoxy-6-phenylbenzo(b)-thiophene-2-carboxylic acid
-
pH 7.0, 22°C
0.03
3-carboxymethoxy-6-thiophen-2-yl-benzo(b)-thiophene-2-carboxylic acid
-
pH 7.0, 22°C
0.119
3-carboxymethoxy-7-chloro-benzo(b)-thiophene-2-carboxylic acid
-
pH 7.0, 22°C
0.037
3-carboxymethoxy-7-methyl-benzo(b)-thiophene-2-carboxylic acid
-
pH 7.0, 22°C
0.011
3-carboxymethoxy-naphtho(1,2-b)thiophene-2-carboxylic acid
-
pH 7.0, 22°C
0.5
3-carboxymethoxy-thieno(3,2-c)quinoline-2-carboxylic acid
-
pH 7.0, 22°C
0.0216
3-[2,5-dimethyl-3-[(3-oxo-2,3-dihydro[1,3]thiazolo[3,2-a]benzimidazol-2-yl)methyl]-1H-pyrrol-1-yl]benzoic acid
pH 7.0, 25°C
0.000026
4-(difluoro(phosphono)methyl)-N-pentadecanoyl-L-phenylalanyl-L-a-aspartyl-4-(difluoro(phosphono)methyl)-L-phenylalaninamide
-
-
0.0023
4-[(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)prop-2-enoyl]phenyl 4-bromobenzoate
-
pH not specified in the publication, temperature not specified in the publication
0.0024
4-[(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)prop-2-enoyl]phenyl 4-tert-butylbenzoate
-
pH not specified in the publication, temperature not specified in the publication
0.0049
4-[(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)prop-2-enoyl]phenyl benzoate
-
pH not specified in the publication, temperature not specified in the publication
0.03
4-[4-[(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)prop-2-enoyl]phenoxy]butanoic acid
-
pH not specified in the publication, temperature not specified in the publication
0.0052
5-chloro-N-[6-chloro-5-(2,3-dichlorophenoxy)-1H-benzimidazol-2-yl]-1-methyl-2-(methylthio)-1H-benz-imidazole-6-carboxamide
pH 7.0, 37°C
0.00037
6-((1-(benzylsulfonyl)piperidin-4-yl)amino)-3-(carboxymethoxy)thieno(3,2-b)(1)benzothiophene-2-carboxylic acid
-
pH 7.0, 22°C
0.042
6-bromo-3-carboxymethoxy-benzo(b)-thiophene-2-carboxylic acid
-
pH 7.0, 22°C
0.00023
acrolein
-
in sodium acetate (100 mM), bis-Tris (50 mM), Tris (50 mM), diethylenetriaminepentaacetic acid (5 mM), and 2,5-dimethylfuran (5% v/v), at pH 7 and 25°C
0.00001
aquastatin A
-
-
0.00014 - 0.0148
bis(2-ethyl-maltolato)oxidovanadium(IV)
0.0382
bis(3-hydroxy-2-methyl-4(1H)pyridinonato)oxidovanadium(IV)
pH 5.0, 22°C, recombinant enzyme, versus 4-nitrophenyl phosphate
0.00016 - 0.0065
bis(acetylacetonato)oxidovanadium(IV)
0.0108
ethyl 4-[4-[(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)prop-2-enoyl]phenoxy]butanoate
-
pH not specified in the publication, temperature not specified in the publication
0.0152
ethyl [4-[(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)prop-2-enoyl]phenoxy]acetate
-
pH not specified in the publication, temperature not specified in the publication
0.000017 - 0.00037
fluorescein arsenical hairpin binder
-
0.006 - 0.196
H2O2
0.0118
lupenone
-
pH 6.0, 37°C
0.0034
lupeol
-
pH 6.0, 37°C
0.0000024
N-((4-(difluoro(phosphono)methyl)phenyl)acetyl)-L-alpha-aspartyl-4-(difluoro(phosphono)methyl)-L-phenylalaninamide
-
-
0.0034
N-[4-[(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)prop-2-enoyl]phenyl]-4-tert-butylbenzamide
-
pH not specified in the publication, temperature not specified in the publication
0.0413
N-[6-chloro-5-(2,3-dichlorophenoxy)-1H-benzimidazol-2-yl]-2,2,2-trifluoroacetamide
pH 7.0, 37°C
0.0003 - 0.0007
orthovanadate
0.00073 - 0.0107
phenylhydrazonopyrazolone sulfonate 1
0.017
PO43-
-
active site-directed inhibitor
0.0053 - 0.0057
suramin
0.002 - 0.0031
ursolic acid
0.0000056
Zn2+
at pH 7.4 and 25°C
0.03
[4-[(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)prop-2-enoyl]phenoxy]acetic acid
-
pH not specified in the publication, temperature not specified in the publication
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00927
(1R,3aS,3bS,10aR,10bS,12aR)-1-[(2R)-4-carboxybutan-2-yl]-6,6,10a,12a-tetramethyl-1,2,3,3a,3b,4,6,7,10,10a,10b,11,12,12a-tetradecahydrocyclopenta[5,6]naphtho[1,2-f]indazole-9-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.01433
(2alpha,3alpha)-2,3-dihydroxyolean-12-en-28-oic acid
Homo sapiens
-
PTPB1
0.00493
(2beta,3beta)-2,3-dihydroxyolean-12-en-28-oic acid
Homo sapiens
-
PTPB1
0.05
(2E)-1-(2,4-dihydroxyphenyl)-3-(4-hydroxyphenyl)prop-2-en-1-one
Homo sapiens
-
above, pH 6.0, 37°C
0.05
(2E)-3-(4-hydroxy-2-methoxyphenyl)-1-(4-hydroxyphenyl)prop-2-en-1-one
Homo sapiens
-
above, pH 6.0, 37°C
0.0183
(2E)-3-[2,4-dimethoxy-5-(2-methylbut-3-en-2-yl)phenyl]-1-(4-hydroxyphenyl)prop-2-en-1-one
Homo sapiens
-
pH 6.0, 37°C
0.0198
(2E)-3-[2,4-dimethoxy-5-(2-methylbut-3-en-2-yl)phenyl]-1-(4-methoxyphenyl)prop-2-en-1-one
Homo sapiens
-
pH 6.0, 37°C
0.0309
(2E)-3-[4-hydroxy-2-methoxy-3-(3-methylbut-2-en-1-yl)phenyl]-1-(4-hydroxyphenyl)prop-2-en-1-one
Homo sapiens
-
pH 6.0, 37°C
0.0191
(2E)-3-[4-hydroxy-2-methoxy-5-(2-methylbut-3-en-2-yl)phenyl]-1-(4-hydroxyphenyl)prop-2-en-1-one
Homo sapiens
-
pH 6.0, 37°C
0.0117
(2E)-3-[4-hydroxy-2-methoxy-5-(2-methylbut-3-en-2-yl)phenyl]-1-(4-methoxyphenyl)prop-2-en-1-one
Homo sapiens
-
pH 6.0, 37°C
0.0207
(2E)-3-[4-hydroxy-2-methoxy-5-(3-methylbut-3-en-2-yl)phenyl]-1-(4-hydroxyphenyl)prop-2-en-1-one
Homo sapiens
-
pH 6.0, 37°C
0.00017
(2R)-2-benzyl-3-[2,6-dibromo-4-(6-bromo-5a,11a-dihydrobenzo[b]naphtho[2,3-d]furan-11-yl)phenyl]propanoic acid
Homo sapiens
-
0.0632
(2Z)-2-([5-[4-(1H-tetrazol-1-yl)phenyl]furan-2-yl]methylidene)[1,3]thiazolo[3,2-a]benzimidazol-3(2H)-one
Homo sapiens
pH 7.0, 25°C
0.3
(2Z)-2-[[5-(2-methyl-5-nitrophenyl)furan-2-yl]methylidene][1,3]thiazolo[3,2-a]benzimidazol-3(2H)-one
Homo sapiens
above, pH 7.0, 25°C
0.0083
(3alpha,5beta,8alpha,9beta,10alpha,13alpha)-3-[[(2E)-4-phenylbut-2-enoyl]oxy]kaur-16-en-18-oic acid
Homo sapiens
pH 6.0, 37°C
0.00479
(3beta)-3-(acetyloxy)olean-12-en-28-oic acid
Homo sapiens
-
in 50 mM citrate (pH 6.0), 1 mM dithiothreitol, 1 mM EDTA, and 0.1 M NaCl, at 37°C
0.00534
(3beta)-3-hydroxyolean-12-en-28-oic acid
Homo sapiens
-
in 50 mM citrate (pH 6.0), 1 mM dithiothreitol, 1 mM EDTA, and 0.1 M NaCl, at 37°C
0.0064
(3beta)-3-hydroxyoleana-11,13(18)-dien-28-oic acid
Homo sapiens
-
in 50 mM citrate (pH 6.0), 1 mM dithiothreitol, 1 mM EDTA, and 0.1 M NaCl, at 37°C
0.03
(4aR,6aR,6bS,8aR,12aS,14aR,14bR)-8a-hydroxy-4,4,6a,6b,11,11,14b-heptamethyl-1,4a,5,6,6a,6b,7,8a,9,10,11,12,12a,14,14a,14b-hexadecahydropicene-3,8(2H,4H)-dione
Homo sapiens
-
in 50 mM citrate (pH 6.0), 1 mM dithiothreitol, 1 mM EDTA, and 0.1 M NaCl, at 37°C
0.00377
(4aR,6aS,6bR,8aR,10S,12aR,12bR,14bS)-4a,10-dihydroxy-2,2,6a,6b,9,9,12a-heptamethyl-2,3,4,4a,6,6a,6b,7,8,8a,9,10,11,12,12a,12b,13,14b-octadecahydropicen-5(1H)-one
Homo sapiens
-
in 50 mM citrate (pH 6.0), 1 mM dithiothreitol, 1 mM EDTA, and 0.1 M NaCl, at 37°C
0.00148 - 0.00493
(4aS,6aS,6bR,13aR)-10-acetyl-2,2,6a,6b,9,9,13a-heptamethyl-1,2,3,4,5,6,6a,6b,7,8,8a,9,10,13,13a,13b,14,15b-octadecahydro-4aH-chryseno[1,2-f]indazole-4a-carboxylic acid
0.00175 - 0.00566
(4aS,6aS,6bR,13aR)-10-hexanoyl-2,2,6a,6b,9,9,13a-heptamethyl-1,2,3,4,5,6,6a,6b,7,8,8a,9,10,13,13a,13b,14,15b-octadecahydro-4aH-chryseno[1,2-f]indazole-4a-carboxylic acid
0.00192 - 0.00644
(4aS,6aS,6bR,13aR)-11-amino-2,2,6a,6b,9,9,13a-heptamethyl-1,3,4,5,6,6a,6b,7,8,8a,9,13,13a,13b,14,15b-hexadecahydropiceno[3,2-d][1,3]thiazole-4a(2H)-carboxylic acid
0.00165 - 0.00599
(4aS,6aS,6bR,13aR)-2,2,6a,6b,9,9,13a-heptamethyl-1,2,3,4,5,6,6a,6b,7,8,8a,9,10,13,13a,13b,14,15b-octadecahydro-4aH-chryseno[1,2-f]indazole-4a-carboxylic acid
0.0026 - 0.00844
(4aS,6aS,6bR,13aR)-2,2,6a,6b,9,9,13a-heptamethyl-1,3,4,5,6,6a,6b,7,8,8a,9,13,13a,13b,14,15b-hexadecahydropiceno[2,3-d][1,2]oxazole-4a(2H)-carboxylic acid
0.00064 - 0.00439
(4aS,6aS,6bR,13aR)-2,2,6a,6b,9,9,13a-heptamethyl-10-(pyridin-3-ylcarbonyl)-1,2,3,4,5,6,6a,6b,7,8,8a,9,10,13,13a,13b,14,15b-octadecahydro-4aH-chryseno[1,2-f]indazole-4a-carboxylic acid
0.00081 - 0.00362
(4aS,6aS,6bR,13aR)-2,2,6a,6b,9,9,13a-heptamethyl-10-(pyridin-4-ylcarbonyl)-1,2,3,4,5,6,6a,6b,7,8,8a,9,10,13,13a,13b,14,15b-octadecahydro-4aH-chryseno[1,2-f]indazole-4a-carboxylic acid
0.00139 - 0.0038
(4aS,6aS,6bR,13aR)-2,2,6a,6b,9,9,13a-heptamethyl-10-phenyl-1,2,3,4,5,6,6a,6b,7,8,8a,9,10,13,13a,13b,14,15b-octadecahydro-4aH-chryseno[1,2-f]indazole-4a-carboxylic acid
0.00178 - 0.00551
(4aS,6aS,6bR,14aR)-11-amino-2,2,6a,6b,9,9,14a-heptamethyl-1,3,4,5,6,6a,6b,7,8,8a,9,14,14a,14b,15,16b-hexadecahydrochryseno[1,2-g]quinazoline-4a(2H)-carboxylic acid
0.00261 - 0.0065
(4aS,6aS,6bR,14aR)-2,2,6a,6b,9,9,11,14a-octamethyl-1,3,4,5,6,6a,6b,7,8,8a,9,14,14a,14b,15,16b-hexadecahydrochryseno[1,2-g]quinazoline-4a(2H)-carboxylic acid
0.00273 - 0.00819
(4aS,6aS,6bR,14aR)-2,2,6a,6b,9,9,14a-heptamethyl-1,3,4,5,6,6a,6b,7,8,8a,9,14,14a,14b,15,16b-hexadecahydrochryseno[1,2-g]quinazoline-4a(2H)-carboxylic acid
0.00179 - 0.00831
(4aS,6aS,6bR,14aR)-2,2,6a,6b,9,9,14a-heptamethyl-1,3,4,5,6,6a,6b,7,8,8a,9,14,14a,14b,15,16b-hexadecahydrochryseno[1,2-g]quinoxaline-4a(2H)-carboxylic acid
0.00544
(4aS,6aS,6bR,14aR)-2,2,6a,6b,9,9,14a-heptamethyl-11-(methylamino)-1,3,4,5,6,6a,6b,7,8,8a,9,14,14a,14b,15,16b-hexadecahydrochryseno[1,2-g]quinazoline-4a(2H)-carboxylic acid
Homo sapiens
-
PTPB1
0.00061 - 0.0016
(4aS,6aS,6bR,15aR)-2,2,6a,6b,9,9,15a-heptamethyl-1,2,3,4,5,6,6a,6b,7,8,8a,9,10,15,15a,15b,16,17b-octadecahydro-4aH-chryseno[2,1-b]carbazole-4a-carboxylic acid
0.00143 - 0.00588
(4aS,6aS,6bR,16aR)-2,2,6a,6b,9,9,16a-heptamethyl-1,3,4,5,6,6a,6b,7,8,8a,9,16,16a,16b,17,18b-hexadecahydrochryseno[1,2-b]phenazine-4a(2H)-carboxylic acid
0.00411
(4R)-4-[(1R,3aS,3bS,10aR,10bS,12aR)-6,6,10a,12a-tetramethyl-1,2,3,3a,3b,4,6,6a,7,9a,10,10a,10b,11,12,12a-hexadecahydrocyclopenta[5,6]naphtho[1,2-f]indazol-1-yl]pentanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.03944
(4R)-4-[(1R,3aS,3bS,10aR,10bS,12aR)-6,6,10a,12a-tetramethyl-2,3,3a,3b,4,6,10,10a,10b,11,12,12a-dodecahydro-1H-cyclopenta[7,8]phenanthro[2,3-d][1,2,3]thiadiazol-1-yl]pentanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00913
(4R)-4-[(1R,3aS,3bS,10aR,10bS,12aR)-6,6,10a,12a-tetramethyl-2,3,3a,3b,4,6,6a,9a,10,10a,10b,11,12,12a-tetradecahydro-1H-cyclopenta[7,8]phenanthro[3,2-d][1,2]oxazol-1-yl]pentanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00162
(4R)-4-[(1R,3aS,3bS,10aR,10bS,12aR)-6,6,10a,12a-tetramethyl-7-phenyl-1,2,3,3a,3b,4,6,6a,7,9a,10,10a,10b,11,12,12a-hexadecahydrocyclopenta[5,6]naphtho[1,2-f]indazol-1-yl]pentanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00557
(4R)-4-[(1R,3aS,3bS,10aR,10bS,12aR)-8-amino-6,6,10a,12a-tetramethyl-2,3,3a,3b,4,6,10,10a,10b,11,12,12a-dodecahydro-1H-cyclopenta[7,8]phenanthro[2,3-d][1,3]thiazol-1-yl]pentanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.01165
(4R)-4-[(1R,3aS,3bS,11aR,11bS,13aR)-6,6,11a,13a-tetramethyl-2,3,3a,3b,4,6,11,11a,11b,12,13,13a-dodecahydro-1H-cyclopenta[5,6]naphtho[1,2-g]quinazolin-1-yl]pentanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00862
(4R)-4-[(1R,3aS,3bS,11aR,11bS,13aR)-6,6,11a,13a-tetramethyl-2,3,3a,3b,4,6,11,11a,11b,12,13,13a-dodecahydro-1H-cyclopenta[5,6]naphtho[1,2-g]quinoxalin-1-yl]pentanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00911
(4R)-4-[(1R,3aS,3bS,11aR,11bS,13aR)-6,6,8,11a,13a-pentamethyl-2,3,3a,3b,4,6,11,11a,11b,12,13,13a-dodecahydro-1H-cyclopenta[5,6]naphtho[1,2-g]quinazolin-1-yl]pentanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00361
(4R)-4-[(1R,3aS,3bS,11aR,11bS,13aR)-8-amino-6,6,11a,13a-tetramethyl-2,3,3a,3b,4,6,11,11a,11b,12,13,13a-dodecahydro-1H-cyclopenta[5,6]naphtho[1,2-g]quinazolin-1-yl]pentanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.028
(5beta,8alpha,9beta,10alpha,13alpha)-kaur-16-en-18-oic acid
Homo sapiens
pH 6.0, 37°C
0.0066
(5Z)-3-benzyl-5-(5-bromo-4-butoxy-2-methoxybenzylidene)-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.03
(5Z)-3-benzyl-5-[2-methoxy-5-(prop-2-en-1-yl)-4-(tetrahydro-2H-pyran-2-yloxy)benzylidene]-1,3-thiazolidine-2,4-dione
Homo sapiens
IC50 above 0.03 mM, in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.0072
(5Z)-3-benzyl-5-[4-hydroxy-2-methoxy-5-(prop-2-en-1-yl)benzylidene]-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.0206
(5Z)-3-butyl-5-[2-methoxy-5-(prop-2-en-1-yl)-4-(tetrahydro-2H-pyran-2-yloxy)benzylidene]-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.0096
(5Z)-3-butyl-5-[4-hydroxy-2-methoxy-5-(prop-2-en-1-yl)benzylidene]-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.0298
(5Z)-5-(4-hydroxy-2-methoxybenzylidene)-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.0142
(5Z)-5-(5-bromo-2,4-dimethoxybenzylidene)-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.0082
(5Z)-5-(5-bromo-2,4-dimethoxybenzylidene)-3-(4-methylpent-3-en-1-yl)-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.0121
(5Z)-5-(5-bromo-2,4-dimethoxybenzylidene)-3-butyl-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.0223
(5Z)-5-(5-bromo-2,4-dimethoxybenzylidene)-3-methyl-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.0049
(5Z)-5-(5-bromo-4-butoxy-2-methoxybenzylidene)-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.0123
(5Z)-5-(5-bromo-4-butoxy-2-methoxybenzylidene)-3-(4-methylpent-3-en-1-yl)-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.03
(5Z)-5-(5-bromo-4-butoxy-2-methoxybenzylidene)-3-butyl-1,3-thiazolidine-2,4-dione
Homo sapiens
IC50 above 0.03 mM, in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.0113
(5Z)-5-(5-bromo-4-hydroxy-2-methoxybenzylidene)-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.0122
(5Z)-5-[2-methoxy-5-(prop-2-en-1-yl)-4-(tetrahydro-2H-pyran-2-yloxy)benzylidene]-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.0227
(5Z)-5-[2-methoxy-5-(prop-2-en-1-yl)-4-(tetrahydro-2H-pyran-2-yloxy)benzylidene]-3-(3-methylbut-2-en-1-yl)-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.03
(5Z)-5-[2-methoxy-5-(prop-2-en-1-yl)-4-(tetrahydro-2H-pyran-2-yloxy)benzylidene]-3-(prop-2-en-1-yl)-1,3-thiazolidine-2,4-dione
Homo sapiens
IC50 above 0.03 mM, in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.03
(5Z)-5-[2-methoxy-5-(prop-2-en-1-yl)-4-(tetrahydro-2H-pyran-2-yloxy)benzylidene]-3-(propan-2-yl)-1,3-thiazolidine-2,4-dione
Homo sapiens
IC50 above 0.03 mM, in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.03
(5Z)-5-[2-methoxy-5-(prop-2-en-1-yl)-4-(tetrahydro-2H-pyran-2-yloxy)benzylidene]-3-methyl-1,3-thiazolidine-2,4-dione
Homo sapiens
IC50 above 0.03 mM, in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.0076
(5Z)-5-[4-(benzyloxy)-5-bromo-2-methoxybenzylidene]-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.0103
(5Z)-5-[4-(benzyloxy)-5-bromo-2-methoxybenzylidene]-3-(4-methylpent-3-en-1-yl)-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.0081
(5Z)-5-[4-(benzyloxy)-5-bromo-2-methoxybenzylidene]-3-methyl-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.0293
(5Z)-5-[4-hydroxy-2-methoxy-5-(prop-2-en-1-yl)benzylidene]-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.012
(5Z)-5-[4-hydroxy-2-methoxy-5-(prop-2-en-1-yl)benzylidene]-3-(3-methylbut-2-en-1-yl)-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.03
(5Z)-5-[4-hydroxy-2-methoxy-5-(prop-2-en-1-yl)benzylidene]-3-(prop-2-en-1-yl)-1,3-thiazolidine-2,4-dione
Homo sapiens
IC50 above 0.03 mM, in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.0064
(5Z)-5-[4-hydroxy-2-methoxy-5-(prop-2-en-1-yl)benzylidene]-3-(propan-2-yl)-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.03
(5Z)-5-[4-hydroxy-2-methoxy-5-(prop-2-en-1-yl)benzylidene]-3-methyl-1,3-thiazolidine-2,4-dione
Homo sapiens
IC50 above 0.03 mM, in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.0081
(5Z)-5-[5-bromo-2-methoxy-4-(prop-2-en-1-yloxy)benzylidene]-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.017
(5Z)-5-[5-bromo-2-methoxy-4-(prop-2-en-1-yloxy)benzylidene]-3-(4-methylpent-3-en-1-yl)-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.0079
(5Z)-5-[5-bromo-2-methoxy-4-(prop-2-en-1-yloxy)benzylidene]-3-butyl-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.0046
(5Z)-5-[5-bromo-2-methoxy-4-(propan-2-yloxy)benzylidene]-3-(4-methylpent-3-en-1-yl)-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.0097
(5Z)-5-[5-bromo-2-methoxy-4-(propan-2-yloxy)benzylidene]-3-butyl-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.0053
(5Z)-5-[5-bromo-2-methoxy-4-[(3-methylbut-2-en-1-yl)oxy]benzylidene]-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.01
(5Z)-5-[5-bromo-2-methoxy-4-[(4-methylpent-3-en-1-yl)oxy]benzylidene]-3-(4-methylpent-3-en-1-yl)-1,3-thiazolidine-2,4-dione
Homo sapiens
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA and 1 mM dithiothreitol, at 37°C
0.00466
(6aS,6bR,8aR,10S,12aS,12bR)-10-hydroxy-2,2,6a,6b,9,9,12a-heptamethyl-2,3,4,4a,6,6a,6b,7,8,8a,9,10,11,12,12a,12b-hexadecahydropicen-5(1H)-one
Homo sapiens
-
in 50 mM citrate (pH 6.0), 1 mM dithiothreitol, 1 mM EDTA, and 0.1 M NaCl, at 37°C
0.022
(E)-N-(4,5-diphenyl-1,3-thiazol-2-yl)-2-naphthalen-2-ylethenesulfonamide
Homo sapiens
-
0.021
(E)-N-[4-(4-chlorophenyl)-5-propyl-1,3-thiazol-2-yl]-2-(3,4-dichlorophenyl)ethenesulfonamide
Homo sapiens
-
0.0229 - 0.0324
(Z)-2-(2-(5-(N-(4-chloro-3-(trifluoromethyl)benzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
0.0008 - 0.0154
(Z)-3-(2-(2-carboxyphenyl)hydrazono)-2-oxoindoline-5-carboxylic acid
0.0468 - 0.0967
(Z)-3-(2-(2-nitrophenyl)hydrazono)-2-oxoindoline-5-sulfonic acid
0.0158 - 0.0724
(Z)-3-(2-(3-carboxyphenyl)hydrazono)-2-oxoindoline-5-carboxylic acid
0.0194 - 0.3
(Z)-3-(2-(5-(4-chlorobenzylcarbamoyl)-2-oxoindolin-3-ylidene)-hydrazinyl)benzoic acid
0.0052 - 0.0734
(Z)-3-(2-(5-(N-(2,4-dichlorophenethyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
0.0055 - 0.0194
(Z)-3-(2-(5-(N-(2-chlorobenzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
0.0048 - 0.1228
(Z)-3-(2-(5-(N-(3-chloro-4-fluorobenzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
0.0038 - 0.0425
(Z)-3-(2-(5-(N-(3-chlorobenzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
0.0106 - 0.0742
(Z)-3-(2-(5-(N-(4-chloro-3-(trifluoromethyl)benzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
0.0014 - 0.0188
(Z)-3-(2-(5-(N-(4-chlorobenzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
0.001 - 0.0183
(Z)-3-(2-(5-(N-(4-fluorobenzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
0.005 - 0.0326
(Z)-3-(2-(5-(N-(4-methylbenzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
0.0074 - 0.0608
(Z)-4-(2-(5-(N-(2-chlorobenzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
0.0083 - 0.0431
(Z)-4-(2-(5-(N-(4-chloro-3-(trifluoromethyl)benzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
0.0059 - 0.0181
(Z)-4-(2-(5-(N-(4-chlorobenzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
0.0063 - 0.0114
(Z)-4-(2-(5-(N-(4-fluorobenzyl)sulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl)benzoic acid
0.0013 - 0.0071
(Z)-4-(2-(5-(N-benzylsulfamoyl)-2-oxoindolin-3-ylidene)hydrazinyl) benzoic acid
0.0028
1,1'-(piperazine-1,4-diyl)bis(4-(3-(dibenzylamino)phenyl)butane-1,2,4-trione)
Homo sapiens
-
in 50 mM MOPS, pH 6.5, at 30°C
0.2
1-(2,6-dihydroxy-4-methoxy-3-methylphenyl)ethanone
Homo sapiens
-
above
0.013
15-hydroxykaur-9(11),16-dien-19-oic acid
Homo sapiens
pH 6.0, 37°C
0.0081
19alpha,24-dihydroxyurs-12-en-3-on-28-oic acid
Homo sapiens
-
-
0.00074
2',4'-dihydroxy-1,1'-biphenyl
Homo sapiens
pH 7.0, 37°C, PTP-B1
0.00389
2,2'-[benzene-1,4-diylbis(methanediyloxybenzene-4,1-diyl)]bis(oxoacetic acid)
Homo sapiens
-
pH and temperature not specified in the publication
0.001
2,5-dihydroxy-3-[7-(2-methylbenzyl)-1H-indol-3-yl]cyclohexa-2,5-diene-1,4-dione
Homo sapiens
-
0.0056
2,5-dihydroxy-3-[7-(3-methylbut-2-en-1-yl)-1H-indol-3-yl]cyclohexa-2,5-diene-1,4-dione
Homo sapiens
-
0.005 - 0.0143
2-(4-hydroxyphenyl)-3-[(3,4-dihydroxy-1,1'-biphenyl-4-yl)methyl]-4H-1-benzopyran-4-one
0.0007 - 0.0057
2-(4-hydroxyphenyl)-3-[(4-carboxy-3-hydroxy-1,1'-biphenyl-4-yl)methyl]-4H-1-benzopyran-4-one
0.0084
2-[6-chloro-5-(1-naphthalyloxy)-1H-benzimidazol-2-yl]thio-N-(thiazol-2-yl)acetamide
Homo sapiens
pH 7.0, 37°C
0.0128
24-hydroxyursolic acid
Homo sapiens
-
-
0.00072
28-(10-decanoic)-oleanolic acid
Homo sapiens
-
0.00059
28-(12-dodecanoic)-oleanolic acid
Homo sapiens
-
0.0021
28-(2-acetic)-oleanolic acid
Homo sapiens
-
0.00133
28-(4-butyric)-oleanolic acid
Homo sapiens
-
0.00088
28-(6-hexanoic)-oleanolic acid
Homo sapiens
-
0.00078
28-(8-octanoic)-oleanolic acid
Homo sapiens
-
0.01544
28-(glycine)-oleanolic acid amide
Homo sapiens
-
0.01635
28-(L-glutamic acid)-oleanolic acid amide
Homo sapiens
-
0.00331
28-(L-phenylalanine)-oleanolic acid amide
Homo sapiens
-
0.00319
28-(p-carboxyphenyl)-oleanolic acid amide
Homo sapiens
-
0.00074
28-[4-butyric((R)-1-carboxy-phenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00059
28-[4-butyric((S)-1-carboxy-3-indole-ethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00462
28-[4-butyric((S)-1-carboxy-5-imidazole-ethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00055
28-[4-butyric((S)-1-carboxy-methylthioethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00057
28-[4-butyric((S)-1-carboxy-phenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00066
28-[4-butyric(1-carboxy-2,3-dimethoxyphenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00082
28-[4-butyric(1-carboxy-3,4-dimethoxyphenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00044
28-[4-butyric(1-carboxy-3,4-oxymethyleneoxyphenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00063
28-[4-butyric(1-carboxy-3,5-dimethoxyphenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00051
28-[4-butyric(1-carboxy-m-chlorophenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00052
28-[4-butyric(1-carboxy-m-methoxyphenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00056
28-[4-butyric(1-carboxy-o-chlorophenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00053
28-[4-butyric(1-carboxy-o-methoxyphenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00055
28-[4-butyric(1-carboxy-o-methylphenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00061
28-[4-butyric(1-carboxy-p-chlorophenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00057
28-[4-butyric(1-carboxy-p-fluorophenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.0006
28-[4-butyric(1-carboxy-p-methoxyphenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00065
28-[4-butyric(1-carboxy-p-methylphenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00045
28-[4-butyric(1-carboxy-p-nitrophenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00593
2beta,3beta-2,3-dihydroxyolean-12-en-28-oic acid
Homo sapiens
-
PTPB1
0.01623
3,16-dioxo-olean-12(13),17(18)-diene
Homo sapiens
-
in 50 mM citrate (pH 6.0), 1 mM dithiothreitol, 1 mM EDTA, and 0.1 M NaCl, at 37°C
0.00233
3-(2,2'-dimethyl-carboxypropanoyloxy)-oleanolic acid
Homo sapiens
-
0.00272
3-(2-carboxy-benzyloxy)-oleanolic acid
Homo sapiens
-
0.00458
3-(2-carboxybenzoyloxy)-oleanolic acid
Homo sapiens
-
0.008
3-(3,5-dibromo-4-hydroxybenzoyl)-2-ethyl-N-[4-(1,3-thiazol-2-ylsulfamoyl)phenyl]-1-benzofuran-6-sulfonamide
Homo sapiens
pH and temperature not specified in the publication
0.00062
3-(3-carboxy-benzyloxy)-oleanolic acid
Homo sapiens
-
0.00015
3-(4-carboxy-benzyloxy)-28-[4-butyric((s)-1-carboxyphenylethyl)-amide]-DELTA12-oleanene
Homo sapiens
-
0.00054
3-(4-carboxy-benzyloxy)-oleanolic acid
Homo sapiens
-
0.3
3-([2-chloro-6-methoxy-4-[(E)-(3-oxo[1,3]thiazolo[3,2-a]benzimidazol-2(3H)-ylidene)methyl]phenoxy]methyl)benzoic acid
Homo sapiens
above, pH 7.0, 25°C
0.00267
3-benzyloxy-oleanolic acid
Homo sapiens
-
0.00686
3-butyl-7-(2,4-dihydroxy-6-pentylphenoxy)-3,5-dimethoxy-2-benzofuran-1(3H)-one
Homo sapiens
-
-
0.00597
3-carboxypropanoyloxy-oleanolic acid
Homo sapiens
-
0.00261
3-dehydroxy-oleanolic acid
Homo sapiens
-
0.00289
3-ethyl oxalyl-oleanolic acid
Homo sapiens
-
0.0635
3-hydroxy-4-(methoxycarbonyl)-2,5-dimethylphenyl 3-acetyl-2,4-dihydroxy-6-methylbenzoate
Homo sapiens
-
-
0.017
3-hydroxy-4-(methoxycarbonyl)-5-methylphenyl 4-(beta-D-galactopyranosyloxy)-2-hydroxy-6-pentadecylbenzoate
Homo sapiens
-
-
0.00285
3-methylene-oleanolic acid
Homo sapiens
-
0.00286
3-oxalyl-oleanolic acid
Homo sapiens
-
0.00532
3-oxo-oleanolic acid
Homo sapiens
-
0.00248
3-[(1-butyl-1,6-dimethoxy-3-oxo-1,3-dihydro-2-benzofuran-4-yl)oxy]-4,6-dihydroxy-2-pentylbenzoic acid
Homo sapiens
-
-
0.0119 - 0.1566
3-[(2-nitrophenyl)hydrazono]-2-oxo-2,3-dihydro-1H-indole-5-sulfonamide
0.0044 - 0.0409
3-[(2-nitrophenyl)hydrazono]-2-oxo-2,3-dihydro-1H-indole-5-sulfonic acid 4-chlorobenzylamide
0.3
3-[(E)-(3-oxo[1,3]thiazolo[3,2-a]benzimidazol-2(3H)-ylidene)methyl]benzoic acid
Homo sapiens
above, pH 7.0, 25°C
0.0083
3-[2,5-dimethyl-3-[(3-oxo-2,3-dihydro[1,3]thiazolo[3,2-a]benzimidazol-2-yl)methyl]-1H-pyrrol-1-yl]benzoic acid
Homo sapiens
pH 7.0, 25°C
0.0329
3-[3-(2,4-dichlorophenyl)propanoyl]-2-hydroxycyclohepta-2,4,6-trien-1-one
Homo sapiens
pH 7.0, 25°C
0.0045 - 0.0371
3-[N'-(5-isopropylsulfamoyl-2-oxo-1,2-dihydroindol-3-ylidene)-hydrazino]benzoic acid
0.0077
3alpha-cinnamoyloxypterokaurene L3
Homo sapiens
pH 6.0, 37°C
0.00505
3alpha-oleanolic acid
Homo sapiens
-
0.00394
3beta,16a,17-trihydroxy-olean-12-ene
Homo sapiens
-
in 50 mM citrate (pH 6.0), 1 mM dithiothreitol, 1 mM EDTA, and 0.1 M NaCl, at 37°C
0.05
3beta-acetoxy-17beta-hydroxy-28-norolean-12-ene
Homo sapiens
-
IC50 above 0.05 mM, in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA, and 1 mM dithiothreitol, at 37°C
0.044
3beta-acetoxy-28-hydroxyolean-12-ene
Homo sapiens
-
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA, and 1 mM dithiothreitol, at 37°C
0.0078
3beta-acetoxyolean-12-en-28-acid
Homo sapiens
-
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA, and 1 mM dithiothreitol, at 37°C
0.0093
3beta-acetoxyolean-12-en-28-aldehyde
Homo sapiens
-
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA, and 1 mM dithiothreitol, at 37°C
0.0052
3beta-hydroxyolean-12-en-28-oic acid
Homo sapiens
-
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA, and 1 mM dithiothreitol, at 37°C
0.00119
4'-[(2-butyl-1-benzofuran-3-yl)methyl]biphenyl-4-ol
Homo sapiens
pH 7.0, 37°C, PTP-B3
0.00108
4'-[2-(4-hydroxybutyl)-1-benzofuran-3-yl]biphenyl-4-ol
Homo sapiens
pH 7.0, 37°C, PTP-B2
0.00573
4,4'-[benzene-1,4-diylbis(methanediyloxy)]dibenzoic acid
Homo sapiens
-
0.01
4-(((5Z)-2-(4-fluorophenylimino)-4-oxo-5-[(3-phenoxyphenyl)methylidene]thiazolidin-3-yl)methyl)benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0042
4-(((5Z)-2-(4-fluorophenylimino)-4-oxo-5-[(3-phenylmethoxyphenyl)methylidene]thiazolidin-3-yl)methyl)benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0051
4-(((5Z)-2-(4-fluorophenylimino)-4-oxo-5-[(4-phenoxyphenyl)methylidene]thiazolidin-3-yl) methyl)benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0019
4-(((5Z)-2-(4-fluorophenylimino)-4-oxo-5-[(4-phenylmethoxyphenyl)methylidene]thiazolidin-3-yl)methyl)benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0071
4-(((5Z)-4-oxo-5-[(3-phenoxyphenyl)methylidene]-2-thioxothiazolidin-3-yl)methyl)benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0057
4-(((5Z)-4-oxo-5-[(3-phenylmethoxyphenyl)methylidene]-2-thioxothiazolidin-3-yl)methyl)benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0106
4-(((5Z)-4-oxo-5-[(4-phenoxyphenyl)methylidene]-2-thioxothiazolidin-3-yl)methyl)benzoic acid
Homo sapiens
pH 7.0, 37°C
0.005
4-(((5Z)-4-oxo-5-[(4-phenylmethoxyphenyl)methylidene]-2-thioxothiazolidin-3-yl)methyl)benzoic acid
Homo sapiens
pH 7.0, 37°C
0.02
4-(3-(dibenzylamino)phenyl)-2,4-dioxobutanoic acid
Homo sapiens
-
in 50 mM MOPS, pH 6.5, at 30°C
0.2732
4-(5-bromo-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-2-hydroxybenzoic acid
Homo sapiens
pH 7.0, 25°C
0.00059
4-(beta-D-galactopyranosyloxy)-2-hydroxy-6-pentadecylbenzoic acid
Homo sapiens
-
-
0.0109
4-([(2E,5Z)-2-[(4-methoxyphenyl)imino]-4-oxo-5-[(3-phenoxyphenyl)methylidene]-1,3-thiazolidin-3-yl]methyl)benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0025
4-([(2E,5Z)-2-[(4-methoxyphenyl)imino]-4-oxo-5-[(4-phenoxyphenyl)methylidene]-1,3-thiazolidin-3-yl]methyl)benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0104
4-([(2E,5Z)-2-[(4-tert-butylphenyl)imino]-4-oxo-5-[(3-phenoxyphenyl)methylidene]-1,3-thiazolidin-3-yl]methyl)benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0022
4-([(2E,5Z)-2-[(4-tert-butylphenyl)imino]-4-oxo-5-[(4-phenoxyphenyl)methylidene]-1,3-thiazolidin-3-yl]methyl)benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0051
4-([(2E,5Z)-5-[[3-(benzyloxy)phenyl]methylidene]-2-[(4-methoxyphenyl)imino]-4-oxo-1,3-thiazolidin-3-yl]methyl)benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0056
4-([(2E,5Z)-5-[[3-(benzyloxy)phenyl]methylidene]-2-[(4-tert-butylphenyl)imino]-4-oxo-1,3-thiazolidin-3-yl]methyl)benzoic acid
Homo sapiens
pH 7.0, 37°C
0.003
4-([(2E,5Z)-5-[[4-(benzyloxy)phenyl]methylidene]-2-[(4-methoxyphenyl)imino]-4-oxo-1,3-thiazolidin-3-yl]methyl)benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0014
4-([(2E,5Z)-5-[[4-(benzyloxy)phenyl]methylidene]-2-[(4-tert-butylphenyl)imino]-4-oxo-1,3-thiazolidin-3-yl]methyl)benzoic acid
Homo sapiens
pH 7.0, 37°C
0.018
4-([(5Z)-2,4-dioxo-5-[(3-phenoxyphenyl)methylidene]-1,3-thiazolidin-3-yl]methyl)benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0028
4-([(5Z)-2,4-dioxo-5-[(4-phenoxyphenyl)methylidene]-1,3-thiazolidin-3-yl]methyl)benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0145
4-([(5Z)-2-(4-fluorophenylimino)-4-oxo-5-([3-(2-phenylethoxy)phenyl]methylidene)thiazolidin-3-yl]methyl)benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0015
4-([(5Z)-2-(4-fluorophenylimino)-4-oxo-5-([4-(2-phenylethoxy)phenyl]methylidene)thiazolidin-3-yl]methyl)benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0019
4-([(5Z)-4-oxo-5-[[3-(2-phenylethoxy)phenyl]methylidene)-2-thioxothiazolidin-3-yl]methyl]benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0035
4-([(5Z)-4-oxo-5-[[4-(2-phenylethoxy)phenyl]methylidene)-2-thioxothiazolidin-3-yl]methyl]benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0796
4-methoxy-3-(5-methoxy-1-benzofuran-6-yl)-5-(4-methoxyphenyl)isoxazole
Homo sapiens
-
0.0804
4-methoxy-3-(5-methoxy-1-benzofuran-6-yl)-5-phenylisoxazole
Homo sapiens
-
0.005
4-oxo-8-(phenylsulfanyl)-1,4-dihydro-1,7-naphthyridine-3-carboxylic acid
Homo sapiens
-
0.0173
4-[(1E)-3-(4-hydroxyphenyl)-3-oxoprop-1-en-1-yl]-5-methoxy-2-(2-methylbut-3-en-2-yl)phenyl acetate
Homo sapiens
-
pH 6.0, 37°C
0.00022
4-[(2,4-dihydroxy-6-pentadecylbenzoyl)oxy]-2-hydroxy-6-methylbenzoic acid
Homo sapiens
-
-
0.0292
4-[(2E)-3-[2,4-dimethoxy-5-(2-methylbut-3-en-2-yl)phenyl]prop-2-enoyl]phenyl acetate
Homo sapiens
-
pH 6.0, 37°C
0.05
4-[(2E)-3-[4-(acetyloxy)-2-methoxy-5-(2-methylbut-3-en-2-yl)phenyl]prop-2-enoyl]phenyl acetate
Homo sapiens
-
above, pH 6.0, 37°C
0.0192
4-[(2E)-3-[4-hydroxy-2-methoxy-5-(2-methylbut-3-en-2-yl)phenyl]prop-2-enoyl]phenyl acetate
Homo sapiens
-
pH 6.0, 37°C
0.3
4-[2-[(5-chloro-1,3-benzoxazol-2-yl)sulfanyl]acetamido]benzoic acid
Homo sapiens
above, pH 7.0, 25°C
0.0045 - 0.0277
4-[N'-(5-isopropylsulfamoyl-2-oxo-1,2-dihydroindol-3-ylidene)-hydrazino]benzoic acid
0.0019
4-[[(2E,5Z)-4-oxo-5-[(3-phenoxyphenyl)methylidene]-2-(phenylimino)-1,3-thiazolidin-3-yl]methyl]benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0011
4-[[(2E,5Z)-4-oxo-5-[(4-phenoxyphenyl)methylidene]-2-(phenylimino)-1,3-thiazolidin-3-yl]methyl]benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0046
4-[[(2E,5Z)-4-oxo-5-[[3-(2-phenylethoxy)phenyl]methylidene]-2-(phenylimino)-1,3-thiazolidin-3-yl]methyl]benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0015
4-[[(2E,5Z)-4-oxo-5-[[4-(2-phenylethoxy)phenyl]methylidene]-2-(phenylimino)-1,3-thiazolidin-3-yl]methyl]benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0038
4-[[(2E,5Z)-5-[[3-(benzyloxy)phenyl]methylidene]-4-oxo-2-(phenylimino)-1,3-thiazolidin-3-yl]methyl]benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0011
4-[[(2E,5Z)-5-[[4-(benzyloxy)phenyl]methylidene]-4-oxo-2-(phenylimino)-1,3-thiazolidin-3-yl]methyl]benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0095
4-[[(5Z)-2,4-dioxo-5-[[3-(2-phenylethoxy)phenyl]methylidene]-1,3-thiazolidin-3-yl]methyl]benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0026
4-[[(5Z)-2,4-dioxo-5-[[4-(2-phenylethoxy)phenyl]methylidene]-1,3-thiazolidin-3-yl]methyl]benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0011
4-[[(5Z)-5-[[3-(benzyloxy)phenyl]methylidene]-2,4-dioxo-1,3-thiazolidin-3-yl]methyl]benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0016
4-[[(5Z)-5-[[4-(benzyloxy)phenyl]methylidene]-2,4-dioxo-1,3-thiazolidin-3-yl]methyl]benzoic acid
Homo sapiens
pH 7.0, 37°C
0.0075
5-chloro-N-[6-chloro-5-(2,3-dichlorophenoxy)-1H-benzimidazol-2-yl]-1-methyl-2-(methylthio)-1H-benz-imidazole-6-carboxamide
Homo sapiens
pH 7.0, 37°C
0.0194
5-methoxy-4-[(1E)-3-(4-methoxyphenyl)-3-oxoprop-1-en-1-yl]-2-(2-methylbut-3-en-2-yl)phenyl acetate
Homo sapiens
-
pH 6.0, 37°C
0.0011 - 0.003
6,7-dihydroxy-2-(4-hydroxyphenyl)-3-[(1,1-biphenyl-4-yl)methyl]-4H-1-benzopyran-4-one
0.0003
6-chloro-7-(2,3-dihydro-1H-inden-1-ylamino)quinoline-5,8-dione
Homo sapiens
-
0.00021
6-chloro-7-[(2-morpholin-4-ylethyl)amino]quinoline-5,8-dione
Homo sapiens
-
0.0086 - 0.0172
6-hydroxy-2-(4-hydroxybenzyl)-3-[(1,1-biphenyl-4-yl)methyl]-4H-1-benzopyran-4-one
0.0046
6-hydroxy-3-[1-[4-(naphthalen-1-ylamino)-4-oxobutyl]-1H-1,2,3-triazol-4-yl]-2-phenyl-1-benzofuran-5-carboxylic acid
Homo sapiens
-
-
0.3
6-oxo-6H-cyclohepta[b]furan-5,7-dicarboxylic acid
Homo sapiens
above, pH 7.0, 25°C
0.003
7-(2-((1H-imidazol-2-yl)thio)ethoxy)-2-phenyl-4H-chromen-4-one
Homo sapiens
pH 7.2, 37°C
0.0016
7-(2-(1H-1,2,4-triazol-1-yl)ethoxy)-2-phenyl-4H-chromen-4-one
Homo sapiens
pH 7.2, 37°C
0.004
7-(2-(2-methyl-5-nitro-1H-imidazol-1-yl)ethoxy)-2-phenyl-4H-chromen-4-one
Homo sapiens
pH 7.2, 37°C
0.005
7-(2-(4-nitro-1H-imidazol-1-yl)ethoxy)-2-phenyl-4H-chromen-4-one
Homo sapiens
pH 7.2, 37°C
0.0079
7-(2-(5-methyl-1H-tetrazol-1-yl)ethoxy)-2-phenyl-4H-chromen-4-one
Homo sapiens
pH 7.2, 37°C
0.007
7-(3-(4-nitro-1H-imidazol-1-yl)propoxy)-2-phenyl-4H-chromen-4-one
Homo sapiens
pH 7.2, 37°C
0.0039
7-(4-((1H-imidazol-2-yl)thio)butoxy)-2-phenyl-4H-chromen-4-one
Homo sapiens
pH 7.2, 37°C
0.0036
7-(4-(1H-1,2,4-triazol-1-yl)butoxy)-2-phenyl-4H-chromen-4-one
Homo sapiens
pH 7.2, 37°C
0.0069
7-(4-(2-methyl-5-nitro-1H-imidazol-1-yl)butoxy)-2-phenyl-4H-chromen-4-one
Homo sapiens
pH 7.2, 37°C
0.0151
7-(4-(5-methyl-1H-tetrazol-1-yl)butoxy)-2-phenyl-4H-chromen-4-one
Homo sapiens
pH 7.2, 37°C
0.00082
7-chloro-6-[(2-morpholin-4-ylethyl)amino]quinoline-5,8-dione
Homo sapiens
-
0.0074 - 0.0124
7-hydroxy-2-(4'-hydroxyphenyl)-3-[(3'',4''-dihydroxy-1,1'-biphenyl-4-yl)methyl]-4H-1-benzopyran-4-one
0.0062 - 0.0268
7-hydroxy-2-(4'-hydroxyphenyl)-3-[(3''-carboxy-1,1'-biphenyl-4-yl)methyl]-4H-1-benzopyran-4-one
0.001 - 0.0022
7-hydroxy-2-(4'-hydroxyphenyl)-3-[(4''-carboxy-3''-hydroxy-1,1'-biphenyl-4-yl)methyl]-4H-1-benzopyran-4-one
0.0082 - 0.0184
7-hydroxy-2-(4'-hydroxyphenyl)-3-[(4''-hydroxy-1,1'-biphenyl-4-yl)methyl]-4H-1-benzopyran-4-one
0.05
7-hydroxy-2-(4-hydroxyphenyl)-2,3-dihydro-4H-chromen-4-one
Homo sapiens
-
above, pH 6.0, 37°C
0.0065 - 0.0173
7-hydroxy-2-(4-hydroxyphenylethyl)-3-[(1,1-biphenyl-4-yl)methyl]-4H-1-benzopyran-4-one
0.0053 - 0.0175
7-hydroxy-2-(4-hydroxyphenylmethyl)-3-[(1,1'-biphenyl-4-yl)methyl]-4H-1-benzopyran-4-one
0.00087
8-hydroxy-3-methoxy-11-oxo-1-pentanoyl-6-pentyl-11H-dibenzo[b,e][1,4]dioxepine-7-carboxylic acid
Homo sapiens
-
-
0.00019
aquastatin A
Homo sapiens
-
-
0.0081
benzyl oleanolic acid amide
Homo sapiens
-
0.00861
benzyl oleanolic acid ester
Homo sapiens
-
0.0013
CinnGel 2ME
Homo sapiens
-
-
0.012
ent-3beta-angeloyloxykaur-16-en-19-oic acid
Homo sapiens
pH 6.0, 37°C
0.012
ent-3beta-tigloyloxykaur-16-en-19-oic acid
Homo sapiens
pH 6.0, 37°C
0.01916
ethyl (4R)-4-[(1R,3aS,3bS,10aR,10bS,12aR)-6,6,10a,12a-tetramethyl-1,2,3,3a,3b,4,6,6a,7,9a,10,10a,10b,11,12,12a-hexadecahydrocyclopenta[5,6]naphtho[1,2-f]indazol-1-yl]pentanoate
Homo sapiens
-
pH and temperature not specified in the publication
0.04
ethyl (4R)-4-[(1R,3aS,3bS,11aR,11bS,13aR)-8-amino-6,6,11a,13a-tetramethyl-2,3,3a,3b,4,6,11,11a,11b,12,13,13a-dodecahydro-1H-cyclopenta[5,6]naphtho[1,2-g]quinazolin-1-yl]pentanoate
Homo sapiens
-
IC50 above 0.04 mM, pH and temperature not specified in the publication
0.0138
glycyrrhetic acid
Homo sapiens
-
in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA, and 1 mM dithiothreitol, at 37°C
0.01274 - 0.02045
lithocholic acid
0.0137
lupenone
Homo sapiens
-
pH 6.0, 37°C
0.0056
lupeol
Homo sapiens
-
pH 6.0, 37°C
0.01947
maslinic acid
Homo sapiens
-
TCPTP
0.00904
methyl (4R)-4-[(1R,3aS,3bS,10aR,10bS,12aR)-8-amino-6,6,10a,12a-tetramethyl-2,3,3a,3b,4,6,10,10a,10b,11,12,12a-dodecahydro-1H-cyclopenta[7,8]phenanthro[2,3-d][1,3]thiazol-1-yl]pentanoate
Homo sapiens
-
pH and temperature not specified in the publication
0.02822
methyl (4R)-4-[(1R,3aS,3bS,11aR,11bS,13aR)-6,6,11a,13a-tetramethyl-2,3,3a,3b,4,6,11,11a,11b,12,13,13a-dodecahydro-1H-cyclopenta[5,6]naphtho[1,2-g]quinoxalin-1-yl]pentanoate
Homo sapiens
-
pH and temperature not specified in the publication
0.2
methyl 2,4-dihydroxy-6-methylbenzoate
Homo sapiens
-
above
0.00742
methyl 3,8-dimethoxy-11-oxo-1-pentanoyl-6-pentyl-11H-dibenzo[b,e][1,4]dioxepine-7-carboxylate
Homo sapiens
-
-
0.2
methyl 3-formyl-2,4-dihydroxy-6-methylbenzoate
Homo sapiens
-
above
0.01321
methyl 4,4-dimethyl-3-oxochol-5-en-24-oate
Homo sapiens
-
pH and temperature not specified in the publication
0.00037
methyl 5-amino-6-(7-amino-6-methoxy-5,8-dioxo-5,8-dihydroquinolin-2-yl)-4-(2-hydroxy-3,4-dimethoxyphenyl)-3-methylpyridine-2-carboxylate
Homo sapiens
-
0.00302
methyl 8-hydroxy-3-methoxy-11-oxo-1-pentanoyl-6-pentyl-11H-dibenzo[b,e][1,4]dioxepine-7-carboxylate
Homo sapiens
-
-
0.0092
methyl oleanolic acid amide
Homo sapiens
-
0.00444
methyl oleanolic acid ester
Homo sapiens
-
0.0018
N,N'-[benzene-1,4-diylbis(propane-2,2-diylbenzene-4,1-diyl)]bis(1,1,1-trifluoromethanesulfonamide)
Homo sapiens
-
-
0.00089
N-(1,4-dioxo-1,4-dihydronaphthalen-2-yl)-N-(4-methylphenyl)acetamide
Homo sapiens
-
0.00062
N-(3-[(4-chlorophenyl)sulfanyl]-1,4-dioxo-1,4-dihydronaphthalen-2-yl)acetamide
Homo sapiens
-
0.01
N-([4-[difluoro(phosphono)methyl]phenyl]acetyl)-a-aspartyl-4-[difluoro(phosphono)methyl]phenylalaninamide
Homo sapiens
-
-
0.0039
N-[5-(dimethylamino)-2-hydroxy-3-methoxybenzyl]-N-methyl-2-(4-nitrophenyl)ethanaminium
Homo sapiens
-
0.0313
N-[6-chloro-5-(2,3-dichlorophenoxy)-1H-benzimidazol-2-yl]-2,2,2-trifluoroacetamide
Homo sapiens
pH 7.0, 37°C
0.0025
NAT6-297775
Homo sapiens
-
Shp2, in 25 mM MOPS (pH 7.0), 50 mM NaCl, 0.05% (v/v) Tween 20, 1 mM dithiothreitol, at 25°C
0.0003
NSC-87877
Homo sapiens
-
Shp2, in 25 mM MOPS (pH 7.0), 50 mM NaCl, 0.05% (v/v) Tween 20, 1 mM dithiothreitol, at 25°C
0.0037 - 0.0076
oleanolic acid
0.00476
oleanolic acid amide
Homo sapiens
-
0.02
oleanolic alcohol
Homo sapiens
IC50 above 0.02 mM
0.0035
oleanonic acid
Homo sapiens
-
-
0.0039
pomolic acid
Homo sapiens
-
-
0.0011
rilobolide-6-O-methacrylate
Homo sapiens
pH 6.0, 37°C
0.0041 - 0.0045
RK-682
0.0109
rotungenic acid
Homo sapiens
-
-
0.002
small t antigen
Homo sapiens
-
using p-nitrophenyl phosphate as a substrate
-
0.0562
Sodium vanadate
Homo sapiens
-
0.0188
spathodic acid
Homo sapiens
-
-
0.05
stigmasterol
Homo sapiens
-
IC50 above 0.05 mM, in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA, and 1 mM dithiothreitol, at 37°C
0.05
taraxerol
Homo sapiens
-
IC50 above 0.05 mM, in 50 mM citrate (pH 6.0), 0.1 M NaCl, 1 mM EDTA, and 1 mM dithiothreitol, at 37°C
0.022
tetrachyrin
Homo sapiens
pH 6.0, 37°C
0.0025 - 0.004
ursolic acid
0.0156
uvaol
Homo sapiens
-
-
0.0158
[2-bromo-4-[(E)-(7,8-dimethyl-3-oxo[1,3]thiazolo[3,2-a]benzimidazol-2(3H)-ylidene)methyl]-6-ethoxyphenoxy]acetic acid
Homo sapiens
pH 7.0, 25°C
0.3
[[1-(4-chlorophenyl)-2-methyl-1H-indol-5-yl]oxy]acetic acid
Homo sapiens
above, pH 7.0, 25°C
0.00219
[[4'-(2-butyl-1-benzofuran-3-yl)biphenyl-4-yl]oxy]acetic acid
Homo sapiens
pH 7.0, 37°C, PTP-B4
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
106
-
substrate 4-nitrophenyl phosphate
15700
purified recombinant catalytic domain, pH 7.0, 37°C, substrate 4-nitrophenyl phosphate
19.7
-
cytoplasmic enzyme
32300
-
pH 5.0
42.7
-
membrane-bound enzyme
6.6
-
substrate bovine serum albumin, calculated as micromol phosphate released per min
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 5.5
-
substrate 4-nitrophenyl phosphate, subtype 1A
5 - 5.6
-
substrates 4-nitrophenyl phosphate and ENDpYINASL, enzymes PTP2C and DELTASH2-PTP2C
5 - 7
-
-
5.5 - 6
-
substrate 4-nitrophenyl phosphate, subtype 1B
5.6
-
substrate 4-nitrophenyl phosphate
6 - 7
-
-
6.4
assay at
6.5 - 7.5
-
substrates lysozyme and myelin basic protein, enzymes PTP2C and DELTASH2-PTP2C
7 - 7.3
-
-
7.4
-
assay at
7.5
-
substrate myelin basic protein
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 8
-
-
4 - 4.5
-
islet cell antigen-related PTP
4 - 9
activity range of the recombinant catalytic enzyme domain, profile overview
5 - 6.7
-
less than half-maximal activity above and below
5 - 9
-
pH 5: 13% of maximal activity, pH 9: 50% of maximum activity
6 - 8.5
-
-
7
-
30-40% of the activity at optimal pH-value
additional information
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22 - 25
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26 - 42
over 50% of maximal activity within this range, recombinant catalytic enzyme domain, profile overview
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
human glioblastoma cell line
Manually annotated by BRENDA team
-
breast carcinoma, high expression
Manually annotated by BRENDA team
-
increased expression in umbilical vascular endothelial cells and microvascular endothelial cells upon exposure to phorbol 12-myristate 13-acetate
Manually annotated by BRENDA team
-
HCL cells display increased expression of the phosphatases SPH-1 and SPH-2 as compared with normal B-lymphocytes, HCL cells require protein-tyrosine phosphatase activity for preservation of their viability
Manually annotated by BRENDA team
-
LMW-PTP is the predominant tyrosine phosphatase expressed in lens
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
a melphalan-sensitive myeloma cell line, from the peripheral blood cells of a patient with IgA myeloma, secretes lambda L chain, is negative for the presence of the EBV genome, and expresses leukocyte antigen DR, plasma cell Ag-1, and T9 and T10 antigens
Manually annotated by BRENDA team
-
receptor-type protein tyrosine phosphatase CD148
Manually annotated by BRENDA team
-
a head and neck squamous cell carcinoma cell line
Manually annotated by BRENDA team
-
neuroblastoma cell, high expression of enzyme
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
receptor protein tyrosine phosphatases (PTPRs) are a family of cell surface receptor proteins
Manually annotated by BRENDA team
-
50% membrane-bound, 30% bound to the cytoskeleton, 20% cytosolic
Manually annotated by BRENDA team
-
isolation from cell lysate
-
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
protein tyrosine phosphatases (PTPs) play critical roles in cell signaling pathways. Together with the protein kinases, they control the balance of phosphorylated species, enabling specific and varied signaling responses
evolution
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PTN3_HUMAN
913
0
103990
Swiss-Prot
Mitochondrion (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
116000
-
x * 116000, enzyme from A172 cells, SDS-PAGE
16900
-
x * 16900, SDS-PAGE
185000
-
x * 185000, receptor tyrosine phosphatase, SDS-PAGE
37000
-
non-specific proteolytic cleavage of PTP1B yields a band migrating at approximately 37000 Da, SDS-PAGE
38000
-
1 * 38000, SDS-PAGE
38500
-
1 * 38500, deduced from gene sequence
40000
-
gel filtration
45000
-
1 * 45000, SHPTP1 catalytic domain, SDS-PAGE
46000
-
truncated form of PTP1B that is missing the COOH-terminal hydrophobic domain, SDS-PAGE
48000
-
truncated form of PTP1B that is missing the COOH-terminal hydrophobic domain, SDS-PAGE
50000
53000
-
SHPTP1, catalytic domain, gel filtration
55209 - 55943
recombinant monomeric thioredoxin-fused enzyme, mass spectrometry
63000
-
1 * 63000, SHPTP1, full length enzyme, SDS-PAGE
64816
recombinant monomeric thioredoxin-fused enzyme, gel filtration
68000
72000
-
SHPTP1, full length enzyme, gel filtration
76770
-
splicing variant SV3 of LMW-PTP, calculation from nucleotide sequence
77000
-
x * 77000, splicing variant SV3 of LMW-PTP, SDS-PAGE
80000
-
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
N-linked glycosylation
no modification
-
-
phosphoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme mutants D811A/C842S, D811E/C842S, D811A/H812F/C842S/M883G, Y676I, and D811E in complex with substrate Eps15846-854, and with mutant Eps15846-854 P450V, X-ray diffraction structure determination and analysis at 1.26-1.72 A resolution
active site mutant C215S in complex with substrates bis-(para-phosphophenyl) methane and 4-nitrophenyl phosphate
both wild-type PTP-1B and its mutant L119V
-
C-terminal truncated form, ligand-free, in auto-inhibited conformation
-
catalytic domain and C455S mutant of catalytic domain, in complex with peptide substrates
catalytically active, monomeric D1 domain
-
cytoplasmic D1D2 segment of CD45, in native and phosphotyrosyl peptide-bound form
-
enzyme in oxovanadium-complexes, termed [VIVO(SAA)(2,2'-bipyridine)]0.25bpy and [VIVO(SAA)(1,10-phenanthroline)]0.33H2O, overview
-
hanging drop vapour diffusion method with 0.05 M Bis-Tris (pH 7.0), 24% (v/v) PEG3350, 0.1 M lithium sulfate, 0.2 M magnesium sulfate and 10 mM dithiothreitol
hanging drop vapour diffusion method with 0.1 M HEPES-NaOH pH 7.5, 10% 2-propanol, 10 mM magnesium acetate and 20% (w/v) PEG 4000 at 18°C
-
hanging drop vapour diffusion method with 0.2 M MgCl2, 4.5% PEG 10000 (w/v) and 0.1 M HEPES (pH 7.5)
-
hanging drop vapour diffusion method with 1.5 M sodium chloride, 10% (v/v) ethanol, and 10 mM dithiothreitol
-
hanging drop vapour diffusion method with 18-22% PEG 8000, 200 mM MgCl2, 100 mM Tris-HCl pH 8.0, and 1% (v/v) beta-mercaptoethanol
in complex with inhibitors 3-(3,5-dibromo-4-hydroxybenzoyl)-2-ethyl-N,N-dimethyl-1-benzofuran-6-sulfonamide, 3-((3,5-dibromo-4-hydroxyphenyl)carbonyl)-2-ethyl-N-(4-(1,3-thiazol-2-ylsulfamoyl)phenyl)-1-benzofuran-6-sulfonamide and 3-((3,5-dibromo-4-hydroxyphenyl)carbonyl)-2-ethyl-N-(4-sulfamoylphenyl)-1-benzofuran-6-sulfonamide
in complex with monophosphorylated and dually phosphorylated Erk2 peptides, sitting drop vapour diffusion method, in 0.2 M ammonium tartrate, pH 6.6, and 20% (w/v) PEG 3350 or and 1.0 M lithium chloride, 0.1 M citrate, pH 5.0, and 20% (w/v) PEG 6000
molecular dynamics simulations of the crystal structure of the enzyme catalytic domain and of mutant R47V/D48N/M258C/G259Q, both in complex with substrate 4-nitrophenyl phosphate and as cysteine-phosphor complex
phosphotyrosine phosphatase 1B
-
PTP1B and PTP1B mutant F182H in complex with inhibitors
purified recombinant detagged enzyme, hanging drop vapor diffusion method, mixing of 0.0018 ml of protein solution, containing 18 mg/ml protein in 20 mM HEPES-NaOH, pH 7.0, 0.2 M NaCl, 5 mM MgCl2, 20 mM DTT, and 5% glycerol, with an equal volume of reservoir solution containing 0.1 M bis-Tris, pH 6.0, and 2.4 M NaCl, 18°C, 3 days, X-ray diffraction structure determination and analysis at 2.4 A resolution
purified recombinant wild-type and mutant isolated membrane-proximal D1 and distal D2 domains of protein tyrosine phosphatase epsilon, and PTPepsilon (A455N/V457Y/E597D) D2 domain mutant, hanging drop vapour diffusion method, for PTPepsilon D1 domain mixing of 0.002 ml of 13.9 mg/ml protein solution with 0.002 ml of reservoir solution containing 0.1 M Tris-HCl, pH 8.5, 0.2 M sodium chloride, and 22% w/v PEG 3350, for wild-type PTPepsilon D2 domain mixing of 0.001 ml of 5.0 mg/ml protein solution with 0.003 ml of reservoir solution containing 0.1 M bicine/trizma base, pH 8.5, 0.03 mM diethylene glycol, 0.03 M triethylene glycol, 0.03 M tetraethylene glycol, 0.03 M pentaethylene glycol, 10% w/v PEG 4000, and 20% v/v glycerol, and for mutant A455N/V457Y/E597D PTPepsilon D2 domain mixing of 0.002 ml of 9.0 mg/ml protein solution with 0.002 ml of reservoir solution containing 0.1 M imidazole, pH 8.0, 0.2 M calcium acetate hydrate, 20% w/v PEG 1000, in all cases equilibration against 0.5 ml reservoir solution, X-ray diffraction structure determination and analysis at 1.67-2.27 A resolution
recombinant N-terminally His-tagged inactive enzyme mutant C227S, im complex with the consensus peptide substrate or SKAP-HOM, a bona fide Lyp substrate, 3-5 days, X-ray diffraction structure determmination and analysis at 2.5 A and 2.9 A resolution, respectively, molecular replacement
-
SHP-1, in the open, active conformation, hanging-drop vapor diffusion, 4°C, mixing of 0.0025 ml of protein solution, containing 3.6 mg/ml protein in 25 mM Tris-HCl, pH 7.5, 0-1 M NaCl,2 mM 2-mercaptoethanol, 1 mM EDTA, with 0.0025 ml of reservoir solution, containing 1.8 M ammonium sulfate, 0.1 M glycine, 0.1 M Tris-HCl, pH 7.0, and additon of 0.5 ml 14 mM deoxy Big Chap detergent, X-ray diffraction crystal structure determination and analysis at 3.1 A resolution, molecular replacement
-
sitting drop vapour diffusion method using 25% PEG-3350, 0.2 M LiSO4, and 100 mM Bis-Tris, pH 5.5, or 0.15 M malic acid, pH 7.0, 20% PEG-3350 and 2.0 M (NH4)H2PO4, 0.1 M Tris/HCl, pH 8.5
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two transition-state analogues, by sitting drop vapor diffusion method, 4°C, mixing of 0.002 ml of protein solution, containing native PTPB1, peptide DADEYL, and Na3VO4 in 10 mM Tris, pH 7.5, 25 mM NaCl, 0.2 mM EDTA, and 3 mM DTT, with 0.0005 ml of sucrose 30% v/v solution, and 0.003 ml of precipitant solution, containing 0.1 M HEPES, pH 7.5, 0.2 M magnesium acetate and 15-17% PEG 8000, 3 days, X-ray diffraction structure determination and analysis at 2.25-2.3 A resolution
wild type and C215D mutant, both are structurally identical
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D811A/C842S
site-directed mutagenesis, analysis of binding structure of substrate Eps15846-854 compared to wild-type enzyme and enzyme PTP1B
D811A/H812F/C842S/M883G
site-directed mutagenesis, analysis of binding structure of substrate Eps15846-854 compared to wild-type enzyme and enzyme PTP1B. THe mutant acts as a surrogate of the PTP1B active site, in complex with substrate Eps15846-854. Introduction of M883G substitution increased the flexibility of the side chain of Q886, thus facilitating interaction between F812 and the pTyr-Pro motif. In this complex structure, the phenyl side chain of F812 is shifted 3.7 A away from the active site pocket
D811E
D811E/C842S
site-directed mutagenesis, analysis of binding structure of substrate Eps15846-854 compared to wild-type enzyme and enzyme PTP1B
H812F
Y676I
site-directed mutagenesis, analysis of binding structure of substrate Eps15846-854 compared to wild-type enzyme and enzyme PTP1B, mutant Y676I mutant loses the catalytic activity completely
416AA
-
of PTPalpha, Km-value similar to wild-type, up to 2fold activation by tetrasodium 2-(((2-(3-(((3-(5-((2,5-disulfonatophenyl)carbamoyl)-1H-benzimidazol-2-yl)phenyl)carbamoyl)amino)phenyl)-1H-benzimidazol-5-yl)carbonyl)amino)benzene-1,4-disulfonate
529AA
-
of PTPalpha, Km-value similar to wild-type, up to 11.6fold activation by tetrasodium 2-(((2-(3-(((3-(5-((2,5-disulfonatophenyl)carbamoyl)-1H-benzimidazol-2-yl)phenyl)carbamoyl)amino)phenyl)-1H-benzimidazol-5-yl)carbonyl)amino)benzene-1,4-disulfonate
A122F
site-directed mutagenesis, affects inhibition by abietic acid and 2-[(carboxycarbonyl)amino]-4,5,6,7-tetrahydro-thieno[2,3-c]-pyridine-3-carboxylic acid
A122S
site-directed mutagenesis, affects inhibition by abietic acid
A189S
site-directed mutagenesis, affects inhibition by 3-(3,5-dibromo-4-hydroxybenzoyl)-2-ethylbenzofuran-6-sulfonic acid-[4-(thiazol-2-ylsulfamyl)phenyl]-amide and 2-[(carboxycarbonyl)amino]-4,5,6,7-tetrahydro-thieno[2,3-c]-pyridine-3-carboxylic acid
A455N/V457Y/E597D
site-directed mutagenesis, the triple mutant of the PTPepsilon D2 domain is constructed to reconstitute the residues of the PTPepsilon D1 catalytic domain that are important for phosphatase activity, resulting in only a slight increase in the phosphatase activity compared with the wild-type D2 protein. The mutant is used for structure-based drug design
C1108S
-
mutant lacks catalytic activity
C1239S
-
catalytically inactive
C124S
-
site-directed mutagenesis, inactive mutant
C129S
-
decreased activity
C195A
-
site-directed mutagenesis, catalytically inactive mutant comprising residues 1-294, specific interaction between the Lyp substrate-trapping mutant and SKAP-HOM
C215D
active-site mutant, similar Km-values as wild type, but reduced kcat-values and activation by 1,2-epoxy-3-(p-nitrophenoxy)propane, use as substrate-trapping mutant
C215S
C216S
-
phosphatase-dead mutant of TCPTP
C227S
-
site-directed mutagenesis, catalytically inactive mutant comprising residues 1-294, specific interaction between the Lyp substrate-trapping mutant and SKAP-HOM
C231S
-
phosphatase-dead mutant of PEST
C258M
-
isoform PTP1B, mutation turns 1B isoform to PTPalpha-like enzyme in substrate recognition
C270A
inactive, substrate-trapping mutant of the HePTP catalytic domain (HePTP residues 44-339)
C270S
inactive, substrate-trapping mutant of the HePTP catalytic domain (HePTP residues 44-339)
C270S/T106D
inactive, substrate-trapping mutant of the HePTP catalytic domain (HePTP residues 44-339)
C377S
catalytically inactive Cdc25C
C433S
-
phosphatase-dead mutant of PTPalpha
C455S
crystallization data
C459S
-
substrate-trapping mutant of SHP2
C473D
active site mutant, weak substrate affinity and dissociates rapidly
C473S
strong substrate affinity and dissociates slowly
C488S
catalytically inactive Cdc25B
C92A
site-directed mutagenesis, affects inhibition by abietic acid and 2-[(carboxycarbonyl)amino]-4,5,6,7-tetrahydro-thieno[2,3-c]-pyridine-3-carboxylic acid
C945S
-
site-directed mutagenesis of the essential cysteine residue to a serine in the islet cell antigen-related PTP results in the expression of the intracellular region which does not catalyze hydrolysis of 4-nitrophenyl phosphate
D181A
D181A/Q262A
D182A
inactive
D195A/C227S
-
optimized substrate-trap mutant, used for identification of physiological enzyme substrates
D236A
substrate-trapping mutant of the HePTP catalytic domain (HePTP residues 44-339), shows 420fold reduced activity compared to the wild type enzyme
D236A/C270A/Q314A
inactive, substrate-trapping mutant of the HePTP catalytic domain (HePTP residues 44-339)
D236A/C270S/Q314A
inactive, substrate-trapping mutant of the HePTP catalytic domain (HePTP residues 44-339)
D236A/Q314A
substrate-trapping mutant of the HePTP catalytic domain (HePTP residues 44-339), shows 1255fold reduced activity compared to the wild type enzyme
D284A
-
catalytically inactive, no significant effect on proliferation in human umbilical vein endothelial cells
D48N
-
isoform PTP1B, mutation turns 1B isoform to PTPalpha-like enzyme in substrate recognition
D61G
-
the mutation causes hyperactivation of the SHP2 catalytic activity
D92A
-
site-directed mutagenesis, the D92A mutation causes a 250 to 700fold reduction in phospholipid phosphatase activity of PTEN, the mutation perturbs the structure and function of the active site imposing significantly different impacts on the two activities of PTEN
E187C
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
E187C/S188C
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
F135Y
site-directed mutagenesis, affects inhibition by abietic acid, 3-(3,5-dibromo-4-hydroxybenzoyl)-2-ethylbenzofuran-6-sulfonic acid-[4-(thiazol-2-ylsulfamyl)phenyl]-amide, and 2-[(carboxycarbonyl)amino]-4,5,6,7-tetrahydro-thieno[2,3-c]-pyridine-3-carboxylic acid
F182H
isoform PTP1B, exchange of residue 182 with that of isoform PTPH1, modulation of functionality of catalytic center
F182Y
site-directed mutagenesis, affects inhibition by abietic acid and 2-[(carboxycarbonyl)amino]-4,5,6,7-tetrahydro-thieno[2,3-c]-pyridine-3-carboxylic acid
F183C
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
F196Y
site-directed mutagenesis, affects inhibition by abietic acid and 2-[(carboxycarbonyl)amino]-4,5,6,7-tetrahydro-thieno[2,3-c]-pyridine-3-carboxylic acid
F280Y
site-directed mutagenesis, does not affect abietane-type diterpenoids as inhibitors
F28A
-
decreased activity
G117E
-
mutant of PTP-1B, 45% increase in Km-value, decrease in kcat-value
G129E
-
naturally occuring mutation, the Cowden syndrome-associated G129E mutation abrogates the phospholipid phosphatase activity but not the phosphoprotein phosphatase activity of PTEN, the mutation perturbs the structure and function of the active site imposing significantly different impacts on the two activities of PTEN, complete loss of phospholipid phosphatase activity of the G129E PTEN mutant
G184C
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
G259Q
-
isoform PTP1B, mutation turns 1B isoform to PTPalpha-like enzyme in substrate recognition
G259S
site-directed mutagenesis, affects inhibition by 2-[(carboxycarbonyl)amino]-4,5,6,7-tetrahydro-thieno[2,3-c]-pyridine-3-carboxylic acid
G496V
-
of PTPalpha, 70% increase in Km-value, up to 13.5fold activation by tetrasodium 2-(((2-(3-(((3-(5-((2,5-disulfonatophenyl)carbamoyl)-1H-benzimidazol-2-yl)phenyl)carbamoyl)amino)phenyl)-1H-benzimidazol-5-yl)carbonyl)amino)benzene-1,4-disulfonate
H175A
site-directed mutagenesis, affects inhibition by abietic acid and 2-[(carboxycarbonyl)amino]-4,5,6,7-tetrahydro-thieno[2,3-c]-pyridine-3-carboxylic acid
H182F
isoform PTP1B, exchange of residue 182 with that of isoform PTPB1, modulation of functionality of catalytic center
K138A
-
increased activity
L119V
-
of PTP-1B, 30% decrease in kcat-value, crystallization data
L29A
-
decreased activity
M114V
-
mutant of PTP-1B, activity similar to wild-type
M258C
-
isoform PTPalpha, mutation turns alpha isoform to PTP1B-like enzyme in substrate recognition
N48D
-
isoform PTPalpha, mutation turns alpha isoform to PTP1B-like enzyme in substrate recognition
P181C
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
P181C/E187C
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
P181C/P186C
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
P186C
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
P186C/E187C
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
P87C/A122C
mutant asPTP1B, design of non-natural allosteric-inhibition sites in PTPs, in which a tricysteine moiety is engineered within the PTP catalytic domain at a conserved location outside of the active site. Introduction of the tricysteine motif, which does not exist in any wild-type PTP, serves to sensitize target PTPs to inhibition by a biarsenical compound, providing a generalizable strategy for the generation of allosterically sensitized (as) PTPs. The potency, selectivity, and kinetics of asPTP inhibition can be significantly improved by exploring the inhibitory action of a range of biarsenical compounds that differ in interarsenical distance, steric bulk, and electronic structure
Q259G
-
isoform PTPalpha, mutation turns alpha isoform to PTP1B-like enzyme in substrate recognition
Q314A
substrate-trapping mutant of the HePTP catalytic domain (HePTP residues 44-339), shows 13fold reduced activity compared to the wild type enzyme
R112A
site-directed mutagenesis, affects inhibition by abietic acid, 3-(3,5-dibromo-4-hydroxybenzoyl)-2-ethylbenzofuran-6-sulfonic acid-[4-(thiazol-2-ylsulfamyl)phenyl]-amide, and 2-[(carboxycarbonyl)amino]-4,5,6,7-tetrahydro-thieno[2,3-c]-pyridine-3-carboxylic acid
R33A
-
decreased activity
R362K
-
the Shp2 mutant shows a strongly decreased affinity for the inhibitor phenylhydrazonopyrazolone sulfonate 1
R47V
-
isoform PTP1B, mutation turns 1B isoform to PTPalpha-like enzyme in substrate recognition
R47V/D48N/M258C/G259Q
molecular dynamics simulations of the crystal structure, in comparison to wild-type, movement of Q262 is restricted
R492L
hotspot mutant, dramatically decreased activity despite showing no significant changes in crystal structure
S19A
site-directed mutagenesis, mutant PTPN12-S19A is efficient in inhibiting EGF-induced cell migration, the mutant does not produce significant differences in PTPN12's recognition of all HER2-phospho-peptides compared to wild-type PTPN12
S19E
site-directed mutagenesis, mutant PTPN12-S19E is less efficient in inhibiting EGF-induced cell migration, the mutant does not produce significant differences in PTPN12's recognition of all HER2-phospho-peptides compared to wild-type PTPN12
S295F
affects minimally catalytic activity, significantly reduces the potency of inhibitors derived from 7-bromo-6-difluoromethylphosphonate 3-naphthalenenitrile
S35E
-
decreased activity
S35E/T36E
-
increased activity
S39E
site-directed mutagenesis, the mutant impairs activity of PTPN12 toward all HER2-phosphopeptide by 2-3fold compared to wild-type, mutation S39E decreases the activity of PTPN12 toward all tested HER2 pY sites in vitro, the mutation directly affected the interaction between the PTPN12 and the residues flanking the pY of the HER2 phosphorylation sites
T106D
KIM-PTP specific substrate-trapping mutant, the introduced aspartate side chain facilitates the coordination of the bound peptides, thereby stabilizing the active dephosphorylation complex
T36E
-
decreased activity
up
-
hypoxia inducible factor-2, HIF-2, preferential activation of PTPRZ1 by HIF-2, involving ELK1, an E26 transformation-specific factor that can bind to HIF-2alpha but not HIF-1alpha. A deletion mutation of one of the two Ets binding motifs located near the principal hypoxia response element similarly decreases activation of the PTPRZ1 promoter by HIF-2. IFand Ets both bind to motifs on the PTPRZ1 promoter and cooperate inpreferential upregulation of PTPRZ1, binding of HIF-2 and ELK1 to nearby sites on the PTPRZ1 promoter region, overview
V113I
-
mutant of PTP-1B, activity similar to wild-type
V113I/M114V
-
mutant of PTP-1B, 50% decrease in kcat-value
V113T
site-directed mutagenesis, does not affect abietane-type diterpenoids as inhibitors
V121L
-
of isoform TCPTP, high increase in sensitivity against 4-((3E)-1-(1H-benzotriazol-1-yl)-1-(4-(difluoro(phosphono)methyl)benzyl)-4-phenylbut-3-en-1-yl)benzoic acid and (difluoro(4-((4E)-2-((4-fluorophenyl)carbonyl)-2-(4-(3-methyl-1,2,4-oxadiazol-5-yl)phenyl)-5-phenylpent-4-en-1-yl)phenyl)methyl)phosphonic acid
V185C
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
V451M
site-directed mutagenesis, the mutation lies in a conserved motif adjacent to the protein tyrosine phosphatase (PTP) consensus sequence and alters catalytic function. Mutant V451M possesses increased catalytic activity as compared to the wild-type enzyme. When assayed with 4-nitrophenyl phosphatase as substrate, mutant V451M shows higher activity regardless of the pNPP substrate concentration used. The mutant shows increased thermolability compared to wild-type
V457Y/E597D
site-directed mutagenesis
V47R
-
isoform PTPalpha, mutation turns alpha isoform to PTP1B-like enzyme in substrate recognition
W179F
site-directed mutagenesis, the mutation in PTP1B causes only a minor reduction in kcat of about 2fold at pH 5.5, and the pH-rate profile remains fully bell-shaped. The kinetic isotopic effects are similar to those of the wild-type PTP1B showing that general acid catalysis remains effective. The affinity of the competitive inhibitors tungstate and molybdate for the active site is not affected by the W179F mutation. Crystal structures of the W179F mutant of PTP1B show the availability of both the normal loop open and closed positions, consistent with the kinetic results
Y152A/Y153A
site-directed mutagenesis, the mutation attenuates allosteric communication between the C-terminus and the WPD loop, affects inhibition by abietic acid, 3-(3,5-dibromo-4-hydroxybenzoyl)-2-ethylbenzofuran-6-sulfonic acid-[4-(thiazol-2-ylsulfamyl)phenyl]-amide, and 2-[(carboxycarbonyl)amino]-4,5,6,7-tetrahydro-thieno[2,3-c]-pyridine-3-carboxylic acid
Y46A
site-directed mutagenesis, substitution of Y46 with alalnine in PTP1B results in a 380fold increase in Km using pNPP as a substrate
Y497A
shows a significantly slower rate constant for association compared to that of the wild type enzyme
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
unstable in imidazole buffers
95006
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24
-
stable below
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
EDTA and dithiothreitol stabilize
-
sensitive to freezing and thawing
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM Hepes, pH 7.2, 0.1% 2-mercaptoethanol, 50% glycerol
-
-70°C, 10 mM imidazole-HCl, pH 7.2, 20% v/v glycerol, 0.1% 2-mercaptoethanol, pepstatin A, leupeptin, kallikrein, 0.1% Triton X-100
-
-70°C, 20% glycerol, no loss of activity
-70°C, 50 mM imidazole-HCl, pH 7.2, 2 mM EDTA, 0.1% v/v 2-mercaptoethanol, 1 mM benzamidine, 0.002% w/v PMSF, 50% v/v glycerol, half-life: 3 months
-
-80°C, 20% v/v glycerol, stable for more than 4 months
-
4°C, 10 mM phosphate, 10 mM sodium acetate, pH 5.0, 0.5 mg/ml enzyme, 10% v/v glycerol, stable for 6 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CM-Sepharose column chromatography
-
glutathione affinity column chromatography, Source 15Q column chromatography, and Superdex 200 gel filtration
-
glutathione Sepharose column chromatography
-
His-bind resin chromatography
-
HisTrap HP column chromatography and Superdex 75 gel filtration
Ni2+-Sepharose affinity HiTrap HP column chromatography, Superdex 200 16/60 gel filtration, DEAE-cellulose resin chromatography, and HiTrapQ column chromatography
-
nickel-affinity chromatography, Q-Sepharose chromatography and gel filtration
POROS 20SP column chromatography and Source 30Q column chromatography
-
protein G-Sepharose chromatography
-
protein G-Sepharose column chromatography
-
Q-15 ion-exchange resin chromatography
Q-Sepharose clumn chromatography
-
recombinant enzyme SHP-1 from Escherichia coli strain BL21 (DE3) by ion exchange chromatography and affinity chromataography on L-histidyldiazobenzylphosphonic acid, and dialysis
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage by thrombin, and gel filtration
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His6-tagged enzyme from Escherichia coli
recombinant isolated His6-tagged intracellular catalytic domain of PTP-oc 6.8fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant protein expressed Escherichia coli
-
recombinant thioredoxin-fused insulinoma associated protein tyrosine phosphatase 2 (IA-2) from Escherichia coli strains GI698 and GI724 by phenylarsine oxide-resin affinity chromatography
recombinant wild-type and mutant GST-tagged enzymes from Escherichia coli by glutathione affinity chromatography
recombinant wild-type and mutant PTEN from Spodoptera fruiperda Sf9 cells by anion exchange chromatography
-
recombinant wild-type and mutant TEV protease-cleavable, N-terminally His6-tagged maltose-binding protein-PTPepsilon D1 and D2 fusion proteins from Escherichia coli strain Rosetta 2 (DE3) by nickel affinity chromatography, ultrafiltration, and cleavage of the tag/fusion protein, followed by gel filtration and ultrafiltration
using glutathione Sepharose 4B beads
-
using nickel chelated discs
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons, expression of the His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in strain DH5alpha
enzyme SHP-1 expression in Escherichia coli strain BL21 (DE3)
-
enzyme SHPTP1 and its catalytic domain, lacking the N-terminal SH2-domains, expression in Escherichia coli
-
expressed in CHO cells and L6 cells
expressed in COS-7 cells
-
expressed in Escherichia coli
expressed in Escherichia coli BL21 (DE3) cells
expressed in Escherichia coli BL21 and HEK293T cells
-
expressed in Escherichia coli BL21 DE3 cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells and HEK-293T cells
-
expressed in Escherichia coli BL21-CodonPlus (DE3) cells
expressed in Escherichia coli DH5alpha cells
expressed in Escherichia coli strain BJ5183
expressed in Escherichia coli strain BL21 (DE3)
-
expressed in HCT-116 colon cancer cell line
-
expressed in in Ba/F3 cells and in primary bone marrow hematopoietic progenitor cells
-
expressed in insect cells
-
expressed in K-562 cells
expressed in rat INS-1 cells
-
expressed in Saccharomyces cerevisiae YPH499 cells
-
expression in Sf9 cells
-
expression of N-terminally His-tagged enzyme mutant C227S, expression of Myc-tagged lymphoid-specific tyrosine phosphatase in HEK-293 cells, co-expression with SKAP-HOM, a cytosolic adaptor protein required for proper activation of the immune system, a bona fide Lyp substrate
-
expression of PTP2C and DELTASH2-PTP2C in Escherichia coli
-
expression of splicing variant SV3 of LMW-PTP in Escherichia coli
-
expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
expression of truncated forms encoding the catalytic domain which is independent of the regulatory influence of the C-terminus
-
expression of wild-type and mutant PTEN in Spodoptera fruiperda Sf9 cells
-
full length form and a truncated form lacking the SH-domains and exhibiting a higher catalytic activity, GenBank, EMBL Data Bank L07527
gene PTP1B, recombinant expression of C-terminally His-tagged wild-type and mutant enzymes (PTP1B residues 1-321) in Escherichia coli strain BL21(DE3)
gene PTPN12, recombinant expression of wild-type and mutant GST-tagged enzymes in Escherichia coli
gene PTPN6, recombinant expression of wild-type full-length enzyme and isolated catalytic enzyme domain SHP-1cat, and of V451M mutant full-length enzyme and isolated catalytic enzyme domain SHP-1cat in Escherichia coli
gene PTPRD, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
gene PTPRE, located on chromosome 12p12-p13, recombinant expression of isolated C-terminally His6-tagged intracellular catalytic domain of PTP-oc (DELTAPTP-oc) in Escherichia coli strain BL21(DE3), method evaluation
gene PTPRR, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
lymphoid-specific enzyme
overexpression of PTP1B in HEK-293 cells
-
p52shc and p66shc expression analysis, overexpression of p66shc
-
recombinant expression of the TEV protease-cleavable, N-terminally His6-tagged maltose-binding protein-PTPepsilon D1(Ser107-Gly398) fusion protein and of wild-type and mutant TEV protease-cleavable, N-terminally His6-tagged-maltose-binding protein D2 domain of PTPepsilon D2(Gly425-Lys700) in Escherichia coli strain Rosetta 2 (DE3)
recombinant expression of thioredoxin-fused insulinoma associated protein tyrosine phosphatase 2 (IA-2) in Escherichia coli strains GI698 and GI724
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
guggulsterone, a farnesoid X receptor antagonist, induces the expression of both the protein and mRNA for tyrosine protein phosphatase SHP-1, which is not due to demethylation of the SHP-1 promoter previously implicated in the epigenetic silencing of SHP-1. Induction of SHP-1 leads to inhibition of activation of protein tyrosine kinases Janus-activated kinase 2 and c-Src, and of subsequent activation of STAT3, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
decreased PTPN12 protein level is associated with poor prognosis of several types of cancers
drug development
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Boivin, P.; Galand, C.
The human red cell acid phosphatase is a phosphotyrosine protein phosphatase which dephosphorylates the membrane protein band 3
Biochem. Biophys. Res. Commun.
134
557-564
1986
Homo sapiens
Manually annotated by BRENDA team
Roome, J.; O'Hare, T.; Pilch, P.F.; Brautigan, D.L.
Protein phosphotyrosine phosphatase purified from the particulate fraction of human placenta dephosphorylates insulin and growth-factor receptors
Biochem. J.
256
493-500
1988
Homo sapiens
Manually annotated by BRENDA team
Tonks, N.K.; Diltz, C.D.; Fischer, E.H.
Characterization of the major protein-tyrosine-phosphatases of human placenta
J. Biol. Chem.
263
6731-6737
1988
Homo sapiens
Manually annotated by BRENDA team
Tonks, N.K.; Diltz, C.D.; Fischer, E.H.
Purification of the major protein-tyrosine-phosphatases of human placenta
J. Biol. Chem.
263
6722-6730
1988
Homo sapiens
Manually annotated by BRENDA team
Waheed, A.; Laidler, P.M.; Wo, Y.Y.P.; Van Etten, R.L.
Purification and physicochemical characterization of a human placental acid phosphatase possessing phosphotyrosyl protein phosphatase activity
Biochemistry
27
4265-4273
1988
Homo sapiens
Manually annotated by BRENDA team
Clari, G.; Brunati, A.M.; Moret, V.
Partial purification and characterization of phosphotyrosyl-protein phosphatase(s) from human erythrocyte cytosol
Biochem. Biophys. Res. Commun.
137
566-572
1986
Homo sapiens
Manually annotated by BRENDA team
Zhao, Z.; Laroque, R.; Ho, W.T.; Fischer, E.H.; Shen, S.H.
Purification and characterization of PTP2C, a widely distributed protein tyrosine phosphatase containing two SH2 domains
J. Biol. Chem.
269
8780-8785
1994
Homo sapiens
Manually annotated by BRENDA team
Brautigan, D.L.; Bornstein, P.; Gallis, B.
Phosphotyrosyl-protein phosphatase. Specific inhibition by Zn
J. Biol. Chem.
256
6519-6522
1981
Homo sapiens
Manually annotated by BRENDA team
Foulkes, J.G.
Phosphotyrosyl-protein phosphatases
Curr. Top. Microbiol. Immunol.
107
163-180
1983
Gallus gallus, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Lau, K.H.W.; Farley, J.R.; Baylink, D.J.
Phosphotyrosyl protein phosphatases
Biochem. J.
257
23-36
1989
Gallus gallus, Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Modesti, A.; Marzocchini, R.; Raugei, G.; Chiti, F.; Sereni, A.; Magherini, F.; Ramponi, G.
Cloning, expression and characterization of new human low Mr phosphotyrosine protein phosphatase originating by alternative splicing
FEBS Lett.
431
111-115
1998
Homo sapiens
Manually annotated by BRENDA team
Hundt, M.; Schmidt, R.E.
Functional characterization of receptor-type protein tyrosine phosphatase CD148 (HPTPeta/DEP-1) in Fcgamma receptor IIa signal transduction of human neutrophils
Eur. J. Immunol.
27
3532-3535
1997
Homo sapiens
Manually annotated by BRENDA team
Gu, M.; Majerus, P.W.
The properties of the protein tyrosine phosphatase PTPMEG
J. Biol. Chem.
271
27751-27759
1996
Homo sapiens
Manually annotated by BRENDA team
Cui, L.; Yu, W.P.; DeAizpurua, H.J.; Schmidli, R.S.; Pallen, C.J.
Cloning and characterization of islet cell antigen-related protein-tyrosine phosphatase (PTP), a novel receptor-like PTP and autoantigen in insulin-dependent diabetis
J. Biol. Chem.
271
24817-24823
1996
Homo sapiens
Manually annotated by BRENDA team
Sorio, C.; Mendrola, J.; Lou, Z.; LaForgia, S.; Croce, C.M.; Huebner, K.
Characterization of the receptor protein tyrosine phosphatase gene product PTPgamma: binding and activation by triphosphorylated nucleotides
Cancer Res.
55
4855-4864
1995
Homo sapiens
Manually annotated by BRENDA team
Dechert, U.; Adam, M.; Harder, K.W.; Clark-Lewis, I.; Jirik, F.
Characterization of protein tyrosine phosphatase SH-PTP2. Study of phosphopeptide substrates and possible regulatory role of SH2 domains
J. Biol. Chem.
269
5602-5611
1984
Homo sapiens (Q06124)
Manually annotated by BRENDA team
Hoppe, E.; Berne, P.F.; Stock, D.; Rasmussen, J.S.; Moller, N.P.H.
Expression, purification and crystallization of human phosphotyrosine phosphatase 1B
Eur. J. Biochem.
223
1069-1077
1994
Homo sapiens
Manually annotated by BRENDA team
Harder, K.W.; Owen, P.; Wong, L.K.H.; Aebersold, R.; Clark-Lewis, I.; Jirik, F.R.
Characterization and kinetic analysis of the intracellular domain of human protein tyrosine phosphatase beta (HPTPbeta) using synthetic phosphopeptides
Biochem. J.
298
395-401
1994
Homo sapiens
-
Manually annotated by BRENDA team
Sugimoto, S.; Lechleider, R.J.; Shoelson, S.E.; Neel, B.G.; Walsh, C.T.
Expression, purification, and characterization of SH2-containing protein tyrosine phosphatase, SH-PTP2
J. Biol. Chem.
268
227711-22776
1993
Homo sapiens
-
Manually annotated by BRENDA team
Pei, D.; Neel, B.G.; Walsh, C.T.
Overexpression, purification, and characterization of SHPTPa, a src homology 2-containing protein-tyrosine-phosphatase
Proc. Natl. Acad. Sci. USA
90
1092-1096
1993
Homo sapiens
Manually annotated by BRENDA team
Cohen, S.; Dadi, H.; Shaoul, E.; Sharfe, N.; Riofam, C.M.
Cloning and characterization of a lymphoid-specific inducible human protein tyrosine phosphatase, Lyp
Blood
93
2013-2024
1999
Homo sapiens (Q9Y2R2), Homo sapiens
Manually annotated by BRENDA team
Daum, G.; Zander, N.F.; Morse, B.; Hurwitz, D.; Schlessinger, J.; Fischer, E.H.
Characterization of a human recombinant receptor-like protein tyrosine phosphatase
J. Biol. Chem.
266
12211-12215
1991
Homo sapiens
Manually annotated by BRENDA team
Tonks, N.K.; Diltz, C.D.; Fischer, E.H.
CD45, an integral membrane protein tyrosine phosphatase. Characterization of enzyme activity
J. Biol. Chem.
256
10674-10680
1990
Homo sapiens
Manually annotated by BRENDA team
Barford, D.; Flint, A.J.; Tonks, N.K.
Crystal structure of human protein tyrosine phosphatase 1B
Science
263
1397-1404
1994
Homo sapiens
Manually annotated by BRENDA team
Thompson, L.J.; Jiang, J.; Madamanchi, N.; Runge, M.S.; Patterson, C.
PTP-epsilon, a tyrosine phosphatase expressed in endothelium, negatively regulates endothelial cell proliferation
Am. J. Physiol.
281
H396-H403
2001
Homo sapiens
Manually annotated by BRENDA team
Romsicki, Y.; Kennedy, B.P.; Asante-Appiah, E.
Purification and characterization of T cell protein tyrosine phosphatase reveals significant functional homology to protein tyrosine phosphatase-1B
Arch. Biochem. Biophys.
414
40-50
2003
Homo sapiens
Manually annotated by BRENDA team
Pedersen, A.K.; Guo, X.L.; Moller, K.B.; Peters, G.H.; Andersen, H.S.; Kastrup, J.S.; Mortensen, S.B.; Iversen, L.F.; Zhang, Z.Y.; Moller, N.P.H.
Residue 182 influences the second step of protein-tyrosine phosphatase-mediated catalysis
Biochem. J.
378
421-433
2004
Homo sapiens (P18031)
Manually annotated by BRENDA team
Xie, L.; Zhang, Y.L.; Zhang, Z.Y.
Design and characterization of an improved protein tyrosine phosphatase substrate-trapping mutant
Biochemistry
41
4032-4039
2002
Homo sapiens
Manually annotated by BRENDA team
Raugei, G.; Ramponi, G.; Chiarugi, P.
Low molecular weight protein tyrosine phosphatases: small, but smart
Cell. Mol. Life Sci.
59
941-949
2002
Homo sapiens, Mammalia
Manually annotated by BRENDA team
Zhang, Z.Y.
Protein tyrosine phosphatases: prospects for therapeutics
Curr. Opin. Chem. Biol.
5
416-423
2001
Homo sapiens
Manually annotated by BRENDA team
Kolmodin, K.; Aqvist, J.
The catalytic mechanism of protein tyrosine phosphatases revisited
FEBS Lett.
498
208-213
2001
Saccharomyces cerevisiae, Homo sapiens, Yersinia enterocolitica
Manually annotated by BRENDA team
Peters, G.H.; Iversen, L.F.; Branner, S.; Andersen, H.S.; Mortensen, S.B.; Olsen, O.H.; Moller, K.B.; Moller, N.P.H.
Residue 259 is a key determinant of substrate specificity of protein-tyrosine phosphatases 1B and alpha
J. Biol. Chem.
275
18201-18209
2000
Homo sapiens
Manually annotated by BRENDA team
Vetter, S.W.; Keng, Y.F.; Lawrence, D.S.; Zhang, Z.Y.
Assessment of protein-tyrosine phosphatase 1B substrate specificity using "inverse alanine scanning"
J. Biol. Chem.
275
2265-2268
2000
Homo sapiens
Manually annotated by BRENDA team
Yang, J.; Cheng, Z.; Niu, T.; Liang, X.; Zhao, Z.J.; Zhou, G.W.
Structural basis for substrate specificity of protein-tyrosine phosphatase SHP-1
J. Biol. Chem.
275
4066-4071
2000
Homo sapiens (P29350)
Manually annotated by BRENDA team
Romsicki, Y.; Scapin, G.; Beaulieu-Audy, V.; Patel, S.; Becker, J.W.; Kennedy, B.P.; Asante-Appiah, E.
Functional characterization and crystal structure of the C215D mutant of protein-tyrosine phosphatase-1B
J. Biol. Chem.
278
29009-29015
2003
Homo sapiens (P18031)
Manually annotated by BRENDA team
Yang, J.; Liu, L.; He, D.; Song, X.; Liang, X.; Zhao, Z.J.; Zhou, G.W.
Crystal structure of human protein-tyrosine phosphatase SHP-1
J. Biol. Chem.
278
6516-6520
2003
Homo sapiens
Manually annotated by BRENDA team
Qi, Y.; Zhao, R.; Cao, H.; Sui, X.; Krantz, S.B.; Zhao, Z.J.
Purification and characterization of protein tyrosine phosphatase PTP-MEG2
J. Cell. Biochem.
86
79-89
2002
Homo sapiens
Manually annotated by BRENDA team
Wabakken, T.; Hauge, H.; Funderud, S.; Aasheim, H.C.
Characterization, expression and functional aspects of a novel protein tyrosine phosphatase epsilon isoform
Scand. J. Immunol.
56
276-285
2002
Homo sapiens (Q8TE48), Homo sapiens
Manually annotated by BRENDA team
Welte, S.; Baringhaus, K.H.; Schmider, W.; Mueller, G.; Petry, S.; Tennagels, N.
6,8-Difluoro-4-methylumbiliferyl phosphate: a fluorogenic substrate for protein tyrosine phosphatases
Anal. Biochem.
338
32-38
2005
Homo sapiens, Yersinia sp.
Manually annotated by BRENDA team
Park, J.; Pei, D.
Trans-b-nitrostyrene derivatives as slow-binding inhibitors of protein tyrosine phosphatases
Biochemistry
43
15014-15021
2004
Homo sapiens
Manually annotated by BRENDA team
Peters, G.H.; Iversen, L.F.; Andersen, H.S.; Moller, N.P.; Olsen, O.H.
Residue 259 in protein-tyrosine phosphatase PTP1B and PTPalpha determines the flexibility of glutamine 262
Biochemistry
43
8418-8428
2004
Homo sapiens (P18031)
Manually annotated by BRENDA team
Lee, H.; Xie, L.; Luo, Y.; Lee, S.Y.; Lawrence, D.S.; Wang, X.B.; Sotgia, F.; Lisanti, M.P.; Zhang, Z.Y.
Identification of phosphocaveolin-1 as a novel protein tyrosine phosphatase 1B substrate
Biochemistry
45
234-240
2006
Homo sapiens
Manually annotated by BRENDA team
Shim, Y.S.; Kim, K.C.; Lee, K.A.; Shrestha, S.; Lee, K.H.; Kim, C.K.; Cho, H.
Formylchromone derivatives as irreversible and selective inhibitors of human protein tyrosine phosphatase 1B. Kinetic and modeling studies
Bioorg. Med. Chem.
13
1325-1332
2005
Homo sapiens (P18031), Homo sapiens
Manually annotated by BRENDA team
Moretto, A.F.; Kirincich, S.J.; Xu, W.X.; Smith, M.J.; Wan, Z.K.; Wilson, D.P.; Follows, B.C.; Binnun, E.; Joseph-McCarthy, D.; Foreman, K.; Erbe, D.V.; Zhang, Y.L.; Tam, S.K.; Tam, S.Y.; Lee, J.
Bicyclic and tricyclic thiophenes as protein tyrosine phosphatase 1B inhibitors
Bioorg. Med. Chem.
14
2162-2177
2006
Homo sapiens
Manually annotated by BRENDA team
Puius, Y.A.; Zhao, Y.; Sullivan, M.; Lawrence, D.S.; Almo, S.C.; Zhang, Z.Y.
Identification of a second aryl phosphate-binding site in protein-tyrosine phosphatase 1B: a paradigm for inhibitor design
Proc. Natl. Acad. Sci. USA
94
13420-13425
1997
Homo sapiens (P18031), Homo sapiens
Manually annotated by BRENDA team
Na, M.; Oh, W.K.; Kim, Y.H.; Cai, X.F.; Kim, S.; Kim, B.Y.; Ahn, J.S.
Inhibition of protein tyrosine phosphatase 1B by diterpenoids isolated from Acanthopanax koreanum
Bioorg. Med. Chem. Lett.
16
3061-3064
2006
Homo sapiens
Manually annotated by BRENDA team
McCain, D.F.; Wu, L.; Nickel, P.; Kassack, M.U.; Kreimeyer, A.; Gagliardi, A.; Collins, D.C.; Zhang, Z.Y.
Suramin derivatives as inhibitors and activators of protein-tyrosine phosphatases
J. Biol. Chem.
279
14713-14725
2004
Homo sapiens, Yersinia sp.
Manually annotated by BRENDA team
Lund, I.K.; Andersen, H.S.; Iversen, L.F.; Olsen, O.H.; Moller, K.B.; Pedersen, A.K.; Ge, Y.; Holsworth, D.D.; Newman, M.J.; Axe, F.U.; Moller, N.P.
Structure-based design of selective and potent inhibitors of protein-tyrosine phosphatase beta
J. Biol. Chem.
279
24226-24235
2004
Homo sapiens (P18031), Homo sapiens
Manually annotated by BRENDA team
Zabolotny, J.M.; Haj, F.G.; Kim, Y.B.; Kim, H.J.; Shulman, G.I.; Kim, J.K.; Neel, B.G.; Kahn, B.B.
Transgenic overexpression of protein-tyrosine phosphatase 1B in muscle causes insulin resistance, but overexpression with leukocyte antigen-related phosphatase does not additively impair insulin action
J. Biol. Chem.
279
24844-24851
2004
Homo sapiens
Manually annotated by BRENDA team
Lin, S.Y.; Raval, S.; Zhang, Z.; Deverill, M.; Siminovitch, K.A.; Branch, D.R.; Haimovich, B.
The protein-tyrosine phosphatase SHP-1 regulates the phosphorylation of alpha-actinin
J. Biol. Chem.
279
25755-25764
2004
Homo sapiens
Manually annotated by BRENDA team
Liang, F.; Lee, S.Y.; Liang, J.; Lawrence, D.S.; Zhang, Z.Y.
The role of protein-tyrosine phosphatase 1B in integrin signaling
J. Biol. Chem.
280
24857-24863
2005
Homo sapiens
Manually annotated by BRENDA team
Xu, Y.; Tan, L.J.; Grachtchouk, V.; Voorhees, J.J.; Fisher, G.J.
Receptor-type protein-tyrosine phosphatase-kappa regulates epidermal growth factor receptor function
J. Biol. Chem.
280
42694-42700
2005
Homo sapiens
Manually annotated by BRENDA team
Wu, J.; Katrekar, A.; Honigberg, L.A.; Smith, A.M.; Conn, M.T.; Tang, J.; Jeffery, D.; Mortara, K.; Sampang, J.; Williams, S.R.; Buggy, J.; Clark, J.M.
Identification of substrates of human protein-tyrosine phosphatase PTPN22
J. Biol. Chem.
281
11002-11010
2006
Homo sapiens
Manually annotated by BRENDA team
Montalibet, J.; Skorey, K.; McKay, D.; Scapin, G.; Asante-Appiah, E.; Kennedy, B.P.
Residues distant from the active site influence protein-tyrosine phosphatase 1B inhibitor binding
J. Biol. Chem.
281
5258-5266
2006
Homo sapiens (P18031)
Manually annotated by BRENDA team
Asante-Appiah, E.; Patel, S.; Desponts, C.; Taylor, J.M.; Lau, C.; Dufresne, C.; Therien, M.; Friesen, R.; Becker, J.W.; Leblanc, Y.; Kennedy, B.P.; Scapin, G.
Conformation-assisted inhibition of protein-tyrosine phosphatase-1B elicits inhibitor selectivity over T-cell protein-tyrosine phosphatase
J. Biol. Chem.
281
8010-8015
2006
Homo sapiens
Manually annotated by BRENDA team
Nam, H.J.; Poy, F.; Saito, H.; Frederick, C.A.
Structural basis for the function and regulation of the receptor protein tyrosine phosphatase CD45
J. Exp. Med.
201
441-452
2005
Homo sapiens
Manually annotated by BRENDA team
Rouleau, C.; Roy, A.; St Martin, T.; Dufault, M.R.; Boutin, P.; Liu, D.; Zhang, M.; Puorro-Radzwill, K.; Rulli, L.; Reczek, D.; Bagley, R.; Byrne, A.; Weber, W.; Roberts, B.; Klinger, K.; Brondyk, W.; Nacht, M.; Madden, S.; Burrier, R.; Shankara, S.; Teicher, B.A.
Protein tyrosine phosphatase PRL-3 in malignant cells and endothelial cells: expression and function
Mol. Cancer Ther.
5
219-229
2006
Homo sapiens
Manually annotated by BRENDA team
Wiesmann, C.; Barr, K.J.; Kung, J.; Zhu, J.; Erlanson, D.A.; Shen, W.; Fahr, B.J.; Zhong, M.; Taylor, L.; Randal, M.; McDowell, R.S.; Hansen, S.K.
Allosteric inhibition of protein tyrosine phosphatase 1B
Nat. Struct. Mol. Biol.
11
730-737
2004
Homo sapiens (P18031), Homo sapiens
Manually annotated by BRENDA team
Na, M.; Oh, W.K.; Kim, Y.H.; Cai, X.F.; Kim, S.; Kim, B.Y.; Ahn, J.S.
Na, M.; Yang, S.; He, L.; Oh, H.; Kim, B.S.; Oh, W.K.; Kim, B.Y.; Ahn, J.S.: Inhibition of protein tyrosine phosphatase 1B by ursane-type triterpenes isolated from Symplocos paniculata
Planta Med.
72
261-263
2006
Homo sapiens
Manually annotated by BRENDA team
Eswaran, J.; Debreczeni, J.E.; Longman, E.; Barr, A.J.; Knapp, S.
The crystal structure of human receptor protein tyrosine phosphatase kappa phosphatase domain 1
Protein Sci.
15
1500-1505
2006
Homo sapiens
Manually annotated by BRENDA team
Evdokimov, A.G.; Pokross, M.; Walter, R.; Mekel, M.; Cox, B.; Li, C.; Bechard, R.; Genbauffe, F.; Andrews, R.; Diven, C.; Howard, B.; Rastogi, V.; Gray, J.; Maier, M.; Peters, K.G.
Engineering the catalytic domain of human protein tyrosine phosphatase beta for structure-based drug discovery
Acta Crystallogr. Sect. D
62
1435-1445
2006
Homo sapiens (P23467), Homo sapiens
Manually annotated by BRENDA team
Jeong, D.G.; Cho, Y.H.; Yoon, T.S.; Kim, J.H.; Son, J.H.; Ryu, S.E.; Kim, S.J.
Structure of human DSP18, a member of the dual-specificity protein tyrosine phosphatase family
Acta Crystallogr. Sect. D
62
582-588
2006
Homo sapiens
Manually annotated by BRENDA team
Eswaran, J.; von Kries, J.P.; Marsden, B.; Longman, E.; Debreczeni, J.E.; Ugochukwu, E.; Turnbull, A.; Lee, W.H.; Knapp, S.; Barr, A.J.
Crystal structures and inhibitor identification for PTPN5, PTPRR and PTPN7: a family of human MAPK-specific protein tyrosine phosphatases
Biochem. J.
395
483-491
2006
Homo sapiens
Manually annotated by BRENDA team
Rudolph, J.
Cdc25 phosphatases: structure, specificity, and mechanism
Biochemistry
46
3595-3604
2007
Homo sapiens
Manually annotated by BRENDA team
Sohn, J.; Buhrman, G.; Rudolph, J.
Kinetic and structural studies of specific protein-protein interactions in substrate catalysis by Cdc25B phosphatase
Biochemistry
46
807-818
2007
Homo sapiens (P30305)
Manually annotated by BRENDA team
Forte, E.; Orsatti, L.; Talamo, F.; Barbato, G.; De Francesco, R.; Tomei, L.
Ezrin is a specific and direct target of protein tyrosine phosphatase PRL-3
Biochim. Biophys. Acta
1783
334-344
2008
Homo sapiens
Manually annotated by BRENDA team
Ferreira, C.V.; Justo, G.Z.; Souza, A.C.; Queiroz, K.C.; Zambuzzi, W.F.; Aoyama, H.; Peppelenbosch, M.P.
Natural compounds as a source of protein tyrosine phosphatase inhibitors: application to the rational design of small-molecule derivatives
Biochimie
88
1859-1873
2006
Homo sapiens, Homo sapiens (P30304), Homo sapiens (P30305), Homo sapiens (P30307)
Manually annotated by BRENDA team
Sohn, J.; Rudolph, J.
Temperature dependence of binding and catalysis for the Cdc25B phosphatase
Biophys. Chem.
125
549-555
2007
Homo sapiens
Manually annotated by BRENDA team
Kochinyan, S.; Sun, L.; Ghosh, I.; Barshevsky, T.; Xu, J.; Xu, M.Q.
Use of intein-mediated phosphoprotein arrays to study substrate specificity of protein phosphatases
Biotechniques
42
63-69
2007
Homo sapiens
Manually annotated by BRENDA team
Iervolino, A.; Iuliano, R.; Trapasso, F.; Viglietto, G.; Melillo, R.M.; Carlomagno, F.; Santoro, M.; Fusco, A.
The receptor-type protein tyrosine phosphatase J antagonizes the biochemical and biological effects of RET-derived oncoproteins
Cancer Res.
66
6280-6287
2006
Homo sapiens
Manually annotated by BRENDA team
Seiner, D.R.; LaButti, J.N.; Gates, K.S.
Kinetics and mechanism of protein tyrosine phosphatase 1B inactivation by acrolein
Chem. Res. Toxicol.
20
1315-1320
2007
Homo sapiens
Manually annotated by BRENDA team
Lavecchia, A.; Cosconati, S.; Limongelli, V.; Novellino, E.
Modeling of Cdc25B dual specificity protein phosphatase inhibitors: docking of ligands and enzymatic inhibition mechanism
ChemMedChem
1
540-550
2006
Homo sapiens (P30305), Homo sapiens
Manually annotated by BRENDA team
Nascimento, M.; Zhang, W.W.; Ghosh, A.; Houston, D.R.; Berghuis, A.M.; Olivier, M.; Matlashewski, G.
Identification and characterization of a protein-tyrosine phosphatase in Leishmania: Involvement in virulence
J. Biol. Chem.
281
36257-36268
2006
Homo sapiens, Leishmania infantum, Leishmania major, Leishmania donovani (Q0PEE2), Leishmania major Friedlin V9, Leishmania donovani 1S/Cl2D (Q0PEE2)
Manually annotated by BRENDA team
Varmeh-Ziaie, S.; Manfredi, J.J.
The dual specificity phosphatase Cdc25B, but not the closely related Cdc25C, is capable of inhibiting cellular proliferation in a manner dependent upon its catalytic activity
J. Biol. Chem.
282
24633-24641
2007
Homo sapiens (P30305), Homo sapiens (P30307), Homo sapiens
Manually annotated by BRENDA team
Picha, K.M.; Patel, S.S.; Mandiyan, S.; Koehn, J.; Wennogle, L.P.
The role of the C-terminal domain of protein tyrosine phosphatase-1B in phosphatase activity and substrate binding
J. Biol. Chem.
282
2911-2917
2007
Homo sapiens
Manually annotated by BRENDA team
Jeong, D.G.; Yoon, T.S.; Kim, J.H.; Shim, M.Y.; Jung, S.K.; Son, J.H.; Ryu, S.E.; Kim, S.J.
Crystal structure of the catalytic domain of human MAP kinase phosphatase 5: structural insight into constitutively active phosphatase
J. Mol. Biol.
360
946-955
2006
Homo sapiens (Q16828), Homo sapiens (Q99956), Homo sapiens (Q9Y6W6), Homo sapiens
Manually annotated by BRENDA team
Chen, Y.; Xu, Y.; Bao, Q.; Xing, Y.; Li, Z.; Lin, Z.; Stock, J.B.; Jeffrey, P.D.; Shi, Y.
Structural and biochemical insights into the regulation of protein phosphatase 2A by small t antigen of SV40
Nat. Struct. Mol. Biol.
14
527-534
2007
Homo sapiens
Manually annotated by BRENDA team
Owens, D.M.; Keyse, S.M.
Differential regulation of MAP kinase signalling by dual-specificity protein phosphatases
Oncogene
26
3203-3213
2007
Homo sapiens
Manually annotated by BRENDA team
Yu, X.; Sun, J.P.; He, Y.; Guo, X.; Liu, S.; Zhou, B.; Hudmon, A.; Zhang, Z.Y.
Structure, inhibitor, and regulatory mechanism of Lyp, a lymphoid-specific tyrosine phosphatase implicated in autoimmune diseases
Proc. Natl. Acad. Sci. USA
104
19767-19772
2007
Homo sapiens
Manually annotated by BRENDA team
Zhang, X.; Guo, A.; Yu, J.; Possemato, A.; Chen, Y.; Zheng, W.; Polakiewicz, R.D.; Kinzler, K.W.; Vogelstein, B.; Velculescu, V.E.; Wang, Z.J.
Identification of STAT3 as a substrate of receptor protein tyrosine phosphatase T
Proc. Natl. Acad. Sci. USA
104
4060-4064
2007
Homo sapiens
Manually annotated by BRENDA team
Kim, S.J.; Jeong, D.G.; Yoon, T.S.; Son, J.H.; Cho, S.K.; Ryu, S.E.; Kim, J.H.
Crystal structure of human TMDP, a testis-specific dual specificity protein phosphatase: implications for substrate specificity
Proteins
66
239-245
2007
Homo sapiens
Manually annotated by BRENDA team
Barr, A.J.; Knapp, S.
MAPK-specific tyrosine phosphatases: new targets for drug discovery?
Trends Pharmacol. Sci.
27
525-530
2006
Homo sapiens (P35236), Homo sapiens (P54829), Homo sapiens (Q15256), Homo sapiens
Manually annotated by BRENDA team
Korporaal, S.J.; Koekman, C.A.; Verhoef, S.; van der Wal, D.E.; Bezemer, M.; Van Eck, M.; Akkerman, J.W.
Downregulation of platelet responsiveness upon contact with LDL by the protein-tyrosine phosphatases SHP-1 and SHP-2
Arterioscler. Thromb. Vasc. Biol.
29
372-379
2009
Homo sapiens
Manually annotated by BRENDA team
Critton, D.A.; Tortajada, A.; Stetson, G.; Peti, W.; Page, R.
Structural basis of substrate recognition by hematopoietic tyrosine phosphatase
Biochemistry
47
13336-13345
2008
Homo sapiens (P35236)
Manually annotated by BRENDA team
Zhang, X.Y.; Chen, V.L.; Rosen, M.S.; Blair, E.R.; Lone, A.M.; Bishop, A.C.
Allele-specific inhibition of divergent protein tyrosine phosphatases with a single small molecule
Bioorg. Med. Chem.
16
8090-8097
2008
Homo sapiens (P18031)
Manually annotated by BRENDA team
Zhang, Y.N.; Zhang, W.; Hong, D.; Shi, L.; Shen, Q.; Li, J.Y.; Li, J.; Hu, L.H.
Oleanolic acid and its derivatives: new inhibitor of protein tyrosine phosphatase 1B with cellular activities
Bioorg. Med. Chem.
16
8697-8705
2008
Homo sapiens (P29350)
Manually annotated by BRENDA team
Bhattacharya, S.; Labutti, J.N.; Seiner, D.R.; Gates, K.S.
Oxidative inactivation of protein tyrosine phosphatase 1B by organic hydroperoxides
Bioorg. Med. Chem. Lett.
18
5856-5859
2008
Homo sapiens
Manually annotated by BRENDA team
Wimmer-Kleikamp, S.H.; Nievergall, E.; Gegenbauer, K.; Adikari, S.; Mansour, M.; Yeadon, T.; Boyd, A.W.; Patani, N.R.; Lackmann, M.
Elevated protein tyrosine phosphatase activity provokes Eph/ephrin-facilitated adhesion of pre-B leukemia cells
Blood
112
721-732
2008
Homo sapiens
Manually annotated by BRENDA team
Kiyan, J.; Haller, H.; Dumler, I.
The tyrosine phosphatase SHP-2 controls urokinase-dependent signaling and functions in human vascular smooth muscle cells
Exp. Cell Res.
315
1029-1039
2008
Homo sapiens
Manually annotated by BRENDA team
Hendriks, W.J.; Elson, A.; Harroch, S.; Stoker, A.W.
Protein tyrosine phosphatases: functional inferences from mouse models and human diseases
FEBS J.
275
816-830
2008
Homo sapiens, Homo sapiens (O14522), Homo sapiens (P10586), Homo sapiens (P17706), Homo sapiens (P18031), Homo sapiens (P18433), Homo sapiens (P23467), Homo sapiens (P23468), Homo sapiens (P23469), Homo sapiens (P23470), Homo sapiens (P23471), Homo sapiens (P26045), Homo sapiens (P28827), Homo sapiens (P29074), Homo sapiens (P29350), Homo sapiens (P35236), Homo sapiens (P43378), Homo sapiens (P54829), Homo sapiens (Q05209), Homo sapiens (Q06124), Homo sapiens (Q0VAE8), Homo sapiens (Q12913), Homo sapiens (Q12923), Homo sapiens (Q13332), Homo sapiens (Q15256), Homo sapiens (Q15262), Homo sapiens (Q15678), Homo sapiens (Q16825), Homo sapiens (Q16827), Homo sapiens (Q16849), Homo sapiens (Q4JDK3), Homo sapiens (Q92729), Homo sapiens (Q92932), Homo sapiens (Q99952), Homo sapiens (Q9H3S7), Homo sapiens (Q9HD43), Homo sapiens (Q9UMZ3), Homo sapiens (Q9Y2R2)
Manually annotated by BRENDA team
Tabernero, L.; Aricescu, A.R.; Jones, E.Y.; Szedlacsek, S.E.
Protein tyrosine phosphatases: structure-function relationships
FEBS J.
275
867-882
2008
Homo sapiens, Yersinia sp.
Manually annotated by BRENDA team
Xu, D.; Qu, C.K.
Protein tyrosine phosphatases in the JAK/STAT pathway
Front. Biosci.
13
4925-4932
2008
Homo sapiens
Manually annotated by BRENDA team
Kakazu, A.; Sharma, G.; Bazan, H.E.
Association of protein tyrosine phosphatases (PTPs)-1B with c-Met receptor and modulation of corneal epithelial wound healing
Invest. Ophthalmol. Vis. Sci.
49
2927-2935
2008
Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Carlucci, A.; Gedressi, C.; Lignitto, L.; Nezi, L.; Villa-Moruzzi, E.; Avvedimento, E.V.; Gottesman, M.; Garbi, C.; Feliciello, A.
Protein-tyrosine phosphatase PTPD1 regulates focal adhesion kinase autophosphorylation and cell migration
J. Biol. Chem.
283
10919-10929
2008
Homo sapiens
Manually annotated by BRENDA team
Welters, H.J.; Oknianska, A.; Erdmann, K.S.; Ryffel, G.U.; Morgan, N.G.
The protein tyrosine phosphatase-BL, modulates pancreatic beta-cell proliferation by interaction with the Wnt signalling pathway
J. Endocrinol.
197
543-552
2008
Homo sapiens
Manually annotated by BRENDA team
Lawrence, H.R.; Pireddu, R.; Chen, L.; Luo, Y.; Sung, S.S.; Szymanski, A.M.; Yip, M.L.; Guida, W.C.; Sebti, S.M.; Wu, J.; Lawrence, N.J.
Inhibitors of Src homology-2 domain containing protein tyrosine phosphatase-2 (Shp2) based on oxindole scaffolds
J. Med. Chem.
51
4948-4956
2008
Homo sapiens
Manually annotated by BRENDA team
Thuong, P.T.; Lee, C.H.; Dao, T.T.; Nguyen, P.H.; Kim, W.G.; Lee, S.J.; Oh, W.K.
Triterpenoids from the leaves of Diospyros kaki (persimmon) and their inhibitory effects on protein tyrosine phosphatase 1B
J. Nat. Prod.
71
1775-1778
2008
Homo sapiens
Manually annotated by BRENDA team
Allsup, D.; Harris, R.; Baker, P.; Cawley, J.
Protein-tyrosine phosphatase activity maintains the viability of hairy cells and modulates their response to interferon-alpha
Leuk. Lymphoma
49
2351-2358
2008
Homo sapiens
Manually annotated by BRENDA team
Kunnumakkara, A.B.; Nair, A.S.; Sung, B.; Pandey, M.K.; Aggarwal, B.B.
Boswellic acid blocks signal transducers and activators of transcription 3 signaling, proliferation, and survival of multiple myeloma via the protein tyrosine phosphatase SHP-1
Mol. Cancer Res.
7
118-128
2009
Homo sapiens
Manually annotated by BRENDA team
Chabot, C.; Spring, K.; Gratton, J.P.; Elchebly, M.; Royal, I.
New role for the protein tyrosine phosphatase DEP-1 in Akt activation and endothelial cell survival
Mol. Cell. Biol.
29
241-253
2009
Homo sapiens
Manually annotated by BRENDA team
Ishino, Y.; Zhu, C.; Harris, D.L.; Joyce, N.C.
Protein tyrosine phosphatase-1B (PTP1B) helps regulate EGF-induced stimulation of S-phase entry in human corneal endothelial cells
Mol. Vis.
14
61-70
2008
Homo sapiens
Manually annotated by BRENDA team
Choi, J.Y.; Na, M.; Hyun Hwang, I.; Ho Lee, S.; Young Bae, E.; Yeon Kim, B.; Seog Ahn, J.
Isolation of betulinic acid, its methyl ester and guaiane sesquiterpenoids with protein tyrosine phosphatase 1B inhibitory activity from the roots of Saussurea lappa C.B.Clarke
Molecules
14
266-272
2009
Homo sapiens
Manually annotated by BRENDA team
Gopishetty, B.; Ren, L.; Waller, T.M.; Wavreille, A.S.; Lopez, M.; Thakkar, A.; Zhu, J.; Pei, D.
Synthesis of 3,5-difluorotyrosine-containing peptides: application in substrate profiling of protein tyrosine phosphatases
Org. Lett.
10
4605-4608
2008
Homo sapiens
Manually annotated by BRENDA team
Kwon, J.H.; Chang, M.J.; Seo, H.W.; Lee, J.H.; Min, B.S.; Na, M.; Kim, J.C.; Woo, M.H.; Choi, J.S.; Lee, H.K.; Bae, K.
Triterpenoids and a sterol from the stem-bark of Styrax japonica and their protein tyrosine phosphatase 1B inhibitory activities
Phytother. Res.
22
1303-1306
2008
Homo sapiens
Manually annotated by BRENDA team
Hellmuth, K.; Grosskopf, S.; Lum, C.T.; Wuertele, M.; Roeder, N.; von Kries, J.P.; Rosario, M.; Rademann, J.; Birchmeier, W.
Specific inhibitors of the protein tyrosine phosphatase Shp2 identified by high-throughput docking
Proc. Natl. Acad. Sci. USA
105
7275-7280
2008
Homo sapiens
Manually annotated by BRENDA team
Boivin, B.; Zhang, S.; Arbiser, J.L.; Zhang, Z.Y.; Tonks, N.K.
A modified cysteinyl-labeling assay reveals reversible oxidation of protein tyrosine phosphatases in angiomyolipoma cells
Proc. Natl. Acad. Sci. USA
105
9959-9964
2008
Homo sapiens
Manually annotated by BRENDA team
Zhang, X.Y.; Bishop, A.C.
Engineered inhibitor sensitivity in the WPD loop of a protein tyrosine phosphatase
Biochemistry
47
4491-4500
2008
Homo sapiens (P17706)
Manually annotated by BRENDA team
Bustanji, Y.; Taha, M.O.; Al-Masri, I.M.; Mohammad, M.K.
Docking simulations and in vitro assay unveil potent inhibitory action of papaverine against protein tyrosine phosphatase 1B
Biol. Pharm. Bull.
32
640-645
2009
Homo sapiens (P18031), Homo sapiens
Manually annotated by BRENDA team
Seo, C.; Sohn, J.H.; Ahn, J.S.; Yim, J.H.; Lee, H.K.; Oh, H.
Protein tyrosine phosphatase 1B inhibitory effects of depsidone and pseudodepsidone metabolites from the Antarctic lichen Stereocaulon alpinum
Bioorg. Med. Chem. Lett.
19
2801-2803
2009
Homo sapiens
Manually annotated by BRENDA team
Yoon, G.; Lee, W.; Kim, S.N.; Cheon, S.H.
Inhibitory effect of chalcones and their derivatives from Glycyrrhiza inflata on protein tyrosine phosphatase 1B
Bioorg. Med. Chem. Lett.
19
5155-5157
2009
Homo sapiens
Manually annotated by BRENDA team
Seo, C.; Sohn, J.H.; Oh, H.; Kim, B.Y.; Ahn, J.S.
Isolation of the protein tyrosine phosphatase 1B inhibitory metabolite from the marine-derived fungus Cosmospora sp. SF-5060
Bioorg. Med. Chem. Lett.
19
6095-6097
2009
Homo sapiens
Manually annotated by BRENDA team
Qiu, W.W.; Shen, Q.; Yang, F.; Wang, B.; Zou, H.; Li, J.Y.; Li, J.; Tang, J.
Synthesis and biological evaluation of heterocyclic ring-substituted maslinic acid derivatives as novel inhibitors of protein tyrosine phosphatase 1B
Bioorg. Med. Chem. Lett.
19
6618-6622
2009
Homo sapiens
Manually annotated by BRENDA team
Forghieri, M.; Laggner, C.; Paoli, P.; Langer, T.; Manao, G.; Camici, G.; Bondioli, L.; Prati, F.; Costantino, L.
Synthesis, activity and molecular modeling of a new series of chromones as low molecular weight protein tyrosine phosphatase inhibitors
Bioorg. Med. Chem.
17
2658-2672
2009
Homo sapiens (P24666)
Manually annotated by BRENDA team
Ahn, K.S.; Sethi, G.; Sung, B.; Goel, A.; Ralhan, R.; Aggarwal, B.B.
Guggulsterone, a farnesoid X receptor antagonist, inhibits constitutive and inducible STAT3 activation through induction of a protein tyrosine phosphatase SHP-1
Cancer Res.
68
4406-4415
2008
Homo sapiens
Manually annotated by BRENDA team
Maccari, R.; Ottana, R.; Ciurleo, R.; Paoli, P.; Manao, G.; Camici, G.; Laggner, C.; Langer, T.
Structure-based optimization of benzoic acids as inhibitors of protein tyrosine phosphatase 1B and low molecular weight protein tyrosine phosphatase
ChemMedChem
4
957-962
2009
Homo sapiens (P18031)
Manually annotated by BRENDA team
Fukuda, S.; Ohta, T.; Sakata, S.; Morinaga, H.; Ito, M.; Nakagawa, Y.; Tanaka, M.; Matsushita, M.
Pharmacological profiles of a novel protein tyrosine phosphatase 1B inhibitor, JTT-551
Diabetes Obes. Metab.
12
299-306
2010
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Jung, S.K.; Jeong, D.G.; Chung, S.J.; Kim, J.H.; Park, B.C.; Tonks, N.K.; Ryu, S.E.; Kim, S.J.
Crystal structure of ED-Eya2: insight into dual roles as a protein tyrosine phosphatase and a transcription factor
FASEB J.
24
560-569
2010
Homo sapiens (O00167), Homo sapiens
Manually annotated by BRENDA team
Brandao, T.A.; Hengge, A.C.; Johnson, S.J.
Insights into the reaction of protein tyrosine phosphatase 1B. Crystal structures for transition-state analogs of both catalytic steps
J. Biol. Chem.
285
15874-15883
2010
Homo sapiens (P18031)
Manually annotated by BRENDA team
Yuan, C.; Lu, L.; Gao, X.; Wu, Y.; Guo, M.; Li, Y.; Fu, X.; Zhu, M.
Ternary oxovanadium(IV) complexes of ONO-donor Schiff base and polypyridyl derivatives as protein tyrosine phosphatase inhibitors: synthesis, characterization, and biological activities
J. Biol. Inorg. Chem.
14
841-851
2009
Homo sapiens
Manually annotated by BRENDA team
Fang, L.; Zhang, H.; Cui, W.; Ji, M.
Studies of the mechanism of selectivity of protein tyrosine phosphatase 1B (PTP1B) bidentate inhibitors using molecular dynamics simulations and free energy calculations
J. Chem. Inf. Model.
48
2030-2041
2008
Homo sapiens
Manually annotated by BRENDA team
Na, M.; Kim, B.Y.; Osada, H.; Ahn, J.S.
Inhibition of protein tyrosine phosphatase 1B by lupeol and lupenone isolated from Sorbus commixta
J. Enzyme Inhib. Med. Chem.
24
1056-1059
2009
Homo sapiens
Manually annotated by BRENDA team
Krishnamurthy, D.; Karver, M.R.; Fiorillo, E.; Orru, V.; Stanford, S.M.; Bottini, N.; Barrios, A.M.
Gold(I)-mediated inhibition of protein tyrosine phosphatases: a detailed in vitro and cellular study
J. Med. Chem.
51
4790-4795
2008
Homo sapiens, Yersinia enterolytica
Manually annotated by BRENDA team
Price, K.A.; Caragounis, A.; Paterson, B.M.; Filiz, G.; Volitakis, I.; Masters, C.L.; Barnham, K.J.; Donnelly, P.S.; Crouch, P.J.; White, A.R.
Sustained activation of glial cell epidermal growth factor receptor by bis(thiosemicarbazonato) metal complexes is associated with inhibition of protein tyrosine phosphatase activity
J. Med. Chem.
52
6606-6620
2009
Homo sapiens
Manually annotated by BRENDA team
Xi, G.; Shen, X.; Clemmons, D.R.
p66shc negatively regulates insulin-like growth factor I signal transduction via inhibition of p52shc binding to Src homology 2 domain-containing protein tyrosine phosphatase substrate-1 leading to impaired growth factor receptor-bound protein-2 membrane
Mol. Endocrinol.
22
2162-2175
2008
Homo sapiens
Manually annotated by BRENDA team
Bae, D.; Camilli, T.C.; Chun, G.; Lal, M.; Wright, K.; OBrien, T.J.; Patierno, S.R.; Ceryak, S.
Bypass of hexavalent chromium-induced growth arrest by a protein tyrosine phosphatase inhibitor: enhanced survival and mutagenesis
Mutat. Res.
660
40-46
2009
Homo sapiens
Manually annotated by BRENDA team
Rodriguez-Ubreva, F.J.; Cariaga-Martinez, A.E.; Cortes, M.A.; Romero-De Pablos, M.; Ropero, S.; Lopez-Ruiz, P.; Colas, B.
Knockdown of protein tyrosine phosphatase SHP-1 inhibits G1/S progression in prostate cancer cells through the regulation of components of the cell-cycle machinery
Oncogene
29
345-355
2010
Homo sapiens
Manually annotated by BRENDA team
Dao, T.T.; Nguyen, P.H.; Thuong, P.T.; Kang, K.W.; Na, M.; Ndinteh, D.T.; Mbafor, J.T.; Oh, W.K.
Pterocarpans with inhibitory effects on protein tyrosine phosphatase 1B from Erythrina lysistemon Hutch
Phytochemistry
70
2053-2057
2009
Homo sapiens
Manually annotated by BRENDA team
Wang, V.; Davis, D.A.; Veeranna, R.P.; Haque, M.; Yarchoan, R.
Characterization of the activation of protein tyrosine phosphatase, receptor-type, Z polypeptide 1 (PTPRZ1) by hypoxia inducible factor-2 alpha
PLoS ONE
5
e9641
2010
Homo sapiens
Manually annotated by BRENDA team
Zhao, Y.; Zhang, X.; Guda, K.; Lawrence, E.; Sun, Q.; Watanabe, T.; Iwakura, Y.; Asano, M.; Wei, L.; Yang, Z.; Zheng, W.; Dawson, D.; Willis, J.; Markowitz, S.D.; Satake, M.; Wang, Z.
Identification and functional characterization of paxillin as a target of protein tyrosine phosphatase receptor T
Proc. Natl. Acad. Sci. USA
107
2592-2597
2010
Homo sapiens
Manually annotated by BRENDA team
Ren, L.; Chen, X.; Luechapanichkul, R.; Selner, N.G.; Meyer, T.M.; Wavreille, A.S.; Chan, R.; Iorio, C.; Zhou, X.; Neel, B.G.; Pei, D.
Substrate specificity of protein tyrosine phosphatases 1B, RPTPalpha, SHP-1, and SHP-2
Biochemistry
50
2339-2356
2011
Homo sapiens
Manually annotated by BRENDA team
Chia, J.Y.; Gajewski, J.E.; Xiao, Y.; Zhu, H.J.; Cheng, H.C.
Unique biochemical properties of the protein tyrosine phosphatase activity of PTEN-demonstration of different active site structural requirements for phosphopeptide and phospholipid phosphatase activities of PTEN
Biochim. Biophys. Acta
1804
1785-1795
2010
Homo sapiens
Manually annotated by BRENDA team
Liu, Z.; Lee, W.; Kim, S.N.; Yoon, G.; Cheon, S.H.
Design, synthesis, and evaluation of bromo-retrochalcone derivatives as protein tyrosine phosphatase 1B inhibitors
Bioorg. Med. Chem. Lett.
21
3755-3758
2011
Homo sapiens
Manually annotated by BRENDA team
Chen, V.L.; Bishop, A.C.
Chemical rescue of protein tyrosine phosphatase activity
Chem. Commun. (Camb. )
46
637-639
2010
Homo sapiens
Manually annotated by BRENDA team
Yu, X.; Chen, M.; Zhang, S.; Yu, Z.H.; Sun, J.P.; Wang, L.; Liu, S.; Imasaki, T.; Takagi, Y.; Zhang, Z.Y.
Substrate specificity of lymphoid-specific tyrosine phosphatase (Lyp) and identification of Src kinase-associated protein of 55 kDa homolog (SKAP-HOM) as a Lyp substrate
J. Biol. Chem.
286
30526-30534
2011
Homo sapiens
Manually annotated by BRENDA team
Ferrari, E.; Tinti, M.; Costa, S.; Corallino, S.; Nardozza, A.P.; Chatraryamontri, A.; Ceol, A.; Cesareni, G.; Castagnoli, L.
Identification of new substrates of the protein-tyrosine phosphatase PTP1B by Bayesian integration of proteome evidence
J. Biol. Chem.
286
4173-4185
2011
Homo sapiens
Manually annotated by BRENDA team
Wang, W.; Liu, L.; Song, X.; Mo, Y.; Komma, C.; Bellamy, H.D.; Zhao, Z.J.; Zhou, G.W.
Crystal structure of human protein tyrosine phosphatase SHP-1 in the open conformation
J. Cell. Biochem.
112
2062-2071
2011
Homo sapiens
Manually annotated by BRENDA team
Harris, L.K.; Frumm, S.M.; Bishop, A.C.
A general assay for monitoring the activities of protein tyrosine phosphatases in living eukaryotic cells
Anal. Biochem.
435
99-105
2013
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Mitra, A.; Sasikumar, K.; Parthasaradhi, B.V.; Radha, V.
The tyrosine phosphatase TC48 interacts with and inactivates the oncogenic fusion protein BCR-Abl but not cellular Abl
Biochim. Biophys. Acta
1832
275-284
2013
Homo sapiens (P17706), Homo sapiens
Manually annotated by BRENDA team
Meng, F.G.; Zhang, Z.Y.
Redox regulation of protein tyrosine phosphatase activity by hydroxyl radical
Biochim. Biophys. Acta
1834
464-469
2013
Homo sapiens
Manually annotated by BRENDA team
He, H.B.; Gao, L.X.; Deng, Q.F.; Ma, W.P.; Tang, C.L.; Qiu, W.W.; Tang, J.; Li, J.Y.; Li, J.; Yang, F.
Synthesis and biological evaluation of 4,4-dimethyl lithocholic acid derivatives as novel inhibitors of protein tyrosine phosphatase 1B
Bioorg. Med. Chem. Lett.
22
7237-7242
2012
Homo sapiens
Manually annotated by BRENDA team
Wang, Z.; Liu, Z.; Lee, W.; Kim, S.N.; Yoon, G.; Cheon, S.H.
Design, synthesis and docking study of 5-(substituted benzylidene)thiazolidine-2,4-dione derivatives as inhibitors of protein tyrosine phosphatase 1B
Bioorg. Med. Chem. Lett.
24
3337-3340
2014
Homo sapiens (P18031)
Manually annotated by BRENDA team
Zhi, Y.; Gao, L.X.; Jin, Y.; Tang, C.L.; Li, J.Y.; Li, J.; Long, Y.Q.
4-Quinolone-3-carboxylic acids as cell-permeable inhibitors of protein tyrosine phosphatase 1B
Bioorg. Med. Chem.
22
3670-3683
2014
Homo sapiens
Manually annotated by BRENDA team
Bellomo, E.; Massarotti, A.; Hogstrand, C.; Maret, W.
Zinc ions modulate protein tyrosine phosphatase 1B activity
Metallomics
6
1229-1239
2014
Homo sapiens (P18031), Homo sapiens
Manually annotated by BRENDA team
Yin, J.P.; Tang, C.L.; Gao, L.X.; Ma, W.P.; Li, J.Y.; Li, Y.; Li, J.; Nan, F.J.
Design and synthesis of paracaseolide A analogues as selective protein tyrosine phosphatase 1B inhibitors
Org. Biomol. Chem.
12
3441-3445
2014
Homo sapiens
Manually annotated by BRENDA team
Uddin, M.N.; Sharma, G.; Yang, J.L.; Choi, H.S.; Lim, S.I.; Kang, K.W.; Oh, W.K.
Oleanane triterpenes as protein tyrosine phosphatase 1B (PTP1B) inhibitors from Camellia japonica
Phytochemistry
103
99-106
2014
Homo sapiens
Manually annotated by BRENDA team
Li, S.; Zhang, J.; Lu, S.; Huang, W.; Geng, L.; Shen, Q.; Zhang, J.
The mechanism of allosteric inhibition of protein tyrosine phosphatase 1B
PLoS ONE
9
e97668
2014
Homo sapiens (P18031)
Manually annotated by BRENDA team
Bakke, J.; Haj, F.G.
Protein-tyrosine phosphatase 1B substrates and metabolic regulation
Semin. Cell Dev. Biol.
37
58-65
2015
Homo sapiens
Manually annotated by BRENDA team
Tanase, C.A.
Histidine domain-protein tyrosine phosphatase interacts with Grb2 and GrpL
PLoS ONE
5
e14339
2010
Homo sapiens
Manually annotated by BRENDA team
Lountos, G.; Kurussi, S.; Zhao, B.; Dyas, B.; Burke, T.J.; Ulrich, R.; Waugh, D.
High-resolution crystal structures of the D1 and D2 domains of protein tyrosine phosphatase epsilon for structure-based drug design
Acta Crystallogr. Sect. D
74
1015-1026
2018
Homo sapiens (P23469), Homo sapiens
Manually annotated by BRENDA team
Bishop, A.C.
A missense methionine mutation augments catalytic activity but reduces thermal stability in two protein tyrosine phosphatases
Biochem. Biophys. Res. Commun.
481
153-158
2016
Homo sapiens (P29350), Homo sapiens
Manually annotated by BRENDA team
Srinivasan, B.; Marks, H.; Mitra, S.; Smalley, D.M.; Skolnick, J.
Catalytic and substrate promiscuity distinct multiple chemistries catalysed by the phosphatase domain of receptor protein tyrosine phosphatase
Biochem. J.
473
2165-2177
2016
Homo sapiens (P23468), Homo sapiens (Q15256)
Manually annotated by BRENDA team
Tabernero, L.; Woodman, P.
Dissecting the role of His domain protein tyrosine phosphatase/PTPN23 and ESCRTs in sorting activated epidermal growth factor receptor to the multivesicular body
Biochem. Soc. Trans.
46
1037-1046
2018
Saccharomyces cerevisiae, Homo sapiens (Q9H3S7)
Manually annotated by BRENDA team
Hjortness, M.; Riccardi, L.; Hongdusit, A.; Ruppe, A.; Zhao, M.; Kim, E.; Zwart, P.; Sankaran, B.; Arthanari, H.; Sousa, M.; De Vivo, M.; Fox, J.
Abietane-type diterpenoids inhibit protein tyrosine phosphatases by stabilizing an inactive enzyme conformation
Biochemistry
57
5886-5896
2018
Homo sapiens (P18031)
-
Manually annotated by BRENDA team
Hengge, A.C.
Kinetic isotope effects in the characterization of catalysis by protein tyrosine phosphatases
Biochim. Biophys. Acta
1854
1768-1775
2015
Yersinia sp., Homo sapiens (P18031), Homo sapiens (P51452), Homo sapiens (Q9BVJ7), Mus musculus (P35821), Schizosaccharomyces pombe (P41893), Schizosaccharomyces pombe ATCC 24843 (P41893)
Manually annotated by BRENDA team
Zhang, L.; Ge, Y.; Song, H.M.; Wang, Q.M.; Zhou, C.H.
Design, synthesis of novel azolyl flavonoids and their protein tyrosine Phosphatase-1B inhibitory activities
Bioorg. Chem.
80
195-203
2018
Homo sapiens (P18031)
Manually annotated by BRENDA team
Peti, W.; Page, R.
Strategies to make protein serine/threonine (PP1, calcineurin) and tyrosine phosphatases (PTP1B) druggable Achieving specificity by targeting substrate and regulatory protein interaction sites
Bioorg. Med. Chem.
23
2781-2785
2015
Homo sapiens (P18031)
Manually annotated by BRENDA team
Korntner, S.; Pomorski, A.; Krezel, A.; Bishop, A.C.
Optimized allosteric inhibition of engineered protein tyrosine phosphatases with an expanded palette of biarsenical small molecules
Bioorg. Med. Chem.
26
2610-2620
2018
Homo sapiens (P18031)
Manually annotated by BRENDA team
Ge, L.; Li, K.S.; Li, M.M.; Xiao, P.; Hou, X.B.; Chen, X.; Liu, H.D.; Lin, A.; Yu, X.; Ren, G.J.; Fang, H.; Sun, J.P.
Identification of a benzo imidazole thiazole derivative as the specific irreversible inhibitor of protein tyrosine phosphatase
Bioorg. Med. Chem. Lett.
26
4795-4798
2016
Homo sapiens (P54829), Homo sapiens
Manually annotated by BRENDA team
Guerra, L.L.; Faccinetti, N.I.; Trabucchi, A.; Rovitto, B.D.; Sabljic, A.V.; Poskus, E.; Iacono, R.F.; Valdez, S.N.
Novel prokaryotic expression of thioredoxin-fused insulinoma associated protein tyrosine phosphatase 2 (IA-2), its characterization and immunodiagnostic application
BMC Biotechnol.
16
84
2016
Homo sapiens (Q16849)
Manually annotated by BRENDA team
Abdjul, D.B.; Yamazaki, H.; Kanno, S.I.; Kirikoshi, R.; Tomizawa, A.; Takahashi, O.; Maarisit, W.; Losung, F.; Rotinsulu, H.; Wewengkang, D.S.; Sumilat, D.A.; Kapojos, M.M.; Namikoshi, M.
Absolute structures of wedelolide derivatives and structure-activity relationships of protein tyrosine phosphatase 1B inhibitory ent-kaurene diterpenes from aerial parts of Wedelia spp. collected in Indonesia and Japan
Chem. Pharm. Bull.
66
682-687
2018
Homo sapiens (P18031), Homo sapiens
Manually annotated by BRENDA team
Ottana, R.; Paoli, P.; Nass, A.; Lori, G.; Cardile, V.; Adornato, I.; Rotondo, A.; Graziano, A.C.E.; Wolber, G.; Maccari, R.
Discovery of 4-[(5-arylidene-4-oxothiazolidin-3-yl)methyl]benzoic acid derivatives active as novel potent allosteric inhibitors of protein tyrosine phosphatase 1B in silico studies and in vitro evaluation as insulinomimetic and anti-inflammatory agents
Eur. J. Med. Chem.
127
840-858
2017
Homo sapiens (P18031)
Manually annotated by BRENDA team
Li, H.; Yang, D.; Ning, S.; Xu, Y.; Yang, F.; Yin, R.; Feng, T.; Han, S.; Guo, L.; Zhang, P.; Qu, W.; Guo, R.; Song, C.; Xiao, P.; Zhou, C.; Xu, Z.; Sun, J.P.; Yu, X.
Switching of the substrate specificity of protein tyrosine phosphatase N12 by cyclin-dependent kinase 2 phosphorylation orchestrating 2 oncogenic pathways
FASEB J.
32
73-82
2018
Homo sapiens (Q05209), Homo sapiens
Manually annotated by BRENDA team
Hon, J.; Hwang, M.S.; Charnetzki, M.A.; Rashed, I.J.; Brady, P.B.; Quillin, S.; Makinen, M.W.
Kinetic characterization of the inhibition of protein tyrosine phosphatase-1B by vanadyl (VO2+) chelates
J. Biol. Inorg. Chem.
22
1267-1279
2017
Homo sapiens (P18031)
Manually annotated by BRENDA team
Sarabia-Sanchez, M.J.; Trejo-Soto, P.J.; Velazquez-Lopez, J.M.; Carvente-Garcia, C.; Castillo, R.; Hernandez-Campos, A.; Avitia-Dominguez, C.; Enriquez-Mendiola, D.; Sierra-Campos, E.; Valdez-Solana, M.; Salas-Pacheco, J.M.; Tellez-Valencia, A.
Novel mixed-type inhibitors of protein tyrosine phosphatase 1B. Kinetic and computational studies
Molecules
22
2262-2278
2017
Homo sapiens (P18031)
Manually annotated by BRENDA team
Jiang, H.; Sui, Y.; Cui, Y.; Lin, P.; Li, W.; Xing, S.; Wang, D.; Hu, M.; Fu, X.
Expression, purification, and characterization of human osteoclastic protein-tyrosine phosphatase catalytic domain in Escherichia coli
Protein Expr. Purif.
107
7-12
2015
Homo sapiens (P23469), Homo sapiens
Manually annotated by BRENDA team
Parker, E.J.
The molecular basis for the substrate specificity of protein tyrosine phosphatase PTPN3
Structure
23
608-609
2015
Homo sapiens (P26045)
Manually annotated by BRENDA team
Chen, K.E.; Li, M.Y.; Chou, C.C.; Ho, M.R.; Chen, G.C.; Meng, T.C.; Wang, A.H.
Substrate specificity and plasticity of FERM-containing protein tyrosine phosphatases
Structure
23
653-664
2015
Homo sapiens (P18031), Homo sapiens (P26045), Homo sapiens (Q12923), Homo sapiens (Q15678), Homo sapiens (Q16825)
Manually annotated by BRENDA team