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Information on EC 3.4.24.86 - ADAM 17 endopeptidase and Organism(s) Homo sapiens and UniProt Accession P78536
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3.4.24.86 ADAM 17 endopeptidaseSpecify your search results
Word Map
- 3.4.24.86
- adam10
- ectodomains
- sheddase
- metalloproteinases
- endothelial
-
phorbol
- sirna
-
amyloid
- egf
- alzheimer
- notch
- angiotensin
-
membrane-anchored
- arthritis
- amphiregulin
- ace2
- hb-egf
- hydroxamate
- timp-3
-
heparin-binding
- l-selectin
-
trans-signaling
-
angiotensin-converting
- covid-19
- alpha-secretase
- mmp-2
- sars-cov-2
-
egf-like
-
juxtamembrane
- medicine
- prodomains
- furin
-
secretase
- tgf-alpha
-
membrane-proximal
- tmprss2
-
sil-6r
-
non-amyloidogenic
- cxcl16
- rhomboid
- epiregulin
- gamma-secretase
- neuregulins
- molecular biology
- adamalysins
-
metzincins
-
membrane-tethered
- fractalkine
- betacellulin
- marimastat
- analysis
-
egfr-dependent
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
adam17, adam-17, tnf-alpha converting enzyme, tace/adam17, a disintegrin and metalloproteinase 17, tumor necrosis factor-alpha converting enzyme, a disintegrin and metalloprotease 17, tumor necrosis factor-alpha-converting enzyme, metalloproteinase adam17, tumor necrosis factor alpha-converting enzyme, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADAM17
-
ADAM17
-
-
ADAM17 proteinase
-
-
-
-
metalloprotease TACE
-
-
-
-
metalloproteinase ADAM17
-
-
-
-
pro tumor necrosis factor cleavage enzyme
-
-
-
-
pro-tumor necrosis factor-alpha-processing enzyme
-
-
-
-
proteinase, pro-tumor necrosis factor (9CI)
-
-
-
-
TACE
TACE proteinase
-
-
-
-
TNF-alpha convertase
-
-
-
-
TNF-alpha converting enzyme
TNF-alpha processing protease
-
-
-
-
tumor necrosis factor alpha convertase
-
-
-
-
tumor necrosis factor alpha-converting enzyme
tumor necrosis factor-alpha converting enzyme
TACE
-
-
-
-
TACE
-
-
TNF-alpha converting enzyme
-
-
-
-
TNF-alpha converting enzyme
-
-
tumor necrosis factor alpha-converting enzyme
-
-
-
-
tumor necrosis factor-alpha converting enzyme
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
151769-16-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
amyloid precursor protein + H2O
soluble amyloid precursor protein alpha fragment + C83
-
-
-
?
CD16 + H2O
?
substrates CD16a and CD16b are IgG Fc receptors expressed by human natural killer cells and neutrophils, respectively. Substrates contain three separate cleavage sites in close proximity at P1/P1' positions Ala195/Val196, Val196/Ser197, and Thr198/Ile199, revealing a membrane proximal cleavage region in CD16. Mutation S197P effectively blocks CD16a and CD16b cleavage in cell-based assays. Mutant CD16a/S197P is resistant to cleavage when expressed in cells. The S197P mutation does not disrupt IgG binding by the receptor or its activation of NK92 cells by antibody-treated tumor cells
-
-
?
CD16b + H2O
?
human IgG Fc receptor CD16, i.e. FcgammaRIII. CD16b plasma levels are significantly decreased in patients administered a selective inhibitor targeting the metalloproteases ADAM10 and ADAM17. Inhibition of ADAM17 significantly blocks the cleavage of CD16b following neutrophil activation and apoptosis
-
-
?
cell surface VEGF receptor Flt + H2O
?
-
release of an N-terminal extracellular fragment which can antagonize the effects of vascular endothelial growth factor, substrate can be cleaved to release an N-terminal extracellular fragment. Overexpression of ADAM10, EC 3.4.24.81, and ADAM17 increase cleavage while knockdown of ADAM10 and ADAM17 reduce N-terminal cleavage
-
?
CSF-1 receptor + H2O
?
TACE cleaves the receptor between residues Gln503 and Ser504. Replacement of fourteen residues at the end of the CSF-1 extracellular domain blocks TACE cleavage
-
-
?
Glu(EDANS)-Pro-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser(4O-(beta-D-Gal-(1->3)-alpha-D-GalNAc))-Ser-Lys(DABCYL) + H2O
Glu(EDANS)-Pro-Leu-Ala-Gln-Ala + Val-Arg-Ser-Ser(4O-(beta-D-Gal-(1->3)-alpha-D-GalNAc))-Ser-Lys(DABCYL)
-
-
-
?
Glu(EDANS)-Pro-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser-Ser-Lys(DABCYL) + H2O
Glu(EDANS)-Pro-Leu-Ala-Gln-Ala + Val-Arg-Ser-Ser-Ser-Lys(DABCYL)
-
-
-
?
intercellular adhesion molecule 1 + H2O
soluble intercellular adhesion molecule 1 + ?
-
-
-
?
MHC class I polypeptide-related sequence A + H2O
soluble MHC class I polypeptide-related sequence A + ?
-
-
-
?
PLAAAVFSS + H2O
PLAAA + VFSS
mutant peptide derived from TNF-alpha, very poor substrate
-
-
?
PLAMAVMSS + H2O
PLAMA + VMSS
mutant peptide derived from TNF-alpha, very poor substrate
-
-
?
Pro-BTC + H2O
?
the cleavage site by ADAM17 is CVVA31-/-DGNS, N-linked glycosylation site is Asn34
-
-
?
pro-EPR + H2O
?
the cleavage site by ADAM17 is DNPR59-/-VAQV, N-linked glycosylation site is Asn47
-
-
?
pro-HB-EGF + H2O
?
the cleavage site by ADAM17 is RKVR62-/-DLQE, O-linked glycosylation sites are Thr75 and Thr85
-
-
?
pro-TGFalpha + H2O
?
the cleavage site by ADAM17 is VAAA39-/-VVSH, N-linked glycosylation site is Asn25
-
-
?
pro-tumor necrosis factor alpha + H2O
?
with and without a glycan moiety attached, glycosylation increases the enzyme activity. The cleavage site of TNFalpha by ADAM17 is only four residues away from a glycosylated residues, whereas glycosylation occurs 14 residues away from the TGFalpha cleavage site. Cleavage site for ADAM-17 is LAQA76-/-VRSS, O-linked glycosylation site is Ser80
-
-
?
proheparin-binding EGF-like growth factor + H2O
?
-
cleavage occurs between residues RKVR62-DLQE. Substrate shows O-linked glycosylation 13 residues apart from scissile bond
-
?
proTNF-alpha + H2O
soluble TNF-alpha
-
cleavage occurs between residues LAQA76-VRSS. Substrate shows O-linked glycosylation 4 residues apart from scissile bond
-
?
protransforming growth factor alpha + H2O
?
-
cleavage occurs between residues AAA39-VVSH. Substrate shows N-linked glycosylation 14 residues apart from scissile bond
-
?
S80-glycosylated (EDANS)-ELAQAVRSSSRK-(DABCYL) + H2O
?
TNF-alpha derived substrate
-
-
?
S80-glycosylated (EDANS)-EPLAQAVRSSSK-(DABCYL) + H2O
?
TNF-alpha derived substrate
-
-
?
TGF-alpha + H2O
?
ADAM17, but not related ADAM10, is required for amphiregulin, TGF-alpha, and TNFR1 shedding
-
-
?
transferrin receptor protein 1 + H2O
?
-
cleavage occurs between residues ECER100-LAGT. Substrate shows O-linked glycosylation 4 residues apart from scissile bond
-
?
TRP1 + H2O
?
the cleavage site by ADAM17 is ECER100-/-LAGT, O-linked glycosylation sites are: Thr104, Asn251, Asn317, Asn727
-
-
?
tumor necrosis factor receptor 1 + H2O
?
ADAM17, but not related ADAM10, is required for amphiregulin, TGF-alpha, and TNFR1 shedding
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-KSPLAQA-VRSSSRK(2,4-dinitrophenyl)-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Ala-Gln-Ala-Val-[N-3-[2,4-dinitrophenyl]-L-2,3-diaminopropionyl]-Arg-Ser-Ser-Ser-Arg-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-SPLAQAVRSSSRK-(2,4-dinitrophenyl)-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Ser-Pro-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser-Ser-Arg-Lys(Dnp)-NH2 + H2O
?
-
-
-
-
?
4',5'-dimethoxyfluoresceinyl-SPLAQAVRSSSR-cys(4-(3-succinimid-1-yl)fluorescein)-NH2 + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-(yl)acetyl-Pro-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser-Ser-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Arg-NH2 + H2O
?
-
an internally quenched peptide substrate is used
-
-
?
7-methoxycoumarin-4-yl-acetyl-Lys-Pro-Leu-Gly-Pro-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg + H2O
?
-
-
-
-
?
heparin-binding EGF-like growth factor + H2O
?
-
ADAM17 may be involved in heparin-binding EGF-like growth factor cleavage in response to injury
-
-
?
LAQAVRSSSR + H2O
?
-
fluorimetric assay for TACE, fluorogenic substrate, a 10-amino-acid peptide capped with an o-aminobenzoyl group on the N-terminal end and with a 3-(2,4-dinitrophenyl)-L-2,3-diaminopropionic amide group on the C-terminal end, enzymatic conversion of the substrate results in a fluorescence enhancement of 11fold
-
-
?
Mca-PLAQAV-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl amide-RSSSR-NH2 + H2O
?
-
-
-
-
?
MHC class I-related chain + H2O
?
-
i.e. transmembrane protein expressed in pathological conditions, ligands for the activating receptor NKG2D found on cytotoxic lymphocytes. The recruitment of both enzyme and substrate to detergent-resistant membrane microdomains is crucial for efficient proteolysis
-
-
?
NH2-LAQAVRSSSR-OH + H2O
?
-
uncapped counterpart of the fluorogenic substrate
-
-
?
Notch 1 + H2O
?
-
ADAM17 is required for Notch1 receptor proteolysis in NSCLC cells in vitro and in vivo
-
-
?
o-aminobenzoyl-LAQAFRSSSR-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl amide + H2O
o-aminobenzoyl-LAQA + FRSSSR-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl amide
-
enzymatic cleavage 22%
-
-
?
o-aminobenzoyl-LAQAIRSSSR-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl amide + H2O
o-aminobenzoyl-LAQA + IRSSSR-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl amide
-
enzymatic cleavage 66%
-
-
?
o-aminobenzoyl-LAQALRSSSR-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl amide + H2O
o-aminobenzoyl-LAQA + LRSSSR-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl amide
-
enzymatic cleavage 92%
-
-
?
o-aminobenzoyl-LAQAVRSSSR-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl amide + H2O
o-aminobenzoyl-LAQA + VRSSSR-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl amide
-
enzymatic cleavage 90%
-
-
?
o-aminobenzoyl-LAQFVRSSSR-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl amide + H2O
o-aminobenzoyl-LAQF + RSSSR-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl amide
-
enzymatic cleavage 39%
-
-
?
o-aminobenzoyl-LAQGVRSSSR-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl amide + H2O
o-aminobenzoyl-LAQG + VRSSSR-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl amide
-
enzymatic cleavage 11%
-
-
?
o-aminobenzoyl-LAQLVRSSSR-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl amide + H2O
o-aminobenzoyl-LAQL + VRSSSR-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl amide
-
enzymatic cleavage 34%
-
-
?
o-aminobenzoyl-LAQVARSSSR-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl amide + H2O
o-aminobenzoyl-LAQVA + RSSSR-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl amide
-
enzymatic cleavage 19%
-
-
?
pro amphiregulin + H2O
?
-
TACE is capable of cleaving both N- and C-terminal sites in the pro-amphiregulin ectodomain
-
-
?
pro heparin-binding epidermal growth factor + H2O
?
-
purified soluble TACE cleaves a single site in the juxtamembrane stalk of pro heparin-binding epidermal growth factor
-
-
?
proTNF-alpha + H2O
soluble TNF-alpha + 9000 Da membrane-bound fragment of TNF-alpha
-
-
-
-
?
amphiregulin + H2O
?
ADAM17, but not related ADAM10, is required for amphiregulin, TGF-alpha, and TNFR1 shedding
-
-
?
interleukin-6 receptor + H2O
?
the cleavage site by ADAM17 is LPVQ357-/-DSSV, N-linked glycosylation sites are: Asn55, Asn93, Asn221, Asn350
-
-
?
syndecan-1 + H2O
?
both ADAM10 and ADAM17 contribute to SDC1 shedding
-
-
?
Alzheimer's disease amyloid precursor protein + H2O
?
-
TACE is involved in shedding of Alzheimer's disease amyloid precursor protein
-
-
?
beta-amyloid precursor protein + H2O
?
-
Alzheimer amyloid precursor protein
-
-
?
CD30 + H2O
?
-
shedding of CD30 upon inhibition of the proteasome is catalyzed by ADAM17
-
-
?
glycoprotein Ibalpha + H2O
?
-
ADAM17 is the key enzyme mediating shedding of glycoprotein Ibalpha
-
-
?
L-selectin + H2O
?
-
regulates plasma membrane composition and releases soluble signaling molecules and receptors from cells
-
-
?
p75 tumour necrosis factor receptor + H2O
?
-
-
-
-
?
preadipocyte factor 1 + H2O
?
-
TACE is the major protease responsible for conversion of membrane-bound Pref-1 to the biologically active diffusible form
-
-
?
proTNF-alpha + H2O
soluble TNF-alpha
-
-
-
-
?
proTNF-alpha + H2O
soluble TNF-alpha
-
-
638993, 638994, 638995, 638996, 638997, 638998, 638999, 639000, 639001, 639002, 639003, 639004, 639005, 639006, 639007, 639008, 639009, 639010, 639011, 639012, 639013, 677450, 679641, 681665, 682211, 682570, 682629, 719165
-
-
?
proTNF-alpha + H2O
soluble TNF-alpha
-
-
release of proTNFalpha from cellular membranes
?
proTNF-alpha + H2O
soluble TNF-alpha
-
-
release of membrane-bound TNF-alpha
?
proTNF-alpha + H2O
soluble TNF-alpha
-
membrane-bound tumor necrosis factor alpha undergoes proteolysis
-
-
?
receptor tyrosine kinase c-Kit + H2O
?
-
ADAM-17 controls mast cell survival by regulating shedding and surface expression of c-Kit
-
-
?
TNF-alpha + H2O
soluble TNF-alpha
-
membrane-bound tumor necrosis factor alpha undergoes proteolysis
-
-
?
transforming growth factor alpha + H2O
?
-
-
-
-
?
transforming growth factor alpha + H2O
?
-
-
638993, 638994, 638995, 638996, 638997, 638998, 638999, 639000, 639001, 639002, 639003, 639004, 639005, 639006, 639007, 639008, 639009, 639010, 639011, 639012, 639013
-
-
?
additional information
?
-
affinity for TACE is measured by an internally quenched peptide substrate with its sequence derived from the pro-TNF-alpha cleavage site using a catalytic domain of recombinant human TACE enzyme
-
-
?
additional information
?
-
analysis of ADAM cognate substrates reveals that glycosylation is often present in the vicinity of the scissile bond
-
-
?
additional information
?
-
high throughput screening assays are developed using glycosylated and non-glycosylated substrate, and positional scanning, substrate specificity, overview
-
-
?
additional information
?
-
mutations at the P2 site and the P2' site of the substrate peptide largely affect the peptide cleavage efficiency in the enzymaticassay. The P2/P2'sites may affect the efficiency of the conformation search for the correct peptide orientation, which in turn affects the substrate cleavage efficiency. Peptide PRYEA?YKMG is not a substrate
-
-
?
additional information
?
-
noncatalytic domains of ADAM17 do not directly bind to TNF-alpha derived substrates used but affect the binding nevertheless, most likely because of steric hindrance. Noncatalytic domains of ADAM17 affect the size/shape of the carbohydrate-binding pocket contained within the catalytic domain of ADAM17. Protease shows significantly decreased activity when the TNF-alpha-derived sequence is induced into alpha-helical conformation
-
-
?
additional information
?
-
-
TACE is a multidomain, type I transmembrane protein, contains a pro-domain which is removed by proteolysis to generate the active enzyme and a zinc-dependent metalloprotease catalytic domain, TACE cleaves peptides containing the sequence of the processing site at the physiolocically relevant peptide bond
-
-
?
additional information
?
-
TACE is a multidomain, type I transmembrane protein, contains a pro-domain which is removed by proteolysis to generate the active enzyme and a zinc-dependent metalloprotease catalytic domain, TACE cleaves peptides containing the sequence of the processing site at the physiolocically relevant peptide bond
-
-
?
additional information
?
-
-
o-aminobenzoyl-LAQVARSSSR-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl diaminopropionic amide is no substrate
-
-
?
additional information
?
-
-
4-dinitrophenyl)-L-2,3-diaminopropionyl diaminopropionic amide-PChaGC(Me)HK(NMA)-NH2 is not cleaved at all by TACE
-
-
?
additional information
?
-
-
TACE is the only enzyme confirmed to process TNF-alpha in vitro and in vivo
-
-
?
additional information
?
-
-
ectodomain shedding of the hypoxia-induced carbonic anhydrase IX is a metalloprotease-dependent process regulated by TACE/ADAM17
-
-
?
additional information
?
-
-
TACE is not involved in shedding of angiotensin converting enzyme
-
-
?
additional information
?
-
-
TACE may have a role in phorbol myristate acetate-induced shedding of epiregulin
-
-
?
additional information
?
-
-
a comparison of the binding sites of matrix metalloproteinases and tumor necrosis factor-alpha converting enzyme
-
-
?
additional information
?
-
-
protein in the absence of salt or inhibitor shows a rapid and specific autocleavage between residues Y352-V353 which resides within the surrounding sequence TLGLAYVGSPRN
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
amyloid precursor protein + H2O
soluble amyloid precursor protein alpha fragment + C83
-
-
-
?
intercellular adhesion molecule 1 + H2O
soluble intercellular adhesion molecule 1 + ?
-
-
-
?
MHC class I polypeptide-related sequence A + H2O
soluble MHC class I polypeptide-related sequence A + ?
-
-
-
?
Alzheimer's disease amyloid precursor protein + H2O
?
-
TACE is involved in shedding of Alzheimer's disease amyloid precursor protein
-
-
?
glycoprotein Ibalpha + H2O
?
-
ADAM17 is the key enzyme mediating shedding of glycoprotein Ibalpha
-
-
?
Notch 1 + H2O
?
-
ADAM17 is required for Notch1 receptor proteolysis in NSCLC cells in vitro and in vivo
-
-
?
preadipocyte factor 1 + H2O
?
-
TACE is the major protease responsible for conversion of membrane-bound Pref-1 to the biologically active diffusible form
-
-
?
proTNF-alpha + H2O
soluble TNF-alpha + 9000 Da membrane-bound fragment of TNF-alpha
-
-
-
-
?
receptor tyrosine kinase c-Kit + H2O
?
-
ADAM-17 controls mast cell survival by regulating shedding and surface expression of c-Kit
-
-
?
TNF-alpha + H2O
soluble TNF-alpha
-
membrane-bound tumor necrosis factor alpha undergoes proteolysis
-
-
?
additional information
?
-
analysis of ADAM cognate substrates reveals that glycosylation is often present in the vicinity of the scissile bond
-
-
?
additional information
?
-
-
ectodomain shedding of the hypoxia-induced carbonic anhydrase IX is a metalloprotease-dependent process regulated by TACE/ADAM17
-
-
?
additional information
?
-
-
TACE is not involved in shedding of angiotensin converting enzyme
-
-
?
additional information
?
-
-
TACE may have a role in phorbol myristate acetate-induced shedding of epiregulin
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zinc
pronounced diversity in electronic and chemical properties between the catalytic zinc sites of tumor necrosis factor-alpha-converting enzyme and matrix metalloproteinases despite their high structural similarity
Zn2+
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,2S)-1-(3-fluoro-4-[[2-(1-methyl-1H-pyrazol-5-yl)quinolin-4-yl]methoxy]benzyl)-N2-hydroxycyclopropane-1,2-dicarboxamide
-
(1R,2S)-1-(3-fluoro-4-[[2-(methylamino)quinolin-4-yl]methoxy]benzyl)-N2-hydroxycyclopropane-1,2-dicarboxamide
-
(1R,2S)-1-[3-fluoro-4-[(2-morpholin-4-ylquinolin-4-yl)methoxy]benzyl]-N2-hydroxycyclopropane-1,2-dicarboxamide
-
(1R,2S)-1-[3-fluoro-4-[(2-phenylquinolin-4-yl)methoxy]benzyl]-N2-hydroxy-N1,N1-dimethylcyclopropane-1,2-dicarboxamide
-
(1R,2S)-1-[3-fluoro-4-[(2-phenylquinolin-4-yl)methoxy]benzyl]-N2-hydroxycyclopropane-1,2-dicarboxamide
-
(1R,2S)-1-[3-fluoro-4-[(2-pyridin-3-ylquinolin-4-yl)methoxy]benzyl]-N2-hydroxycyclopropane-1,2-dicarboxamide
-
(1R,2S)-1-[3-fluoro-4-[(2-pyrrolidin-1-ylquinolin-4-yl)methoxy]benzyl]-N2-hydroxycyclopropane-1,2-dicarboxamide
-
(1R,2S)-1-[4-[(2-ethylquinolin-4-yl)methoxy]benzyl]-N2-hydroxycyclopropane-1,2-dicarboxamide
-
(1R,2S)-N2-hydroxy-1-[4-[(2-methylquinolin-4-yl)methoxy]benzyl]cyclopropane-1,2-dicarboxamide
-
(1R,2S)-N2-hydroxy-1-[4-[(2-phenylquinolin-4-yl)methoxy]benzyl]-N1-(piperidin-4-ylmethyl)cyclopropane-1,2-dicarboxamide
-
(1R,2S)-N2-hydroxy-1-[4-[(2-phenylquinolin-4-yl)methoxy]benzyl]cyclopropane-1,2-dicarboxamide
-
(1R,2S)-N2-hydroxy-N1,N1-dimethyl-1-[4-[(2-phenylquinolin-4-yl)methoxy]benzyl]cyclopropane-1,2-dicarboxamide
-
(1S,2R)-2-[[(3R)-3-(dimethylamino)pyrrolidin-1-yl]carbonyl]-N-hydroxy-2-[4-[(2-phenylquinolin-4-yl)methoxy]benzyl]cyclopropanecarboxamide
-
(1S,2R)-2-[[(3S)-3-(dimethylamino)pyrrolidin-1-yl]carbonyl]-N-hydroxy-2-[4-[(2-phenylquinolin-4-yl)methoxy]benzyl]cyclopropanecarboxamide
-
(1S,2R)-N-hydroxy-2-[[(2S)-2-(hydroxymethyl)pyrrolidin-1-yl]carbonyl]-2-[4-[(2-phenylquinolin-4-yl)methoxy]benzyl]cyclopropanecarboxamide
-
(1S,2R)-N-hydroxy-2-[[(3S)-3-hydroxypyrrolidin-1-yl]carbonyl]-2-[4-[(2-phenylquinolin-4-yl)methoxy]benzyl]cyclopropanecarboxamide
-
(1S,2S)-2-((S)-cyano(4-((2-phenylquinolin-4-yl)methoxy)phenyl)methyl)-N-hydroxycyclopropanecarboxamide
-
(5R)-4-(2-((1R,3R)-adamantan-1-yl)ethyl)-5-(4-hydroxybenzyl)-1-((2R)-1-(2-(((R)-6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl)-methyl)pyrrolidin-1-yl)-3-(naphthalen-2-yl)propan-2-yl)piperazine-2,3-dione
-
(5S)-1-((S)-1-((S)-2-(((S)-2,3-dioxo-6-propylpiperazin-1-yl)-methyl)pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl)-5-(4-hydroxybenzyl)-4-(2-phenylbutyl)piperazine-2,3-dione
-
(5S)-4-(cyclopentylmethyl)-5-(4-hydroxybenzyl)-1-[(2S)-1-(2-[[(6S)-6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(naphthalen-2-yl)propan-2-yl]piperazine-2,3-dione
90% inhibition at 0.04 mM
(5S)-5-(4-hydroxybenzyl)-1-[(2S)-1-(2-[[(6S)-6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(naphthalen-2-yl)propan-2-yl]-4-[2-(tricyclo[3.3.1.13,7]dec-1-yl)ethyl]piperazine-2,3-dione
95% inhibition at 0.04 mM
(R)-4-(2-((3R,5R,7R)-adamantan-1-yl)ethyl)-1-((S)-1-((S)-2-(((S)-2,3-dioxo-6-propylpiperazin-1-yl)methyl)pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl)-5-(4-hydroxybenzyl)piperazine-2,3-dione
-
(R)-4-(2-((3R,5R,7R)-adamantan-1-yl)ethyl)-1-((S)-1-((S)-2-(((S)-2,3-dioxo-6-propylpiperazin-1-yl)methyl)pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl)-5-(naphthalen-2-ylmethyl)piperazine-2,3-dione
-
(R)-4-(2-((3R,5R,7R)-adamantan-1-yl)ethyl)-1-((S)-1-(4-hydroxyphenyl)-3-((S)-2-(((R)-6-(naphthalen-2-ylmethyl)-2,3-dioxopiperazin-1-yl)methyl)pyrrolidin-1-yl)propan-2-yl)-5-(naphthalen-2-ylmethyl)piperazine-2,3-dione
-
(R)-4-(2-((3R,5R,7R)-adamantan-1-yl)ethyl)-5-(4-hydroxybenzyl)-1-((S)-1-(4-hydroxyphenyl)-3-((S)-2-(((R)-6-(naphthalen-2-ylmethyl)-2,3-dioxopiperazin-1-yl)methyl)pyrrolidin-1-yl)propan-2-yl)-piperazine-2,3-dione
-
(S)-1((R)-1((S)-2-(((S)-6-benzyl-2,3-dioxopiperazin-1-yl)methyl)-pyrrolidin-1-yl)-3-cyclohexylpropan-2-yl)-5-(4-hydroxybenzyl)-4-phenethylpiperazine-2,3-dione
-
(S)-4-((3S,5S,7S)-adamantan-1 -ylmethyl)-1-((S)-1-((S)-2-(((S)-2,3-dioxo-6-propylpiperazin-1-yl)methyl)pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl)-5-(4-hydroxybenzyl)piperazine-2,3-dione
-
(S)-4-((4-(tert-butyl)cyclohexyl)methyl)-1-((S)-1-((S)-2-(((S)-2,3-dioxo-6-propylpiperazin-1-yl)methyl)pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl)-5-(4-hydroxybenzyl)piperazine-2,3-dione
-
(S)-4-(2-((3S,5S,7S)-adamantan-1-yl)ethyl)-1-((S)-1-((S)-2-(((S)-2,3-dioxo-6-propylpiperazin-1-yl)methyl)pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl)-5-(4-hydroxybenzyl)piperazine-2,3-dione
-
(S)-4-(2-((3S,5S,7S)-adamantan-1-yl)ethyl)-1-((S)-1-((S)-2-(((S)-2,3-dioxo-6-propylpiperazin-1-yl)methyl)pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl)-5-(naphthalen-2-ylmethyl)piperazine-2,3-dione
-
(S)-4-(2-((3S,5S,7S)-adamantan-1-yl)ethyl)-1-((S)-1-(4-hydroxyphenyl)-3-((S)-2-(((R)-6-(naphthalen-2-ylmethyl)-2,3-dioxopiperazin-1-yl)methyl)pyrrolidin-1-yl)propan-2-yl)-5-(naphthalen-2-ylmethyl)piperazine-2,3-dione
-
(S)-4-(2-((3S,5S,7S)-adamantan-1-yl)ethyl)-5-(4-hydroxybenzyl)-1-((S)-1-(4-hydroxyphenyl)-3-((S)-2-(((R)-6-(naphthalen-2-ylmethyl)-2,3-dioxopiperazin-1-yl)methyl)pyrrolidin-1-yl)propan-2-yl)-piperazine-2,3-dione
-
(S)-4-(2-((3S,5S,7S)-adamantan-1-yl)ethyl)-5-butyl-1-((S)-1-((S)-2-(((S)-2,3-dioxo-6-propylpiperazin-1-yl)methyl)pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl)piperazine-2,3-dione
-
(S)-4-(2-(adamantan-1-yl)ethyl)-5-butyl-1-((S)-1-(4-hydroxyphenyl)-3-((S)-2-(((R)-6-(naphthalen-2-ylmethyl)-2,3-dioxopiperazin-1-yl)methyl)pyrrolidin-1-yl)propan-2-yl)piperazine-2,3-dione
-
(S)-4-(2-(adamantan-1yl)ethyl)-1-((S)-1-((S)-2-(((S)-6-benzyl-2,3-dioxopiperazin-1-yl)methyl)pyrrolidin-1-yl)-3-phenylpropan-2-yl)-5-(4-hydroxybenzyl)piperazine-2,3-dione
-
(S)-4-(cyclobutylmethyl)-1-((S)-1-((S)-2-(((S)-2,3-dioxo-6-propylpiperazin-1-yl)methyl)pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl)-5-(4-hydroxybenzyl)piperazine-2,3-dione
-
(S)-4-(cyclohexylmethyl)-1-((S)-1-((S)-2-(((S)-2,3-dioxo-6-propylpiperazin-1-yl)methyl)pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl)-5-(4-hydroxybenzyl)piperazine-2,3-dione
-
(S)-4-(cyclopentylmethyl)-1-((S)-1-((S)-2-(((S)-2,3-dioxo-6-propylpiperazin-1-yl)methyl)pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl)-5-(4-hydroxybenzyl)piperazine-2,3-dione
-
(S)-5-benzyl-1-((R)-1-((S)-2-(((S)-6-benzyl-2,3-dioxopiperazin-1-yl)methyl)pyrrolidin-1-yl)-3-cyclohexylpropan-2-yl)-4-phenethylpiperazine-2,3-dione
-
(S)-5-benzyl-1-((R)-1-cyclohexyl-3-((S)-2-(((S)-2,3-dioxo-6-propylpiperazin-1-yl)methyl)pyrrolidin-1-yl)propan-2-yl)-4-phenethylpiperazine-2,3-dione
-
1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(4-hydroxyphenyl)propan-2-yl]-5-(4-hydroxybenzyl)-4-[3-adamantylpropyl]piperazine-2,3-dione
-
1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(naphthalen-2-yl)propan-2-yl]-5-(4-hydroxybenzyl)-4-[3-adamantylpropyl]piperazine-2,3-dione
-
4-(2-butylbenzyl)-1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(4-hydroxyphenyl)propan-2-yl]-5-(4-hydroxybenzyl)piperazine-2,3-dione
-
4-(2-butylbenzyl)-1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(naphthalen-2-yl)propan-2-yl]-5-(4-hydroxybenzyl)piperazine-2,3-dione
-
4-(2-butylbenzyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl]piperazine-2,3-dione
-
4-(2-butylbenzyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(naphthalen-2-yl)propan-2-yl]piperazine-2,3-dione
4-(cyclopentylmethyl)-1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(4-hydroxyphenyl)propan-2-yl]-5-(4-hydroxybenzyl)piperazine-2,3-dione
-
4-(cyclopentylmethyl)-1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(naphthalen-2-yl)propan-2-yl]-5-(4-hydroxybenzyl)piperazine-2,3-dione
-
4-(cyclopentylmethyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl]piperazine-2,3-dione
-
4-(cyclopentylmethyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(naphthalen-2-yl)propan-2-yl]piperazine-2,3-dione
5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl]-4-[3-adamantylpropyl]piperazine-2,3-dione
-
5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl]-4-[3-adamanylpropyl]piperazine-2,3-dione
-
5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(naphthalen-2-yl)propan-2-yl]-4-[3-adamantylpropyl]piperazine-2,3-dione
-
ethyl (1R,2S)-1-[3-bromo-4-[(2-methylquinolin-4-yl)methoxy]benzyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
ethyl (1R,2S)-1-[3-chloro-4-[(2-methylquinolin-4-yl)methoxy]benzyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
ethyl (1R,2S)-1-[3-fluoro-4-[(2-methylquinolin-4-yl)methoxy]benzyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
ethyl (1R,2S)-1-[4-[(2-ethylquinolin-4-yl)methoxy]benzyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
ethyl (1R,2S)-2-(hydroxycarbamoyl)-1-(4-[[2-(2-methylpropyl)quinolin-4-yl]methoxy]benzyl)cyclopropanecarboxylate
-
ethyl (1R,2S)-2-(hydroxycarbamoyl)-1-(4-[[2-(trifluoromethyl)quinolin-4-yl]methoxy]benzyl)cyclopropanecarboxylate
-
ethyl (1R,2S)-2-(hydroxycarbamoyl)-1-[4-[(2-methylquinolin-4-yl)methoxy]benzyl]cyclopropanecarboxylate
-
ethyl (1R,2S)-2-(hydroxycarbamoyl)-1-[4-[(2-phenylpyridin-4-yl)methoxy]benzyl]cyclopropanecarboxylate
-
ethyl (1R,2S)-2-(hydroxycarbamoyl)-1-[4-[(2-phenylquinolin-4-yl)methoxy]benzyl]cyclopropanecarboxylate
-
ethyl (1R,2S)-2-(hydroxycarbamoyl)-1-[4-[(2-pyridin-3-ylquinolin-4-yl)methoxy]benzyl]cyclopropanecarboxylate
-
lomofungin
15% residual activity at 0.0125 mM, 6% residual activity at 0.05 mM, 0.03% residual activity at 0.1 mM
methyl (6S,7S)-7-(hydroxycarbamoyl)-6-(4-phenylpiperazin-1-ylcarbonyl)-5-azaspiro[2.5]octane-5-carboxylate
i.e. INCB7839, selective inhibitor of endopeptidases ADAM-10 and ADAM-17
(1R,2R)-2-(3-phenoxylphenyl)-2-trans-carbomethoxylcyclopropane hydroxamic acid
-
-
(1R,2R)-2-trans-carboisopropoxyl-2-[3-(2-methylquinolin-4-yl)methoxylphenyl]cyclopropane hydroxyamic acid
-
-
(1R,2R)-2-trans-N-benzylaminocarbonyl-2-[3-(2-methylquinolin-4-yl)methoxylphenyl]cyclopropane hydroxyamic acid
-
-
(1R,2R)-2-[3-(3,4-dichlorobenzyloxy)phenyl]-2-trans-carbomethoxylcyclopropane hydroxamic acid
-
-
(1R,2R)-N-hydroxy-2-[(4-methylpiperazin-1-yl)carbonyl]-2-[3-[(2-methylquinolin-4-yl)methoxy]phenyl]cyclopropanecarboxamide
-
-
(1R,2R)-N1-benzyl-N2-hydroxy-N1-methyl-1-[3-[(2-methylquinolin-4-yl)methoxy]phenyl]cyclopropane-1,2-dicarboxamide
-
-
(1R,2R)-N1-cyclohexyl-N2-hydroxy-1-[3-[(2-methylquinolin-4-yl)methoxy]phenyl]cyclopropane-1,2-dicarboxamide
-
-
(1R,2R)-N2-hydroxy-1-[3-[(2-methylquinolin-4-yl)methoxy]phenyl]-N1-phenylcyclopropane-1,2-dicarboxamide
-
-
(1R,2R)-N2-hydroxy-N1,N1-dimethyl-1-[3-[(2-methylquinolin-4-yl)methoxy]phenyl]cyclopropane-1,2-dicarboxamide
-
-
(1R,2R)-N2-hydroxy-N1-methyl-1-[3-[(2-methylquinolin-4-yl)methoxy]phenyl]cyclopropane-1,2-dicarboxamide
-
-
(1R,2S)-1-[4-(but-2-yn-1-yloxy)benzyl]-N2-hydroxycyclopropane-1,2-dicarboxamide
-
-
(1R,2S)-N2-hydroxy-1-[4-[(2-methylquinolin-4-yl)methoxy]benzyl]cyclopropane-1,2-dicarboxamide
-
-
(1R,2S)-N2-hydroxy-N1,N1-dimethyl-1-[4-[(2-methylquinolin-4-yl)methoxy]benzyl]cyclopropane-1,2-dicarboxamide
-
-
(1R,2S)-N2-hydroxy-N1-methyl-1-[4-[(2-methylquinolin-4-yl)methoxy]benzyl]cyclopropane-1,2-dicarboxamide
-
-
(1S,2R)-N-hydroxy-2-{4-[(2-imino-1,2-dihydroquinolin-4-yl)methoxy]benzyl}-2-(methoxycarbonyl)cyclopropanecarboximidic acid
-
-
(2R)-5-nitroguanyl-2-([(2R,3S)-2-(cyclohexylmethyl)-3-cyclopropyl-3-[formyl(hydroxy)amino]propanoyl]-amino)-N-(1,3-thiazol-2-yl)pentanamide
-
-
(2R,3S)-N-[(1S)-4-(2-pyridylsulfonyl)guanyl-1-[(1,3-thiazol-2-ylamino)-carbonyl]butyl]-3-[formyl(hydroxy)amino]-2-isobutylhexanamide
-
-
(2R,3S)-N-[(1S)-4-(2-pyridylsulfonyl)guanyl-1-[(1,3-thiazol-2-ylamino)-carbonyl]butyl]-3-[formyl(hydroxy)amino]-2-[(4-methylcyclohexyl)-methyl]hexanamide
-
-
(2R,3S)-N-[(1S)-4-(2-pyridylsulfonyl)guanyl-1-[(1,3-thiazol-2-ylamino)-carbonyl]butyl]-3-[formyl(hydroxy)amino]-2-[(5-methyl-2-thienyl)methyl]hexanamide
-
-
(2R,3S)-N-[(1S)-4-(2-pyridylsulfonyl)guanyl-1-[(1,3-thiazol-2-ylamino)-carbonyl]butyl]-3-[formyl(hydroxy)amino]-4-methyl-2-[(4-methylcyclohexyl)methyl]pentanamide
-
-
(2R,3S)-N-[(1S)-4-methanesulfonylguanyl-1-[(1,3-thiazol-2-ylamino)carbonyl]butyl]-3-[formyl(hydroxy)amino]-2-isobutyl-4-methylpentanamide
-
-
(2R,3S)-N-[(1S)-4-methanesulfonylguanyl-1-[(1,3-thiazol-2-ylamino)carbonyl]butyl]-3-[formyl(hydroxy)amino]-2-isobutylhexanamide
-
-
(2R,3S)-N-[(1S)-4-methanesulfonylguanyl-1-[(1,3-thiazol-2-ylamino)carbonyl]butyl]-3-[formyl(hydroxy)amino]-4-methyl-2-[(4-methylcyclohexyl)methyl]pentanamide
-
-
(2R,3S)-N-[(1S)-4-methanesulfonylguanyl-2-methyl-1-[(1,3-thiazol-2-ylamino)carbonyl]butyl]-3-[formyl-(hydroxy)amino]-2-isobutyl-4-methylpentanamide
-
-
(2R,3S)-N-[(1S)-4-methanesulfonylguanyl-2-methyl-1-[(1,3-thiazol-2-ylamino)carbonyl]butyl]-3-[formyl-(hydroxy)amino]-2-isobutylhexanamide
-
-
(2R,3S)-N-[(1S)-4-methanesulfonylguanyl-2-methyl-1-[(1,3-thiazol-2-ylamino)carbonyl]butyl]-6,6,6-trifluoro-3-[formyl(hydroxy)amino]-2-isobutylhexanamide
-
-
(2R,3S)-N-[(1S)-4-nitroguanyl-1-[(1,3-thiazol-2-ylamino)carbonyl]butyl]-2-(cyclohexylmethyl)-3-[formyl(hydroxy)amino]hexanamide
-
-
(2R,3S)-N-[(1S)-4-nitroguanyl-1-[(1,3-thiazol-2-ylamino)carbonyl]butyl]-2-(cyclohexylmethyl)-6,6,6-trifluoro-3-[formyl(hydroxy)amino]hexanamide
-
-
(2R,3S)-N-[(1S)-4-nitroguanyl-1-[(1,3-thiazol-2-ylamino)carbonyl]butyl]-2-[(1S)-1-[formyl(hydroxy)amino]-2-phenylethyl]-4-methylpentanamide
-
-
(2R,3S)-N-[(1S)-4-nitroguanyl-1-[(1,3-thiazol-2-ylamino)carbonyl]butyl]-3-[formyl(hydroxy)amino]-2-[5-methyl-2-thienylmethyl]hexanamide
-
-
(2R,3S)-N-[(1S)-4-nitroguanyl-1-[(1,3-thiazol-2-ylamino)carbonyl]butyl]-3-[formyl(hydroxy)amino]-4-methyl-2-[(4-methylcyclohexyl)methyl]hexanamide
-
-
(2R,3S)-N-[(1S)-4-nitroguanyl-1-[(1,3-thiazol-2-ylamino)carbonyl]butyl]-3-[formyl(hydroxy)amino]-4-methyl-2-[(4-methylcyclohexyl)methyl]pentanamide
-
-
(2R,3S)-N-[(1S,2R)-4-nitroguanyl-2-methyl-1-[(1,3-thiazol-2-ylamino)carbonyl]butyl]-3-[formyl(hydroxy)amino]-2-isobutylhexanamide
-
-
(2R,3S)-N-{(1R)-4-nitroguanyl-1-[(1,3-thiazol-2-ylamino)carbonyl]butyl}-3-[formyl(hydroxy)amino]-2-isobutylhexanamide
-
-
(2S)-2-amino-5-({(E)-amino[(methylsulfonyl)imino]-methyl}amino)-N-(1,3-thiazol-2-yl)pentanamide hydrochloride
-
-
(2S)-2-[(tert-butoxycarbonyl)amino]-5-({(Z)-(methyl-sulfanyl)[(methylsulfonyl)imino]methyl}amino)pentanoic acid
-
-
(2S,3R)-2-[(tert-butoxycarbonyl)amino]-5-{[imino(2-oxido-2-oxohydrazino)methyl]amino}-3-methylpentanoic acid (3R) Nalpha-boc-Ngamma-nitro-3-methyl L-arginine
-
-
(2S,3R)-2-{[(benzyloxy)carbonyl]amino}-3-methyl-5-({(Z)-(methylsulfanyl)[(methylsulfonyl)imino]methyl}-amino)pentanoic acid
-
-
(2S,3R)-5-methanesulfonylguanyl-2-[((2R)-2-[(1S)-1-[formyl(hydroxy)amino]ethyl]-4-methylpentanoyl)amino]-3-methyl-N-(1,3-thiazol-2-yl)pentanamide
-
-
(2S,3R)-5-nitroguanyl-2-[((2R)-2-[(1S)-1-[formyl(hydroxy)amino]ethyl]-4-methylpentanoyl)amino]-3-methyl-N-(1,3-thiazol-2-yl)pentanamide
-
-
(3S)-4-[[4-(but-2-ynylamino)phenyl]sulfonyl]-N-hydroxy-2,2-dimethylthio-morpholine-3-carboxamide
-
-
(5R)-5-(2',4'-difluorobiphenyl-4-yl)-5-[(6-fluoro-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]imidazolidine-2,4-dione
-
-
(5R)-5-(4'-chlorobiphenyl-4-yl)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]imidazolidine-2,4-dione
-
-
(5R)-5-[(6-fluoro-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[2'-(1-methyl-1H-tetrazol-5-yl)biphenyl-4-yl]imidazolidine-2,4-dione
-
-
(5R)-5-[(6-fluoro-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4'-(trifluoromethyl)biphenyl-4-yl]imidazolidine-2,4-dione
-
-
(5R)-5-[(6-fluoro-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(6-oxo-1,6-dihydropyridin-3-yl)phenyl]imidazolidine-2,4-dione
-
-
(5R)-5-[(6-fluoro-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(pyridin-3-yl)phenyl]imidazolidine-2,4-dione
-
-
(5R)-5-[(6-fluoro-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(quinolin-6-yl)phenyl]imidazolidine-2,4-dione
-
-
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[3'-(2-methyl-1,3-thiazol-4-yl)biphenyl-4-yl]imidazolidine-2,4-dione
-
-
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4'-(1H-pyrazol-3-yl)biphenyl-4-yl]imidazolidine-2,4-dione
-
-
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(1,3-thiazol-2-yl)phenyl]imidazolidine-2,4-dione
-
-
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(1-methyl-1H-pyrazol-4-yl)phenyl]imidazolidine-2,4-dione
-
-
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(1-methyl-1H-pyrrolo[2,3-c]pyridin-5-yl)phenyl]imidazolidine-2,4-dione
-
-
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(2-methyl-2H-indazol-6-yl)phenyl]imidazolidine-2,4-dione
-
-
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(2-methylpyridin-4-yl)phenyl]imidazolidine-2,4-dione
-
-
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(3-phenyl-1,2-oxazol-5-yl)phenyl]imidazolidine-2,4-dione
-
-
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(4-methyl-2,5-dioxoimidazolidin-4-yl)phenyl]imidazolidine-2,4-dione (non-preferred name)
-
-
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(pyrazin-2-yl)phenyl]imidazolidine-2,4-dione
-
-
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(pyridin-2-yl)phenyl]imidazolidine-2,4-dione
-
-
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(pyridin-3-yl)phenyl]imidazolidine-2,4-dione
-
-
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(pyridin-4-yl)phenyl]imidazolidine-2,4-dione
-
-
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(pyrimidin-5-yl)phenyl]imidazolidine-2,4-dione
-
-
(5R)-5-[4-(2-aminopyridin-4-yl)phenyl]-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]imidazolidine-2,4-dione
-
-
(5R)-5-[4-(3,5-dimethyl-1,2-oxazol-4-yl)phenyl]-5-[(6-fluoro-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]imidazolidine-2,4-dione
-
-
(5R)-5-[4-(5-chloro-6-oxo-1,6-dihydropyridin-3-yl)phenyl]-5-[(6-fluoro-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]imidazolidine-2,4-dione
-
-
(5S)-5-(4-fluorophenyl)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]imidazolidine-2,4-dione
-
-
1-(1,3-benzoxazol-2-yl)-4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-N-hydroxypiperidine-4-carboxamide
-
-
1-(1H-benzimidazol-2-yl)-4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-N-hydroxypiperidine-4-carboxamide
-
-
1-(2,2-dimethylpropanoyl)-N-hydroxy-4-[([4-[(2-methylquinolin-4-yl)methyl]phenyl]carbonyl)amino]pyrrolidine-3-carboxamide
-
-
1-(2,2-dimethylpropanoyl)-N-hydroxy-4-[[([4-[(2-methylquinolin-4-yl)methoxy]phenyl]carbonyl)amino]methyl]piperidine-4-carboxamide
-
-
1-(2,2-dimethylpropyl)-N-hydroxy-4-[([4-[(2-methylquinolin-4-yl)methyl]phenyl]carbonyl)amino]pyrrolidine-3-carboxamide
-
-
1-(butylsulfonyl)-N-hydroxy-4-[([4-[(2-methylquinolin-4-yl)methyl]phenyl]carbonyl)amino]pyrrolidine-3-carboxamide
-
-
1-but-2-yn-1-yl-N-hydroxy-4-[([4-[(2-methylquinolin-4-yl)methyl]phenyl]carbonyl)amino]pyrrolidine-3-carboxamide
-
-
1-ethylpropyl 4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-4-(hydroxycarbamoyl)piperidine-1-sulfinate
-
-
1-methyl-2-morpholin-4-ylethyl 4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-4-(hydroxycarbamoyl)piperidine-1-sulfinate
-
-
1-methylethyl (1R,2R)-2-(hydroxycarbamoyl)-1-[3-[(2-methylquinolin-4-yl)methoxy]phenyl]cyclopropanecarboxylate
-
-
1-methylethyl 4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-4-(hydroxycarbamoyl)piperidine-1-sulfinate
-
-
1-[(4-acetylpiperazin-1-yl)sulfonyl]-4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-N-hydroxypiperidine-4-carboxamide
-
-
2(R)-benzyloxymethyl-N-(2,2-dimethyl-1(S)-methyl-carbamoylpropyl)-3-(S)-(4-methoxyphenyl)succinamic acid
-
-
2-morpholin-4-ylethyl 4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-4-(hydroxycarbamoyl)piperidine-1-sulfinate
-
-
2-[3-(2-methylquinolin-4-yl)methoxylphenyl]-2-trans-carboxamidocyclopropane hydroxyamic acid
-
-
2-[3-(2-methylquinolin-4-yl)methoxyphenyl]-2-trans-carbomethoxylcyclopropane hydroxyamic acid
-
-
3(R)-benzyloxymethyl-2-(S)-(4-methoxyphenyl)pent-4-enoic acid (2,2-dimethyl-1-(S)-methylcarbamoylpropyl)amide
-
-
3-([[4-(1,3-dihydrofuro[3,4-b]quinolin-9-ylmethyl)phenyl]carbonyl]amino)-N-hydroxytetrahydro-2H-pyran-2-carboxamide
-
-
3-([[4-(2,3-dihydro-1H-cyclopenta[b]quinolin-9-ylmethyl)phenyl]carbonyl]amino)-N-hydroxytetrahydro-2H-pyran-2-carboxamide
-
-
3-([[4-(2,3-dihydrofuro[2,3-b]quinolin-4-ylmethyl)phenyl]carbonyl]amino)-N-hydroxytetrahydro-2H-pyran-2-carboxamide
-
-
3-[([4-[(2,3-dimethylquinolin-4-yl)methyl]phenyl]carbonyl)amino]-N-hydroxytetrahydro-2H-pyran-2-carboxamide
-
-
3-[([4-[(2-cyclopropylquinolin-4-yl)methyl]phenyl]carbonyl)amino]-N-hydroxytetrahydro-2H-pyran-2-carboxamide
-
-
3-[([4-[(2-ethylquinolin-4-yl)methyl]phenyl]carbonyl)amino]-N-hydroxytetrahydro-2H-pyran-2-carboxamide
-
-
3-[([4-[(3-ethyl-2-methylquinolin-4-yl)methyl]phenyl]carbonyl)amino]-N-hydroxytetrahydro-2H-pyran-2-carboxamide
-
-
3-[4-[2-(hydroxyamino)-2-oxoethyl]-4-[([4-[(2-methylquinolin-4-yl)methoxy]phenyl]carbonyl)amino]piperidin-1-yl]propanoic acid
-
-
3-[[(4-[[2-(dimethylamino)quinolin-4-yl]methyl]phenyl)carbonyl]amino]-N-hydroxytetrahydro-2H-pyran-2-carboxamide
-
-
4'-[(4R)-4-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-2,5-dioxoimidazolidin-4-yl]biphenyl-4-carboxamide
-
-
4-(4-but-2-ynylamino-benzenesulfonylmethyl)-1-(2-methyl-benzoyl)-piperidine-4-carboxylic acid hydroxyamide
-
-
4-(4-but-2-ynylamino-benzenesulfonylmethyl)-1-(2-methyl-butyryl)-piperidine-4-carboxylic acid hydroxyamide
-
-
4-(4-but-2-ynylamino-benzenesulfonylmethyl)-1-(propane-2-sulfonyl)-piperidine-4-carboxylic acid hydroxyamide
-
-
4-(4-but-2-ynylamino-benzenesulfonylmethyl)-1-isobutyryl-piperidine-4-carboxylic acid hydroxyamide
-
-
4-(4-but-2-ynylamino-benzenesulfonylmethyl)-1-pyridin-4-ylmethyl-piperidine-4-carboxylic acid hydroxyamide
-
-
4-(4-but-2-ynylamino-benzenesulfonylmethyl)-piperidine-1,4-dicarboxylic acid 1-diethylamide 4-hydroxyamide
-
-
4-(4-but-2-ynylamino-benzenesulfonylmethyl)-piperidine-4-carboxylic acid hydroxyamide
-
-
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-1-(dimethylsulfamoyl)-N-hydroxypiperidine-4-carboxamide
-
-
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-1-[(2,5-dichlorothiophen-3-yl)sulfonyl]-N-hydroxypiperidine-4-carboxamide
-
-
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-1-[(2,5-dimethyl-1,3-thiazol-4-yl)sulfonyl]-N-hydroxypiperidine-4-carboxamide
-
-
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-1-[(3,5-dichloropyridin-4-yl)carbonyl]-N-hydroxypiperidine-4-carboxamide
-
-
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-1-[(3,5-dichloropyridin-4-yl)methyl]-N-hydroxypiperidine-4-carboxamide
-
-
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-1-[(3,5-dimethyl-1H-pyrazol-4-yl)sulfonyl]-N-hydroxypiperidine-4-carboxamide
-
-
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-1-[(3,5-dimethylisoxazol-4-yl)sulfonyl]-N-hydroxypiperidine-4-carboxamide
-
-
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-1-[(5-chlorothiophen-2-yl)sulfonyl]-N-hydroxypiperidine-4-carboxamide
-
-
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-N-hydroxy-1-(morpholin-4-ylsulfonyl)piperidine-4-carboxamide
-
-
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-N-hydroxy-1-(piperidin-1-ylsulfonyl)piperidine-4-carboxamide
-
-
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-N-hydroxy-1-(pyrrolidin-1-ylsulfonyl)piperidine-4-carboxamide
-
-
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-N-hydroxy-1-pyridin-2-ylpiperidine-4-carboxamide
-
-
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-N-hydroxy-1-pyridin-4-ylpiperidine-4-carboxamide
-
-
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-N-hydroxy-1-[(2-methyl-1H-imidazol-4-yl)sulfonyl]piperidine-4-carboxamide
-
-
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-N-hydroxy-1-[[(2R)-2-(hydroxymethyl)pyrrolidin-1-yl]sulfonyl]piperidine-4-carboxamide
-
-
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-N-hydroxy-1-[[(2S)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]piperidine-4-carboxamide
-
-
4-[([4-[(1,1-dimethylbut-2-yn-1-yl)oxy]phenyl]sulfonyl)methyl]-N-hydroxy-1-(isopropylsulfonyl)piperidine-4-carboxamide
-
-
4-[2-(hydroxyamino)-2-oxoethyl]-N,N-dimethyl-4-[([4-[(2-methylquinolin-4-yl)methoxy]phenyl]carbonyl)amino]piperidine-1-carboxamide
-
-
4-[4-(4-hydroxy-but-2-ynylamino)-benzenesulfonylmethyl]-4-hydroxycarbamoyl-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[[4-(2-butynyloxy)phenyl]sulfonyl]-N-hydroxy-2,2-dimethyl-(3S)-thiomorpholinecarboxamide
-
IC50: 0.009 mM
5-[(5-methoxy-3-oxo-1,3-dihydro-2H-indazol-2-yl)methyl]-5-phenylimidazolidine-2,4-dione
-
-
5-[(6-fluoro-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-(2-phenoxyphenyl)imidazolidine-2,4-dione
-
-
5-[(6-fluoro-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-(3-phenoxyphenyl)imidazolidine-2,4-dione
-
-
5-[(6-fluoro-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(2-oxopyrrolidin-1-yl)phenyl]imidazolidine-2,4-dione
-
-
5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(morpholin-4-yl)phenyl]imidazolidine-2,4-dione
-
-
5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(pyridin-4-yloxy)phenyl]imidazolidine-2,4-dione
-
-
5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(pyrrolidin-1-ylcarbonyl)phenyl]imidazolidine-2,4-dione
-
-
5-[4-(cyclopentyloxy)phenyl]-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]imidazolidine-2,4-dione
-
-
5-[4-(isoquinolin-7-yloxy)phenyl]-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]imidazolidine-2,4-dione
-
-
benzyl (1S,2R)-4-({(E)-amino[(methylsulfonyl)imino]-methyl}amino)-2-methyl-1-[(1,3-thiazol-2-ylamino)carbonyl]butylcarbamate
-
-
cyclohexyl 4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-4-(hydroxycarbamoyl)piperidine-1-sulfinate
-
-
cyclohexylmethyl 4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-4-(hydroxycarbamoyl)piperidine-1-sulfinate
-
-
cyclopentyl 4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-4-(hydroxycarbamoyl)piperidine-1-sulfinate
-
-
cyclopropyl 4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-4-(hydroxycarbamoyl)piperidine-1-sulfinate
-
-
Cys-Gln-Val
-
tripeptide Cys-Gln-Val shows about 50%, 30% and 25% residual activity at 0.0005, 0.00005 and 0.000005 mM, respectively
EGTA
-
1 mM, treatment of cells dramatically inhibits shedding of shedding of FcalphaR, i.e. Fc receptor for immunoglobulin A
ethyl (1R,2R)-2-(hydroxycarbamoyl)-1-[3-[(2-methylquinolin-4-yl)methoxy]phenyl]cyclopropanecarboxylate
-
-
ethyl (1R,2S)-2-(hydroxycarbamoyl)-1-(4-phenoxybenzyl)cyclopropanecarboxylate
-
-
Gln-Cys-Ala
-
tripeptide Gln-Cys-Ala shows about 35%, 20% and 22% residual activity at 0.0005, 0.00005 and 0.000005 mM, respectively
Gln-Cys-Val
-
tripeptide Gln-Cys-Val shows about 45%, 28% and 10% residual activity at 0.0005, 0.00005 and 0.000005 mM, respectively
Gln-Val-Cys
-
tripeptide Gln-Val-Cys shows about 59%, 40% and 8% residual activity at 0.0005, 0.00005 and 0.000005 mM, respectively
IC-3
-
protects TACE from degradation by inhibiting either TACE itself or another metalloprotease
methyl (1R,2R)-1-[3-(2-[3-[(1Z)-buta-1,3-dien-1-yl]phenyl]ethoxy)phenyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
-
methyl (1R,2R)-1-[3-(benzyloxy)phenyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
-
methyl (1R,2R)-1-[3-(but-2-yn-1-yloxy)phenyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
-
methyl (1R,2R)-1-[3-(cyclohexylmethoxy)phenyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
-
methyl (1R,2R)-1-[3-[(4-chlorobenzyl)oxy]phenyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
-
methyl (1R,2R)-2-(hydroxycarbamoyl)-1-(3-methoxyphenyl)cyclopropanecarboxylate
-
-
methyl (1R,2R)-2-(hydroxycarbamoyl)-1-(3-[[3-(trifluoromethyl)benzyl]oxy]phenyl)cyclopropanecarboxylate
-
-
methyl (1R,2R)-2-(hydroxycarbamoyl)-1-(3-[[4-(trifluoromethyl)benzyl]oxy]phenyl)cyclopropanecarboxylate
-
-
methyl (1R,2R)-2-(hydroxycarbamoyl)-1-[3-(2-methylphenoxy)phenyl]cyclopropanecarboxylate
-
-
methyl (1R,2R)-2-(hydroxycarbamoyl)-1-[3-(2-naphthalen-2-ylethoxy)phenyl]cyclopropanecarboxylate
-
-
methyl (1R,2R)-2-(hydroxycarbamoyl)-1-[3-(2-phenylethoxy)phenyl]cyclopropanecarboxylate
-
-
methyl (1R,2R)-2-(hydroxycarbamoyl)-1-[3-(4-methylphenoxy)phenyl]cyclopropanecarboxylate
-
-
methyl (1R,2R)-2-(hydroxycarbamoyl)-1-[3-(naphthalen-2-ylmethoxy)phenyl]cyclopropanecarboxylate
-
-
methyl (1R,2R)-2-(hydroxycarbamoyl)-1-[3-(naphthalen-2-yloxy)phenyl]cyclopropanecarboxylate
-
-
methyl (1R,2R)-2-(hydroxycarbamoyl)-1-[3-[(3-methoxybenzyl)oxy]phenyl]cyclopropanecarboxylate
-
-
methyl (1R,2S)-1-[4-(benzyloxy)benzyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
-
methyl (1R,2S)-1-[4-(but-2-yn-1-yloxy)benzyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
-
methyl (1R,2S)-1-[4-(cyclohexylmethoxy)benzyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
-
methyl (1R,2S)-1-[4-[(2-chlorobenzyl)oxy]benzyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
-
methyl (1R,2S)-1-[4-[(3,4-dichlorobenzyl)oxy]benzyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
-
methyl (1R,2S)-2-(hydroxycarbamoyl)-1-[4-(2-naphthalen-1-ylethoxy)benzyl]cyclopropanecarboxylate
-
-
methyl (1R,2S)-2-(hydroxycarbamoyl)-1-[4-(2-naphthalen-2-ylethoxy)benzyl]cyclopropanecarboxylate
-
-
methyl 3-(hydroxycarbamoyl)-4-[([4-[(2-methylquinolin-4-yl)methyl]phenyl]carbonyl)amino]pyrrolidine-1-carboxylate
-
-
methyl 4'-[(4R)-4-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-2,5-dioxoimidazolidin-4-yl]biphenyl-4-carboxylate
-
-
N(R)-[2-(hydroxyaminocarbonyl)methyl]-4-methylpentanoyl-L-alanine amide
-
IC50: about 0.11 mM
N-hydroxy-1-(2-methylpropyl)-4-[([4-[(2-methylquinolin-4-yl)methyl]phenyl]carbonyl)amino]pyrrolidine-3-carboxamide
-
-
N-hydroxy-1-methyl-4-[([4-[(2-methylquinolin-4-yl)methyl]phenyl]carbonyl)amino]pyrrolidine-3-carboxamide
-
-
N-hydroxy-3-[([4-[(2-morpholin-4-ylquinolin-4-yl)methyl]phenyl]carbonyl)amino]tetrahydro-2H-pyran-2-carboxamide
-
-
N-hydroxy-3-[([4-[(3-methylquinolin-4-yl)methyl]phenyl]carbonyl)amino]tetrahydro-2H-pyran-2-carboxamide
-
-
N-hydroxy-3-[[(4-[[2-(trifluoromethyl)quinolin-4-yl]methyl]phenyl)carbonyl]amino]tetrahydro-2H-pyran-2-carboxamide
-
-
N-hydroxy-4-[([4-[(2-methylquinolin-4-yl)methoxy]phenyl]carbonyl)amino]pyrrolidine-3-carboxamide
-
-
N-hydroxy-4-[([4-[(2-methylquinolin-4-yl)methyl]phenyl]carbonyl)amino]-1-prop-2-yn-1-ylpyrrolidine-3-carboxamide
-
-
N-hydroxy-4-[([4-[(2-methylquinolin-4-yl)methyl]phenyl]carbonyl)amino]tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-[([4-[(2-methylquinolin-4-yl)methyl]phenyl]carbonyl)amino]tetrahydrofuran-3-carboxamide
-
-
N-hydroxy-4-[([4-[(2-methylquinolin-4-yl)oxy]phenyl]carbonyl)amino]pyrrolidine-3-carboxamide
-
-
N-hydroxy-4-[[([4-[(2-methylquinolin-4-yl)methoxy]phenyl]carbonyl)amino]methyl]-1-(methylsulfonyl)piperidine-4-carboxamide
-
-
N-hydroxy-4-[[([4-[(2-methylquinolin-4-yl)methoxy]phenyl]carbonyl)amino]methyl]-1-propylpiperidine-4-carboxamide
-
-
N-hydroxy-4-[[([4-[(2-methylquinolin-4-yl)methoxy]phenyl]carbonyl)amino]methyl]piperidine-4-carboxamide
-
-
N-hydroxy-4-[[([4-[(2-methylquinolin-4-yl)methoxy]phenyl]carbonyl)amino]methyl]tetrahydro-2H-pyran-4-carboxamide
-
-
N-[(4S,5S,7R)-2-[7-(1-benzylpiperidin-4-yl)]methylcarbamoyl-5-hydroxy-2-methyloct-4-yl]-N'-[(R)-1-(4-fluorophenyl)ethyl]-5-[methyl(methylsulfonyl)amino]isophthalamide
-
-
N-[1-(1,1-dimethylprop-2-yn-1-yl)-4-[2-(hydroxyamino)-2-oxoethyl]piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
-
-
N-[1-(2,2-dimethylpropanoyl)-4-[2-(hydroxyamino)-2-oxoethyl]piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
-
-
N-[1-(2,2-dimethylpropyl)-4-[2-(hydroxyamino)-2-oxoethyl]piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
-
-
N-[1-(2-fluoroethyl)-4-[2-(hydroxyamino)-2-oxoethyl]piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
-
-
N-[1-(3,3-dimethylbutanoyl)-4-[2-(hydroxyamino)-2-oxoethyl]piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
-
-
N-[1-(4,5-dihydro-1,3-thiazol-2-yl)-4-[2-(hydroxyamino)-2-oxoethyl]piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
-
-
N-[1-acetyl-4-[2-(hydroxyamino)-2-oxoethyl]piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
-
-
N-[1-ethyl-4-[2-(hydroxyamino)-2-oxoethyl]piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
-
-
N-[1-tert-butyl-4-[2-(hydroxyamino)-2-oxoethyl]piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
-
-
N-[1-[2-(ethylsulfonyl)ethyl]-4-[2-(hydroxyamino)-2-oxoethyl]piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
-
-
N-[1-[2-(hydroxyamino)-2-oxoethyl]cyclohexyl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
-
-
N-[2-(hydroxycarbamoyl)cyclopentyl]-4-[(2-methylquinolin-4-yl)methyl]benzamide
-
-
N-[4-(hydroxyamino)-4-oxo-2-(phenylsulfanyl)butyl]-3-(naphthalen-2-yl)-L-alanyl-N-(2-{[(benzyloxy)carbonyl]amino}ethyl)-L-alaninamide
-
peptidomimetic inhibitor, 54.5% inhibition in in vitro lipopolysaccharide cytotoxicity tests, inhibitory activity in vivo by measuring the expression of mTNFalpha
N-[4-(hydroxyamino)-4-oxo-2-(phenylsulfanyl)butyl]-L-phenylalanyl-N-(2-{[(benzyloxy)carbonyl]amino}ethyl)-L-alaninamide
-
peptidomimetic inhibitor, 54.5% inhibition in in vitro lipopolysaccharide cytotoxicity tests
N-[4-(hydroxyamino)-4-oxo-2-(propan-2-ylsulfanyl)butyl]-L-phenylalanyl-N-(2-{[(benzyloxy)carbonyl]amino}ethyl)-L-alaninamide
-
peptidomimetic inhibitor, 27.3% inhibition in in vitro lipopolysaccharide cytotoxicity tests, molecular docking studies
N-[4-[2-(hydroxyamino)-2-oxoethyl]-1-(2-methylpropanoyl)piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
-
-
N-[4-[2-(hydroxyamino)-2-oxoethyl]-1-(3-methylbutanoyl)piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
-
-
N-[4-[2-(hydroxyamino)-2-oxoethyl]-1-(methylsulfonyl)piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
-
-
N-[4-[2-(hydroxyamino)-2-oxoethyl]-1-methylpiperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
-
-
N-[4-[2-(hydroxyamino)-2-oxoethyl]-1-phenylpiperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
-
-
N-[4-[2-(hydroxyamino)-2-oxoethyl]-1-propanoylpiperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
-
-
N-[4-[2-(hydroxyamino)-2-oxoethyl]-1-propylpiperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
-
-
N-[4-[2-(hydroxyamino)-2-oxoethyl]-1-[2-(methylsulfonyl)ethyl]piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
-
-
N-[4-[2-(hydroxyamino)-2-oxoethyl]tetrahydro-2H-pyran-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
-
-
N-[4-[2-(hydroxyamino)-2-oxoethyl]tetrahydro-2H-pyran-4-yl]-4-[(2-methylquinolin-4-yl)methyl]benzamide
-
-
N-[DL-[2-(hydroxyamino-carbonyl)methyl]-4-methylpentanoyl]-L-3-(tert-butyl)glycyl-L-alanine,2-aminoethylamide
-
-
N-[[1-(hydroxycarbamoyl)cyclohexyl]methyl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
-
-
N1-benzyloxy-2(R)-benzyloxymethyl-N4-(2,2-dimethyl-1(S)-methylcarbamoylpropyl)-3(S)-(4-methoxyphenyl)-succinamide
-
-
N4-(2,2-dimethyl-1(S)-methylcarbamoylpropyl)-N1-hydroxy-2(R)-hydroxymethyl-3(R)-(isobutyl)succinamide
-
-
N4-(2,2-dimethyl-1(S)-methylcarbamoylpropyl)-N1-hydroxy-2(R)-hydroxymethyl-3(S)-(4-methoxyphenyl)succinamide
-
-
N4-(2,2-dimethyl-1(S)-methylcarbamoylpropyl)-N1-hydroxy-2(R)-hydroxymethyl-3(S)-p-tolylsuccinamide
-
-
N4-(2,2-dimethyl-1(S)-methylcarbamoylpropyl)-N1-hydroxy-2(R)-hydroxymethyl-3(S)-phenylsuccinamide
-
-
pyridin-4-ylmethyl 4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-4-(hydroxycarbamoyl)piperidine-1-sulfinate
-
-
Ro32-7315
-
inhibitor specific for ADAM17, blocks shedding of CD30 antigen from cell membrane and a simultaneous release of soluble CD30
tert-butyl (1S,2R)-4-{[imino(2-oxido-2-oxohydrazino)-methyl]amino}-2-methyl-1-[1,3-thiazol-2-ylaminocarbonyl]butylcarbamate
-
-
tert-butyl (2S,3R)-2-{[(benzyloxy)carbonyl]amino}-5-amino-3-methylpentanoate
-
-
tert-butyl (2S,3R)-2-{[(benzyloxy)carbonyl]amino}-5-azido-3-methylpentanoate
-
-
tert-butyl (2S,3R)-2-{[(benzyloxy)carbonyl]amino}-5-hydroxy-3-methylpentanoate
-
-
tert-butyl 3-(hydroxycarbamoyl)-4-[([4-[(2-methylquinolin-4-yl)oxy]phenyl]carbonyl)amino]pyrrolidine-1-carboxylate
-
-
tert-butyl 3-[4-[2-(hydroxyamino)-2-oxoethyl]-4-[([4-[(2-methylquinolin-4-yl)methoxy]phenyl]carbonyl)amino]piperidin-1-yl]propanoate
-
-
tert-butyl 4-(hydroxycarbamoyl)-4-[[([4-[(2-methylquinolin-4-yl)methoxy]phenyl]carbonyl)amino]methyl]piperidine-1-carboxylate
-
-
tert-butyl 4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-4-(hydroxycarbamoyl)piperidine-1-sulfinate
-
-
tert-butyl 4-([[4-(but-2-ynylamino)phenyl]sulfonyl]methyl)-4-[(hydroxyamino)-carbonyl]piperidine-1-carboxylate
-
-
tert-butyl 4-[([4-[but-2-ynyl(methyl)amino]phenyl]sulfonyl)methyl]-4-[(hydroxyamino)carbonyl]piperidine-1-carboxylate
-
-
tert-butyl(1S)-4-({(Z)-(methylsulfanyl)[(methylsulfonyl)-imino]methyl}amino)-1-[(1,3-thiazol-2-ylamino)carbonyl]butylcarbamate
-
-
tumor necrosis factor-alpha-converting enzyme pro domain
-
inhibition of the tumor necrosis factor-alpha-converting enzyme by its isolated pro domain, IC50: 70 nM
-
[((3R,4S)-4-{[(benzyloxy)carbonyl]}-4-carboxy-3-methylbutyl)amino](imino)methanaminium nitrate (3R) 3-methyl L-arginine nitric acid salt
-
-
[N-hydroxy-1-(isopropylsulfonyl)-4-[(4-[(1-methylbut-2-yn-1-yl)oxy]phenyl]sulfonyl)-methyl]piperidine-4-carboxamide
-
-
4-(2-butylbenzyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(naphthalen-2-yl)propan-2-yl]piperazine-2,3-dione
-
4-(2-butylbenzyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(naphthalen-2-yl)propan-2-yl]piperazine-2,3-dione
design and synthesis of the specific inhibitor, overview
4-(2-butylbenzyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(naphthalen-2-yl)propan-2-yl]piperazine-2,3-dione
synthesis of the specific inhibitor, overview
4-(cyclopentylmethyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(naphthalen-2-yl)propan-2-yl]piperazine-2,3-dione
-
4-(cyclopentylmethyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(naphthalen-2-yl)propan-2-yl]piperazine-2,3-dione
design and synthesis of the specific inhibitor, overview
4-(cyclopentylmethyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(naphthalen-2-yl)propan-2-yl]piperazine-2,3-dione
synthesis of the specific inhibitor, overview
EDTA
-
1 mM, treatment of cells dramatically inhibits shedding of shedding of FcalphaR, i.e. Fc receptor for immunoglobulin A
GM6001
-
broad-spectrum metalloproteinase inhibitor, treatment of cells dramatically inhibits shedding of shedding of FcalphaR, i.e. Fc receptor for immunoglobulin A
GW9471
-
hydroxamic acid competitive inhibitor that totally blocks TACE activity
TAPI
-
hydroxamic acid-based broad-spectrum inhibitor of zinc metalloproteinases
TAPI-1
-
TAPI-1 inhibits 19% and 45% of enzyme activity at 0.0001 and 0.0001 mM, respectively
TAPI-2
-
hydroxamate-based inhibitor of matrix metalloproteases that has high activity against TACE
TIMP-3
-
tissue inhibitor of metalloproteases-3, CAS: 147783-68-4, 171039-15-9, 13037-60-4
-
additional information
secondary binding site (exosite) inhibitors provide a viable alternative to active site inhibitors, library screening and inhibitor design and synthesis, ADAM17 inhibition occurs via a non-zinc-binding mechanism, kinetic study, overview
-
additional information
-
endothelial protein C receptor shedding is not influenced by DMSO, TIMP-1 or TIMP-2
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
12-HPETE
-
i.e. 12-hydroperoxy-5Z,8Z,10E,14Z-eicosatetraenoic acid, a peroxide synthesized in the platelet lipoxygenase pathway, induces TACE-mediated receptor cleavage
anti-Ro/SSA autoantibody
-
i.e. antinuclear autoantibodies in the blood directed against Ro/Sjögren's syndrome ribonucleoprotein A antigen. Adalimumab appears to be significantly more efficacious than Etanercept in preventing TACE activation caused by anti-Ro/SSA autoantibodies
-
bortezomib
-
stimulates ADAM17-catalyzed shedding of CD30, blocks bortezomib-stimulated sCD30 release from L540 cells with an IC50 of approximately 230 nM
glucose oxidase
-
oxidative damage via glucose oxidase or hydrogen peroxide activates TACE and induces shedding of its targets, glycoprotein Ibalpha and glycoprotein V, in murine and human platelets. The TACE activation is independent of platelet activation. TACE activation induced by hydrogen peroxide is dependent on p38 mitogen-activated protein kinase signalling, whereas protein kinase C, phosphoinositide 3-kinase, and caspases are not involved. Inhibition of p38 cytoplasmic targets, phospholipase A2 and heat shock protein 27, does not prevent shedding, whereas blocking 12-lipoxygenase or Src kinase slightly inhibits TACE activation
-
granulocyte-macrophage colony-stimulating factor
-
granulocyte-macrophage colony-stimulating factor GM-CSF and interleukin-4 in combination potently up-regulate tumor necrosis factor-alpha coverting enzyme TACE and activity in monocytes, causing ectodomain shedding of M-CSF receptor
-
heparan sulfate
-
removal of cell surface heparan sulfate increases TACE activity and TACE-dependent formation of ErbB4 80 kDa intracellular domain
interleukin-4
-
granulocyte-macrophage colony-stimulating factor GM-CSF and interleukin-4 in combination potently up-regulate tumor necrosis factor-alpha coverting enzyme TACE and activity in monocytes, causing ectodomain shedding of M-CSF receptor
-
N-formyl-L-methionyl-phenylalanine
-
ADAM17 substrates undergo efficient turnover during extended neutrophil activation by N-formyl-L-methionyl-phenylalanine
additional information
substrate glycosylation increases the enzyme activity, overview
-
additional information
-
no apparent change in mRNA contents of TACE upon stimulation with IFN alpha, IFN beta and IFN gamma
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.003
Glu(EDANS)-Pro-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser(4O-(beta-D-Gal-(1->3)-alpha-D-GalNAc))-Ser-Lys(DABCYL)
pH 7.5, 22°C
0.012
Glu(EDANS)-Pro-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser-Ser-Lys(DABCYL)
pH 7.5, 22°C
0.0072
(EDANS)-ELAQAVRSSSRK-(DABCYL)
extracellular domain, 25°C, pH not specified in the publication
0.016
(EDANS)-ELAQAVRSSSRK-(DABCYL)
catalytic domain, 25°C, pH not specified in the publication
0.0034
(EDANS)-EPLAQAVRSSSK-(DABCYL)
catalytic domain, presence of L-galactose, 25°C, pH not specified in the publication
0.004
(EDANS)-EPLAQAVRSSSK-(DABCYL)
catalytic domain, 25°C, pH not specified in the publication
0.004
(EDANS)-EPLAQAVRSSSK-(DABCYL)
extracellular domain, presence of L-galactose, 25°C, pH not specified in the publication
0.012
(EDANS)-EPLAQAVRSSSK-(DABCYL)
extracellular domain, 25°C, pH not specified in the publication
0.0076
S80-glycosylated (EDANS)-ELAQAVRSSSRK-(DABCYL)
extracellular domain, 25°C, pH not specified in the publication
0.068
S80-glycosylated (EDANS)-ELAQAVRSSSRK-(DABCYL)
catalytic domain, 25°C, pH not specified in the publication
0.003
S80-glycosylated (EDANS)-EPLAQAVRSSSK-(DABCYL)
extracellular domain, 25°C, pH not specified in the publication
0.0032
S80-glycosylated (EDANS)-EPLAQAVRSSSK-(DABCYL)
extracellular domain, presence of L-galactose, 25°C, pH not specified in the publication
0.0069
S80-glycosylated (EDANS)-EPLAQAVRSSSK-(DABCYL)
catalytic domain, 25°C, pH not specified in the publication
0.01
S80-glycosylated (EDANS)-EPLAQAVRSSSK-(DABCYL)
catalytic domain, presence of L-galactose, 25°C, pH not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.25
Glu(EDANS)-Pro-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser(4O-(beta-D-Gal-(1->3)-alpha-D-GalNAc))-Ser-Lys(DABCYL)
pH 7.5, 22°C
0.14
Glu(EDANS)-Pro-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser-Ser-Lys(DABCYL)
pH 7.5, 22°C
0.05
(EDANS)-ELAQAVRSSSRK-(DABCYL)
catalytic domain, 25°C, pH not specified in the publication
0.2
(EDANS)-ELAQAVRSSSRK-(DABCYL)
extracellular domain, 25°C, pH not specified in the publication
0.06
(EDANS)-EPLAQAVRSSSK-(DABCYL)
catalytic domain, presence of L-galactose, 25°C, pH not specified in the publication
0.07
(EDANS)-EPLAQAVRSSSK-(DABCYL)
catalytic domain, 25°C, pH not specified in the publication
0.1
(EDANS)-EPLAQAVRSSSK-(DABCYL)
extracellular domain, presence of L-galactose, 25°C, pH not specified in the publication
0.14
(EDANS)-EPLAQAVRSSSK-(DABCYL)
extracellular domain, 25°C, pH not specified in the publication
0.08
S80-glycosylated (EDANS)-ELAQAVRSSSRK-(DABCYL)
catalytic domain, 25°C, pH not specified in the publication
0.42
S80-glycosylated (EDANS)-ELAQAVRSSSRK-(DABCYL)
extracellular domain, 25°C, pH not specified in the publication
0.08
S80-glycosylated (EDANS)-EPLAQAVRSSSK-(DABCYL)
extracellular domain, presence of L-galactose, 25°C, pH not specified in the publication
0.22
S80-glycosylated (EDANS)-EPLAQAVRSSSK-(DABCYL)
catalytic domain, 25°C, pH not specified in the publication
0.25
S80-glycosylated (EDANS)-EPLAQAVRSSSK-(DABCYL)
extracellular domain, 25°C, pH not specified in the publication
0.36
S80-glycosylated (EDANS)-EPLAQAVRSSSK-(DABCYL)
catalytic domain, presence of L-galactose, 25°C, pH not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
76
Glu(EDANS)-Pro-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser(4O-(beta-D-Gal-(1->3)-alpha-D-GalNAc))-Ser-Lys(DABCYL)
pH 7.5, 22°C
12
Glu(EDANS)-Pro-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser-Ser-Lys(DABCYL)
pH 7.5, 22°C
12
(EDANS)-EPLAQAVRSSSK-(DABCYL)
extracellular domain, 25°C, pH not specified in the publication
17
(EDANS)-EPLAQAVRSSSK-(DABCYL)
catalytic domain, 25°C, pH not specified in the publication
18
(EDANS)-EPLAQAVRSSSK-(DABCYL)
catalytic domain, presence of L-galactose, 25°C, pH not specified in the publication
19
(EDANS)-EPLAQAVRSSSK-(DABCYL)
extracellular domain, presence of L-galactose, 25°C, pH not specified in the publication
1.1
S80-glycosylated (EDANS)-ELAQAVRSSSRK-(DABCYL)
catalytic domain, 25°C, pH not specified in the publication
61
S80-glycosylated (EDANS)-ELAQAVRSSSRK-(DABCYL)
extracellular domain, 25°C, pH not specified in the publication
23
S80-glycosylated (EDANS)-EPLAQAVRSSSK-(DABCYL)
extracellular domain, presence of L-galactose, 25°C, pH not specified in the publication
32
S80-glycosylated (EDANS)-EPLAQAVRSSSK-(DABCYL)
catalytic domain, 25°C, pH not specified in the publication
36
S80-glycosylated (EDANS)-EPLAQAVRSSSK-(DABCYL)
catalytic domain, presence of L-galactose, 25°C, pH not specified in the publication
76
S80-glycosylated (EDANS)-EPLAQAVRSSSK-(DABCYL)
extracellular domain, 25°C, pH not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00000015
(1R,2S)-1-(3-fluoro-4-[[2-(1-methyl-1H-pyrazol-5-yl)quinolin-4-yl]methoxy]benzyl)-N2-hydroxycyclopropane-1,2-dicarboxamide
-
0.00000076
(1R,2S)-1-(3-fluoro-4-[[2-(methylamino)quinolin-4-yl]methoxy]benzyl)-N2-hydroxycyclopropane-1,2-dicarboxamide
-
0.00000021
(1R,2S)-1-[3-fluoro-4-[(2-morpholin-4-ylquinolin-4-yl)methoxy]benzyl]-N2-hydroxycyclopropane-1,2-dicarboxamide
-
0.00000036
(1R,2S)-1-[3-fluoro-4-[(2-phenylquinolin-4-yl)methoxy]benzyl]-N2-hydroxy-N1,N1-dimethylcyclopropane-1,2-dicarboxamide
-
0.00000014
(1R,2S)-1-[3-fluoro-4-[(2-phenylquinolin-4-yl)methoxy]benzyl]-N2-hydroxycyclopropane-1,2-dicarboxamide
-
0.00000014
(1R,2S)-1-[3-fluoro-4-[(2-pyridin-3-ylquinolin-4-yl)methoxy]benzyl]-N2-hydroxycyclopropane-1,2-dicarboxamide
-
0.00000015
(1R,2S)-1-[3-fluoro-4-[(2-pyrrolidin-1-ylquinolin-4-yl)methoxy]benzyl]-N2-hydroxycyclopropane-1,2-dicarboxamide
-
0.000001
(1R,2S)-1-[4-[(2-ethylquinolin-4-yl)methoxy]benzyl]-N2-hydroxycyclopropane-1,2-dicarboxamide
-
0.000003
(1R,2S)-N2-hydroxy-1-[4-[(2-methylquinolin-4-yl)methoxy]benzyl]cyclopropane-1,2-dicarboxamide
-
0.00000063
(1R,2S)-N2-hydroxy-1-[4-[(2-phenylquinolin-4-yl)methoxy]benzyl]-N1-(piperidin-4-ylmethyl)cyclopropane-1,2-dicarboxamide
-
0.00000018
(1R,2S)-N2-hydroxy-1-[4-[(2-phenylquinolin-4-yl)methoxy]benzyl]cyclopropane-1,2-dicarboxamide
-
0.00000028
(1R,2S)-N2-hydroxy-N1,N1-dimethyl-1-[4-[(2-phenylquinolin-4-yl)methoxy]benzyl]cyclopropane-1,2-dicarboxamide
-
0.00000038
(1S,2R)-2-[[(3R)-3-(dimethylamino)pyrrolidin-1-yl]carbonyl]-N-hydroxy-2-[4-[(2-phenylquinolin-4-yl)methoxy]benzyl]cyclopropanecarboxamide
-
0.00000054
(1S,2R)-2-[[(3S)-3-(dimethylamino)pyrrolidin-1-yl]carbonyl]-N-hydroxy-2-[4-[(2-phenylquinolin-4-yl)methoxy]benzyl]cyclopropanecarboxamide
-
0.0000003
(1S,2R)-N-hydroxy-2-[[(2S)-2-(hydroxymethyl)pyrrolidin-1-yl]carbonyl]-2-[4-[(2-phenylquinolin-4-yl)methoxy]benzyl]cyclopropanecarboxamide
-
0.00000025
(1S,2R)-N-hydroxy-2-[[(3S)-3-hydroxypyrrolidin-1-yl]carbonyl]-2-[4-[(2-phenylquinolin-4-yl)methoxy]benzyl]cyclopropanecarboxamide
-
0.000004
(1S,2S)-2-((S)-cyano(4-((2-phenylquinolin-4-yl)methoxy)phenyl)methyl)-N-hydroxycyclopropanecarboxamide
-
0.000381
ethyl (1R,2S)-1-[3-bromo-4-[(2-methylquinolin-4-yl)methoxy]benzyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
0.000158
ethyl (1R,2S)-1-[3-chloro-4-[(2-methylquinolin-4-yl)methoxy]benzyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
0.000005
ethyl (1R,2S)-1-[3-fluoro-4-[(2-methylquinolin-4-yl)methoxy]benzyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
0.000002
ethyl (1R,2S)-1-[4-[(2-ethylquinolin-4-yl)methoxy]benzyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
0.000018
ethyl (1R,2S)-2-(hydroxycarbamoyl)-1-(4-[[2-(2-methylpropyl)quinolin-4-yl]methoxy]benzyl)cyclopropanecarboxylate
-
0.000003
ethyl (1R,2S)-2-(hydroxycarbamoyl)-1-(4-[[2-(trifluoromethyl)quinolin-4-yl]methoxy]benzyl)cyclopropanecarboxylate
-
0.000006
ethyl (1R,2S)-2-(hydroxycarbamoyl)-1-[4-[(2-methylquinolin-4-yl)methoxy]benzyl]cyclopropanecarboxylate
-
0.000037
ethyl (1R,2S)-2-(hydroxycarbamoyl)-1-[4-[(2-phenylpyridin-4-yl)methoxy]benzyl]cyclopropanecarboxylate
-
0.000012
ethyl (1R,2S)-2-(hydroxycarbamoyl)-1-[4-[(2-phenylquinolin-4-yl)methoxy]benzyl]cyclopropanecarboxylate
-
0.000022
ethyl (1R,2S)-2-(hydroxycarbamoyl)-1-[4-[(2-pyridin-3-ylquinolin-4-yl)methoxy]benzyl]cyclopropanecarboxylate
-
0.0011
(1R,2R)-2-(3-phenoxylphenyl)-2-trans-carbomethoxylcyclopropane hydroxamic acid
-
-
0.000008
(1R,2R)-2-trans-carboisopropoxyl-2-[3-(2-methylquinolin-4-yl)methoxylphenyl]cyclopropane hydroxyamic acid
-
-
0.00014
(1R,2R)-2-trans-N-benzylaminocarbonyl-2-[3-(2-methylquinolin-4-yl)methoxylphenyl]cyclopropane hydroxyamic acid
-
-
0.000011
(1R,2R)-2-[3-(3,4-dichlorobenzyloxy)phenyl]-2-trans-carbomethoxylcyclopropane hydroxamic acid
-
-
0.005
(1R,2R)-N-hydroxy-2-[(4-methylpiperazin-1-yl)carbonyl]-2-[3-[(2-methylquinolin-4-yl)methoxy]phenyl]cyclopropanecarboxamide
-
-
0.003
(1R,2R)-N1-benzyl-N2-hydroxy-N1-methyl-1-[3-[(2-methylquinolin-4-yl)methoxy]phenyl]cyclopropane-1,2-dicarboxamide
-
-
0.000009
(1R,2R)-N1-cyclohexyl-N2-hydroxy-1-[3-[(2-methylquinolin-4-yl)methoxy]phenyl]cyclopropane-1,2-dicarboxamide
-
-
0.000011
(1R,2R)-N2-hydroxy-1-[3-[(2-methylquinolin-4-yl)methoxy]phenyl]-N1-phenylcyclopropane-1,2-dicarboxamide
-
-
0.0027
(1R,2R)-N2-hydroxy-N1,N1-dimethyl-1-[3-[(2-methylquinolin-4-yl)methoxy]phenyl]cyclopropane-1,2-dicarboxamide
-
-
0.0001
(1R,2R)-N2-hydroxy-N1-methyl-1-[3-[(2-methylquinolin-4-yl)methoxy]phenyl]cyclopropane-1,2-dicarboxamide
-
-
0.00036
(1R,2S)-1-[4-(benzyloxy)benzyl]-N2-hydroxycyclopropane-1,2-dicarboxamide
-
-
0.00008
(1R,2S)-1-[4-(but-2-yn-1-yloxy)benzyl]-N2-hydroxycyclopropane-1,2-dicarboxamide
-
-
0.000003
(1R,2S)-N2-hydroxy-1-[4-[(2-methylquinolin-4-yl)methoxy]benzyl]cyclopropane-1,2-dicarboxamide
-
-
0.000001
(1R,2S)-N2-hydroxy-N1,N1-dimethyl-1-[4-[(2-methylquinolin-4-yl)methoxy]benzyl]cyclopropane-1,2-dicarboxamide
-
-
0.000014
(1R,2S)-N2-hydroxy-N1-methyl-1-[4-[(2-methylquinolin-4-yl)methoxy]benzyl]cyclopropane-1,2-dicarboxamide
-
-
0.000012
(1S,2R)-N-hydroxy-2-{4-[(2-imino-1,2-dihydroquinolin-4-yl)methoxy]benzyl}-2-(methoxycarbonyl)cyclopropanecarboximidic acid
-
-
0.000002
(5R)-5-(2',4'-difluorobiphenyl-4-yl)-5-[(6-fluoro-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.000002
(5R)-5-(4'-chlorobiphenyl-4-yl)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.00001
(5R)-5-[(6-fluoro-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[2'-(1-methyl-1H-tetrazol-5-yl)biphenyl-4-yl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.000018
(5R)-5-[(6-fluoro-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4'-(trifluoromethyl)biphenyl-4-yl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.0000002
(5R)-5-[(6-fluoro-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(6-oxo-1,6-dihydropyridin-3-yl)phenyl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.000001
(5R)-5-[(6-fluoro-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(pyridin-3-yl)phenyl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.0000008
(5R)-5-[(6-fluoro-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(quinolin-6-yl)phenyl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.000031
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[3'-(2-methyl-1,3-thiazol-4-yl)biphenyl-4-yl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.000002
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4'-(1H-pyrazol-3-yl)biphenyl-4-yl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.0000006
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(1,3-thiazol-2-yl)phenyl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.000002
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(1-methyl-1H-pyrazol-4-yl)phenyl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.000003
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(1-methyl-1H-pyrrolo[2,3-c]pyridin-5-yl)phenyl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.000002
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(2-methyl-2H-indazol-6-yl)phenyl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.0000005
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(2-methylpyridin-4-yl)phenyl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.000028
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(3-phenyl-1,2-oxazol-5-yl)phenyl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.0000026
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(4-methyl-2,5-dioxoimidazolidin-4-yl)phenyl]imidazolidine-2,4-dione (non-preferred name)
-
pH and temperature not specified in the publication
0.0000012
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(pyrazin-2-yl)phenyl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.0000005
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(pyridin-2-yl)phenyl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.0000008
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(pyridin-3-yl)phenyl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.0000006
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(pyridin-4-yl)phenyl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.0000009
(5R)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(pyrimidin-5-yl)phenyl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.0000014
(5R)-5-[4-(2-aminopyridin-4-yl)phenyl]-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.0000005
(5R)-5-[4-(3,5-dimethyl-1,2-oxazol-4-yl)phenyl]-5-[(6-fluoro-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.0000001
(5R)-5-[4-(5-chloro-6-oxo-1,6-dihydropyridin-3-yl)phenyl]-5-[(6-fluoro-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.0000008
(5S)-5-(4-fluorophenyl)-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.000005
1-methylethyl (1R,2R)-2-(hydroxycarbamoyl)-1-[3-[(2-methylquinolin-4-yl)methoxy]phenyl]cyclopropanecarboxylate
-
-
0.00019
2-(3-benzyloxyphenyl)-2-trans-carbomethoxylcyclopropane hydroxyamic acid
-
-
0.0007
2-[3-(2-methylquinolin-4-yl)methoxylphenyl]-2-trans-carboxamidocyclopropane hydroxyamic acid
-
-
0.000008
2-[3-(2-methylquinolin-4-yl)methoxyphenyl]-2-trans-carbomethoxylcyclopropane hydroxyamic acid
-
-
0.000003
4'-[(4R)-4-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-2,5-dioxoimidazolidin-4-yl]biphenyl-4-carboxamide
-
pH and temperature not specified in the publication
0.000006
5-[(5-methoxy-3-oxo-1,3-dihydro-2H-indazol-2-yl)methyl]-5-phenylimidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.000029
5-[(6-fluoro-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-(2-phenoxyphenyl)imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.000027
5-[(6-fluoro-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-(3-phenoxyphenyl)imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.000008
5-[(6-fluoro-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(2-oxopyrrolidin-1-yl)phenyl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.000006
5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(morpholin-4-yl)phenyl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.000007
5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(pyridin-4-yloxy)phenyl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.000006
5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-5-[4-(pyrrolidin-1-ylcarbonyl)phenyl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.000003
5-[4-(cyclopentyloxy)phenyl]-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.000008
5-[4-(isoquinolin-7-yloxy)phenyl]-5-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]imidazolidine-2,4-dione
-
pH and temperature not specified in the publication
0.000016
ethyl (1R,2R)-2-(hydroxycarbamoyl)-1-[3-[(2-methylquinolin-4-yl)methoxy]phenyl]cyclopropanecarboxylate
-
-
0.0031
ethyl (1R,2S)-2-(hydroxycarbamoyl)-1-(4-phenoxybenzyl)cyclopropanecarboxylate
-
-
0.00005
methyl (1R,2R)-1-[3-(2-[3-[(1Z)-buta-1,3-dien-1-yl]phenyl]ethoxy)phenyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
-
0.0012
methyl (1R,2R)-1-[3-(benzyloxy)phenyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
-
0.0016
methyl (1R,2R)-1-[3-(but-2-yn-1-yloxy)phenyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
-
0.0009
methyl (1R,2R)-1-[3-(cyclohexylmethoxy)phenyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
-
0.00005
methyl (1R,2R)-1-[3-[(4-chlorobenzyl)oxy]phenyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
-
0.003
methyl (1R,2R)-2-(hydroxycarbamoyl)-1-(3-methoxyphenyl)cyclopropanecarboxylate
-
-
0.00007
methyl (1R,2R)-2-(hydroxycarbamoyl)-1-(3-[[3-(trifluoromethyl)benzyl]oxy]phenyl)cyclopropanecarboxylate
-
-
0.000018
methyl (1R,2R)-2-(hydroxycarbamoyl)-1-(3-[[4-(trifluoromethyl)benzyl]oxy]phenyl)cyclopropanecarboxylate
-
-
0.00024
methyl (1R,2R)-2-(hydroxycarbamoyl)-1-[3-(2-methylphenoxy)phenyl]cyclopropanecarboxylate
-
-
0.00006
methyl (1R,2R)-2-(hydroxycarbamoyl)-1-[3-(2-naphthalen-2-ylethoxy)phenyl]cyclopropanecarboxylate
-
-
0.00029
methyl (1R,2R)-2-(hydroxycarbamoyl)-1-[3-(2-phenylethoxy)phenyl]cyclopropanecarboxylate
-
-
0.00014
methyl (1R,2R)-2-(hydroxycarbamoyl)-1-[3-(4-methylphenoxy)phenyl]cyclopropanecarboxylate
-
-
0.003
methyl (1R,2R)-2-(hydroxycarbamoyl)-1-[3-(naphthalen-2-ylmethoxy)phenyl]cyclopropanecarboxylate
-
-
0.00007
methyl (1R,2R)-2-(hydroxycarbamoyl)-1-[3-(naphthalen-2-yloxy)phenyl]cyclopropanecarboxylate
-
-
0.00011
methyl (1R,2R)-2-(hydroxycarbamoyl)-1-[3-[(3-methoxybenzyl)oxy]phenyl]cyclopropanecarboxylate
-
-
0.0008
methyl (1R,2S)-1-[4-(benzyloxy)benzyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
-
0.00042
methyl (1R,2S)-1-[4-(but-2-yn-1-yloxy)benzyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
-
0.026
methyl (1R,2S)-1-[4-(cyclohexylmethoxy)benzyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
-
0.00026
methyl (1R,2S)-1-[4-[(2-chlorobenzyl)oxy]benzyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
-
0.00013
methyl (1R,2S)-1-[4-[(3,4-dichlorobenzyl)oxy]benzyl]-2-(hydroxycarbamoyl)cyclopropanecarboxylate
-
-
0.1
methyl (1R,2S)-2-(hydroxycarbamoyl)-1-[4-(2-naphthalen-1-ylethoxy)benzyl]cyclopropanecarboxylate
-
-
0.1
methyl (1R,2S)-2-(hydroxycarbamoyl)-1-[4-(2-naphthalen-2-ylethoxy)benzyl]cyclopropanecarboxylate
-
-
0.000009
methyl 4'-[(4R)-4-[(6-methoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)methyl]-2,5-dioxoimidazolidin-4-yl]biphenyl-4-carboxylate
-
pH and temperature not specified in the publication
0.00008
N-[(4S,5S,7R)-2-[7-(1-benzylpiperidin-4-yl)]methylcarbamoyl-5-hydroxy-2-methyloct-4-yl]-N'-[(R)-1-(4-fluorophenyl)ethyl]-5-[methyl(methylsulfonyl)amino]isophthalamide
-
-
additional information
additional information
inhibition kinetics, overview
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0042
(5R)-4-(2-((1R,3R)-adamantan-1-yl)ethyl)-5-(4-hydroxybenzyl)-1-((2R)-1-(2-(((R)-6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl)-methyl)pyrrolidin-1-yl)-3-(naphthalen-2-yl)propan-2-yl)piperazine-2,3-dione
Homo sapiens
at pH 7.5 and 37°C
0.015
(5S)-1-((S)-1-((S)-2-(((S)-2,3-dioxo-6-propylpiperazin-1-yl)-methyl)pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl)-5-(4-hydroxybenzyl)-4-(2-phenylbutyl)piperazine-2,3-dione
Homo sapiens
at pH 7.5 and 37°C
0.0054
(R)-4-(2-((3R,5R,7R)-adamantan-1-yl)ethyl)-1-((S)-1-((S)-2-(((S)-2,3-dioxo-6-propylpiperazin-1-yl)methyl)pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl)-5-(4-hydroxybenzyl)piperazine-2,3-dione
Homo sapiens
at pH 7.5 and 37°C
0.0079
(R)-4-(2-((3R,5R,7R)-adamantan-1-yl)ethyl)-1-((S)-1-((S)-2-(((S)-2,3-dioxo-6-propylpiperazin-1-yl)methyl)pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl)-5-(naphthalen-2-ylmethyl)piperazine-2,3-dione
Homo sapiens
at pH 7.5 and 37°C
0.0057
(R)-4-(2-((3R,5R,7R)-adamantan-1-yl)ethyl)-1-((S)-1-(4-hydroxyphenyl)-3-((S)-2-(((R)-6-(naphthalen-2-ylmethyl)-2,3-dioxopiperazin-1-yl)methyl)pyrrolidin-1-yl)propan-2-yl)-5-(naphthalen-2-ylmethyl)piperazine-2,3-dione
Homo sapiens
at pH 7.5 and 37°C
0.015
(R)-4-(2-((3R,5R,7R)-adamantan-1-yl)ethyl)-5-(4-hydroxybenzyl)-1-((S)-1-(4-hydroxyphenyl)-3-((S)-2-(((R)-6-(naphthalen-2-ylmethyl)-2,3-dioxopiperazin-1-yl)methyl)pyrrolidin-1-yl)propan-2-yl)-piperazine-2,3-dione
Homo sapiens
at pH 7.5 and 37°C
0.0054
(S)-1((R)-1((S)-2-(((S)-6-benzyl-2,3-dioxopiperazin-1-yl)methyl)-pyrrolidin-1-yl)-3-cyclohexylpropan-2-yl)-5-(4-hydroxybenzyl)-4-phenethylpiperazine-2,3-dione
Homo sapiens
at pH 7.5 and 37°C
0.01
(S)-4-((3S,5S,7S)-adamantan-1 -ylmethyl)-1-((S)-1-((S)-2-(((S)-2,3-dioxo-6-propylpiperazin-1-yl)methyl)pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl)-5-(4-hydroxybenzyl)piperazine-2,3-dione
Homo sapiens
at pH 7.5 and 37°C
0.01
(S)-4-((4-(tert-butyl)cyclohexyl)methyl)-1-((S)-1-((S)-2-(((S)-2,3-dioxo-6-propylpiperazin-1-yl)methyl)pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl)-5-(4-hydroxybenzyl)piperazine-2,3-dione
Homo sapiens
at pH 7.5 and 37°C
0.0059
(S)-4-(2-((3S,5S,7S)-adamantan-1-yl)ethyl)-1-((S)-1-((S)-2-(((S)-2,3-dioxo-6-propylpiperazin-1-yl)methyl)pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl)-5-(4-hydroxybenzyl)piperazine-2,3-dione
Homo sapiens
at pH 7.5 and 37°C
0.01
(S)-4-(2-((3S,5S,7S)-adamantan-1-yl)ethyl)-1-((S)-1-((S)-2-(((S)-2,3-dioxo-6-propylpiperazin-1-yl)methyl)pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl)-5-(naphthalen-2-ylmethyl)piperazine-2,3-dione
Homo sapiens
at pH 7.5 and 37°C
0.0084
(S)-4-(2-((3S,5S,7S)-adamantan-1-yl)ethyl)-1-((S)-1-(4-hydroxyphenyl)-3-((S)-2-(((R)-6-(naphthalen-2-ylmethyl)-2,3-dioxopiperazin-1-yl)methyl)pyrrolidin-1-yl)propan-2-yl)-5-(naphthalen-2-ylmethyl)piperazine-2,3-dione
Homo sapiens
at pH 7.5 and 37°C
0.0081
(S)-4-(2-((3S,5S,7S)-adamantan-1-yl)ethyl)-5-(4-hydroxybenzyl)-1-((S)-1-(4-hydroxyphenyl)-3-((S)-2-(((R)-6-(naphthalen-2-ylmethyl)-2,3-dioxopiperazin-1-yl)methyl)pyrrolidin-1-yl)propan-2-yl)-piperazine-2,3-dione
Homo sapiens
at pH 7.5 and 37°C
0.0065
(S)-4-(2-((3S,5S,7S)-adamantan-1-yl)ethyl)-5-butyl-1-((S)-1-((S)-2-(((S)-2,3-dioxo-6-propylpiperazin-1-yl)methyl)pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl)piperazine-2,3-dione
Homo sapiens
at pH 7.5 and 37°C
0.0057
(S)-4-(2-(adamantan-1-yl)ethyl)-5-butyl-1-((S)-1-(4-hydroxyphenyl)-3-((S)-2-(((R)-6-(naphthalen-2-ylmethyl)-2,3-dioxopiperazin-1-yl)methyl)pyrrolidin-1-yl)propan-2-yl)piperazine-2,3-dione
Homo sapiens
at pH 7.5 and 37°C
0.011
(S)-4-(2-(adamantan-1yl)ethyl)-1-((S)-1-((S)-2-(((S)-6-benzyl-2,3-dioxopiperazin-1-yl)methyl)pyrrolidin-1-yl)-3-phenylpropan-2-yl)-5-(4-hydroxybenzyl)piperazine-2,3-dione
Homo sapiens
at pH 7.5 and 37°C
0.094
(S)-4-(cyclobutylmethyl)-1-((S)-1-((S)-2-(((S)-2,3-dioxo-6-propylpiperazin-1-yl)methyl)pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl)-5-(4-hydroxybenzyl)piperazine-2,3-dione
Homo sapiens
at pH 7.5 and 37°C
0.029
(S)-4-(cyclohexylmethyl)-1-((S)-1-((S)-2-(((S)-2,3-dioxo-6-propylpiperazin-1-yl)methyl)pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl)-5-(4-hydroxybenzyl)piperazine-2,3-dione
Homo sapiens
at pH 7.5 and 37°C
0.035
(S)-4-(cyclopentylmethyl)-1-((S)-1-((S)-2-(((S)-2,3-dioxo-6-propylpiperazin-1-yl)methyl)pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl)-5-(4-hydroxybenzyl)piperazine-2,3-dione
Homo sapiens
at pH 7.5 and 37°C
0.0085
(S)-5-benzyl-1-((R)-1-((S)-2-(((S)-6-benzyl-2,3-dioxopiperazin-1-yl)methyl)pyrrolidin-1-yl)-3-cyclohexylpropan-2-yl)-4-phenethylpiperazine-2,3-dione
Homo sapiens
at pH 7.5 and 37°C
0.0043
(S)-5-benzyl-1-((R)-1-cyclohexyl-3-((S)-2-(((S)-2,3-dioxo-6-propylpiperazin-1-yl)methyl)pyrrolidin-1-yl)propan-2-yl)-4-phenethylpiperazine-2,3-dione
Homo sapiens
at pH 7.5 and 37°C
0.05 - 0.06
1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(4-hydroxyphenyl)propan-2-yl]-5-(4-hydroxybenzyl)-4-[3-adamantylpropyl]piperazine-2,3-dione
0.051 - 0.058
1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(naphthalen-2-yl)propan-2-yl]-5-(4-hydroxybenzyl)-4-[3-adamantylpropyl]piperazine-2,3-dione
0.031 - 0.045
4-(2-butylbenzyl)-1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(4-hydroxyphenyl)propan-2-yl]-5-(4-hydroxybenzyl)piperazine-2,3-dione
0.054 - 0.056
4-(2-butylbenzyl)-1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(naphthalen-2-yl)propan-2-yl]-5-(4-hydroxybenzyl)piperazine-2,3-dione
0.05 - 0.059
4-(2-butylbenzyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl]piperazine-2,3-dione
0.00536 - 0.057
4-(2-butylbenzyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(naphthalen-2-yl)propan-2-yl]piperazine-2,3-dione
0.017 - 0.032
4-(cyclopentylmethyl)-1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(4-hydroxyphenyl)propan-2-yl]-5-(4-hydroxybenzyl)piperazine-2,3-dione
0.051 - 0.056
4-(cyclopentylmethyl)-1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(naphthalen-2-yl)propan-2-yl]-5-(4-hydroxybenzyl)piperazine-2,3-dione
0.034 - 0.042
4-(cyclopentylmethyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl]piperazine-2,3-dione
0.00432 - 0.09
4-(cyclopentylmethyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(naphthalen-2-yl)propan-2-yl]piperazine-2,3-dione
0.056 - 0.06
5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl]-4-[3-adamantylpropyl]piperazine-2,3-dione
0.062
5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl]-4-[3-adamanylpropyl]piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.061 - 0.095
5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(naphthalen-2-yl)propan-2-yl]-4-[3-adamantylpropyl]piperazine-2,3-dione
0.0000023
(3S)-4-[[4-(but-2-ynylamino)phenyl]sulfonyl]-N-hydroxy-2,2-dimethylthio-morpholine-3-carboxamide
Homo sapiens
-
-
0.0000011
1-(1,3-benzoxazol-2-yl)-4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-N-hydroxypiperidine-4-carboxamide
Homo sapiens
-
-
0.000001
1-(1H-benzimidazol-2-yl)-4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-N-hydroxypiperidine-4-carboxamide
Homo sapiens
-
IC50 above 0.000001 mM
0.0000015
1-(2,2-dimethylpropanoyl)-N-hydroxy-4-[([4-[(2-methylquinolin-4-yl)methyl]phenyl]carbonyl)amino]pyrrolidine-3-carboxamide
Homo sapiens
-
-
0.0000023
1-(2,2-dimethylpropanoyl)-N-hydroxy-4-[[([4-[(2-methylquinolin-4-yl)methoxy]phenyl]carbonyl)amino]methyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.0000016
1-(2,2-dimethylpropyl)-N-hydroxy-4-[([4-[(2-methylquinolin-4-yl)methyl]phenyl]carbonyl)amino]pyrrolidine-3-carboxamide
Homo sapiens
-
-
0.0000011
1-(butylsulfonyl)-N-hydroxy-4-[([4-[(2-methylquinolin-4-yl)methyl]phenyl]carbonyl)amino]pyrrolidine-3-carboxamide
Homo sapiens
-
-
0.000001
1-but-2-yn-1-yl-N-hydroxy-4-[([4-[(2-methylquinolin-4-yl)methyl]phenyl]carbonyl)amino]pyrrolidine-3-carboxamide
Homo sapiens
-
-
0.0000012
1-ethylpropyl 4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-4-(hydroxycarbamoyl)piperidine-1-sulfinate
Homo sapiens
-
-
0.0000014
1-methyl-2-morpholin-4-ylethyl 4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-4-(hydroxycarbamoyl)piperidine-1-sulfinate
Homo sapiens
-
-
0.0000015
1-methylethyl 4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-4-(hydroxycarbamoyl)piperidine-1-sulfinate
Homo sapiens
-
-
0.0000015
1-[(4-acetylpiperazin-1-yl)sulfonyl]-4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-N-hydroxypiperidine-4-carboxamide
Homo sapiens
-
-
0.00003
2-(6-methyl-2-oxo-2H-chromen-3-ylmethyl)-pent-4-enoic acid hydroxyamide
Homo sapiens
-
at 25°C
0.000005
2-benzyl-N-hydroxy-3-(6-methyl-2-oxo-2H-chromen-3-yl)-propionamide
Homo sapiens
-
at 25°C
0.0000022
2-morpholin-4-ylethyl 4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-4-(hydroxycarbamoyl)piperidine-1-sulfinate
Homo sapiens
-
-
0.0000026
3-([[4-(1,3-dihydrofuro[3,4-b]quinolin-9-ylmethyl)phenyl]carbonyl]amino)-N-hydroxytetrahydro-2H-pyran-2-carboxamide
Homo sapiens
-
-
0.000001
3-([[4-(2,3-dihydro-1H-cyclopenta[b]quinolin-9-ylmethyl)phenyl]carbonyl]amino)-N-hydroxytetrahydro-2H-pyran-2-carboxamide
Homo sapiens
-
-
0.0000013
3-([[4-(2,3-dihydrofuro[2,3-b]quinolin-4-ylmethyl)phenyl]carbonyl]amino)-N-hydroxytetrahydro-2H-pyran-2-carboxamide
Homo sapiens
-
-
0.0000012
3-[([4-[(2,3-dimethylquinolin-4-yl)methyl]phenyl]carbonyl)amino]-N-hydroxytetrahydro-2H-pyran-2-carboxamide
Homo sapiens
-
-
0.0000013
3-[([4-[(2-cyclopropylquinolin-4-yl)methyl]phenyl]carbonyl)amino]-N-hydroxytetrahydro-2H-pyran-2-carboxamide
Homo sapiens
-
-
0.0000017
3-[([4-[(2-ethylquinolin-4-yl)methyl]phenyl]carbonyl)amino]-N-hydroxytetrahydro-2H-pyran-2-carboxamide
Homo sapiens
-
-
0.0000078
3-[([4-[(3-ethyl-2-methylquinolin-4-yl)methyl]phenyl]carbonyl)amino]-N-hydroxytetrahydro-2H-pyran-2-carboxamide
Homo sapiens
-
-
0.0000032
3-[4-[2-(hydroxyamino)-2-oxoethyl]-4-[([4-[(2-methylquinolin-4-yl)methoxy]phenyl]carbonyl)amino]piperidin-1-yl]propanoic acid
Homo sapiens
-
-
0.0000012
3-[[(4-[[2-(dimethylamino)quinolin-4-yl]methyl]phenyl)carbonyl]amino]-N-hydroxytetrahydro-2H-pyran-2-carboxamide
Homo sapiens
-
-
0.0000025
4-(4-but-2-ynylamino-benzenesulfonylmethyl)-1-(2-methyl-benzoyl)-piperidine-4-carboxylic acid hydroxyamide
Homo sapiens
-
-
0.0000035
4-(4-but-2-ynylamino-benzenesulfonylmethyl)-1-(2-methyl-butyryl)-piperidine-4-carboxylic acid hydroxyamide
Homo sapiens
-
-
0.000002
4-(4-but-2-ynylamino-benzenesulfonylmethyl)-1-(propane-2-sulfonyl)-piperidine-4-carboxylic acid hydroxyamide
Homo sapiens
-
-
0.0000023
4-(4-but-2-ynylamino-benzenesulfonylmethyl)-1-isobutyryl-piperidine-4-carboxylic acid hydroxyamide
Homo sapiens
-
-
0.0000064
4-(4-but-2-ynylamino-benzenesulfonylmethyl)-1-pyridin-4-ylmethyl-piperidine-4-carboxylic acid hydroxyamide
Homo sapiens
-
-
0.000001
4-(4-but-2-ynylamino-benzenesulfonylmethyl)-piperidine-1,4-dicarboxylic acid 1-diethylamide 4-hydroxyamide
Homo sapiens
-
IC50 below 0.000001 mM
0.000064
4-(4-but-2-ynylamino-benzenesulfonylmethyl)-piperidine-4-carboxylic acid hydroxyamide
Homo sapiens
-
-
0.0000018
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-1-(dimethylsulfamoyl)-N-hydroxypiperidine-4-carboxamide
Homo sapiens
-
-
0.000001
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-1-[(2,5-dichlorothiophen-3-yl)sulfonyl]-N-hydroxypiperidine-4-carboxamide
Homo sapiens
-
IC50 below 0.000001 mM
0.000001
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-1-[(2,5-dimethyl-1,3-thiazol-4-yl)sulfonyl]-N-hydroxypiperidine-4-carboxamide
Homo sapiens
-
IC50 below 0.000001 mM
0.0000017
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-1-[(3,5-dichloropyridin-4-yl)carbonyl]-N-hydroxypiperidine-4-carboxamide
Homo sapiens
-
-
0.0000016
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-1-[(3,5-dichloropyridin-4-yl)methyl]-N-hydroxypiperidine-4-carboxamide
Homo sapiens
-
-
0.000001
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-1-[(3,5-dimethyl-1H-pyrazol-4-yl)sulfonyl]-N-hydroxypiperidine-4-carboxamide
Homo sapiens
-
IC50 below 0.000001 mM
0.0000022
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-1-[(3,5-dimethylisoxazol-4-yl)sulfonyl]-N-hydroxypiperidine-4-carboxamide
Homo sapiens
-
-
0.000007
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-1-[(5-chlorothiophen-2-yl)sulfonyl]-N-hydroxypiperidine-4-carboxamide
Homo sapiens
-
-
0.000001
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-N-hydroxy-1-(morpholin-4-ylsulfonyl)piperidine-4-carboxamide
Homo sapiens
-
-
0.0000012
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-N-hydroxy-1-(piperidin-1-ylsulfonyl)piperidine-4-carboxamide
Homo sapiens
-
-
0.000001
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-N-hydroxy-1-(pyrrolidin-1-ylsulfonyl)piperidine-4-carboxamide
Homo sapiens
-
-
0.00000133
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-N-hydroxy-1-pyridin-2-ylpiperidine-4-carboxamide
Homo sapiens
-
-
0.0000056
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-N-hydroxy-1-pyridin-4-ylpiperidine-4-carboxamide
Homo sapiens
-
-
0.000003
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-N-hydroxy-1-[(2-methyl-1H-imidazol-4-yl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.0000014
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-N-hydroxy-1-[[(2R)-2-(hydroxymethyl)pyrrolidin-1-yl]sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.0000015
4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-N-hydroxy-1-[[(2S)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.000027
4-[([4-[(1,1-dimethylbut-2-yn-1-yl)oxy]phenyl]sulfonyl)methyl]-N-hydroxy-1-(isopropylsulfonyl)piperidine-4-carboxamide
Homo sapiens
-
-
0.0000028
4-[2-(hydroxyamino)-2-oxoethyl]-N,N-dimethyl-4-[([4-[(2-methylquinolin-4-yl)methoxy]phenyl]carbonyl)amino]piperidine-1-carboxamide
Homo sapiens
-
-
0.00001
4-[4-(4-hydroxy-but-2-ynylamino)-benzenesulfonylmethyl]-4-hydroxycarbamoyl-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
-
0.009
4-[[4-(2-butynyloxy)phenyl]sulfonyl]-N-hydroxy-2,2-dimethyl-(3S)-thiomorpholinecarboxamide
Homo sapiens
-
IC50: 0.009 mM
0.0000028
cyclohexyl 4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-4-(hydroxycarbamoyl)piperidine-1-sulfinate
Homo sapiens
-
-
0.000001
cyclohexylmethyl 4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-4-(hydroxycarbamoyl)piperidine-1-sulfinate
Homo sapiens
-
IC50 above 0.000001 mM
0.0000013
cyclopentyl 4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-4-(hydroxycarbamoyl)piperidine-1-sulfinate
Homo sapiens
-
-
0.0000016
cyclopropyl 4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-4-(hydroxycarbamoyl)piperidine-1-sulfinate
Homo sapiens
-
-
0.000317
GM6001
Homo sapiens
-
in 25 mM Tris-HCl buffer, pH 9, 0.0025 mM ZnCl2 and 0.005% (v/v) Brij-35, at 37°C
0.0000033
methyl 3-(hydroxycarbamoyl)-4-[([4-[(2-methylquinolin-4-yl)methyl]phenyl]carbonyl)amino]pyrrolidine-1-carboxylate
Homo sapiens
-
-
0.11
N(R)-[2-(hydroxyaminocarbonyl)methyl]-4-methylpentanoyl-L-alanine amide
Homo sapiens
-
IC50: about 0.11 mM
0.0000016
N-hydroxy-1-(2-methylpropyl)-4-[([4-[(2-methylquinolin-4-yl)methyl]phenyl]carbonyl)amino]pyrrolidine-3-carboxamide
Homo sapiens
-
-
0.0000025
N-hydroxy-1-methyl-4-[([4-[(2-methylquinolin-4-yl)methyl]phenyl]carbonyl)amino]pyrrolidine-3-carboxamide
Homo sapiens
-
-
0.000175
N-hydroxy-2-(2-oxo-2H-chromen-3-yl)acetamide
Homo sapiens
-
in 25 mM Tris-HCl buffer, pH 9.0, 0.0025 mM ZnCl2 and 0.005% (v/v) Brij-35, at 37°C
0.000003
N-hydroxy-2-methyl-3-(6-methyl-2-oxo-2H-chromen-3-yl)-propionamide
Homo sapiens
-
at 25°C
0.0000016
N-hydroxy-3-[([4-[(2-morpholin-4-ylquinolin-4-yl)methyl]phenyl]carbonyl)amino]tetrahydro-2H-pyran-2-carboxamide
Homo sapiens
-
-
0.0000015
N-hydroxy-3-[([4-[(3-methylquinolin-4-yl)methyl]phenyl]carbonyl)amino]tetrahydro-2H-pyran-2-carboxamide
Homo sapiens
-
-
0.0000022
N-hydroxy-3-[[(4-[[2-(trifluoromethyl)quinolin-4-yl]methyl]phenyl)carbonyl]amino]tetrahydro-2H-pyran-2-carboxamide
Homo sapiens
-
-
0.0000063
N-hydroxy-4-[([4-[(2-methylquinolin-4-yl)methoxy]phenyl]carbonyl)amino]pyrrolidine-3-carboxamide
Homo sapiens
-
-
0.0000043
N-hydroxy-4-[([4-[(2-methylquinolin-4-yl)methyl]phenyl]carbonyl)amino]-1-prop-2-yn-1-ylpyrrolidine-3-carboxamide
Homo sapiens
-
-
0.000001
N-hydroxy-4-[([4-[(2-methylquinolin-4-yl)methyl]phenyl]carbonyl)amino]tetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
-
0.000002
N-hydroxy-4-[([4-[(2-methylquinolin-4-yl)methyl]phenyl]carbonyl)amino]tetrahydrofuran-3-carboxamide
Homo sapiens
-
-
0.0000035
N-hydroxy-4-[([4-[(2-methylquinolin-4-yl)oxy]phenyl]carbonyl)amino]pyrrolidine-3-carboxamide
Homo sapiens
-
-
0.0000019
N-hydroxy-4-[[([4-[(2-methylquinolin-4-yl)methoxy]phenyl]carbonyl)amino]methyl]-1-(methylsulfonyl)piperidine-4-carboxamide
Homo sapiens
-
-
0.000011
N-hydroxy-4-[[([4-[(2-methylquinolin-4-yl)methoxy]phenyl]carbonyl)amino]methyl]-1-propylpiperidine-4-carboxamide
Homo sapiens
-
-
0.0000049
N-hydroxy-4-[[([4-[(2-methylquinolin-4-yl)methoxy]phenyl]carbonyl)amino]methyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.0000023
N-hydroxy-4-[[([4-[(2-methylquinolin-4-yl)methoxy]phenyl]carbonyl)amino]methyl]tetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
-
0.0000023
N-[1-(1,1-dimethylprop-2-yn-1-yl)-4-[2-(hydroxyamino)-2-oxoethyl]piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
Homo sapiens
-
-
0.0000021
N-[1-(2,2-dimethylpropanoyl)-4-[2-(hydroxyamino)-2-oxoethyl]piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
Homo sapiens
-
-
0.0000026
N-[1-(2,2-dimethylpropyl)-4-[2-(hydroxyamino)-2-oxoethyl]piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
Homo sapiens
-
-
0.0000026
N-[1-(2-fluoroethyl)-4-[2-(hydroxyamino)-2-oxoethyl]piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
Homo sapiens
-
-
0.0000019
N-[1-(3,3-dimethylbutanoyl)-4-[2-(hydroxyamino)-2-oxoethyl]piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
Homo sapiens
-
-
0.0000012
N-[1-(4,5-dihydro-1,3-thiazol-2-yl)-4-[2-(hydroxyamino)-2-oxoethyl]piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
Homo sapiens
-
-
0.0000019
N-[1-acetyl-4-[2-(hydroxyamino)-2-oxoethyl]piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
Homo sapiens
-
-
0.0000022
N-[1-ethyl-4-[2-(hydroxyamino)-2-oxoethyl]piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
Homo sapiens
-
-
0.0000037
N-[1-tert-butyl-4-[2-(hydroxyamino)-2-oxoethyl]piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
Homo sapiens
-
-
0.0000014
N-[1-[2-(ethylsulfonyl)ethyl]-4-[2-(hydroxyamino)-2-oxoethyl]piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
Homo sapiens
-
-
0.0000077
N-[1-[2-(hydroxyamino)-2-oxoethyl]cyclohexyl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
Homo sapiens
-
-
0.0000018
N-[2-(hydroxycarbamoyl)cyclopentyl]-4-[(2-methylquinolin-4-yl)methyl]benzamide
Homo sapiens
-
-
0.0000012
N-[4-[2-(hydroxyamino)-2-oxoethyl]-1-(2-methylpropanoyl)piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
Homo sapiens
-
-
0.0000022
N-[4-[2-(hydroxyamino)-2-oxoethyl]-1-(3-methylbutanoyl)piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
Homo sapiens
-
-
0.000001
N-[4-[2-(hydroxyamino)-2-oxoethyl]-1-(methylsulfonyl)piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
Homo sapiens
-
-
0.0000031
N-[4-[2-(hydroxyamino)-2-oxoethyl]-1-methylpiperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
Homo sapiens
-
-
0.0000019
N-[4-[2-(hydroxyamino)-2-oxoethyl]-1-phenylpiperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
Homo sapiens
-
-
0.0000027
N-[4-[2-(hydroxyamino)-2-oxoethyl]-1-propanoylpiperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
Homo sapiens
-
-
0.000002
N-[4-[2-(hydroxyamino)-2-oxoethyl]-1-propylpiperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
Homo sapiens
-
-
0.0000012
N-[4-[2-(hydroxyamino)-2-oxoethyl]-1-[2-(methylsulfonyl)ethyl]piperidin-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
Homo sapiens
-
-
0.0000014
N-[4-[2-(hydroxyamino)-2-oxoethyl]tetrahydro-2H-pyran-4-yl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
Homo sapiens
-
-
0.000097
N-[4-[2-(hydroxyamino)-2-oxoethyl]tetrahydro-2H-pyran-4-yl]-4-[(2-methylquinolin-4-yl)methyl]benzamide
Homo sapiens
-
-
0.0000086
N-[[1-(hydroxycarbamoyl)cyclohexyl]methyl]-4-[(2-methylquinolin-4-yl)methoxy]benzamide
Homo sapiens
-
-
0.000002
pyridin-4-ylmethyl 4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-4-(hydroxycarbamoyl)piperidine-1-sulfinate
Homo sapiens
-
-
0.0000013
tert-butyl 3-(hydroxycarbamoyl)-4-[([4-[(2-methylquinolin-4-yl)oxy]phenyl]carbonyl)amino]pyrrolidine-1-carboxylate
Homo sapiens
-
-
0.0000019
tert-butyl 3-[4-[2-(hydroxyamino)-2-oxoethyl]-4-[([4-[(2-methylquinolin-4-yl)methoxy]phenyl]carbonyl)amino]piperidin-1-yl]propanoate
Homo sapiens
-
-
0.0000024
tert-butyl 4-(hydroxycarbamoyl)-4-[[([4-[(2-methylquinolin-4-yl)methoxy]phenyl]carbonyl)amino]methyl]piperidine-1-carboxylate
Homo sapiens
-
-
0.000001
tert-butyl 4-([[4-(but-2-yn-1-yloxy)phenyl]sulfonyl]methyl)-4-(hydroxycarbamoyl)piperidine-1-sulfinate
Homo sapiens
-
IC50 above 0.000001 mM
0.0000016
tert-butyl 4-([[4-(but-2-ynylamino)phenyl]sulfonyl]methyl)-4-[(hydroxyamino)-carbonyl]piperidine-1-carboxylate
Homo sapiens
-
-
0.0000033
tert-butyl 4-[([4-[but-2-ynyl(methyl)amino]phenyl]sulfonyl)methyl]-4 [(hydroxyamino)carbonyl]piperidine-1-carboxylate
Homo sapiens
-
-
0.00007
tumor necrosis factor-alpha-converting enzyme pro domain
Homo sapiens
-
inhibition of the tumor necrosis factor-alpha-converting enzyme by its isolated pro domain, IC50: 70 nM
-
0.000004
[N-hydroxy-1-(isopropylsulfonyl)-4-[(4-[(1-methylbut-2-yn-1-yl)oxy]phenyl]sulfonyl)-methyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.05
1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(4-hydroxyphenyl)propan-2-yl]-5-(4-hydroxybenzyl)-4-[3-adamantylpropyl]piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.054
1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(4-hydroxyphenyl)propan-2-yl]-5-(4-hydroxybenzyl)-4-[3-adamantylpropyl]piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.059
1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(4-hydroxyphenyl)propan-2-yl]-5-(4-hydroxybenzyl)-4-[3-adamantylpropyl]piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.06
1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(4-hydroxyphenyl)propan-2-yl]-5-(4-hydroxybenzyl)-4-[3-adamantylpropyl]piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.051
1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(naphthalen-2-yl)propan-2-yl]-5-(4-hydroxybenzyl)-4-[3-adamantylpropyl]piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.058
1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(naphthalen-2-yl)propan-2-yl]-5-(4-hydroxybenzyl)-4-[3-adamantylpropyl]piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.031
4-(2-butylbenzyl)-1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(4-hydroxyphenyl)propan-2-yl]-5-(4-hydroxybenzyl)piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.039
4-(2-butylbenzyl)-1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(4-hydroxyphenyl)propan-2-yl]-5-(4-hydroxybenzyl)piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.04
4-(2-butylbenzyl)-1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(4-hydroxyphenyl)propan-2-yl]-5-(4-hydroxybenzyl)piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.045
4-(2-butylbenzyl)-1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(4-hydroxyphenyl)propan-2-yl]-5-(4-hydroxybenzyl)piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.054
4-(2-butylbenzyl)-1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(naphthalen-2-yl)propan-2-yl]-5-(4-hydroxybenzyl)piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.056
4-(2-butylbenzyl)-1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(naphthalen-2-yl)propan-2-yl]-5-(4-hydroxybenzyl)piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.05
4-(2-butylbenzyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl]piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.053
4-(2-butylbenzyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl]piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.058
4-(2-butylbenzyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl]piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.059
4-(2-butylbenzyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl]piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.00536
4-(2-butylbenzyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(naphthalen-2-yl)propan-2-yl]piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.054
4-(2-butylbenzyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(naphthalen-2-yl)propan-2-yl]piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.057
4-(2-butylbenzyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(naphthalen-2-yl)propan-2-yl]piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.017
4-(cyclopentylmethyl)-1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(4-hydroxyphenyl)propan-2-yl]-5-(4-hydroxybenzyl)piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.018
4-(cyclopentylmethyl)-1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(4-hydroxyphenyl)propan-2-yl]-5-(4-hydroxybenzyl)piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.032
4-(cyclopentylmethyl)-1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(4-hydroxyphenyl)propan-2-yl]-5-(4-hydroxybenzyl)piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.051
4-(cyclopentylmethyl)-1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(naphthalen-2-yl)propan-2-yl]-5-(4-hydroxybenzyl)piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.056
4-(cyclopentylmethyl)-1-[1-[2-[(2,3-dioxo-6-propylpiperazin-1-yl)methyl]pyrrolidin-1-yl]-3-(naphthalen-2-yl)propan-2-yl]-5-(4-hydroxybenzyl)piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.034
4-(cyclopentylmethyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl]piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.035
4-(cyclopentylmethyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl]piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.038
4-(cyclopentylmethyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl]piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.042
4-(cyclopentylmethyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl]piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.00432
4-(cyclopentylmethyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(naphthalen-2-yl)propan-2-yl]piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.066
4-(cyclopentylmethyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(naphthalen-2-yl)propan-2-yl]piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.09
4-(cyclopentylmethyl)-5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(naphthalen-2-yl)propan-2-yl]piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.056
5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl]-4-[3-adamantylpropyl]piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.06
5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(4-hydroxyphenyl)propan-2-yl]-4-[3-adamantylpropyl]piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.061
5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(naphthalen-2-yl)propan-2-yl]-4-[3-adamantylpropyl]piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
0.095
5-(4-hydroxybenzyl)-1-[1-(2-[[6-(4-hydroxybenzyl)-2,3-dioxopiperazin-1-yl]methyl]pyrrolidin-1-yl)-3-(naphthalen-2-yl)propan-2-yl]-4-[3-adamantylpropyl]piperazine-2,3-dione
Homo sapiens
pH 7.5, 22°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
ADAM17 proteolytic targets, amphiregulin, transforming growth factor (TGF-alpha), syndecan-1 (SDC1), and tumor necrosis factor receptor 1 (TNFR1), are shed from HVECs in response to staphylococcal superantigen toxic shock syndrome toxin TSST-1. ADAM17, but not related ADAM10, is required for amphiregulin, TGF-alpha, and TNFR1 shedding. Both ADAM10 and ADAM17 contribute to SDC1 shedding and IL-8 production by HVECs in response to TSST-1
-
TACE expression measured by immunohistochemical analysis is observed in 183 of 383 breast carcinomas. TACE expression is predominantly seen in tumors with high levels of released human epidermal growth factor-4 receptor intracellular domain (4ICD) and membranous human epidermal growth factor-4 receptor
-
metalloproteases ADAM-9, ADAM-15, and ADAM-17 are upregulated in advanced human atherosclerotic lesions in samples from carotid, aortic, and femoral territories compared to samples from internal thoracic artery free of atherosclerotic plaques. ADAM-9, ADAM-15, and ADAM-17-expressing cells colocalize with CD68-positive cells of monocytic origin in the atherosclerotic plaques, in the carotid territory, cells expressing the ADAMs codistribute also with smooth muscle cells
-
metalloproteases ADAM-9, ADAM-15, and ADAM-17 are upregulated in advanced human atherosclerotic lesions in samples from carotid, aortic, and femoral territories compared to samples from internal thoracic artery free of atherosclerotic plaques. ADAM-9, ADAM-15, and ADAM-17-expressing cells colocalize with CD68-positive cells of monocytic origin in the atherosclerotic plaques, in the femoral territory, cells expressing the ADAMs codistribute also with CD31-positive endothelial cells
-
sural nerve biopsies from Guillain-Barre syndrome patients. ADAM-17-expressing T cells can be localized primarily within the epi- and perineurium, whereas in control sections from patients with non-inflammatory neuropathies, no axpression can be depected. The enzyme may contribute to the pathogenesis of inflammatory demyelination of the peripheral nervous system
-
TACE expression measured by immunohistochemical analysis is observed in 39 of 217 ovarian carcinomas.TACE expression is predominantly seen in tumors with high levels of released human epidermal growth factor-4 receptor intracellular domain (4ICD) and membranous human epidermal growth factor-4 receptor
-
ADAM17/TACE mRNA is expressed in 3 of 10 normal pancreatic tissues, 6 of 8 samples from patients with chronic pancreatitis
-
ADAM17/TACE mRNA is expressed in 10 of 10 PDAC tissues. ADAM17/TACE mRNA expression is down-regulated in pancreatic cancer cells arrested in G2 -M phase. Critical involvement of ADAM17/TACE in the invasion behavior of pancreatic cancer cells
-
ADAM17/TACE mRNA is expressed in 10 of 10 PDAC tissues. ADAM17/TACE expression is a later event in progression of pancreatic intraepithelial neoplasia to pancreatic ductal adenocarcinoma
-
by analyzing villous samples representing different gestational ages, it is shown that TACE is continuously expressed in the placentas throughout gestation and that the levels of TACE are positively correlated with the levels of TGF-alpha, heparin-binding epidermal growth factor-like growth factor, and amphiregulin
-
Villous explant cultures or cytotrophoblastic cells are used. Preadministration of TACE inhibitor in villous explant cultures or transfection of cytotrophoblastic cells with TACE-specific small interference RNA decreases the shedding of heparin-binding epidermal growth factor-like growth factor and amphiregulin. Hypoxia (2% O2) causes an increase in the levels of TACE mRNA and protein in villous explants and primary cytotrophoblastic cells in vitro
-
TACE expression measured by immunohistochemical analysis is observed in 16 of 24 and 17 of 24 hormone-sensitive and hormone-insensitive prostate carcinomas. TACE expression is predominantly seen in tumors with high levels of released human epidermal growth factor-4 receptor intracellular domain (4ICD) and membranous human epidermal growth factor-4 receptor
-
metalloproteases ADAM-9, ADAM-15, and ADAM-17 are upregulated in advanced human atherosclerotic lesions in samples from carotid, abdominal aortic, and femoral territories compared to samples from internal thoracic artery free of atherosclerotic plaques. ADAM-9, ADAM-15, and ADAM-17-expressing cells colocalize with CD68-positive cells of monocytic origin in the atherosclerotic plaques
-
neocortex, cerebellum, pyramidal neurons of the cerebral cortex and granular cell layer neurons in the hippocampus
-
TACE amounts in gingival crevicular fluid are higher in persons with chronic and aggressive periodontitis than in those with gingivitis or in healthy persons. TACE concentrations in gingival crevicular fluid are higher in persons with chronic and aggressive periodontitis than in those with gingivitis, although not significantly higher than in healthy persons. Persons with chronic periodontitis receiving immunosuppressive treatment exhibit over 10fold lower TACE levels than the other periodontitis groups. TACE is positively correlated with probing pocket depth, clinical attachment levels, and receptor activator of NF-kappaB ligand concentrations in gingival crevicular fluid
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
most mature ADAM17 is localised intracellularly, with only a small amount at the cell surface
-
ADAM-17 is located diffusely within the cell cytoplasm, and treatment with TNF-alpha does not alter the level of expression or the cytoplasmic distribution of ADAM-17
-
detergent-resistant membrane microdomain, i.e. regions of the membrane enriched in cholesterol and sphingolipids
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
enzyme inhibition prevents progression of aneurysmal growth. Enzyme deficiency in smooth muscle and endothelial cells is sufficient to suppress thoracic aortic aneurysm dilation markedly. Enzyme deficiency in smooth muscle cells prevented the contractile-to-synthetic phenotypic switching in these cells after TAA induction, preventing perivascular fibrosis, inflammation, and adverse aortic remodeling. Loss of enzyme in endothelial cells protects the integrity of the intimal barrier by preserving the adherens junction (vascular endothelial-cadherin) and tight junctions (junctional adhesion molecule-A and claudin)
physiological function
malfunction
physiological function
physiological function
angiotensin II treatment of Huh-7 cells leads to angiotensin II type 1 receptor-dependent metalloproteinase mediated shedding of ACE2 while transfection with siTACE prevents shedding of ACE2
physiological function
ectopic over-expression of ADAM17 results in increased cell proliferation. ADAM17 promotes G1 to S phase transition concomitantly with upregulation of cyclin E, CDK2 and downregulation of p21 and p27 proteins. ADAM17 over-expression cells show more TGF-alpha released to the supernatant and activate the EGFR/PI3K/AKT pathway. Silencing ADAM17 leads to the opposite effect. Both siRNAs knockdown of ADAM17 and blocking the EGFR/PI3K/AKT pathway cause downregulation of cyclin E,CDK2,and upregulation of p21 and p27 in prostate cancer cells
physiological function
inhibitor TAPI-1, as well as antagonists of epidermal growth factor receptor and angiotensin II type-1 receptor, attenuate angiotensin II-induced epidermal growth factor receptor transactivation and proliferation of LI90 cells. Silencing of ADAM17 inhibits angiotensin II-induced secretion of mature amphiregulin in addition to epidermal growth factor receptor transactivation
physiological function
overexpression of ADAM10 and ADAM17 increase cleavage of cell surface VEGF receptor Flt while knockdown of ADAM10 and ADAM17 reduce N-terminal cleavage suggesting that these metalloproteases are responsible for Flt1 cleavage
physiological function
treatment of cells with TPI2155-14 and TPI2155-17, specific inhibitors for ADAM-17 protease, results in a significant decrease in non-membrane bound form of neprilysin, EC 3.4.24.11, activity in media, implicating a possible role for ADAM-17 in neprilysin release
physiological function
from one hand, ADAM17 is neuroprotective, since it cleaves amyloid precursor protein as alpha-secretase to inhibit Abeta generation. From the other hand, ADAM17 is neurotoxic, since it is also the sheddase of many pro-inflammatory factors
physiological function
the increased expression of the enzyme promotes the progression of gastric cancer, potentially via Notch and/or Wnt signaling pathway activation
malfunction
-
to determine the involvement of ADAM10 and ADAM17 in G protein coupled receptor P2Y2 nucleotide receptor-mediated EGFR activation, human salivary gland cells are transfected with small interfering RNA targeting either ADAM10 or ADAM17 mRNA. Transfection of human salivary gland cells with ADAM10 or ADAM17 siRNA partially suppress EGFR and ERK1/2 phosphorylation induced by UTP, whereas co-transfection with both ADAM10 and ADAM17 siRNA almost completely preventd UTP-induced EGFR and ERK1/2 phosphorylation
malfunction
-
transient transfection with siRNAs targeting ADAM17, which ablates its expression by up to 90%, inhibits phenyl mercuric acetate-stimulated shedding activity by up to 70%, indicating that ADAM17 is the major sheddase
malfunction
-
ADAM17 knockdown leads to a dramatic cell growth suppression in NCI-H292 cells
malfunction
-
inhibition of ADAM17 leads to the upregulation of transforming growth factor-beta signaling
physiological function
-
a cell-based ADAM17 assay is used to show that thiol isomerases, specifically protein disulfide isomerase, could be responsible for maintaining ADAM17 in an inactive form. Down-regulation of thiol isomerases, by changes in the redox environment markedly enhances ADAM17 activation
physiological function
-
ADAM10 and ADAM17 are activated by G protein-coupled receptor P2Y2
physiological function
-
ADAM17 is physically associated with active extracellular signal-regulated kinases ERK1/2 and is phosphorylated at serine residues in an ERK-dependent manner in wounded cells
physiological function
-
addition of human recombinant TACE promotes gene expression of endothelial specific markers including vWF, CD31, VE-cadherin, Flk-1 and Flt-1 in differentiating rat marrow stromal cells. Inhibition of TACE with TAPI-2 or inhibition of TNF-alpha with Etanercept attenuates endothelial differentiation of marrow stromal cells in direct co-culture condition with rain microvascular endothelial cells
physiological function
-
anti-Ro/SSA autoantibodies determine TACE pro-domain shedding suggesting that TACE activity is necessary for the release of TNF-alpha observed in anti-Ro/SSA autoantibody-stimulated cells. Adalimumab appears to be significantly more efficacious than Etanercept in preventing TACE activation caused by anti-Ro/SSA autoantibodies. Regulation of TACE may participate in the pathogenic role of autoantibodies and the modulation of TACE expression by TNF-alpha antagonists might contribute to the beneficial effect of these drugs in inflammatory and autoimmune diseases
physiological function
-
granulocyte-macrophage colony-stimulating factor GM-CSF and interleukin-4 in combination potently up-regulate tumor necrosis factor-alpha coverting enzyme TACE and activity in monocytes, causing ectodomain shedding of macrophage colony-stimulating factor M-CSF receptor, resulting in the disruption of its phosphorylation by M-CSF as well as the induction of osteoclastogenesis from monocytes by M-CSF and receptor activator of nuclear factor-kappaB RANK ligand. TACE inhibition robustly causes the resumption of the surface expression of M-CSF receptor on monocytes, facilitating M-CSF-mediated phosphorylation of M-CSF receptor and macrophage/osteoclast differentiation while impairing GM-CSF- and IL-4-mediated dendritic cell differentiation from monocytes
physiological function
-
increased expression and shedding of fractalkine by endothelial cells under pro-inflammatory conditions is not regulated by an increased activity of ADAM-17
physiological function
-
inhibition and knockdown of ADAM17/TACE blocks the shedding of MHC class I-related chain. The recruitment of both enzyme and substrate to detergent-resistant membrane microdomains is crucial for efficient proteolysis
physiological function
-
knockdown of both endogenous ADAM10 and endogenous ADAM17 by siRNA inhibits FcalphaR, i.e. Fc receptor for immunoglobulin A, shedding
physiological function
-
knocking down ADAM-17 expression using lentivirus-delivered siRNA in HUVECs inhibits cell proliferation and the ability of cells to form close contact in two-dimensional cultures. Similarly, ADAM-17 depletion inhibits the ability of HUVECs to form capillary-like networks on top of three-dimensional Matrigel as well as in coculture with fibroblasts within a three dimensional scaffold. Both baseline and VEGF-induced MMP-2 activation and Matrigel invasion are inhibited by ADAM-17 depletion
physiological function
-
Notch1 signaling independent of ligands requires ADAM17, while ADAM10 is absolutely required for Notch1 signaling induced by ligands. Both proteases participate in signaling intrinsic to Notch mutations associated with leukemia
physiological function
-
Porphyromonas gingivalis challenge results in a concentration-dependent enhancement of TACE messenger RNA expression and protein release by Jurkat cells. The induction of TACE by T-cells in response to Porphyromonas gingivalis may in turn favour the shedding of host cell-bound cytokines into the local microenvironment, potentially amplifying the inflammatory response
physiological function
-
shRNA-approach to knock down ADAM17 expression in Jurkat cells show that during early events of death receptor-mediated neutrophil apoptosis, L-selectin downregulation occurs primarily by ADAM17-mediated shedding. The downregulation of L-selectin occurs by ectodomain shedding
physiological function
-
silencing of ADAM17 by siRNA leads to significant inhibition of cell proliferation compared to the control groups at 24, 48 and 72 hours, and apoptosis is significantly increased at 48 hours. Cells that received a combination of siRNA transfection and genistein treatment, show a further significant decrease of proliferation and increase in apoptosis compared with either treatment alone
physiological function
-
silencing of ADAM17, but not ADAM15, expression using small interfering RNA interferes with endothelial cell invasion, resulting in decreased density of invading cells and decreased invasion distance. Stable endothelial cell lines expressing short hairpin RNA directed to ADAM17 are similarly inhibited. Expression of ADAM17 dominant negative mutant, but not ADAM10 or ADAM15 dominant negative mutants, decreases invasion density and distance. ADAM17 dominant negative mutant cells exhibit far greater numbers of protruding sprouts compared to control, suggesting an inability of extended processes to retract properly. Data suggest a role for ADAM17 in modulating endothelial sprouting events during angiogenesis
physiological function
-
small interfering RNA-mediated silencing of ADAM17 in AGS cells inhibits the repression of wild-type HKalpha promoter, i.e. gastric H, K-adenosine triphosphatase alpha-subunit promoter, and reduces ADAM17 activity and heparin-binding epidermal growth factor production, compared to controls
physiological function
-
ADAM17 regulates epidermal growth factor receptor expression through the activation of Notch1 in non-small cell lung cancer. ADAM17 mediates cell growth, survival, and tumorigenicity by epidermal growth factor receptor-independent mechanisms
physiological function
-
the enzyme increases receptor activator of nuclear factor-kappaB ligand secretion and decreases osteoprotegerin protein expression in osteoblasts
physiological function
-
through the cleavage of vasorin, ADAM17 controls transforming growth factor-beta-mediated epithelial-to-mesenchymal transition
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ADA17_HUMAN
824
1
93021
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
-
100 kDa reduced form represents mature TACE lacking the prodomain, immunoprecipitation
120000
-
full length form of TACE migrates as a 120 kDa protein under reducing conditions, immunoprecipitation
80000
-
migrates as a 80 kDa protein under non-reducing conditions, immunoprecipitation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
in wounded cells, ADAM17 is phosphorylated at serine residues in an extracellular signal-regulated kinases ERK1/2-dependent manner
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
docking of nine-residue peptide PLAQA-VRSS from proTNF-alpha. The peptide adopts an anti-parallel beta-sheet conformation against a nearby beta-sheet of the protein. In the complexmodel, the side-chains of residues P2 and P2' are largely exposed,and do not form highly favorable interactions
hanging drop vapour diffusion method with 15% polyethylene glycol 4000, 10% 2-propanol, 100 mM sodium citrate (pH 5.6)
-
molecular docking studies of inhibitor 2-(N-benzoxycarbonyl)aminoethyl-N-(4-hydroxyamino-4-oxo-2-(isopropylthio)butanoyl)-L-3-phenylalanyl-L-alanyl amide
-
TACE mutant V353G is crystallized with the respective inhibitors with a resolution of 1.7 A using the hanging drop method
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D616N
the mutant reveals significantly lower activity with interleukin 6 receptor and normal shedding activity towards pro-TNFalpha compared to the wild type enzyme
D647Q/E650Q/D654Q
the mutant shows no significant change in activity compared to the wild type enzyme
D657A
the mutant reveals significantly lower activity with pro-TNFalpha and normal shedding activity towards interleukin 6 receptor compared to the wild type enzyme
R177C
R177C is a cancer-associated point mutation within the pro-domain of ADAM17 which is most impaired in its proteolytic activity and tracking to the cell membrane. The mutant enzyme shows greatly diminished shedding activity with pro-TNF-alpha and interleukin 6 receptor
R725H
the mutant reveals significantly lower activity with interleukin 6 receptor and normal shedding activity towards pro-TNFalpha compared to the wild type enzyme
S266A/N452Q
-
the catalytic domain of recombinant human TNF-converting enzyme (residues 215-477) with two mutations S266A and N452Q is used
V353G
additional information
-
study on the association of ADAM-17 single nucleotide polymorphisms with insulin-resistance phenotypes and obesity risk. G allele carriers at the ADAM17_m1254A > G polymorphism exhibit significantly higher risk of obesity, are shorter, have higher insulin, and lower HDL-C concentrations than AA subjects. For the ADAM17_i33708A > G single nucleotide polymorphism, homozygotes for the A allele display higher risk of obesity, are heavier, have higher body-mass-index and higher waist measurements than GG subjects. There is a significant gene-diet interaction, in which the deleterious association of the i33708A allele with obesity is observed in subjects with low intakes from n-6 polyunsaturated fatty acids, whereas no differences in obesity risk are seen among subjects with high n-6 polyunsaturated fatty acid intake
V353G
-
highly resistant to autoproteolysis, shows similar kinetic properties to wild type TACE
V353G
-
TACE mutant V353G is crystallized with the respective inhibitors with a resolution of 1.7 A using the hanging drop method
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
in absence of cell activators the enzyme is long-lived, with a half-life of more than 8h
-
surface-biotinylated TACE is stable in Jurkat cells with a half-life of at least 8h
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA encoding TACE, full-length human TACE, inefficiently expressed in insect cells, baculovirus particles in Sf9 cell line from Spodoptera frugiperda
-
cDNA fragment coding for the prodomain of human TACE, expressed and purified from a baculoviral expression system
-
recombinantly expressed human TACE in plasmid transfected chinese hamster ovary cells
-
the catalytic domain of recombinant human TNF-converting enzyme (residues 215-477 with two mutations S266A and N452Q) and a His-tagged tail is purified from the baculovirus/Hi5 cells expression system using affinity chromatography
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in aneurysmal thoracic aorta from patients, the enzyme Is increased in tunica media and intima
stimulation of lung epithelial A549 tumor cells with phorbol-12-myristate-13-acetate leads to the downregulation of the surface expressed mature form of the enzyme
the enzyme is significantly upregulated in gastric cancer and positive metastatic lymph node tissues
ADAM-17 mRNA increases, but not significantly upon treatment with TNF -alpha and TGF-beta1
-
ADAM-17 mRNA remains at control levels when treated with IL-1beta and IFN-gamma
-
cultured HL-60 neutrophils exposed to tobacco smoke extract show increased enzyme content
-
dose-dependent increase of TACE mRNA expression in anti-Ro/SSA antibodies-treated salivary land epithelial cells, followed by internalization, pro-domain shedding and activation of TACE protein, suggesting that increased TACE activity is necessary for the release of TNF-alpha observed in anti-Ro/SSA antibodies-stimulated salivary gland epithelial cells. Adalimumab treatment brings TACE mRNA and surface TACE expression to levels similar to those observed in untreated salivary gland epithelial cells
-
expression of ADAM-17 is significantly increased in gallbladder carcinoma with high histological grade and pT stage compared with low histological grade and pT stage tumors and is not associated with patients gender, age, histological type, and resection margin involvement
-
granulocyte-macrophage colony-stimulating factor GM-CSF and interleukin-4 in combination potently up-regulate tumor necrosis factor-alpha coverting enzyme TACE and activity in monocytes, causing ectodomain shedding of M-CSF receptor
-
increased TACE mRNA expression in anti-Ro/SSA antibodies-treated salivary gland epithelial cells is restored to normal levels by Adalimumab treatment
-
infection of AGS cells with wild-type H pylori or an H pylori cagL-deficient isogenic mutant that also contains a wild-type version of cagL, P12DeltacagL/cagL, represses HKalpha promoter-Luc reporter activity and stimulates ADAM17 activity. Both responses are inhibited by point mutations in the nuclear factor-kappaB binding site of HKalpha or by infection with P12DeltacagL
-
metalloproteases ADAM-9, ADAM-15, and ADAM-17 are upregulated in advanced human atherosclerotic lesions in samples from carotid, aortic, and femoral territories compared to samples from internal thoracic artery free of atherosclerotic plaques
-
Porphyromonas gingivalis challenge results in a concentration-dependent enhancement of TACE messenger RNA expression and protein release by Jurkat cells. TLCK treatment or heat treatment of Porphyromonas gingivalis culture supernatants decreases TACE release to control levels
-
protein kinase C-activating phorbol ester PMA, often used as a strong inducer of the enzyme, causes not only proteolysis by the enzyme but also a rapid increase of the mature protease at the cell surface. This is followed by internalisation and subsequent degradation of the protease. Eventually, this leads to a substantial downregulation of mature enzyme
-
transcription factor Sp1 binds to the ADAM17 promoter, and Sp1 regulates ADAM17 expression under hypoxia. Suppression of Sp1 decreases invasiveness and migration in U87 tumor cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
molecular biology
-
results indicate that oxygen regulates the expression of TACE and TACE may be important for placental development during human pregnancy
medicine
ADAM17 expression levels are correlated with the invasive ability of androgen-independent prostate cancer cell lines. ADAM17 is overexpressed in cells showing high invasion characteristics, activation of the EGFR-MEK-ERK pathway, up-regulation of MMP-2, MMP-9, and an increased TGF-alpha release into the supernatant. AG1478, PD98059 and antibody against TGF-alpha deactivating the EGFR-MEK-ERK signaling pathway, abolish up-regulation of MMP-2, MMP-9 and prevent cell invasion. Cells with knock-down of ADAM17 by siRNA exhibit low invasive ability, deactivated EGFR-MEK-ERK signaling pathway, reduced TGF-alpha release and down-regulation of MMP-2, MMP-9
medicine
ectopic over-expression of ADAM17 results in increased cell proliferation. ADAM17 promotes G1 to S phase transition concomitantly with upregulation of cyclin E, CDK2 and downregulation of p21 and p27 proteins. ADAM17 over-expression cells show more TGF-alpha released to the supernatant and activate the EGFR/PI3K/AKT pathway. Silencing ADAM17 leads to the opposite effect. Both siRNAs knockdown of ADAM17 and blocking the EGFR/PI3K/AKT pathway cause downregulation of cyclin E,CDK2,and upregulation of p21 and p27 in prostate cancer cells
medicine
human IgG Fc receptor CD16, i.e. FcgammaRIII plasma levels are significantly decreased in patients administered a selective inhibitor targeting the metalloproteases ADAM10 and ADAM17. Inhibition of ADAM17 significantly blocks the cleavage of CD16b following neutrophil activation and apoptosis
medicine
the enzyme activity plays a positive role to predict cardiovascular events
medicine
the enzyme is upregulated in gastric cancer cells with high metastatic potential
medicine
-
over-expression of TNF-alpha has been implicated in diseases such as rheumatoid arthritis, Crohn's disease, septic shock, AIDS, insulin resistance, cachexia and cancer
medicine
-
tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor, activating TACE by pharmacological manipulation might prove beneficial in Alzheimer's disease
medicine
-
targeting this key enzyme for therapeutic intervention in inflammatory diseases, cancer and AIDS
medicine
-
TACE plays a role in the pathogenesis of endometriosis, a benign gynecologic disorder
medicine
-
TACE as target for drug discovery, potential therapeutic target in the areas of arthritis, cancer, diabetes and HIV cachexia
medicine
-
pharmaceutical industry is attempting to design specific TACE inhibitors to treat inflammatory diseases, may also be beneficial in treating certain cancers
medicine
-
isolation of TACE facilitates the development of therapeutically useful inhibitors of TNF-alpha release
medicine
-
putative cellular targets of a therapeutic strategy in neurodegenerative prion diseases
medicine
-
TNF-alpha thought to be a selective anti-tumor agent and a contributor to cachexia in cancer patients, clinical trials for cancer
medicine
-
therapeutic potential of TACE inhibitors benefit in treating autoimmune diseases like Crohn's disease or rheumatoid arthritis
medicine
-
TACE has implications in the pathogenesis of myocarditis and may have influence on advanced cardiac dysfunction in myocarditis
medicine
-
ADAM-17 is a putative target for treatment of neuroinflammatory diseases
medicine
-
ADAM17/TACE might be an important therapeutic target. The blocking of ADAM17/TACE expression and/or the evaluation and development of specific TACE inhibitors might have therapeutic potential even in later stages of cancer. Furthermore, ADAM17/TACE might be useful as a diagnostic marker of pancreatic cancer to distinguish between PDAC and chronic pancreatitis. Aberrant ADAM17/TACE expression might be a diagnostic and therapeutic target in human pancreatic ductal adenocarcinoma
medicine
-
in this study the relationship between long-term alcohol consumption and the concentration of TACE in peripheral blood mononuclear cells and its substrate- soluble TNF-alpha receptor type 1 in plasma in psoriasis patients is analysed. The study is conducted among 44 patients (aged 30-59 years) with early-onset, plaque-type psoriasis. 38 patients (aged 29-61 years) with other than psoriasis chronic dermatologic disorders are controls. The data on alcohol consumption during previous 10 years are obtained with a structured questionnaire. The severity of the disease is assessed using Psoriasis Area and Severity Index (PASI), and concentrations of TACE in peripheral blood mononuclear cells lysate and soluble TNF-alpha receptor type 1 in plasma is assessed with a quantitative sandwich enzyme immunoassay technique. The alcohol abuse contributes to the increase of TACE expression in blood mononuclear cells and also to the elevated plasma soluble TNF-alpha receptor type 1 concentration in psoriasis patients
medicine
-
the data presented herein show TACE expression in endocrine cancers and further support a role for TACE in breast cancer apoptosis
medicine
-
the increased gingival crevicular fluid TACE levels in persons with periodontitis and their positive correlation with receptor activator of NF-kappaB ligand indicate an association of this enzyme with alveolar bone loss
medicine
-
the relationship between ADAM17 and TNF polymorphisms, circulating levels of shed ADAM17 substrates, and cardiovascular risk in a prospective cohort of coronary artery disease patients is investigated. Five tag single-nucleotide polymorphisms (SNPs) of the ADAM17 gene as well as four previously described TNF SNPs are genotyped in the Atherogene Study composed of 1400 coronary artery disease patients among which 136 died from a cardiovascular cause. Soluble TNF, soluble TNF receptor 1, and soluble TNF receptor 2 concentrations are all significantly elevated in patients with future cardiovascular death, independently of other clinical/biological variables. The ADAM17-154A allele is found associated with a 14% increase of soluble TNF levels as compared to the -154C allele. Individuals carrying the 747Leu allele display a borderline increased risk of future cardiovascular death
medicine
-
anti-Ro/SSA autoantibodies determine TACE pro-domain shedding suggesting that TACE activity is necessary for the release of TNF-alpha observed in anti-Ro/SSA autoantibody-stimulated cells. Adalimumab appears to be significantly more efficacious than Etanercept in preventing TACE activation caused by anti-Ro/SSA autoantibodies. Regulation of TACE may participate in the pathogenic role of autoantibodies and the modulation of TACE expression by TNF-alpha antagonists might contribute to the beneficial effect of these drugs in inflammatory and autoimmune diseases
medicine
-
during acute H pylori infection, CagL dissociates ADAM17 from the integrin alpha(5)beta1 and activates ADAM17-dependent, nuclear factor-kappaB-mediated repression of HKalpha, i.e. gastric H, K-adenosine triphosphatase alpha-subunit. This might contribute to transient hypochlorhydria in patients with H pylori infection
medicine
-
expression of ADAM-17 is significantly increased in gallbladder carcinoma with high histological grade and pT stage compared with low histological grade and pT stage tumors and is not associated with patients gender, age, histological type, and resection margin involvement. Patients with high expression of ADAM-17 have a significantly shorter overall survival compared with those with low expression. The prognostic impact of ADAM-17 is independent of conventional prognostic factors for gallbladder carcinoma
medicine
-
increased expression and shedding of fractalkine by endothelial cells under pro-inflammatory conditions is not regulated by an increased activity of ADAM-17
medicine
-
increased TACE activity is necessary for the release of TNF-alpha observed in anti-Ro/SSA antibodies-stimulated salivary gland epithelial cells
medicine
-
inhibition of ADAM17 increases the cytotoxicity of bortezomib and MDX-060 against L-540 cells
medicine
-
metalloproteases ADAM-9, ADAM-15, and ADAM-17 are upregulated in advanced human atherosclerotic lesions in samples from carotid, aortic, and femoral territories compared to samples from internal thoracic artery free of atherosclerotic plaques. The enzymes are in the catalytically active form. ADAM-9, ADAM-15, and ADAM-17-expressing cells colocalize with CD68-positive cells of monocytic origin in the atherosclerotic plaques. Colocalization is demonstrated in all vascular territories
medicine
-
study on the association of ADAM-17 single nucleotide polymorphisms with insulin-resistance phenotypes and obesity risk. G allele carriers at the ADAM17_m1254A > G polymorphism exhibit significantly higher risk of obesity, are shorter, have higher insulin, and lower HDL-C concentrations than AA subjects. For the ADAM17_i33708A > G single nucleotide polymorphism, homozygotes for the A allele display higher risk of obesity, are heavier, have higher body-mass-index and higher waist measurements than GG subjects. There is a significant gene-diet interaction, in which the deleterious association of the i33708A allele with obesity is observed in subjects with low intakes from n-6 polyunsaturated fatty acids, whereas no differences in obesity risk are seen among subjects with high n-6 polyunsaturated fatty acid intake
medicine
-
transcription factor Sp1 binds to the ADAM17 promoter, and Sp1 regulates ADAM17 expression under hypoxia. Suppression of Sp1 decreases invasiveness and migration in U87 tumor cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Buxbaum, J.D.; Liu, K.N.; Luo, Y.; Slack, J.L.; Stocking, K.L.; Peschon, J.J.; Johnson, R.S.; Castner, B.J.; Cerretti, D.P.; Black, R.A.
Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor
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273
27765-27767
1998
Homo sapiens, Mus musculus
Cerretti, D.P.
Characterization of the tumor necrosis factor alpha-converting enzyme, TACE/ADAM17
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27
219-223
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Homo sapiens, Mus musculus
Milla, M.E.; Leesnitzer, M.A.; Moss, M.L.; Clay, W.C.; Carter, H.L.; Miller, A.B.; Su, J.L.; Lambert, M.H.; Willard, D.H.; Sheeley, D.M.; Kost, T.A.; Burkhart, W.; Moyer, M.; Blackburn, R.K.; Pahel, G.L.; Mitchell, J.L.; Hoffman, C.R.; Becherer, J.D.
Specific sequence elements are required for the expression of functional tumor necrosis factor-alpha-converting enzyme (TACE)
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274
30563-30570
1999
Homo sapiens
Moss, M.; Becherer, J.D.; Milla, M.; Pahel, G.; Lambert, M.; Andrews, R.; Frye, S.; Haffner, C.; Cowan, D.; Maloney, P.; Dixon, E.P.; Jansen, M.; Vitek, M.P.; Mitchell, J.; Leesnitzer, T.; Warner, J.; Conway, J.; Bickett, D.M.; Bird, M.; Priest, R.; Reinhard, J.; Lin, P.
TNF.alpha. converting enzyme
Metalloproteinases as targets for anti-inflammatory drugs, (Bottomley, K. M. K; Bradshaw, D. ; Nixon, J. S. eds. )
187-203
1999
Homo sapiens, Mus musculus, Mus musculus C3H/HEN
-
Nelson, K.K.; Schlondorff, J.; Blobel, C.P.
Evidence for an interaction of the metalloprotease-disintegrin tumor necrosis factor alpha convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of the metalloprotease-disintegrin MDC9 with a novel MAD2-related protein, MAD2.beta
Biochem. J.
343
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1999
Homo sapiens
-
Satoh, M.; Nakamura, M.; Saitoh, H.; Satoh, H.; Maesawa, C.; Segawa, I.; Tashiro, A.; Hiramori, K.
Tumor necrosis factor-.alpha.-converting enzyme and tumor necrosis factor-.alpha. in human dilated cardiomyopathy
Circulation
99
3260-3265
1999
Homo sapiens
Becherer, J.D.; Lambert, M.H.; Andrews, R.C.
The tumor necrosis factor-alpha converting enzyme
Handbook of Experimental Pharmacology, (von der Helm, K. ; Korant, B. C. ; Cheronis, J. C. eds. )
140
235-258
2000
Homo sapiens, Mus musculus, Sus scrofa
-
Brou, C.; Logeat, F.; Gupta, N.; Bessia, C.; LeBail, O.; Doedens, J.R.; Cumano, A.; Roux, P.; Black, R.A.; Israel, A.
A novel proteolytic cleavage involved in notch signaling: the role of the disintegrin-metalloprotease TACE
Mol. Cell
5
207-216
2000
Homo sapiens, Mus musculus
Doedens, J.R.; Black, R.A.
Stimulation-induced down-regulation of tumor necrosis factor-alpha converting enzyme
J. Biol. Chem.
275
14598-14607
2000
Homo sapiens
Gottschalk, C.; Malberg, K.; Arndt, M.; Schmitt, J.; Roessner, A.; Schultze, D.; Kleinstein, J.; Ansorge, S.
Matrix metalloproteinases and TACE play a role in the pathogenesis of endometriosis
Adv. Exp. Med. Biol.
477
483-486
2000
Homo sapiens
Reddy, P.; Slack, J.L.; Davis, R.; Cerretti, D.P.; Kozlosky, C.J.; Blanton, R.A.; Shows, D.; Peschon, J.J.; Black, R.A.
Functional analysis of the domain structure of tumor necrosis factor-alpha converting enzyme
J. Biol. Chem.
275
14608-14614
2000
Homo sapiens, Homo sapiens (P78536), Mus musculus, Mus musculus EC-4
Satoh, M.; Nakamura, M.; Satoh, H.; Saitoh, H.; Segawa, I.; Hiramori, K.
Expression of tumor necrosis factor-alpha-converting enzyme and tumor necrosis factor-alpha in human myocarditis
J. Am. Coll. Cardiol.
36
1288-1294
2000
Homo sapiens
Schloendorff, J.; Becherer, J.D.; Blobel, C.P.
Intracellular maturation and localization of the tumor necrosis factor alpha convertase (TACE)
Biochem. J.
347
131-138
2000
Chlorocebus aethiops, Homo sapiens, Mus musculus
-
Zhang, Y.; Jiang, J.; Black, R.A.; Baumann, G.; Frank, S.J.
Tumor necrosis factor-alpha converting enzyme (TACE) is a growth hormone binding protein (GHBP) sheddase: the metalloprotease TACE/ADAM-17 is critical for (PMA-induced) GH receptor proteolysis and GHBP generation
Endocrinology
141
4342-4348
2000
Oryctolagus cuniculus, Homo sapiens, Mus musculus
Garton, K.J.; Gough, P.J.; Blobel, C.P.; Murphy, G.; Greaves, D.R.; Dempsey, P.J.; Raines, E.W.
Tumor necrosis factor-alpha-converting enzyme (ADAM17) mediates the cleavage and shedding of fractalkine (CX3CL1)
J. Biol. Chem.
276
37993-38001
2001
Homo sapiens
Holms, J.; Mast, K.; Marcotte, P.; Elmore, I.; Li, J.; Pease, L.; Glaser, K.; Morgan, D.; Michaelides, M.; Davidsen, S.
Discovery of selective hydroxamic acid inhibitors of tumor necrosis factor-alpha converting enzyme
Bioorg. Med. Chem. Lett.
11
2907-2910
2001
Homo sapiens
Lee, M.H.; Knauper, V.; Becherer, J.D.; Murphy, G.
Full-Length and N-TIMP-3 display equal inhibitory activities toward TNF-alpha convertase
Biochem. Biophys. Res. Commun.
280
945-950
2001
Homo sapiens
Moss, M.L.; White, J.M.; Lambert, M.H.; Andrews, R.C.
TACE and other ADAM proteases as targets for drug discovery
Drug Discov. Today
6
417-426
2001
Homo sapiens
Rabinowitz, M.H.; Andrews, R.C.; Becherer, J.D.; Bickett, D.M.; Bubacz, D.G.; Conway, J.G.; Cowan, D.J.; Gaul, M.; Glennon, K.; Lambert, M.H.; Leesnitzer, M.A.; McDougald, D.L.; Moss, M.L.; Musso, D.L.; Rizzolio, M.C.
Design of selective and soluble inhibitors of tumor necrosis factor-alpha converting enzyme (TACE)
J. Med. Chem.
44
4252-4267
2001
Homo sapiens, Mus musculus, Rattus norvegicus, Rattus norvegicus Lewis
Rovida, E.; Paccagnini, A.; Del Rosso, M.; Peschon, J.; Sbarba, P.D.
TNF-alpha-converting enzyme cleaves the macrophage colony-stimulating factor receptor in macrophages undergoing activation
J. Immunol.
166
1583-1589
2001
Homo sapiens, Mus musculus
Skovronsky, D.M.; Fath, S.; Lee, V.M.Y.; Milla, M.E.
Neuronal localization of the TNFalpha converting enzyme (TACE) in brain tissue and its correlation to amyloid plaques
J. Neurobiol.
49
40-46
2001
Homo sapiens, Mus musculus
Tsou, C.L.; Haskell, C.A.; Charo, I.F.
Tumor necrosis factor-alpha-converting enzyme mediates the inducible cleavage of fractalkine
J. Biol. Chem.
276
44622-44626
2001
Homo sapiens, Mus musculus
Vincent, B.; Paitel, E.; Saftig, P.; Frobert, Y.; Hartmann, D.; De Strooper, B.; Grassi, J.; Lopez-Perez, E.; Checler, F.
The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein
J. Biol. Chem.
276
37743-37746
2001
Homo sapiens, Mus musculus
Xue, C.B.; He, X.; Corbett, R.L.; Roderick, J.; Wasserman, Z.R.; Liu, R.Q.; Jaffee, B.D.; Covington, M.B.; Qian, M.; Trzaskos, J.M.; Newton, R.C.; Magolda, R.L.; Wexler, R.R.; Decicco, C.P.
Discovery of macrocyclic hydroxamic acids containing biphenylmethyl derivatives at P1', a series of selective TNF-alpha converting enzyme inhibitors with potent cellular activity in the inhibition of TNF-alpha release
J. Med. Chem.
44
3351-3354
2001
Homo sapiens, Sus scrofa
Black, R.A.
Tumor necrosis factor-alpha converting enzyme
Int. J. Biochem. Cell Biol.
34
1-5
2002
Homo sapiens, Mus musculus
Jin, G.; Huang, X.; Black, R.; Wolfson, M.; Rauch, C.; McGregor, H.; Ellestad, G.; Cowling, R.
A Continuous fluorimetric assay for tumor necrosis factor-alpha converting enzyme
Anal. Biochem.
302
269-275
2002
Homo sapiens
Kottirsch, G.; Koch, G.; Feifel, R.; Neumann, U.
beta-aryl-succinic acid hydroxamates as dual inhibitors of matrix metalloproteinases and tumor necrosis factor alpha converting enzyme
J. Med. Chem.
45
2289-2293
2002
Homo sapiens
Lee, M.H.; Verma, V.; Maskos, K.; Nath, D.; Knauper, V.; Dodds, P.; Amour, A.; Murphy, G.
Engineering N-terminal domain of tissue inhibitor of metalloproteinase (TIMP)-3 to be a better inhibitor against tumour necrosis factor-alpha-converting enzyme
Biochem. J.
364
227-234
2002
Homo sapiens
Mohan, M.J.; Seaton, T.; Mitchell, J.; Howe, A.; Blackburn, K.; Burkhart, W.; Moyer, M.; Patel, I.; Waitt, G.M.; Becherer, J.D.; Moss, M.L.; Milla, M.E.
The tumor necrosis factor-alpha converting enzyme (TACE): A unique metalloproteinase with highly defined substrate selectivity
Biochemistry
41
9462-9469
2002
Homo sapiens, Mus musculus
Parkin, E.T.; Trew, A.; Christie, G.; Faller, A.; Mayer, R.; Turner, A.J.; Hooper, N.M.
Structure-activity relationship of hydroxamate-based inhibitors on the secretases that cleave the amyloid precursor protein, angiotensin converting enzyme, CD23, and pro-tumor necrosis factor-alpha
Biochemistry
41
4972-4981
2002
Chlorocebus aethiops, Homo sapiens, Mus musculus
Sunnarborg, S.W.; Hinkle, C.L.; Stevenson, M.; Russell, W.E.; Raska, C.S.; Peschon, J.J.; Castner, B.J.; Gerhart, M.J.; Paxton, R.J.; Black, R.A.; Lee, D.C.
Tumor necrosis factor-alpha converting enzyme (TACE) regulates epidermal growth factor receptor ligand availability
J. Biol. Chem.
277
12838-12845
2002
Homo sapiens, Mus musculus
Xu, H.; Uysal, K.T.; Becherer, J.D.; Arner, P.; Hotamisligil, G.S.
Altered tumor necrosis factor-alpha (TNF-alpha) processing in adipocytes and increased expression of transmembrane TNF-alpha in obesity
Diabetes
51
1876-1883
2002
Homo sapiens, Mus musculus
Canault, M.; Peiretti, F.; Kopp, F.; Bonardo, B.; Bonzi, M.; Coudeyre, J.; Alessi, M.; Juhan-Vague, I.; Nalbone, G.
The TNF alpha converting enzyme (TACE/ADAM17) is expressed in the atherosclerotic lesions of apolipoprotein E-deficient mice: Possible contribution to elevated plasma levels of soluble TNF alpha receptors
Atherosclerosis
187
82-91
2006
Homo sapiens, Mus musculus
Zatovicova, M.; Sedlakova, O.; Svastova, E.; Ohradanova, A.; Ciampor, F.; Arribas, J.; Pastorek, J.; Pastorekova, S.
Ectodomain shedding of the hypoxia-induced carbonic anhydrase IX is a metalloprotease-dependent process regulated by TACE/ADAM17
Br. J. Cancer
93
1267-1276
2005
Homo sapiens
Ringel, J.; Jesnowski, R.; Moniaux, N.; Luettges, J.; Ringel, J.; Choudhury, A.; Batra, S.K.; Kloeppel, G.; Loehr, M.
Aberrant expression of a disintegrin and metalloproteinase 17/tumor necrosis factor-alpha converting enzyme increases the malignant potential in human pancreatic ductal adenocarcinoma
Cancer Res.
66
9045-9053
2006
Homo sapiens
Bergmeier, W.; Piffath, C.L.; Cheng, G.; Dole, V.S.; Zhang, Y.; von Andrian, U.H.; Wagner, D.D.
Tumor necrosis factor-alpha-converting enzyme (ADAM17) mediates GPIba shedding from platelets in vitro and in vivo
Circ. Res.
95
677-683
2004
Homo sapiens, Mus musculus
Allinson, T.M.; Parkin, E.T.; Condon, T.P.; Schwager, S.L.; Sturrock, E.D.; Turner, A.J.; Hooper, N.M.
The role of ADAM10 and ADAM17 in the ectodomain shedding of angiotensin converting enzyme and the amyloid precursor protein
Eur. J. Biochem.
271
2539-2547
2004
Homo sapiens
Hinkle, C.L.; Sunnarborg, S.W.; Loiselle, D.; Parker, C.E.; Stevenson, M.; Russell, W.E.; Lee, D.C.
Selective roles for tumor necrosis factor alpha-converting enzyme/ADAM17 in the shedding of the epidermal growth factor receptor ligand family: The juxtamembrane stalk determines cleavage efficiency
J. Biol. Chem.
279
24179-24188
2004
Homo sapiens
Gonzales, P.E.; Solomon, A.; Miller, A.B.; Leesnitzer, M.A.; Sagi, I.; Milla, M.E.
Inhibition of the tumor necrosis factor-alpha-converting enzyme by its pro domain
J. Biol. Chem.
279
31638-31645
2004
Homo sapiens
Solomon, A.; Rosenblum, G.; Gonzales, P.E.; Leonard, J.D.; Mobashery, S.; Milla, M.E.; Sagi, I.
Pronounced diversity in electronic and chemical properties between the catalytic zinc sites of tumor necrosis factor-alpha-converting enzyme and matrix metalloproteinases despite their high structural similarity
J. Biol. Chem.
279
31646-31654
2004
Homo sapiens (P78536)
Cruz, A.C.; Frank, B.T.; Edwards, S.T.; Dazin, P.F.; Peschon, J.J.; Fang, K.C.
Tumor necrosis factor-alpha-converting enzyme controls surface expression of c-Kit and survival of embryonic stem cell-derived mast Cells
J. Biol. Chem.
279
5612-5620
2004
Homo sapiens
Lukacova, V.; Zhang, Y.; Kroll, D.M.; Raha, S.; Comez, D.; Balaz, S.
A comparison of the binding sites of matrix metalloproteinases and tumor necrosis factor-alpha converting enzyme: implications for selectivity
J. Med. Chem.
48
2361-2370
2005
Homo sapiens
Kurz, M.; Pischel, H.; Hartung, H.; Kieseier, B.C.
Tumor necrosis factor-alpha-converting enzyme is expressed in the inflamed peripheral nervous system
J. Peripher. Nerv. Syst.
10
311-318
2005
Homo sapiens, Rattus norvegicus
Wang, Y.; Sul, H.S.
Ectodomain shedding of preadipocyte factor 1 (Pref-1) by tumor necrosis factor alpha converting enzyme (TACE) and inhibition of adipocyte differentiation
Mol. Cell. Biol.
26
5421-5435
2006
Homo sapiens
Canault, M.; Leroyer, A.S.; Peiretti, F.; Leseche, G.; Tedgui, A.; Bonardo, B.; Alessi, M.; Boulanger, C.M.; Nalbone, G.
Microparticles of human atherosclerotic plaques enhance the shedding of the tumor necrosis factor-alpha converting enzyme/ADAM17 substrates, tumor necrosis factor and tumor necrosis factor receptor-1
Am. J. Pathol.
171
1713-1723
2007
Homo sapiens
Huang, A.; Joseph-McCarthy, D.; Lovering, F.; Sun, L.; Wang, W.; Xu, W.; Zhu, Y.; Cui, J.; Zhang, Y.; Levin, J.I.
Structure-based design of TACE selective inhibitors: Manipulations in the S1-S3 pocket
Bioorg. Med. Chem.
15
6170-6181
2007
Homo sapiens
Chun, K.; Park, S.; Kim, H.M.; Choi, Y.; Kim, M.; Park, C.; Joe, B.; Chun, T.G.; Choi, H.; Lee, H.; Hong, S.H.; Kim, M.S.; Nam, K.; Han, G.
Chromen-based TNF-alpha converting enzyme (TACE) inhibitors: Design, synthesis, and biological evaluation
Bioorg. Med. Chem.
16
530-535
2008
Homo sapiens
Condon, J.S.; Joseph-McCarthy, D.; Levin, J.I.; Lombart, H.; Lovering, F.E.; Sun, L.; Wang, W.; Xu, W.; Zhang, Y.
Identification of potent and selective TACE inhibitors via the S1 pocket
Bioorg. Med. Chem. Lett.
17
34-39
2007
Homo sapiens
Walcheck, B.; Herrera, A.H.; St.Hill, C.; Mattila, P.E.; Whitney, A.R.; De Leo, F.R.
ADAM17 activity during human neutrophil activation and apoptosis
Eur. J. Immunol.
36
968-976
2006
Homo sapiens
Schaff, U.; Mattila, P.E.; Simon, S.I.; Walcheck, B.
Neutrophil adhesion to E-selectin under shear promotes the redistribution and co-clustering of ADAM17 and its proteolytic substrate L-selectin
J. Leukocyte Biol.
83
99-105
2008
Homo sapiens
Qu, D.; Wang, Y.; Esmon, N.L.; Esmon, C.T.
Regulated endothelial protein C receptor shedding is mediated by tumor necrosis factor-alpha converting enzyme/ADAM17
J. Thromb. Haemost.
5
395-402
2007
Homo sapiens
Obeid, D.; Nguyen, J.; Lesavre, P.; Bauvois, B.
Differential regulation of tumor necrosis factor-alpha-converting enzyme and angiotensin-converting enzyme by type I and II interferons in human normal and leukemic myeloid cells
Oncogene
26
102-110
2007
Homo sapiens
Solomon, A.; Akabayov, B.; Frenkel, A.; Milla, M.E.; Sagi, I.
Key feature of the catalytic cycle of TNF-alpha converting enzyme involves communication between distal protein sites and the enzyme catalytic core
Proc. Natl. Acad. Sci. USA
104
4931-4936
2007
Homo sapiens
Ingram, R.N.; Orth, P.; Strickland, C.L.; Le, H.V.; Madison, V.; Beyer, B.M.
Stabilization of the autoproteolysis of TNF-alpha converting enzyme (TACE) results in a novel crystal form suitable for structure-based drug design studies
Protein Eng.
19
155-161
2006
Homo sapiens
Kirkegaard, T.; Naresh, A.; Sabine, V.S.; Tovey, S.M.; Edwards, J.; Dunne, B.; Cooke, T.G.; Jones, F.E.; Bartlett, J.M.
Expression of tumor necrosis factor alpha converting enzyme in endocrine cancers
Am. J. Clin. Pathol.
129
735-743
2008
Homo sapiens
Mazzola, R.D.; Zhu, Z.; Sinning, L.; McKittrick, B.; Lavey, B.; Spitler, J.; Kozlowski, J.; Neng-Yang, S.; Zhou, G.; Guo, Z.; Orth, P.; Madison, V.; Sun, J.; Lundell, D.; Niu, X.
Discovery of novel hydroxamates as highly potent tumor necrosis factor-alpha converting enzyme inhibitors, Part II Optimization of the S3 pocket
Bioorg. Med. Chem. Lett.
18
5809-5814
2008
Homo sapiens (P78536)
Murumkar, P.R.; Gupta, S.D.; Zambre, V.P.; Giridhar, R.; Yadav, M.R.
Development of predictive 3D-QSAR CoMFA and CoMSIA models for beta-aminohydroxamic acid-derived tumor necrosis factor-alpha converting enzyme inhibitors
Chem. Biol. Drug Des.
73
97-107
2009
Homo sapiens
Bostanci, N.; Emingil, G.; Afacan, B.; Han, B.; Ilgenli, T.; Atilla, G.; Hughes, F.J.; Belibasakis, G.N.
Tumor necrosis factor-alpha-converting enzyme (TACE) levels in periodontal diseases
J. Dent. Res.
87
273-277
2008
Homo sapiens
Serwin, A.B.; Sokolowska, M.; Dylejko, E.; Chodynicka, B.
Tumour necrosis factor (TNF-alpha) alpha converting enzyme and soluble TNF-alpha receptor type 1 in psoriasis patients in relation to the chronic alcohol consumption
J. Eur. Acad. Dermatol. Venereol.
22
712-717
2008
Homo sapiens
Zhu, Z.; Mazzola, R.; Sinning, L.; McKittrick, B.; Niu, X.; Lundell, D.; Sun, J.; Orth, P.; Guo, Z.; Madison, V.; Ingram, R.; Beyer, B.M.
Discovery of novel hydroxamates as highly potent tumor necrosis factor-alpha converting enzyme inhibitors: Part I--discovery of two binding modes
J. Med. Chem.
51
725-736
2008
Homo sapiens
Morange, P.E.; Tregouet, D.A.; Godefroy, T.; Saut, N.; Bickel, C.; Rupprecht, H.J.; Lackner, K.; Barbaux, S.; Poirier, O.; Peiretti, F.; Nalbone, G.; Juhan-Vague, I.; Blankenberg, S.; Tiret, L.
Polymorphisms of the tumor necrosis factor-alpha (TNF) and the TNF-alpha converting enzyme (TACE/ADAM17) genes in relation to cardiovascular mortality: the AtheroGene study
J. Mol. Med.
86
1153-1161
2008
Homo sapiens
Hung, T.H.; Chen, S.F.; Hsieh, C.C.; Hsu, J.J.; Li, M.J.; Yeh, Y.L.; Hsieh, T.T.
Tumor necrosis factor-alpha converting enzyme in the human placenta throughout gestation
Reprod. Sci.
15
195-209
2008
Homo sapiens
Willems, S.H.; Tape, C.J.; Stanley, P.L.; Taylor, N.A.; Mills, I.G.; Neal, D.E.; McCafferty, J.; Murphy, G.
Thiol isomerases negatively regulate the cellular shedding activity of ADAM17
Biochem. J.
428
439-450
2010
Homo sapiens
Peng, M.; Guo, S.; Yin, N.; Xue, J.; Shen, L.; Zhao, Q.; Zhang, W.
Ectodomain shedding of Fcalpha receptor is mediated by ADAM10 and ADAM17
Immunology
130
83-91
2010
Homo sapiens
Ratchford, A.M.; Baker, O.J.; Camden, J.M.; Rikka, S.; Petris, M.J.; Seye, C.I.; Erb, L.; Weisman, G.A.
P2Y2 nucleotide receptors mediate metalloprotease-dependent phosphorylation of epidermal growth factor receptor and ErbB3 in human salivary gland cells
J. Biol. Chem.
285
7545-7555
2010
Homo sapiens
Oksala, N.; Levula, M.; Airla, N.; Pelto-Huikko, M.; Ortiz, R.M.; Jaervinen, O.; Salenius, J.P.; Ozsait, B.; Komurcu-Bayrak, E.; Erginel-Unaltuna, N.; Huovila, A.P.; Kytoemaeki, L.; Soini, J.T.; Kaehoenen, M.; Karhunen, P.J.; Laaksonen, R.; Lehtimaeki, T.
ADAM-9, ADAM-15, and ADAM-17 are upregulated in macrophages in advanced human atherosclerotic plaques in aorta and carotid and femoral arteries--Tampere vascular study
Ann. Med.
41
279-290
2009
Homo sapiens
Goeoz, P.; Goeoz, M.; Baldys, A.; Hoffman, S.
ADAM-17 regulates endothelial cell morphology, proliferation, and in vitro angiogenesis
Biochem. Biophys. Res. Commun.
380
33-38
2009
Homo sapiens
Hiasa, M.; Abe, M.; Nakano, A.; Oda, A.; Amou, H.; Kido, S.; Takeuchi, K.; Kagawa, K.; Yata, K.; Hashimoto, T.; Ozaki, S.; Asaoka, K.; Tanaka, E.; Moriyama, K.; Matsumoto, T.
GM-CSF and IL-4 induce dendritic cell differentiation and disrupt osteoclastogenesis through M-CSF receptor shedding by up-regulation of TNF-alpha converting enzyme (TACE)
Blood
114
4517-4526
2009
Homo sapiens
Maeaettae, J.A.; Olli, K.; Henttinen, T.; Tuittila, M.T.; Elenius, K.; Salmivirta, M.
Removal of cell surface heparan sulfate increases TACE activity and cleavage of ErbB4 receptor
BMC Cell Biol.
10
5-12
2009
Homo sapiens
Brill, A.; Chauhan, A.K.; Canault, M.; Walsh, M.T.; Bergmeier, W.; Wagner, D.D.
Oxidative stress activates ADAM17/TACE and induces its target receptor shedding in platelets in a p38-dependent fashion
Cardiovasc. Res.
84
137-144
2009
Homo sapiens
Xu, J.; Liu, X.; Chen, J.; Zacharek, A.; Cui, X.; Savant-Bhonsale, S.; Chopp, M.; Liu, Z.
Cell-cell interaction promotes rat marrow stromal cell differentiation into endothelial cell via activation of TACE/TNF-alpha signaling
Cell Transplant.
19
43-53
2010
Homo sapiens, Rattus norvegicus
Saha, A.; Backert, S.; Hammond, C.E.; Gooz, M.; Smolka, A.J.
Helicobacter pylori CagL activates ADAM17 to induce repression of the gastric H, K-ATPase alpha subunit
Gastroenterology
139
239-248
2010
Homo sapiens
Sisto, M.; Lisi, S.; Lofrumento, D.D.; Caprio, S.; Mitolo, V.; DAmore, M.
TNF blocker drugs modulate human TNF-alpha-converting enzyme pro-domain shedding induced by autoantibodies
Immunobiology
215
874-883
2009
Homo sapiens
Sisto, M.; Lisi, S.; Lofrumento, D.D.; Frassanito, M.A.; Cucci, L.; DAmore, S.; Mitolo, V.; DAmore, M.
Induction of TNF-alpha-converting enzyme-ectodomain shedding by pathogenic autoantibodies
Int. Immunol.
21
1341-1349
2009
Homo sapiens
Yin, J.; Yu, F.
ERK1/2 mediate wounding- and G-protein-coupled receptor ligands -induced EGFR activation via regulating ADAM17 and HB-EGF shedding
Invest. Ophthalmol. Vis. Sci.
50
132-139
2009
Homo sapiens
Feng, W.F.; Zhao, Y.B.; Huang, W.; Yang, Y.Z.
Molecular modeling and biological effects of peptidomimetic inhibitors of TACE activity
J. Enzyme Inhib. Med. Chem.
25
459-466
2009
Homo sapiens
Szalad, A.; Katakowski, M.; Zheng, X.; Jiang, F.; Chopp, M.
Transcription factor Sp1 induces ADAM17 and contributes to tumor cell invasiveness under hypoxia
J. Exp. Clin. Cancer Res.
28
129
2009
Homo sapiens
Boutet, P.; Agera-Gonzalez, S.; Atkinson, S.; Pennington, C.; Edwards, D.; Murphy, G.; Reyburn, H.; Vals-Gmez, M.
Cutting edge: The metalloproteinase ADAM17/TNF-alpha-converting enzyme regulates proteolytic shedding of the MHC class I-related chain B protein
J. Immunol.
182
49-53
2009
Homo sapiens
Wang, Y.; Zhang, A.C.; Ni, Z.; Herrera, A.; Walcheck, B.
ADAM17 activity and other mechanisms of soluble L-selectin production during death receptor-induced leukocyte apoptosis
J. Immunol.
184
4447-4454
2010
Homo sapiens, Mus musculus
Liu, Y.; Wang, Z.; Ji, Y.; Li, F.
siRNA of ADAM17 gene induces apoptosis, proliferation inhibition and enhances the effects of genistein on HepG2 cells
J. Nanjing Med. Univ.
23
127-131
2009
Homo sapiens
-
Hurst, L.A.; Bunning, R.A.; Couraud, P.O.; Romero, I.A.; Weksler, B.B.; Sharrack, B.; Woodroofe, M.N.
Expression of ADAM-17, TIMP-3 and fractalkine in the human adult brain endothelial cell line, hCMEC/D3, following pro-inflammatory cytokine treatment
J. Neuroimmunol.
210
108-112
2009
Homo sapiens
Vahdat, A.M.; Reiners, K.S.; Simhadri, V.L.; Eichenauer, D.A.; Boell, B.; Chalaris, A.; Simhadri, V.R.; Wiegmann, K.; Krell, H.W.; Rose-John, S.; Engert, A.; von Strandmann, E.P.; Hansen, H.P.
TNF-alpha-converting enzyme (TACE/ADAM17)-dependent loss of CD30 induced by proteasome inhibition through reactive oxygen species
Leukemia
24
51-57
2010
Homo sapiens
Kwak, H.I.; Mendoza, E.A.; Bayless, K.J.
ADAM17 co-purifies with TIMP-3 and modulates endothelial invasion responses in three-dimensional collagen matrices
Matrix Biol.
28
470-479
2009
Homo sapiens
Wu, K.; Liao, M.; Liu, B.; Deng, Z.
ADAM-17 over-expression in gallbladder carcinoma correlates with poor prognosis of patients
Med. Oncol.
28
475-480
2011
Homo sapiens
Junyent, M.; Parnell, L.D.; Lai, C.Q.; Arnett, D.K.; Tsai, M.Y.; Kabagambe, E.K.; Straka, R.J.; Province, M.; An, P.; Smith, C.E.; Lee, Y.C.; Borecki, I.; Ordovas, J.M.
ADAM17_i33708A>G polymorphism interacts with dietary n-6 polyunsaturated fatty acids to modulate obesity risk in the Genetics of Lipid Lowering Drugs and Diet Network study
Nutr. Metab. Cardiovasc. Dis.
20
698-705
2009
Homo sapiens
Bostanci, N.; Reddi, D.; Rangarajan, M.; Curtis, M.A.; Belibasakis, G.N.
Porphyromonas gingivalis stimulates TACE production by T cells
Oral Microbiol. Immunol.
24
146-151
2009
Homo sapiens
Yu, W.; Tong, L.; Kim, S.; Wong, M.; Chen, L.; Yang, D.; Shankar, B.; Lavey, B.; Zhou, G.; Kosinski, A.; Rizvi, R.; Li, D.; Feltz, R.; Piwinski, J.; Rosner, K.; Shih, N.; Siddiqui, M.; Guo, Z.; Orth, P.; Shah, H.; Sun, J.; Umland, S.; Lundell, D.; Niu, X.
Biaryl substituted hydantoin compounds as TACE inhibitors
Bioorg. Med. Chem. Lett.
20
5286-5289
2010
Homo sapiens
Lee, J.H.; Choi, Y.J.; Heo, S.H.; Lee, J.M.; Cho, J.Y.
Tumor necrosis factor-alpha converting enzyme (TACE) increases RANKL expression in osteoblasts and serves as a potential biomarker of periodontitis
BMB Rep.
44
473-477
2011
Homo sapiens
Baumgart, A.; Seidl, S.; Vlachou, P.; Michel, L.; Mitova, N.; Schatz, N.; Specht, K.; Koch, I.; Schuster, T.; Grundler, R.; Kremer, M.; Fend, F.; Siveke, J.; Peschel, C.; Duyster, J.; Dechow, T.
ADAM17 regulates epidermal growth factor receptor expression through the activation of Notch1 in non-small cell lung cancer
Cancer Res.
70
5368-5378
2010
Homo sapiens
Zhao, Y.; Yu, J.; Gu, J.; Huang, W.
The evaluation of inhibitive effectiveness of the tumour necrosis factor-alpha converting enzyme selective inhibitors by HPLC
J. Enzyme Inhib. Med. Chem.
26
181-187
2011
Homo sapiens
Malapeira, J.; Esselens, C.; Bech-Serra, J.; Canals, F.; Arribas, J.
ADAM17 (TACE) regulates TGFbeta signaling through the cleavage of vasorin
Oncogene
30
1912-1922
2011
Homo sapiens
Kuruppu, S.; Rajapakse, N.W.; Minond, D.; Smith, A.I.
Production of soluble neprilysin by endothelial cells
Biochem. Biophys. Res. Commun.
446
423-427
2014
Homo sapiens (P78536), Homo sapiens
Vahidi, A.; Glenn, G.; Van Der Geer, P.
Identification and mutagenesis of the TACE and gamma-secretase cleavage sites in the colony-stimulating factor 1 receptor
Biochem. Biophys. Res. Commun.
450
782-787
2014
Homo sapiens (P78536)
Wang, Y.; Wu, J.; Newton, R.; Bahaie, N.; Long, C.; Walcheck, B.
ADAM17 cleaves CD16b (FcgammaRIIIb) in human neutrophils
Biochim. Biophys. Acta
1833
680-685
2013
Homo sapiens (P78536), Homo sapiens
Xiao, L.; Lin, P.; Lin, F.; Liu, X.; Qin, W.; Zou, H.; Guo, L.; Liu, W.; Wang, S.; Yu, X.
ADAM17 targets MMP-2 and MMP-9 via EGFR-MEK-ERK pathway activation to promote prostate cancer cell invasion
Int. J. Oncol.
40
1714-1724
2012
Homo sapiens (P78536), Homo sapiens
Breshears, L.M.; Schlievert, P.M.; Peterson, M.L.
A disintegrin and metalloproteinase 17 (ADAM17) and epidermal growth factor receptor (EGFR) signaling drive the epithelial response to Staphylococcus aureus toxic shock syndrome toxin-1 (TSST-1)
J. Biol. Chem.
287
32578-32587
2012
Homo sapiens (P78536), Homo sapiens
Minond, D.; Cudic, M.; Bionda, N.; Giulianotti, M.; Maida, L.; Houghten, R.; Fields, G.
Discovery of novel inhibitors of a disintegrin and metalloprotease 17 (ADAM17) using glycosylated and non-glycosylated substrates
J. Biol. Chem.
287
36473-36487
2012
Homo sapiens (P78536)
Stawikowska, R.; Cudic, M.; Giulianotti, M.; Houghten, R.; Fields, G.; Minond, D.
Activity of ADAM17 (a disintegrin and metalloprotease 17) is regulated by its noncatalytic domains and secondary structure of its substrates
J. Biol. Chem.
288
22871-22879
2013
Homo sapiens (P78536)
Patel, V.B.; Clarke, N.; Wang, Z.; Fan, D.; Parajuli, N.; Basu, R.; Putko, B.; Kassiri, Z.; Turner, A.J.; Oudit, G.Y.
Angiotensin II induced proteolytic cleavage of myocardial ACE2 is mediated by TACE/ADAM-17: a positive feedback mechanism in the RAS
J. Mol. Cell. Cardiol.
66
167-176
2014
Homo sapiens (P78536), Mus musculus (Q9Z0F8)
Oikawa, H.; Maesawa, C.; Tatemichi, Y.; Nishinari, Y.; Nishiya, M.; Mizugai, H.; Ikeda, A.; Oikawa, K.; Takikawa, Y.; Masuda, T.
A disintegrin and metalloproteinase 17 (ADAM17) mediates epidermal growth factor receptor transactivation by angiotensin II on hepatic stellate cells
Life Sci.
97
137-144
2014
Homo sapiens (P78536)
Lin, P.; Sun, X.; Feng, T.; Zou, H.; Jiang, Y.; Liu, Z.; Zhao, D.; Yu, X.
ADAM17 regulates prostate cancer cell proliferation through mediating cell cycle progression by EGFR/PI3K/AKT pathway
Mol. Cell. Biochem.
359
235-243
2012
Homo sapiens (P78536), Homo sapiens
Liu, S.; Liu, S.; Wang, Y.; Liao, Z.
The P2/P2 sites affect the substrate cleavage of TNF-alpha converting enzyme (TACE)
Mol. Immunol.
62
122-128
2014
Homo sapiens (P78536)
Jing, Y.; Ni, Z.; Wu, J.; Higgins, L.; Markowski, T.; Kaufman, D.; Walcheck, B.
Identification of an ADAM17 cleavage region in human CD16 (FcgammaRIII) and the engineering of a non-cleavable version of the receptor in NK cells
PLoS ONE
10
e121788
2015
Homo sapiens (P78536), Homo sapiens
Raikwar, N.; Liu, K.; Thomas, C.
N-terminal cleavage and release of the ectodomain of Flt1 is mediated via ADAM10 and ADAM 17 and regulated by VEGFR2 and the Flt1 intracellular domain
PLoS ONE
9
e112794
2014
Homo sapiens (P78536)
Rizza, S.; Copetti, M.; Cardellini, M.; Menghini, R.; Pecchioli, C.; Luzi, A.; Di Cola, G.; Porzio, O.; Ippoliti, A.; Romeo, F.; Pellegrini, F.; Federici, M.
A score including ADAM17 substrates correlates to recurring cardiovascular event in subjects with atherosclerosis
Atherosclerosis
239
459-464
2015
Homo sapiens (P78536)
Duesterhoeft, S.; Michalek, M.; Kordowski, F.; Oldefest, M.; Sommer, A.; Roeseler, J.; Reiss, K.; Groetzinger, J.; Lorenzen, I.
Extracellular juxtamembrane segment of ADAM17 interacts with membranes and is essential for its shedding activity
Biochemistry
54
5791-5801
2015
Homo sapiens (P78536)
Groth, E.; Pruessmeyer, J.; Babendreyer, A.; Schumacher, J.; Pasqualon, T.; Dreymueller, D.; Higashiyama, S.; Lorenzen, I.; Groetzinger, J.; Cataldo, D.; Ludwig, A.
Stimulated release and functional activity of surface expressed metalloproteinase ADAM17 in exosomes
Biochim. Biophys. Acta
1863
2795-2808
2016
Homo sapiens (P78536)
Qian, M.; Shen, X.; Wang, H.
The distinct role of ADAM17 in APP proteolysis and microglial activation related to Alzheimer's disease
Cell. Mol. Neurobiol.
36
471-482
2016
Homo sapiens (P78536)
Shen, M.; Hu, M.; Fedak, P.; Oudit, G.; Kassiri, Z.
Cell-specific functions of ADAM17 regulate the progression of thoracic aortic aneurysm
Circ. Res.
123
372-388
2018
Mus musculus, Homo sapiens (P78536), Homo sapiens
Arai, J.; Goto, K.; Tanoue, Y.; Ito, S.; Muroyama, R.; Matsubara, Y.; Nakagawa, R.; Kaise, Y.; Lim, L.A.; Yoshida, H.; Kato, N.
Enzymatic inhibition of MICA sheddase ADAM17 by lomofungin in hepatocellular carcinoma cells
Int. J. Cancer
143
2575-2583
2018
Homo sapiens (P78536), Homo sapiens
Li, W.; Wang, D.; Sun, X.; Zhang, Y.; Wang, L.; Suo, J.
ADAM17 promotes lymph node metastasis in gastric cancer via activation of the Notch and Wnt signaling pathways
Int. J. Mol. Med.
43
914-926
2019
Homo sapiens (P78536), Homo sapiens
Pavlenko, E.; Cabron, A.; Arnold, P.; Dobert, J.; Rose-John, S.; Zunke, F.
Functional characterization of colon cancer-associated mutations in ADAM17 Modifications in the pro-domain interfere with trafficking and maturation
Int. J. Mol. Sci.
20
E2198
2019
Homo sapiens (P78536), Homo sapiens
Yoneyama, T.; Gorry, M.; Miller, M.; Gaither-Davis, A.; Lin, Y.; Moss, M.; Griffith, L.; Lauffenburger, D.; Stabile, L.; Herman, J.; Vujanovic, N.
Modification of proteolytic activity matrix analysis (PrAMA) to measure ADAM10 and ADAM17 sheddase activities in cell and tissue lysates
J. Cancer
8
3916-3932
2017
Mus musculus, Homo sapiens (P78536)
Knapinska, A.M.; Dreymuller, D.; Ludwig, A.; Smith, L.; Golubkov, V.; Sohail, A.; Fridman, R.; Giulianotti, M.; LaVoi, T.M.; Houghten, R.A.; Fields, G.B.; Minond, D.
SAR studies of exosite-binding substrate-selective inhibitors of a disintegrin and metalloprotease 17 (ADAM17) and application as selective in vitro probes
J. Med. Chem.
58
5808-5824
2015
Homo sapiens (P78536)
Udechukwu, M.; Tsopmo, A.; Mawhinney, H.; He, R.; Kienesberger, P.; Udenigwe, C.
Inhibition of ADAM17/TACE activity by zinc-chelating rye secalin-derived tripeptides and analogues
RSC Adv.
7
26361-26369
2017
Homo sapiens
-
Lorenzen, I.; Lokau, J.; Korpys, Y.; Oldefest, M.; Flynn, C.M.; Kuenzel, U.; Garbers, C.; Freeman, M.; Groetzinger, J.; Duesterhoeft, S.
Control of ADAM17 activity by regulation of its cellular localisation
Sci. Rep.
6
35067
2016
Homo sapiens
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