Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.4.21.73 - u-Plasminogen activator and Organism(s) Homo sapiens and UniProt Accession P00749

for references in articles please use BRENDA:EC3.4.21.73
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.73 u-Plasminogen activator
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P00749 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Specific cleavage of Arg-/-Val bond in plasminogen to form plasmin
Synonyms
urokinase, urokinase-type plasminogen activator, urokinase plasminogen activator, urokinase type plasminogen activator, urokinase-type pa, urokinase-type plasminogen, urokinase-plasminogen activator, urinary plasminogen activator, cellular plasminogen activator, two-chain urokinase-type plasminogen activator, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Urokinase plasminogen activator
-
urokinase type plasminogen activator
-
Urokinase-type plasminogen activator
-
Abbokinase
-
-
-
-
Cellular plasminogen activator
-
-
-
-
Double-chain urokinase-type plasminogen activator
-
-
-
-
Plasminogen activator, urokinase-type
-
-
-
-
PLAU
-
-
Two-chain urokinase-type plasminogen activator
-
-
-
-
U-plasminogen activator
-
-
-
-
uPA-type Plg activator
-
-
Urinary plasminogen activator
-
-
-
-
Urokinase
Urokinase plasminogen activator
urokinase type plasminogen activator
-
-
urokinase-plasminogen activator
-
-
urokinase-type PA
-
-
urokinase-type plasmin activator
-
-
urokinase-type plasminogen
-
-
Urokinase-type plasminogen activator
urokinase-type Plg activator
-
-
urokine-type plasminogen activator
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
139639-24-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
casein + H2O
?
show the reaction diagram
-
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-diglutamyl-glycyl-L-arginine 4-nitroanilide + H2O
L-diglutamyl-glycyl-L-arginine + 4-nitroaniline
show the reaction diagram
-
-
-
?
plasmin + H2O
?
show the reaction diagram
-
-
-
?
plasminogen + H2O
plasmin + ?
show the reaction diagram
pyro-Glu-Pro-Arg-4-nitroanilide + H2O
pyro-Glu-Pro-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
?
thrombin + H2O
?
show the reaction diagram
-
-
-
?
alpha6 integrin + H2O
?
show the reaction diagram
benzoyl-beta-Ala-Gly-Arg-4-nitroanilide + H2O
benzoyl-beta-Ala-Gly-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Cellular receptor of urokinase-type plasminogen activator + H2O
?
show the reaction diagram
-
cleavage between domains 1 and 2 generating a cell-associated variant of the receptor of urokinase-type plasminogen activator without ligand-binding properties, uPA catalyzed cleavage does not require binding of the protease to the receptor through its epidermal growth factor-like receptor-binding domain, low-molecular weight uPA lacking this domain also cleaves the substrate
-
-
?
D-Glu-Gly-Arg-4-nitroanilide + H2O
D-Glu-Gly-Arg + 4-nitroaniline
show the reaction diagram
-
a uPA substrate S-2444
-
-
?
D-Val-Leu-Lys-4-nitroanilide + H2O
D-Val-Leu-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
epithelial sodium channel gamma subunit + H2O
?
show the reaction diagram
-
of Xenopus laevis ocytes, activation by proteolytic cleavage at 177GR-/-KR180
-
-
?
GSGRSA + H2O
GSGR + Ser-Ala
show the reaction diagram
-
-
-
?
HYGRSA + H2O
HYGR + Ser-Ala
show the reaction diagram
-
-
-
?
L-diglutamyl-glycyl-L-arginine-4-nitroanilide + H2O
L-diglutamyl-glycyl-L-arginine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
L-pyroGlu-Gly-L-Arg-4-nitroanilide + H2O
L-pyroGlu-Gly-L-Arg + 4-nitroaniline
show the reaction diagram
-
i.e. S-2444
-
-
?
L-pyroglutamyl-glycyl-L-arginine-p-nitroanilide + H2O
L-pyroglutamyl-glycyl-L-arginine + 4-nitroaniline
show the reaction diagram
-
-
-
?
PFGRSA + H2O
PFGR + Ser-Ala
show the reaction diagram
-
-
-
?
plasminogen + H2O
?
show the reaction diagram
plasminogen + H2O
plasmin + ?
show the reaction diagram
pyroGlu-Gly-Arg-4-nitroanilide + H2O
pyroGlu-Gly-Arg + 4-nitroaniline
show the reaction diagram
-
i.e. S-2444, a chromogenic substrate
-
-
?
QRGRSA + H2O
QRGR + Ser-Ala
show the reaction diagram
-
-
-
?
S-2444 + H2O
pyroGlu-Gly-Arg + 4-nitroaniline
show the reaction diagram
S2444 + H2O
pyroGlu-Gly-Arg + 4-nitroaniline
show the reaction diagram
-
i.e. 5-oxo-L-Pro-Gly-L-Arg-p-nitroanilide
-
?
t-butyloxycarbonyl-valyl-leucyl-lysine-4-methylcoumaryl-7-amide + H2O
Boc-L-Val-L-Leu-L-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
urokinase plasminogen activator receptor + H2O
?
show the reaction diagram
YGAKAY + H2O
YGAK + Ala-Tyr
show the reaction diagram
-
-
-
?
Z-RRG-7-amido-4-methylcoumarin + H2O
Z-RRG + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
plasminogen + H2O
plasmin + ?
show the reaction diagram
alpha6 integrin + H2O
?
show the reaction diagram
-
alpha6 integrin is present on prostate carcinoma escaping the gland via nerves. Urokinase-dependent cleavage of the laminin binding domain from the prostate tumor cell surface
-
-
?
plasminogen + H2O
?
show the reaction diagram
plasminogen + H2O
plasmin + ?
show the reaction diagram
urokinase plasminogen activator receptor + H2O
?
show the reaction diagram
-
receptor cleavage by u-PA, u-PAR is susceptible to proteolysis by its cognate ligand and several other proteases, biological significance, overview
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-([6-[(3'-carbamimidoylbiphenyl-3-yl)oxy]-3,5-difluoro-4-methylpyridin-2-yl]oxy)-4-(dimethylamino)benzoic acid
-
2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-methylbenzoic acid
-
2-[(6-[[5-amino-3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-methylbenzoic acid
-
3,5-diamino-N-carbamimidoyl-6-chloropyrazine-2-carboxamide
i.e. amiloride, selectively inhibits the enzyme, but not tissue plasminogen activator or other serine protease members of the trypsin superfamily
4'-(6-cyano-2-naphthamido)biphenyl-3-carboxylic acid
slight inhibition
4'-(6-methoxynaphthalene-2-sulfonamido)biphenyl-3-carboxamide
slight inhibition
4-(2-aminoethoxy)-N-[3-chloro-2-ethoxy-5-(piperidin-1-yl)phenyl]-3,5-dimethylbenzamide
-
4-[(E)-(5-oxo-2-phenyl-1,3-oxazol-4(5H)-ylidene)methyl]benzenecarboximidamide
-
6-(phenylcarbamoyl)-2-naphthoic acid
slight inhibition
6-amino-N-phenyl-2-naphthamide
slight inhibition
6-bromo-N-phenyl-2-naphthamide
slight inhibition
6-carbamimidoyl-N-(3,5-dimethoxyphenyl)-2-naphthamide
-
6-carbamimidoyl-N-phenyl-2-naphthamide
-
6-carbamimidoyl-N-phenyl-5,8-dihydronaphthalene-2-carboxamide
-
6-cyano-N-(3'-methoxybiphenyl-4-yl)-2-naphthamide
-
6-cyano-N-(3,5-dimethoxyphenyl)-2-naphthamide
-
6-cyano-N-phenylnaphthalene-2-carboxamide
slight inhibition
6-methoxy-N-(3'-(trifluoromethyl)biphenyl-4-yl)-2-naphthamide
-
6-methoxy-N-(3'-(trifluoromethyl)biphenyl-4-yl)naphthalene-2-sulfonamide
-
6-methoxy-N-(3'-methoxybiphenyl-4-yl)-2-naphthamide
-
6-methoxy-N-(3'-methoxybiphenyl-4-yl)naphthalene-2-sulfonamide
-
6-methoxy-N-(3'-nitrobiphenyl-4-yl)-2-naphthamide
-
6-methoxy-N-(3'-nitrobiphenyl-4-yl)naphthalene-2-sulfonamide
-
6-methoxy-N-(4'-methoxybiphenyl-4-yl)-2-naphthamide
-
6-methoxy-N-(4'-methoxybiphenyl-4-yl)naphthalene-2-sulfonamide
-
6-methoxy-N-phenyl-2-naphthamide
slight inhibition
7-methoxy-8-[1-(methylsulfonyl)-1H-pyrazol-4-yl]naphthalene-2-carboximidamide
-
amiloride
-
bis[(phenylamino)acetyl] [2-(4-carbamimidamidophenyl)-1-[(methoxycarbonyl)amino]ethyl]phosphonate
-
diphenyl [2-(4-carbamimidamidophenyl)-1-[(methoxycarbonyl)amino]ethyl]phosphonate
-
ethyl 4-(3-carbamimidoyl-N-[[2,4,6-tri(propan-2-yl)phenyl]sulfonyl]-L-phenylalanyl)piperazine-1-carboxylate
-
human PAI-1
human plasminogen activator inhibitor-1, complex structure of uPA:PAI-1 Michaelis complex, interaction analysis, the S3-pocket-lining residues of uPA and the P3 residue of both PAI-1 and plasminogen form numerous polar interactions in the human uPA:PAI-1 Michaelis complex, overview
-
methyl 4'-(2-naphthamido)biphenyl-3-carboxylate
-
methyl 4'-(6-amino-2-naphthamido)biphenyl-3-carboxylate
-
methyl 4'-(6-bromo-2-naphthamido)biphenyl-3-carboxylate
-
methyl 4'-(6-carbamoyl-2-naphthamido)biphenyl-3-carboxylate
-
methyl 4'-(6-chloro-2-naphthamido)biphenyl-3-carboxylate
-
methyl 4'-(6-cyano-2-naphthamido)biphenyl-3-carboxylate
-
methyl 4'-(6-methoxy-2-naphthamido)biphenyl-3-carboxylate
-
methyl 4'-(6-methoxynaphthalene-2-sulfonamido)biphenyl-3-carboxylate
-
methyl 4'-(6-methoxynaphthalene-2-sulfonamido)biphenyl-4-carboxylate
-
methyl 4'-(naphthalene-2-sulfonamido)biphenyl-3-carboxylate
-
methyl 4'-(naphthalene-2-sulfonamido)biphenyl-4-carboxylate
-
methyl 6-(3'-(methoxycarbonyl)biphenyl-4-ylcarbamoyl)-2-naphthoate
-
methyl 6-(phenylcarbamoyl)-2-naphthoate
slight inhibition
N-(2,4'-dimethoxybiphenyl-4-yl)-6-methoxynaphthalene-2-sulfonamide
-
N-(2,4-dimethoxybiphenyl-4-yl)-6-methoxy-2-naphthamide
slight inhibition
N-(3',4'-dimethoxybiphenyl-4-yl)-6-methoxy-2-naphthamide
-
N-(3',4'-dimethoxybiphenyl-4-yl)-6-methoxynaphthalene-2-sulfonamide
-
N-(3'-aminobiphenyl-4-yl)-6-methoxynaphthalene-2-sulfonamide
-
N-(3'-chlorobiphenyl-4-yl)-6-methoxynaphthalene-2-sulfonamide
slight inhibition
N-(3'-fluorobiphenyl-4-yl)-6-methoxynaphthalene-2-sulfonamide
slight inhibition
N-(3'-methoxybiphenyl-4-yl)-2-naphthamide
-
N-(3'-methoxybiphenyl-4-yl)naphthalene-2-sulfonamide
-
N-(4-(aminomethyl)phenyl)-6-carbamimidoyl-2-naphthamide trifluoro acetate
-
N-(benzylsulfonyl)-D-seryl-N-(4-carbamimidoylbenzyl)-L-alaninamide
N-(benzylsulfonyl)-D-seryl-N-(4-carbamimidoylbenzyl)-L-prolinamide
comparison of specificity with five additional trypsin-like serine-proteases
N-(benzylsulfonyl)-D-seryl-N-(4-carbamimidoylbenzyl)-L-serinamide
comparison of specificity with five additional trypsin-like serine-proteases
N-(benzylsulfonyl)-D-seryl-N-(4-carbamimidoylbenzyl)glycinamide
comparison of specificity with five additional trypsin-like serine-proteases
N-(biphenyl-4-yl)-6-methoxynaphthalene-2-sulfonamide
-
N-phenyl-2-naphthamide
slight inhibition
N-[(4-aminobenzyl)sulfonyl]-D-seryl-N-(4-carbamimidoylbenzyl)glycinamide
comparison of specificity with five additional trypsin-like serine-proteases
N-[(4-chlorobenzyl)sulfonyl]-D-seryl-N-(4-carbamimidoylbenzyl)-L-alaninamide
comparison of specificity with five additional trypsin-like serine-proteases
N-[(4-chlorobenzyl)sulfonyl]-D-seryl-N-(4-carbamimidoylbenzyl)-L-serinamide
comparison of specificity with five additional trypsin-like serine-proteases
N-[(4-methylbenzyl)sulfonyl]-D-seryl-N-(4-carbamimidoylbenzyl)-L-alaninamide
comparison of specificity with five additional trypsin-like serine-proteases
N-[(4-nitrobenzyl)sulfonyl]-D-seryl-N-(4-carbamimidoylbenzyl)glycinamide
comparison of specificity with five additional trypsin-like serine-proteases
N-[4-(aminomethyl)phenyl]-6-carbamimidoyl-4-(pyrimidin-2-ylamino)naphthalene-2-carboxamide
-
N-[[4-(methoxycarbonyl)benzyl]sulfonyl]-D-seryl-N-(4-carbamimidoylbenzyl)-L-alaninamide
comparison of specificity with five additional trypsin-like serine-proteases
N2-(2,4'-dimethoxybiphenyl-4-yl)naphthalene-2,6-dicarboxamide
-
N2-(3'-(trifluoromethyl)biphenyl-4-yl)naphthalene-2,6-dicarboxamide
-
N2-(3'-methoxybiphenyl-4-yl)naphthalene-2,6-dicarboxamide
-
N2-(3,5-dimethoxyphenyl)naphthalene-2,6-dicarboxamide
-
N2-(3-chlorobiphenyl-4-yl)naphthalene-2,6-dicarboxamide
-
N2-(4-(aminomethyl)phenyl)naphthalene-2,6-dicarboxamide trifluoroacetate
-
N2-phenylnaphthalene-2,6-dicarboxamide
-
NCI004367
-
NCI0135766
-
NCI0144205
-
NCI0666712
-
plasminogen activator inhibitor-1
PAI-1, specifically and rapidly inhibits urokinase-type plasminogen activator uPA and tissue-type plasminogen activator, tPA, EC 3.4.21.68. The PAI-1 reactive center loop serves as a bait to attract uPA onto the top of the PAI-1 molecule. P4–P3' residues of the reactive center loop interact extensively with the uPA catalytic site, accounting for about two-thirds of the total contact area, also almost all uPA exosite loops, including the 37-, 60-, 97-, 147-, and 217-loops, are involved in the interaction with PAI-1, of the residues of the 37-loop, Arg-E37a plays the most important role, Michaelis complex formation, overview. The recombinant stable His-tagged PAI-1 mutant 14-1B containing four point mutations N150H, K154T, Q319L, and M354I, is expressed in Escherichia coli strain C41(DE3) using the expression vector pT7-PL
1-[3'-([3,5-difluoro-6-[5-methyl-2-(1H-tetrazol-1-yl)phenoxy]pyridin-2-yl]oxy)biphenyl-3-yl]methanamine
-
-
2-(1-hydroxynaphthalen-2-yl)-1-H-benzoimidazole-5-carboxamidine
-
-
2-(2,6-dihydroxyphenyl)-1-H-benzoimidazole-5-carboxamidine
-
-
2-(2-hydroxy-3-bromo-5-methylphenyl)-1-H-benzoimidazole-5-carboxamidine
-
-
2-(2-hydroxy-3-bromophenyl)-1-H-benzoimidazole-5-carboxamidine
-
-
2-(2-hydroxy-3-fluorophenyl)-1-H-benzoimidazole-5-carboxamidine
-
-
2-(2-hydroxy-3-methoxyphenyl)-1-H-benzoimidazole-5-carboxamidine
-
-
2-(2-hydroxy-3-methylphenyl)-1-H-benzoimidazole-5-carboxamidine
-
-
2-(2-hydroxy-3-nitrophenyl)-1-H-benzoimidazole-5-carboxamidine
-
-
2-(2-hydroxy-4-diethylaminophenyl)-1-H-benzoimidazole-5-carboxamidine
-
-
2-(2-hydroxy-4-methylphenyl)-1-H-benzoimidazole-5-carboxamidine
-
-
2-(2-hydroxy-5-bromophenyl)-1-H-benzoimidazole-5-carboxamidine
-
-
2-(2-hydroxy-5-chlorobiphenyl-3-yl)-1-H-benzoimidazole-5-carboxamidine
-
-
2-(2-hydroxy-5-fluorophenyl)-1-H-benzoimidazole-5-carboxamidine
-
-
2-(2-hydroxy-5-methoxyphenyl)-1-H-benzoimidazole-5-carboxamidine
-
-
2-(2-hydroxy-5-methylphenyl)-1-H-benzoimidazole-5-carboxamidine
-
-
2-(2-hydroxy-5-nitrophenyl)-1-H-benzoimidazole-5-carboxamidine
-
-
2-(2-hydroxybiphenyl-3-yl)-1-H-benzoimidazole-5-carboxamidine
-
-
2-(2-hydroxyphenyl)-1-H-benzoimidazole-5-carboxamidine
-
-
2-(2-hydroxyphenyl)1H-benzoimidazole-5-carboxamidine
-
-
2-(4-chloro-7-(2-cyano-6-methoxyphenyl)isoquinolin-1-yl)guanidine
-
comparison of selectivity with t-plasminogen activator and plasmin
2-(4-chloro-7-(2-methoxyphenyl)isoquinolin-1-yl)guanidine
-
comparison of selectivity with t-plasminogen activator and plasmin
2-(4-chloro-7-(3-methoxyphenyl)isoquinolin-1-yl)guanidine
-
comparison of selectivity with t-plasminogen activator and plasmin
2-(7-(1,3-benzodioxol-5-yl)-4-chloroisoquinolin-1-yl)guanidine
-
comparison of selectivity with t-plasminogen activator and plasmin
2-(7-(1,3-benzodioxol-5-yl)isoquinolin-1-yl)guanidine
-
comparison of selectivity with t-plasminogen activator and plasmin
2-(7-phenylisoquinolin-1-yl)guanidine
-
comparison of selectivity with t-plasminogen activator and plasmin
2-([6-[(3'-carbamimidoylbiphenyl-3-yl)oxy]-3,5-difluoro-4-methylpyridin-2-yl]oxy)-4-(dimethylamino)benzoic acid
-
-
2-phenethyl-SO2-D-Ser-Ala-Arg-al
-
is an irreversible urokinase inhibitor, and an alkylating agent forming a covalent adduct with an active site of the enzyme
2-phenyl-1-H-benzoimidazole-5-carboxamidine
-
-
2-[(6-[[3',5-bis(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-methylbenzoic acid
-
-
2-[(6-[[3'-(aminomethyl)-5-hydroxybiphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-methylbenzoic acid
-
-
2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-3-methylbenzoic acid
-
-
2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-(dimethylamino)benzoic acid
-
-
2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-(propan-2-yl)benzoic acid
-
-
2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-methoxybenzoic acid
-
-
2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-methylbenzoic acid
-
-
2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-nitrobenzoic acid
-
-
2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-5-methylbenzoic acid
-
-
2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-6-methylbenzoic acid
-
-
2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]benzoic acid
-
-
2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-4-[3-(dimethylamino)pyrrolidin-1-yl]-3,5-difluoropyridin-2-yl)oxy]-4-(dimethylamino)benzoic acid
-
-
2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-4-[[2-(dimethylamino)ethyl](methyl)amino]-3,5-difluoropyridin-2-yl)oxy]-4-(dimethylamino)benzoic acid
-
-
2-[(6-[[4'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-(dimethylamino)benzoic acid
-
-
2-[(6-[[4-amino-3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-methylbenzoic acid
-
-
2-[(6-[[5-amino-3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-methylbenzoic acid
-
-
2-[(6-[[5-amino-3'-(aminomethyl)biphenyl-3-yl]oxy]-4-[3-(dimethylamino)pyrrolidin-1-yl]-3,5-difluoropyridin-2-yl)oxy]-4-methylbenzoic acid
-
-
2-[(6-[[6-amino-3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-methylbenzoic acid
-
-
2-[2-(7-amino-4-chloro-1-oxo-1H-isochromen-3-yloxy)ethyl]isothiourea hydrobromide
-
-
2-[2-(7-benzamido-4-chloro-1-oxo-1H-isochromen-3-yloxy)ethyl]isothiourea hydrobromide
-
-
2-[3-(7-amino-4-chloro-1-oxo-1H-isochromen-3-yloxy)propyl]isothiourea hydrobromide
-
-
2-[3-(7-benzamido-4-chloro-1-oxo-1H-isochromen-3-yloxy]propyl)isothiourea hydrobromide
-
-
2-[[3,5-difluoro-6-([3'-[(methylamino)methyl]biphenyl-3-yl]oxy)pyridin-2-yl]oxy]-4-(dimethylamino)benzoic acid
-
-
2-[[6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoro-4-(methylamino)pyridin-2-yl]oxy]-4-(dimethylamino)benzoic acid
-
-
2-[[6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoro-4-(morpholin-4-yl)pyridin-2-yl]oxy]-4-(dimethylamino)benzoic acid
-
-
2-[[6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoro-4-(piperazin-1-yl)pyridin-2-yl]oxy]-4-(dimethylamino)benzoic acid
-
-
2-[[6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-4-(dimethylamino)-3,5-difluoropyridin-2-yl]oxy]-4-(dimethylamino)benzoic acid
-
-
3-(1-carbamimidoylpiperidin-3-yl)-L-alanine
-
-
3-(1-carbamimidoylpiperidin-4-yl)-L-alanine
-
-
3-(2-bromoethoxy)-7-nitro-1H-isochromen-1-one
-
-
3-(3-bromopropoxy)-4-trifluoroacetyl-1H-isochromen-1-one
-
-
3-(3-bromopropoxy)-7-nitro-1H-isochromen-1-one
-
-
3-(4-chloro-1-((diaminomethylene)amino)isoquinolin-7-yl)-5-methoxybenzoic acid
-
comparison of selectivity with t-plasminogen activator and plasmin
3-(4-chloro-1-((diaminomethylene)amino)isoquinolin-7-yl)benzoic acid
-
comparison of selectivity with t-plasminogen activator and plasmin
3-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]benzoic acid
-
-
3-[2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]phenyl]propanoic acid
-
-
4-(4-chloro-1-((diaminomethylene)amino)isoquinolin-7-yl)benzoic acid
-
comparison of selectivity with t-plasminogen activator and plasmin
4-(dimethylamino)-2-[[6-([3'-[(dimethylamino)methyl]biphenyl-3-yl]oxy)-3,5-difluoropyridin-2-yl]oxy]benzoic acid
-
-
4-aminobenzamidine
-
competitive, no inhibition of the pro-uPA
4-chloro-3-alkoxyisocoumarin
-
competitive reversible inhibition
4-iodobenzo[b]thiophene-2-carboxamidine
-
APC-6860, competitive inhibition
4-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]benzoic acid
-
-
7-amino-3-(2-bromoethoxy)-1H-isochromen-1-one
-
-
alpha-1-Proteinase inhibitor
-
-
-
alpha-2-Macroglobulin
-
-
-
alpha-Benzylsulfonyl-p-aminophenylalanine
-
-
amiloride
antibody DS2
-
isolation and affinity maturation of a fully human recombinant antibody, that is specific to the human uPA and capable of inhibiting its enzymatic activity with an IC50 value in the low nanomolar range, overview. Ability of the DS2 antibody to preferentially localize at the tumor site compared with healthy organs
-
antibody IgG(DS2)
-
-
-
antibody scFv(DS2)
-
-
-
antithrombin
-
-
-
benzamidine
-
-
benzo[b]thiophene-2-carboxamidine
-
APC-7377
concanavalin A
-
-
-
D-Ser-Ala-Arg-NH-(CH2)5-NH2
-
competitive inhibition
D-Ser-Ala-Arg-NH-(CH2)7-NH2
-
-
D-Ser-Ala-Arg-NH-(CH2)8-NH2
-
-
D-Ser-Ala-Arg-NH-(CH2)9-NH2
-
-
diphenyl (N-benzyloxycarbonyl-D-seryl-L-alanyl)amino-(3-guanylpropyl)methanephosphonate
-
50% inhibition at 0.000061 mM
diphenyl (N-benzyloxycarbonyl-D-seryl-L-alanyl)amino-(4-guanylbutyl)methanephosphonate
-
50% inhibition at 0.00025 mM
diphenyl (N-benzyloxycarbonyl-D-seryl-L-alanyl)amino-(4-guanylphenyl)methanephosphonate
-
50% inhibition at 0.0016 mM
diphenyl 1-(N-benzyloxycarbonyl-D-seryl-L-alanyl)amino-2-(4-guanylphenyl)ethanephosphonate
-
50% inhibition at 0.000057 mM
ecotin
-
Endothelial cell/platelet type plasminogen activator inhibitor
-
-
-
Fast-acting uPA inhibitor in plasma
-
-
-
Glu-Gly-Arg chloromethyl ketone
-
-
Glu-Gly-Arg-chloromethyl ketone
-
-
i-Boc-D-Ser-Ala-Arg-al
-
is an alkylating agent, and irreversibly inhibits urokinase by forming a covalent adduct with an active site of the enzyme
maspin
-
regulates uPA-dependent processes in vivo not involving its RCL sequence with Arg340, but is inable to directly inhibit uPA catalytic activity in vitro, binds the enzyme in both singlechain and double-chain forms, maspin is a member of the serpin family with a reactive center loop that is incompatible with proteinase inhibition by the serpin conformational change mechanism, overview
meloxicam
-
reduces enzyme secretion in chondral and synovial cultures downregulating the PA/plasmin system
methylprednisolone
-
reduces enzyme secretion in chondral and synovial cultures downregulating the PA/plasmin system
mupain-1
myristoylated PKI
-
mPLI, a protein kinase A inhibitor, complete inhibition
-
N-[3-(2-bromoethoxy)-4-chloro-1-oxo-1H-isochromen-7-yl]benzamide
-
-
N-[3-(3-bromopropoxy)-4-chloro-1-oxo-1H-isochromen-7-yl]benzamide
-
competitive reversible inhibition mechanism, the bromine occupies the same position as positively charged arginino mimetic groups, molecular modeling
naproxen
-
reduces enzyme secretion in chondral and synovial cultures downregulating the PA/plasmin system
PA inhibitor type 1
-
PAI-1, effects of uPA-PAI-1 are abrogated by the nitric-oxide synthase inhibitor N-D-nitro-L-arginine methyl ester. Dramatically elevated levels in case of acute lung injury
-
PAI-1
-
-
-
PAI-2
-
i.e. plasminogen activator inhibitor type 2, cell-surface enzyme:PAI-2 complex formation is reflective of complete enzyme inhibition, kinetic analysis of inhibition
-
PD 098059
-
hepatocyte growth factor-mediated uPA secretion by Hep-G2 cells is reduced with increasing concentrations of PD 098059
penicilloic acid
-
-
phenethylsulfonamidino-D-seryl-L-alanyl(P2)-L-argininal
-
-
phenethylsulfonamidino-D-seryl-L-alanyl-L-argininal
-
-
plasminogen activator inhibitor
-
PAI-1
-
plasminogen activator inhibitor 1
Plasminogen activator inhibitor 2
-
-
-
plasminogen activator inhibitor type-1
-
plasminogen activator inhibitor-1
plasminogen activator inhibitor-2
-
Plumbagin
-
leads to uPA inhibition and downregulation, inhibits adhesion, migration and invasion in HepG2 cells
Protease nexin I
-
-
-
Protein C inhibitor
-
-
-
staphylokinase
-
competitively inhibits plasminogen activation by endogenous uPA. The N-terminal residues of staphylokinase are important for inhibition
-
thieno[2,3-b]pyridine-2-carboxamidine
-
APC-7538
trans-3,4'-dimethyl-3-hydroxyflavanone
-
i.e. t-flavanone, a synthetic compound with hair growth enhancing activity that is effective against male pattern alopecia, inhibits the enzyme on the surface of keratinocytes, overview
trans-diphenyl N-(N-benzyloxycarbonyl-D-seryl-L-alanyl)amino-(4-(guanylmethyl)-cyclohexyl)methanephosphonate
-
50% inhibition at 0.0011 mM
Trypsin
-
-
-
TX-1877
-
hypoxic cell radiosensitizer. Treatment of nude mice bearing subcutaneously or orthotopically implanted human colon cancer cell lines HCT-116 and HT-29 with TX-1877, irradiation or TX-1877 with irradiation results in significant inhibition of matrix metalloproteinase-9 and uPA. Treatments also inhibit the para-aortic lymph node metastasis, however, do not prolong the survival in orthotopic model. In the subcutaneous model, tumors treated with TX-1877 and irradiation show significant reductions in volume
type-1 plasminogen activator inhibitors
-
primary endogenous inhibitors
-
upain-1
-
competitive, no inhibition of the pro-uPA
WXC-340
-
a selective u-PA inhibitor
-
[2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]phenyl]acetic acid
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,3,8-trihydroxy-6-methylanthraquinone
-
i.e. emodin, an active compound of aloe. Emodin increases the fibrinolytic activity of fibroblast cells in a dose-dependent manner, linked to increased uPA activity and uPA gene up-regulation. Emodin also induces up-regulation of uPA inhibitor PAI-1. Up-regulations are independent of emodin's effect on nuclear factor kappaB. The effect on the uPA system may be via generation of reactive oxygen species
Ile-Ile
-
an Ile-Ile or Ile-Val dipeptide can induce limited enzyme activity in the single-chain zymogen form of uPA or its K158A variant, which cannot be activated proteolytically
Ile-Val
-
an Ile-Ile or Ile-Val dipeptide can induce limited enzyme activity in the single-chain zymogen form of uPA or its K158A variant, which cannot be activated proteolytically
interleukin beta
-
significantly induces uPA expression and activity via protein kinase Calpha-dependent JNK1/2 and NIK cascades. Induction is inhibited by pretreatment with the inhibitors of JNK1/2, SP600125, of protein kinase C, Ro31-8220 and Go6976, or of nuclear factor kappaB, helenalin, and by transfection with dominant negative mutants of protein kinase C alpha, NIK, and IKKbeta, and siRNAs of JNK1/2 and p65
-
phorbol 12-myristate 13-acetate
-
stimulation of dental pulp cells by tumor necrosis factor-alpha results in increased uPA activity. Tumor necrosis factor-alpha-induced PA release is enhanced in the presence of phorbol 12-myristate 13-acetate
SB 203580
-
pretreatment of Hep-G2 cells with SB 203580 increases hepatocyte growth factor-mediated uPA secretion by 50-60%
tumor necrosis factor-alpha
-
stimulation of dental pulp cells results in increased uPA activity. Tumor necrosis factor-alpha-induced PA release is enhanced in the presence of phorbol 12-myristate 13-acetate
-
UK-356202
-
rapid, sensitive and selective method for detection in human plasma
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.052 - 0.6
GSGRSA
0.03 - 3.8
HYGRSA
0.297 - 0.608
L-diglutamyl-glycyl-L-arginine-4-nitroanilide
0.053 - 0.452
L-pyroGlu-Gly-L-Arg-4-nitroanilide
0.014 - 2.2
PFGRSA
0.000243 - 0.017
plasminogen
-
0.1 - 0.13
pyroGlu-Gly-Arg-4-nitroanilide
0.13 - 2.18
QRGRSA
0.051 - 0.089
S2444
0.13 - 2.3
YGAKAY
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0075 - 0.0113
L-diglutamyl-glycyl-L-arginine-4-nitroanilide
0.0383 - 14.1
plasminogen
-
0.73 - 773
pyroGlu-Gly-Arg-4-nitroanilide
0.0077 - 350
S2444
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12 - 99
pyroGlu-Gly-Arg-4-nitroanilide
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000139
6-carbamimidoyl-N-(3,5-dimethoxyphenyl)-2-naphthamide
pH 8.8, 37°C
0.000631
6-carbamimidoyl-N-phenyl-2-naphthamide
pH 8.8, 37°C
0.00063
7-methoxy-8-[1-(methylsulfonyl)-1H-pyrazol-4-yl]naphthalene-2-carboximidamide
pH 7.4, 37°C
0.00041
ethyl 4-(3-carbamimidoyl-N-[[2,4,6-tri(propan-2-yl)phenyl]sulfonyl]-L-phenylalanyl)piperazine-1-carboxylate
pH 8.8, 37°C
0.00004
N-(4-(aminomethyl)phenyl)-6-carbamimidoyl-2-naphthamide trifluoro acetate
pH 8.8, 37°C
0.0000077 - 0.0077
N-(benzylsulfonyl)-D-seryl-N-(4-carbamimidoylbenzyl)-L-alaninamide
0.013
N-(benzylsulfonyl)-D-seryl-N-(4-carbamimidoylbenzyl)-L-prolinamide
-
0.02
N-(benzylsulfonyl)-D-seryl-N-(4-carbamimidoylbenzyl)-L-serinamide
-
0.036
N-(benzylsulfonyl)-D-seryl-N-(4-carbamimidoylbenzyl)glycinamide
-
0.018
N-[(4-aminobenzyl)sulfonyl]-D-seryl-N-(4-carbamimidoylbenzyl)glycinamide
-
0.0076
N-[(4-chlorobenzyl)sulfonyl]-D-seryl-N-(4-carbamimidoylbenzyl)-L-alaninamide
-
0.023
N-[(4-chlorobenzyl)sulfonyl]-D-seryl-N-(4-carbamimidoylbenzyl)-L-serinamide
-
0.01
N-[(4-methylbenzyl)sulfonyl]-D-seryl-N-(4-carbamimidoylbenzyl)-L-alaninamide
-
0.024
N-[(4-nitrobenzyl)sulfonyl]-D-seryl-N-(4-carbamimidoylbenzyl)glycinamide
-
0.0000006
N-[4-(aminomethyl)phenyl]-6-carbamimidoyl-4-(pyrimidin-2-ylamino)naphthalene-2-carboxamide
pH 7.4, 37°C
0.018
N-[[4-(methoxycarbonyl)benzyl]sulfonyl]-D-seryl-N-(4-carbamimidoylbenzyl)-L-alaninamide
-
0.0039
2-(1-hydroxynaphthalen-2-yl)-1-H-benzoimidazole-5-carboxamidine
-
pH 7.4, 37°C
0.0019
2-(2,6-dihydroxyphenyl)-1-H-benzoimidazole-5-carboxamidine
-
pH 7.4, 37°C
0.00028
2-(2-hydroxy-3-bromo-5-methylphenyl)-1-H-benzoimidazole-5-carboxamidine
-
pH 7.4, 37°C
0.00025
2-(2-hydroxy-3-bromophenyl)-1-H-benzoimidazole-5-carboxamidine
-
pH 7.4, 37°C
0.00055
2-(2-hydroxy-3-fluorophenyl)-1-H-benzoimidazole-5-carboxamidine
-
pH 7.4, 37°C
0.0036
2-(2-hydroxy-3-methoxyphenyl)-1-H-benzoimidazole-5-carboxamidine
-
pH 7.4, 37°C
0.008
2-(2-hydroxy-3-methylphenyl)-1-H-benzoimidazole-5-carboxamidine
-
pH 7.4, 37°C
0.0009
2-(2-hydroxy-3-nitrophenyl)-1-H-benzoimidazole-5-carboxamidine
-
pH 7.4, 37°C
0.013
2-(2-hydroxy-4-diethylaminophenyl)-1-H-benzoimidazole-5-carboxamidine
-
pH 7.4, 37°C
0.0036
2-(2-hydroxy-4-methylphenyl)-1-H-benzoimidazole-5-carboxamidine
-
pH 7.4, 37°C
0.0037
2-(2-hydroxy-5-bromophenyl)-1-H-benzoimidazole-5-carboxamidine
-
pH 7.4, 37°C
0.0005
2-(2-hydroxy-5-chlorobiphenyl-3-yl)-1-H-benzoimidazole-5-carboxamidine
-
pH 7.4, 37°C
0.0028
2-(2-hydroxy-5-fluorophenyl)-1-H-benzoimidazole-5-carboxamidine
-
pH 7.4, 37°C
0.0036
2-(2-hydroxy-5-methoxyphenyl)-1-H-benzoimidazole-5-carboxamidine
-
pH 7.4, 37°C
0.0075
2-(2-hydroxy-5-methylphenyl)-1-H-benzoimidazole-5-carboxamidine
-
pH 7.4, 37°C
0.0033
2-(2-hydroxy-5-nitrophenyl)-1-H-benzoimidazole-5-carboxamidine
-
pH 7.4, 37°C
0.0004
2-(2-hydroxybiphenyl-3-yl)-1-H-benzoimidazole-5-carboxamidine
-
pH 7.4, 37°C
0.0055
2-(2-hydroxyphenyl)-1-H-benzoimidazole-5-carboxamidine
-
pH 7.4, 37°C
0.00018
2-(4-chloro-7-(2-cyano-6-methoxyphenyl)isoquinolin-1-yl)guanidine
-
-
0.0001
2-(4-chloro-7-(2-methoxyphenyl)isoquinolin-1-yl)guanidine
-
-
0.000083
2-(4-chloro-7-(3-methoxyphenyl)isoquinolin-1-yl)guanidine
-
-
0.0001
2-(7-(1,3-benzodioxol-5-yl)-4-chloroisoquinolin-1-yl)guanidine
-
-
0.00034
2-(7-(1,3-benzodioxol-5-yl)isoquinolin-1-yl)guanidine
-
-
0.0004
2-(7-phenylisoquinolin-1-yl)guanidine
-
-
0.055
2-phenyl-1-H-benzoimidazole-5-carboxamidine
-
pH 7.4, 37°C
0.00002
2-[2-(7-amino-4-chloro-1-oxo-1H-isochromen-3-yloxy)ethyl]isothiourea hydrobromide
-
pH 8.8, 25°C
0.000084
2-[2-(7-benzamido-4-chloro-1-oxo-1H-isochromen-3-yloxy)ethyl]isothiourea hydrobromide
-
pH 8.8, 25°C
0.000038
2-[3-(7-amino-4-chloro-1-oxo-1H-isochromen-3-yloxy)propyl]isothiourea hydrobromide
-
pH 8.8, 25°C
0.00001
2-[3-(7-benzamido-4-chloro-1-oxo-1H-isochromen-3-yloxy]propyl)isothiourea hydrobromide
-
pH 8.8, 25°C
0.219
3-(1-carbamimidoylpiperidin-3-yl)-L-alanine
-
pH 7.4, 37°C, enzyme mutant H99Y
0.00248
3-(1-carbamimidoylpiperidin-4-yl)-L-alanine
-
pH 7.4, 37°C, enzyme mutant H99Y
0.0042
3-(2-bromoethoxy)-7-nitro-1H-isochromen-1-one
-
pH 8.8, 25°C
0.014
3-(3-bromopropoxy)-4-trifluoroacetyl-1H-isochromen-1-one
-
pH 8.8, 25°C
0.0043
3-(3-bromopropoxy)-7-nitro-1H-isochromen-1-one
-
pH 8.8, 25°C
0.000009
3-(4-chloro-1-((diaminomethylene)amino)isoquinolin-7-yl)-5-methoxybenzoic acid
-
-
0.000037
3-(4-chloro-1-((diaminomethylene)amino)isoquinolin-7-yl)benzoic acid
-
-
0.000082
4-(4-chloro-1-((diaminomethylene)amino)isoquinolin-7-yl)benzoic acid
-
-
0.0395
4-aminobenzamidine
-
pH 7.4, 37°C, mature uPA
0.00021
4-iodobenzo[b]thiophene-2-carboxamidine
-
pH 7.4, 37°C
0.065
7-amino-3-(2-bromoethoxy)-1H-isochromen-1-one
-
pH 8.8, 25°C
0.005
amiloride
-
pH 7.4, 37°C, mature uPA
0.097
benzamidine
-
pH 7.4, 37°C
0.0023
benzo[b]thiophene-2-carboxamidine
-
pH 7.4, 37°C
0.0063
D-Ser-Ala-Arg-NH-(CH2)5-NH2
-
pH 8.8, 37°C
0.0036 - 0.0153
mupain-1
0.0014
N-[3-(2-bromoethoxy)-4-chloro-1-oxo-1H-isochromen-7-yl]benzamide
-
pH 8.8, 25°C
0.000034
N-[3-(3-bromopropoxy)-4-chloro-1-oxo-1H-isochromen-7-yl]benzamide
-
pH 8.8, 25°C
0.000002 - 0.000028
phenethylsulfonamidino-D-seryl-L-alanyl(P2)-L-argininal
0.063
thieno[2,3-b]pyridine-2-carboxamidine
-
pH 7.4, 37°C
0.0022
upain-1
-
pH 7.4, 37°C, mature uPA
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000098
2-([6-[(3'-carbamimidoylbiphenyl-3-yl)oxy]-3,5-difluoro-4-methylpyridin-2-yl]oxy)-4-(dimethylamino)benzoic acid
Homo sapiens
pH 8.8, 37°C
0.00024
2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-methylbenzoic acid
Homo sapiens
pH 8.8, 37°C
0.000039
2-[(6-[[5-amino-3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-methylbenzoic acid
Homo sapiens
pH 8.8, 37°C
0.000072
4-(2-aminoethoxy)-N-[3-chloro-2-ethoxy-5-(piperidin-1-yl)phenyl]-3,5-dimethylbenzamide
Homo sapiens
pH 8.8, 37°C
0.0002
4-[(E)-(5-oxo-2-phenyl-1,3-oxazol-4(5H)-ylidene)methyl]benzenecarboximidamide
Homo sapiens
pH 8.8, 37°C
0.0026
6-carbamimidoyl-N-(3,5-dimethoxyphenyl)-2-naphthamide
Homo sapiens
pH 8.8, 37°C
0.013
6-carbamimidoyl-N-phenyl-2-naphthamide
Homo sapiens
pH 8.8, 37°C
0.02
6-cyano-N-(3'-methoxybiphenyl-4-yl)-2-naphthamide
Homo sapiens
pH 8.8, 37°C
0.0021
6-methoxy-N-(3'-(trifluoromethyl)biphenyl-4-yl)-2-naphthamide
Homo sapiens
pH 8.8, 37°C
0.0041
6-methoxy-N-(3'-(trifluoromethyl)biphenyl-4-yl)naphthalene-2-sulfonamide
Homo sapiens
pH 8.8, 37°C
0.004
6-methoxy-N-(3'-methoxybiphenyl-4-yl)-2-naphthamide
Homo sapiens
pH 8.8, 37°C
0.019
6-methoxy-N-(3'-methoxybiphenyl-4-yl)naphthalene-2-sulfonamide
Homo sapiens
pH 8.8, 37°C
0.0026
6-methoxy-N-(3'-nitrobiphenyl-4-yl)-2-naphthamide
Homo sapiens
pH 8.8, 37°C
0.0069
6-methoxy-N-(3'-nitrobiphenyl-4-yl)naphthalene-2-sulfonamide
Homo sapiens
pH 8.8, 37°C
0.012
6-methoxy-N-(4'-methoxybiphenyl-4-yl)-2-naphthamide
Homo sapiens
pH 8.8, 37°C
0.023
6-methoxy-N-(4'-methoxybiphenyl-4-yl)naphthalene-2-sulfonamide
Homo sapiens
pH 8.8, 37°C
0.0123
amiloride
Homo sapiens
pH 7.4, 37°C
0.0000034
bis[(phenylamino)acetyl] [2-(4-carbamimidamidophenyl)-1-[(methoxycarbonyl)amino]ethyl]phosphonate
Homo sapiens
pH 8.8, 37°C
0.0000031
diphenyl [2-(4-carbamimidamidophenyl)-1-[(methoxycarbonyl)amino]ethyl]phosphonate
Homo sapiens
pH 8.8, 37°C
0.016
methyl 4'-(2-naphthamido)biphenyl-3-carboxylate
Homo sapiens
pH 8.8, 37°C
0.031
methyl 4'-(6-amino-2-naphthamido)biphenyl-3-carboxylate
Homo sapiens
pH 8.8, 37°C
0.011
methyl 4'-(6-bromo-2-naphthamido)biphenyl-3-carboxylate
Homo sapiens
pH 8.8, 37°C
0.0036
methyl 4'-(6-carbamoyl-2-naphthamido)biphenyl-3-carboxylate
Homo sapiens
pH 8.8, 37°C
0.007
methyl 4'-(6-chloro-2-naphthamido)biphenyl-3-carboxylate
Homo sapiens
pH 8.8, 37°C
0.009
methyl 4'-(6-cyano-2-naphthamido)biphenyl-3-carboxylate
Homo sapiens
pH 8.8, 37°C
0.004
methyl 4'-(6-methoxy-2-naphthamido)biphenyl-3-carboxylate
Homo sapiens
pH 8.8, 37°C
0.0028
methyl 4'-(6-methoxynaphthalene-2-sulfonamido)biphenyl-3-carboxylate
Homo sapiens
pH 8.8, 37°C
0.016
methyl 4'-(6-methoxynaphthalene-2-sulfonamido)biphenyl-4-carboxylate
Homo sapiens
pH 8.8, 37°C
0.016
methyl 4'-(naphthalene-2-sulfonamido)biphenyl-3-carboxylate
Homo sapiens
pH 8.8, 37°C
0.0098
methyl 4'-(naphthalene-2-sulfonamido)biphenyl-4-carboxylate
Homo sapiens
pH 8.8, 37°C
0.014
methyl 6-(3'-(methoxycarbonyl)biphenyl-4-ylcarbamoyl)-2-naphthoate
Homo sapiens
pH 8.8, 37°C
0.008
N-(2,4'-dimethoxybiphenyl-4-yl)-6-methoxynaphthalene-2-sulfonamide
Homo sapiens
pH 8.8, 37°C
0.031
N-(3',4'-dimethoxybiphenyl-4-yl)-6-methoxy-2-naphthamide
Homo sapiens
pH 8.8, 37°C
0.008
N-(3',4'-dimethoxybiphenyl-4-yl)-6-methoxynaphthalene-2-sulfonamide
Homo sapiens
pH 8.8, 37°C
0.062
N-(3'-aminobiphenyl-4-yl)-6-methoxynaphthalene-2-sulfonamide
Homo sapiens
pH 8.8, 37°C
0.0098
N-(3'-methoxybiphenyl-4-yl)-2-naphthamide
Homo sapiens
pH 8.8, 37°C
0.031
N-(3'-methoxybiphenyl-4-yl)naphthalene-2-sulfonamide
Homo sapiens
pH 8.8, 37°C
0.0012
N-(4-(aminomethyl)phenyl)-6-carbamimidoyl-2-naphthamide trifluoro acetate
Homo sapiens
pH 8.8, 37°C
0.031
N-(biphenyl-4-yl)-6-methoxynaphthalene-2-sulfonamide
Homo sapiens
pH 8.8, 37°C
0.0064
N2-(2,4'-dimethoxybiphenyl-4-yl)naphthalene-2,6-dicarboxamide
Homo sapiens
pH 8.8, 37°C
0.0024
N2-(3'-(trifluoromethyl)biphenyl-4-yl)naphthalene-2,6-dicarboxamide
Homo sapiens
pH 8.8, 37°C
0.0029
N2-(3'-methoxybiphenyl-4-yl)naphthalene-2,6-dicarboxamide
Homo sapiens
pH 8.8, 37°C
0.03
N2-(3,5-dimethoxyphenyl)naphthalene-2,6-dicarboxamide
Homo sapiens
pH 8.8, 37°C
0.0081
N2-(3-chlorobiphenyl-4-yl)naphthalene-2,6-dicarboxamide
Homo sapiens
pH 8.8, 37°C
0.045
N2-(4-(aminomethyl)phenyl)naphthalene-2,6-dicarboxamide trifluoroacetate
Homo sapiens
pH 8.8, 37°C
0.015
N2-phenylnaphthalene-2,6-dicarboxamide
Homo sapiens
pH 8.8, 37°C
0.0113
NCI004367
Homo sapiens
pH 7.4, 37°C
0.0063
NCI0135766
Homo sapiens
pH 7.4, 37°C
0.0284
NCI0144205
Homo sapiens
pH 7.4, 37°C
0.009
NCI0666712
Homo sapiens
pH 7.4, 37°C
0.013
1-[3'-([3,5-difluoro-6-[5-methyl-2-(1H-tetrazol-1-yl)phenoxy]pyridin-2-yl]oxy)biphenyl-3-yl]methanamine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000098
2-([6-[(3'-carbamimidoylbiphenyl-3-yl)oxy]-3,5-difluoro-4-methylpyridin-2-yl]oxy)-4-(dimethylamino)benzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0027
2-[(6-[[3',5-bis(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-methylbenzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000023
2-[(6-[[3'-(aminomethyl)-5-hydroxybiphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-methylbenzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00054
2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-3-methylbenzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00068
2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-(propan-2-yl)benzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00022
2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-methoxybenzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00024
2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-methylbenzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0013
2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-nitrobenzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0035
2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-5-methylbenzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.026
2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-6-methylbenzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00084
2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]benzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000025
2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-4-[3-(dimethylamino)pyrrolidin-1-yl]-3,5-difluoropyridin-2-yl)oxy]-4-(dimethylamino)benzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0001
2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-4-[[2-(dimethylamino)ethyl](methyl)amino]-3,5-difluoropyridin-2-yl)oxy]-4-(dimethylamino)benzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.03
2-[(6-[[4'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-(dimethylamino)benzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000089
2-[(6-[[4-amino-3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-methylbenzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000039
2-[(6-[[5-amino-3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-methylbenzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000015
2-[(6-[[5-amino-3'-(aminomethyl)biphenyl-3-yl]oxy]-4-[3-(dimethylamino)pyrrolidin-1-yl]-3,5-difluoropyridin-2-yl)oxy]-4-methylbenzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.03
2-[(6-[[6-amino-3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-methylbenzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.03
2-[[3,5-difluoro-6-([3'-[(methylamino)methyl]biphenyl-3-yl]oxy)pyridin-2-yl]oxy]-4-(dimethylamino)benzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00013
2-[[6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoro-4-(methylamino)pyridin-2-yl]oxy]-4-(dimethylamino)benzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0009
2-[[6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoro-4-(morpholin-4-yl)pyridin-2-yl]oxy]-4-(dimethylamino)benzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000065
2-[[6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoro-4-(piperazin-1-yl)pyridin-2-yl]oxy]-4-(dimethylamino)benzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00053
2-[[6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-4-(dimethylamino)-3,5-difluoropyridin-2-yl]oxy]-4-(dimethylamino)benzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
3-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]benzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.03
3-[2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]phenyl]propanoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.03
4-(dimethylamino)-2-[[6-([3'-[(dimethylamino)methyl]biphenyl-3-yl]oxy)-3,5-difluoropyridin-2-yl]oxy]benzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.03
4-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]benzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000089
antibody IgG(DS2)
Homo sapiens
-
pH 7.4, 22°C
-
0.0000067
antibody scFv(DS2)
Homo sapiens
-
pH 7.4, 22°C
-
0.0081
[2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]phenyl]acetic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
enzyme activity in different tissues with and without inhibitor treatment, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.8
assay at
7.5
-
assay at
7.5 - 9.5
-
phosphorylated uPA
8
-
assay at
8.3
-
assay at
8.8
-
assay at
8.8 - 9.5
-
nonphosphorylated uPA
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
enzyme expression in atherosclerotic lesion macrophages
Manually annotated by BRENDA team
myeloid leukemia cell line
Manually annotated by BRENDA team
-
silencing of transmembrane protein Notch1 by siRNA results in significant reduction in the expression of uPA and matrix metalloproteinase-9 gene transcripts. Knock-down of Notch also reduces the mRNA expression and protein levels of uPA and matrix metalloproteinase-9
Manually annotated by BRENDA team
-
melanoma cell
Manually annotated by BRENDA team
-
uPA shows extensive colocalization with alpha-granule proteins in both cultured Quebec platelet disease megakaryocytes and platelets, and with plasminogen in Quebec platelet disease platelets
Manually annotated by BRENDA team
-
plasma cell
Manually annotated by BRENDA team
-
very low enzyme content
Manually annotated by BRENDA team
-
pulmonary arterial
Manually annotated by BRENDA team
-
uPA, seprase and pipeptidylaminopeptidase IV immunoreactivity is found in dysplastic and cancer cells as well as in stromal cells adjacent to dysplasia and cancer sites, but not in normal epithelium. There is a significant association between uPA expression and sex, tumor size and histological classification in carcinomas. Squamous cell carcinoma lines display higher levels of uPA, seprase and dipeptidylaminopeptidase IV than normal esophageal epithelial cell lines
Manually annotated by BRENDA team
-
uPAR is overexpressed in outer root sheath and interfollicle epidermis, and expressed in the outermost epithelial cells of the hair follicle and the basal keratinocytes of epidermis, the expression decreases with the development of the hair follicle
Manually annotated by BRENDA team
-
human recombinant uPA induces stem cell migration. Retrovirus-mediated overexpression of uPA and uPA receptor in neuroblastoma NB-1691 cells induced robust migration of stem cells toward NB-1691 cell-conditioned media, compared with media derived from wild-type NB-1691 cells. Depletion of uPA from PC-3 prostate cancer cell-conditioned medium blocks stem cell migration
Manually annotated by BRENDA team
-
hearts with end-stage failure and fibrosis have macrophage accumulation and elevated plasminogen activator activity, mechanisms that link macrophage accumulation and plasminogen activator activity with cardiac fibrosis, overview
Manually annotated by BRENDA team
-
high enzyme level
Manually annotated by BRENDA team
-
primary
Manually annotated by BRENDA team
-
a hepatic stellate cell line
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
silencing of transmembrane protein Notch1 by siRNA results in significant reduction in the expression of uPA and matrix metalloproteinase-9 gene transcripts. Knock-down of Notch also reduces the mRNA expression and protein levels of uPA and matrix metalloproteinase-9
Manually annotated by BRENDA team
-
human lung cancer cell line H1415, activation of uPA and uPA receptor in malignant solid tumors augments neural and mesenchymal stem cell tropism. Expression levels of uPA receptor on human solid tumor cell linescorrelates with levels of uPA and soluble uPA receptor in tumor cell-conditioned media
Manually annotated by BRENDA team
-
lung fibroblast cell line
Manually annotated by BRENDA team
-
subline of MDA-MB-231, stably transfected with the bacterial lacZ gene
Manually annotated by BRENDA team
-
CD34+ progenitor cells express normal amounts of uPA, while their differentiation into megakaryocytes results in abnormally increased expression of the uPA gene but not the flanking genes for vinculin or calcium/calmodulin-dependent protein kinase IIgamma on chromosome 10. uPA shows extensive colocalization with alpha-granule proteins in both cultured Quebec platelet disease megakaryocytes and platelets, and with plasminogen in Quebec platelet disease platelets
Manually annotated by BRENDA team
-
uPA localizes strongly to natural killer cells of the placental bed, especially at 8-10 weeks of gestation. uPA activity is similar in uterine natural killer cell culture supernatant compared with total unseparated decidual cells. uPA receptor in uterine natural killer cell lysates is significantly stronger than in total decidual cell lysates. Inhibitors PAI-1 and PAI-2 are not detected in uterine natural killer cell culture supernatants
Manually annotated by BRENDA team
-
retrovirus-mediated overexpression of uPA and uPA receptor in neuroblastoma NB-1691 cells induced robust migration of stem cells toward NB-1691 cell-conditioned media, compared with media derived from wild-type NB-1691 cells
Manually annotated by BRENDA team
-
activation of uPA and uPA receptor in malignant solid tumors augments neural and mesenchymal stem cell tropism. Expression levels of uPA receptor on human solid tumor cell lines correlates with levels of uPA and soluble uPA receptor in tumor cell-conditioned media
Manually annotated by BRENDA team
-
activation of uPA and uPA receptor in malignant solid tumors augments neural and mesenchymal stem cell tropism. Expression levels of uPA receptor on human solid tumor cell lines correlates with levels of uPA and soluble uPA receptor in tumor cell-conditioned media
Manually annotated by BRENDA team
-
granulocytes, monocytes
Manually annotated by BRENDA team
-
uPA localizes strongly to natural killer cells of the placental bed, especially at 8-10 weeks of gestation. uPA activity is similar in uterine natural killer cell culture supernatant compared with total unseparated decidual cells. uPA receptor in uterine natural killer cell lysates is significantly stronger than in total decidual cell lysates. Inhibitors PAI-1 and PAI-2 are not detected in uterine natural killer cell culture supernatants
Manually annotated by BRENDA team
-
overexpression of uPA mRNA in various stages of surgically excised pterygia specimens and cultured pterygium fibroblasts, expression is increased significantly following the progression of the pterygium, quantitative real-time PCR analysis, overview
Manually annotated by BRENDA team
-
activation of uPA and uPA receptor in malignant solid tumors augments neural and mesenchymal stem cell tropism. Expression levels of uPA receptor on human solid tumor cell lines correlates with levels of uPA and soluble uPA receptor in tumor cell-conditioned media
Manually annotated by BRENDA team
-
basal keratinocytes of epidermis
Manually annotated by BRENDA team
-
in sputum derived from patients with house dust mite allergic asthma, the medium concentration of uPA is significantly greater than in healthy control patients. The sputum concentration of uPA correlates with sputum total cell count and with logarithmically transformed exhaled nitric oxide concentration, but not with FEV1 or bronchial reactivity to histamine. Tge effect of uPA seems to be independent of its fibrinolytic activity
Manually annotated by BRENDA team
-
fibroblast cell
Manually annotated by BRENDA team
-
activation of uPA and uPA receptor in malignant solid tumors augments neural and mesenchymal stem cell tropism. Expression levels of uPA receptor on human solid tumor cell lines correlates with levels of uPA and soluble uPA receptor in tumor cell-conditioned media
Manually annotated by BRENDA team
-
lung fibroblast cell line
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
UROK_HUMAN
431
0
48523
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
53000
-
x * 53000, pro-uPA, SDS-PAGE
54000
55000
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
proteolytic modification
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with inhibitor N-[(4-chlorobenzyl)sulfonyl]-D-seryl-N-(4-carbamimidoylbenzyl)-L-alaninamide, N-(benzylsulfonyl)-D-seryl-N-(4-carbamimidoylbenzyl)-L-serinamide and N-(benzylsulfonyl)-D-seryl-N-(4-carbamimidoylbenzyl)glycinamide
PAI-1/uPA mutant S195A in a Michaelis complex, hanging drop method, 20°C, mixing of equal volumes of protein solution, containing 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, and 150 mM NaCl, and precipitant solution, containing 1.4 M ammonium sulfate and 0.1 M Tris-HCl, pH 7.4, 4 months, the cryoprotectant solution contains 30% glycerol, 1.6 M ammonium sulfate, and 0.1 M Tris-HCl, pH 7.4, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement
beta-c-uPA in complex with inhibitor UPA-I1, space group P2(1)2(1)2(1), cell constants a = 53.2 A, b = 54.7 A, c = 82.4 A, beta-c-uPA in complex with inhibitor UPA-I3, space group P2(1)2(1)2(1), cell constants a = 52.9 A, b = 54.7 A, c = 81.4 A, beta-c-uPA in complex with inhibitor UPA-I2, space group P2(1)2(1)2(1), cell constants a = 53.0 A, b = 54.4 A, c = 82.2 A, beta-c-uPA in complex with inhibitor UPA-I5, space group P2(1)2(1)2(1), cell constants a = 53.0 A, b = 54.9 A, c = 82.3 A, beta-c-uPA in complex with inhibitor UPA-I6, space group P2(1)2(1)2(1), cell constants a = 53.5 A, b = 54.8 A, c = 82.4 A, complex by soaking, Ybeta-c-uPA in complex with inhibitor UPA-I6, space group P4(3)2(1)2, cell constants a = 76.7 A, b = 76.7 A, c = 127.5 A, complex by Co-crystallization, beta-c-uPA in complex with inhibitor UPA-I4, space group P4(1)2(1)2, cell constants a = 55.0 A, b = 55.0 A, c = 151.6 A, complex by Co-crystallization
-
crystal structure of the catalytic domain of the recombinant nonglycosylated human uPA, complexed with the inhibitor Glu-Gly-Arg chloromethyl ketone at 2.5 A
-
crystallized by vapor diffusion in hanging drops in complex with 4-iodobenzo[b]thiophene-2-carboxamidine and benzamidine, space group C2, ProteinDataBank accession code 1C5Z for uPA-benzamidine, 1C5Y for uPA-thieno[2,3-b]pyridine-2-carboxamidine
-
N-terminal fragment, in complex with urokinase receptor and an antibody against the receptor
-
purified amino-terminal fragment of urokinase-type plasminogen activator, free and complexed with uPA receptor, lacking the cell-surface anchoring sequence, hanging-drop vapor-diffusion method, room temperature, 0.003 ml of 20 or 8 mg/ml protein, respectively, in 20 mM Tris-HCl, pH 8.0, 150 mM NaCl, is mixed with an equal volume of reservoir solution containing 100 mM Ches, pH 10.5, 1.2 M sodium dihydrogen phosphate, 0.8 M potassium hydrogen phosphate, 200 mM lithium sulfate for the free enzyme or 100 mM Bis-Tris, pH 5.5, 22.5% w/v PEG 3350, 200 mM ammonium sulfate for the enzyme fragment-receptor complex, 1 week, cryoprotection by 15% v/v glycerol, X-ray diffraction structure determination and anaylsis at 1.9-3.3 A resolution, molecular modeling
-
purified recombinant enzyme mutant H99Y in complex with mupain-1 inhibitor variants, sitting drop vapour diffusion method, equilibrating of protein against a reservoir solution containing 2.0 M ammonium sulfate, 50 mM sodium citrate, pH 4.6, and 5% PEG 400, room temperature, about 3 days, soaking of crystals in 40% PEG 4000, 100 mM Tris-HCl, pH 7.4 containing 1 mM mupain ligand variant, X-ray diffraction structure determination and analysis at 1.6 A resolution
-
recombinant amino-terminal fragment S1-E143 expressed in Pichia pastoris
-
solution structure of the kringle domain
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L97bG/H99Y/S195A/R217E
site-directed mutagenesis, the mutant shows altered interaction with human plasminogen activator inhibitor-1 compare to wild-type
L97bG/S195A
site-directed mutagenesis, the mutant shows altered interaction with human plasminogen activator inhibitor-1 compare to wild-type
L97bG/S195A/R217E
site-directed mutagenesis, the mutant shows altered interaction with human plasminogen activator inhibitor-1 compare to wild-type
S195A
S195A/R217E
site-directed mutagenesis, the mutant shows altered interaction with human plasminogen activator inhibitor-1 compare to wild-type
C122S
-
mutant of the serine proteinase domain
E301A
-
site-directed mutagenesis
E301D
-
site-directed mutagenesis
E301H
-
site-directed mutagenesis
H99Y/Q192K
-
site-directed mutagenesis, the mutations exchanges the human residues for the murine equivalents, rendering the mutant enzyme susceptible for inhibition by the murine peptide sequence mupain-1, overview
K300A
-
site-directed mutagenesis
K300H
-
site-directed mutagenesis
K300W
-
site-directed mutagenesis
K313A
-
site-directed mutagenesis
P309A
-
60% increase in KM-value for L-pyroGlu-Gly-L-Arg-4-nitroanilide
P309D
-
200% increase in KM-value for L-pyroGlu-Gly-L-Arg-4-nitroanilide, about 15% decrease in activation by Lys-plasmin
P309F
-
500% increase in KM-value for L-pyroGlu-Gly-L-Arg-4-nitroanilide, about 15% decrease in activation by Lys-plasmin
P309G
-
100% increase in KM-value for L-pyroGlu-Gly-L-Arg-4-nitroanilide
P309H
-
400% increase in KM-value for L-pyroGlu-Gly-L-Arg-4-nitroanilide, about 15% decrease in activation by Lys-plasmin
P309L
-
250% increase in KM-value for L-pyroGlu-Gly-L-Arg-4-nitroanilide
P309N
-
150% increase in KM-value for L-pyroGlu-Gly-L-Arg-4-nitroanilide
P309R
-
350% increase in KM-value for L-pyroGlu-Gly-L-Arg-4-nitroanilide, about 15% decrease in activation by Lys-plasmin
P309S
-
50% increase in KM-value for L-pyroGlu-Gly-L-Arg-4-nitroanilide
P309T
-
60% increase in KM-value for L-pyroGlu-Gly-L-Arg-4-nitroanilide, about 15% decrease in activation by Lys-plasmin
P309V
-
80% increase in KM-value for L-pyroGlu-Gly-L-Arg-4-nitroanilide
P309W
-
700% increase in KM-value for L-pyroGlu-Gly-L-Arg-4-nitroanilide
R178A/R179A/R181A
-
site-directed mutagenesis, the mutant shows reduced receptor binding
R340A
-
site-directed mutagenesis, the binding of the mutant enzyme to maspin is not affected
S195A
-
site-directed mutagenesis, the active site mutant is not able to activate the epithelial sodium channel in contrast to the wild-type enzyme
S195A/C122S/N145D
-
inactive variant
S303E
-
site-directed mutagenesis
S356A
-
a catalytically inactive uPA mutant
V41K/H99Y
-
site-directed mutagenesis, the mutations exchanges the human residues for the murine equivalents, rendering the mutant enzyme susceptible for inhibition by the murine peptide sequence mupain-1, overview
V41K/H99Y/Q192K
-
site-directed mutagenesis, the mutations exchanges the human residues for the murine equivalents, rendering the mutant enzyme susceptible for inhibition by the murine peptide sequence mupain-1, overview
Y306G
-
site-directed mutagenesis
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant mutant S195A from Pichia pastoris strain X-33 by nickel affinity chromatography and gel filtration
high-molecular weight uPA expressed in SP2/0 cell culture
-
recombinant enzyme
-
recombinant isolated kringle domain UK1 from Pichia pastoris
-
recombinant mutant enzyme by dialysis and ultrafiltration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of mutant S195A in Pichia pastoris strain X-33
amino-terminal fragment of human uPA cloned and expressed in Saccharomyces cerevisiae
-
cDNA cloning
-
cloning of low molecular weight uPA, expression in Pichia pastoris
-
DNA and amino acid sequence analysis
-
expression in Escherichia coli
-
expression of mutant enzymes in HEK-293T cells
-
expression of the enzyme's kringle domain UK1 in Pichia pastoris
-
expression of wild-type and mutant enzymes in HEK-293T cells
-
functional overexpression of the enzyme in hepatic stellate cells, using an adenoviral vector system
-
mutant C122S expressed in Escherichia coli inclusion bodies, B-chain uPA expressed in S. pastoris
-
recombinant expression of mutant enzyme
-
semiquantitative reverse transcription PCR expression analysis of uPA and uPAR, overview
-
uPA quantitative real-time RT-PCR expression analysis in oral squamous cell carcinoma, overview
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
interleukin-17 induces enzyme production in peripheral blood mesenchymal stem cells, without affecting matrix metalloproteinase expression
downregulation of uPA and uPAR by early growth response 1, EGR1, forced expression of EGR1 decreases the expression of uPA and urokinase receptor uPAR proteins. uPA activity is decreased 0.49fold by EGR1 in Saos-2 cells
-
efficacy of grape seed extract in downregulating uPA expression and cell migration using highly metastatic androgen-independent PC-3 prostate cancer cells as a model. Grape seed extract inhibits DNA-binding activity of the transcription factor nuclear factor kappa B, which in turn decreases NFkB-dependent uPA transcription. Grape seed extract also inhibits NFkB-dependent urokinase plasminogen activator promoter activity
-
endogenous miR-193b expression inhibits uPA expression, anti-miR-193b increases uPA expression and increases cell invasion of breast cancer cells. During breast cancer cell metastasis, miR-193b expression is downregulated leading to increased uPA expression
-
expression of uPA mRNA and enzyme production is increased by the addition of prostaglandin E2, PGE2, in cell lines of lung fibroblasts, although the cell surface uPA level is comparable to that of PGE2 untreated cells, overview
-
inhibition of sphingosine kinase blocks basal expression of uPA and uPAR, as well as glioma cell invasion, however overexpression of sphingosine kinase does not augment sphingosine-1-phosphate receptor-mediated enhancement of uPA activity or invasion
-
inhibitors of p-ERK and p-p38 downregulate uPA in CFPAN-1 and PANC-1 cells, but these inhibitors affect uPAR considerably more than uPA
-
lipopolysaccharide induces u-PA expression. TLR-4 and NF-kappaB inhibition ameliorates LPS-enhanced u-PA and u-PAR expression, tumour cell vitronectin adhesion and ECM invasion
-
macrophage inhibitory cytokine-1, MIC-1, is a critical inducer of apoptosis-related gene products such as activated urokinetype plasminogen activator, PLAU, and PLAU receptor, uPAR. Ribotoxic stress agent anisomycin induces MIC-1 gene expression. Gene expression of apoptosis-mediator MIC-1 is enhanced by activating transcription factor 3, ATF-3, via the p38 MAP kinase signaling pathway, and both promoter activity and mRNA stability of MIC-1 gene are up-regulated by ribotoxic anisomycin via the p38 MAP kinase signaling pathway
-
plumbagin induces the enzyme expression in Hep-G2 cells, liver carcinoma cells, also inhibiting the invasion and migration of the cancer cells, overview
-
sphingosine-1-phosphate, S1P, induces expression of uPA and of its receptor uPAr in gliobalstoma multiforme cells. S1P1 receptor overexpression leads to the most dramatic induction of the uPA system and of spheroid invasion, even in the absence of added S1P, while expression of receptors S1P2 and S1P3 does not affect uPA expression, overview
-
TGF-beta1 induces expression of urokinase type plasminogen activator, but the stimulation by TFG-beta1 is inhibited by Spred2
-
uPA and its endogenous inhibitor PAI-1 are downregulated by grape seed, Vitis ssp., proanthocyanidin extract, both at the RNA and protein levels, due to the extract's antioxidant activity
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
analysis
diagnostics
drug development
medicine
pharmacology
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Loskutoff, D.J.; Schleef, R.R.
Plasminogen activators and their inhibitors
Methods Enzymol.
163
293-302
1988
Homo sapiens
Manually annotated by BRENDA team
Saksela, O.; Rifkin, D.B.
Cell-associated plasminogen activation: regulation and physiological functions
Annu. Rev. Cell Biol.
4
93-126
1988
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Saksela, O.
Plasminogen activation and regulation of pericellular proteolysis
Biochim. Biophys. Acta
823
35-65
1985
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Lijnen, H.R.; van Hoef, B.; Nelles, L.; Collen, D.
Plasminogen activation with single-chain urokinase-type plasminogen activator (scu-PA). Studies with active site mutagenized plasminogen (Ser740----Ala) and plasmin-resistant scu-PA (Lys158----Glu)
J. Biol. Chem.
265
5232-5236
1990
Homo sapiens
Manually annotated by BRENDA team
Takahashi, K.; Kwaan, H.C.; Koh, E.; Tanabe, M.
Enzymatic properties of the phosphorylated urokinase-type plasminogen activator isolated from a human carcinomatous cell line
Biochem. Biophys. Res. Commun.
182
1473-1481
1992
Homo sapiens
Manually annotated by BRENDA team
Yoshimoto, M.; Ushiyama, Y.; Sakai, M.; Tamaki, S.; Hara, H.; Takahashi, K.; Sawasaki, Y.; Hanada, K.
Characterization of single chain urokinase-type plasminogen activator with a novel amino-acid substitution in the kringle structure
Biochim. Biophys. Acta
1293
83-89
1996
Homo sapiens
Manually annotated by BRENDA team
Magdolen, V.; Rettenberger, P.; Koppitz, M.; Goretzki, L.; Kessler, H.; Weidle, U.H.; Knig, B.; Graeff, H.; Schmitt, M.; Wilhelm, O.
Systematic mutational analysis of the receptor-binding region of the human urokinase-type plasminogen activator
Eur. J. Biochem.
237
743-751
1996
Homo sapiens
Manually annotated by BRENDA team
Schmitt, M.; Jnicke, F.; Moniwa, N.; Chucholowski, N.; Pache, L.; Graeff, H.
Tumor-associated urokinase-type plasminogen activator: biological and clinical significance
Biol. Chem. Hoppe-Seyler
373
611-622
1992
Homo sapiens
Manually annotated by BRENDA team
Wang, C.I.; Yang, Q.; Craik, C.S.
Isolation of a high affinity inhibitor of urokinase-type plasminogen activator by phage display of ecotin
J. Biol. Chem.
270
12250-12256
1995
Homo sapiens, Mammalia
Manually annotated by BRENDA team
Lijnen, H.R.; De Cock, F.; Collen, D.
Characterization of the binding of urokinase-type plasminogen activator (u-PA) to plasminogen, to plasminogen-activator inhibitor-1 and to the u-PA receptor
Eur. J. Biochem.
224
567-574
1994
Homo sapiens, Mammalia
Manually annotated by BRENDA team
Li, Y.; Bokman, A.M.; Llinas, M.; Smith, R.A.G.; Dobson, C.M.
Solution structure of the kringle domain from urokinase-type plasminogen activator
J. Mol. Biol.
235
1548-1559
1994
Homo sapiens
Manually annotated by BRENDA team
Keski-Oja, J.; Lohi, J.; Tuuttila, A.; Tryggvason, K.; Vartio, T.
Proteolytic processing of the 72,000-Da type IV collagenase by urokinase plasminogen activator
Exp. Cell Res.
202
471-476
1992
Homo sapiens
Manually annotated by BRENDA team
Li, X.K.; Lijnen, H.R.; Nelles, L.; Hu, M.H.; Collen, D.
Biochemical properties of recombinant mutants of nonglycosylated single chain urokinase-type plasminogen activator
Biochim. Biophys. Acta
1159
37-43
1992
Homo sapiens, Mammalia
Manually annotated by BRENDA team
Hoyer-Hansen, G.; Ronne, E.; Solberg, H.; Behrendt, N.; Ploug, M.; Lund, L.R.; Ellis, V.; Dano, K.
Urokinase plasminogen activator cleaves its cell surface receptor releasing the ligand-binding domain
J. Biol. Chem.
267
18224-18229
1992
Homo sapiens, Mammalia
Manually annotated by BRENDA team
Franco, P.; Mastronicola, M.R.; De Cesare, D.; Nolli, M.L.; Wun, T.C.; Verde, P.; Blasi, F.; Stoppelli, M.P.
Separation and characterization of nonphosphorylated and serine-phosphorylated urokinase. Catalytic properties and sensitivity to plasminogen activator inhibitor type 1
J. Biol. Chem.
267
19369-19372
1992
Homo sapiens
Manually annotated by BRENDA team
Novokhatny, V.; Medved, L.; Mazar, A.; Marcotte, P.; Henkin, J.; Ingham, K.
Domain structure and interactions of recombinant urokinase-type plasminogen activator
J. Biol. Chem.
267
3878-3885
1992
Homo sapiens, Mammalia
Manually annotated by BRENDA team
Hamelin, J.; Sarmientos, P.; Orsini, G.; Galibert, F.
Implication of cysteine residues in the activity of single-chain urokinase-plasminogen activator
Biochem. Biophys. Res. Commun.
194
978-985
1993
Homo sapiens
Manually annotated by BRENDA team
Spraggon, G.; Phillips, C.; Nowak, U.K.; Ponting, C.P.; Saunders, D.; Dobson, C.M.; Stuart, D.I.; Jones, E.Y.
The crystal structure of the catalytic domain of human urokinase-type plasminogen activator
Structure
3
681-691
1995
Homo sapiens
Manually annotated by BRENDA team
Bergstrom, R.C.; Coombs, G.S.; Ye, S.; Madison, E.L.; Goldsmith, E.J.; Corey, D.R.
Binding of nonphysiological protein and peptide substrates to proteases: differences between urokinase-type plasminogen activator and trypsin and contributions to the evolution of regulated proteolysis
Biochemistry
42
5395-5402
2003
Homo sapiens
Manually annotated by BRENDA team
Katz, B.A.; Mackman, R.; Luong, C.; Radika, K.; Martelli, A.; Sprengeler, P.A.; Wang, J.; Chan, H.; Wong, L.
Structural basis for selectivity of a small molecule, S1-binding, submicromolar inhibitor of urokinase-type plasminogen activator
Chem. Biol.
7
299-312
2000
Homo sapiens
Manually annotated by BRENDA team
Sun, Z.; Jiang, Y.; Ma, Z.; Wu, H.; Liu, B.F.; Xue, Y.; Tang, W.; Chen, Y.; Li, C.; Zhu, D.; Gurewich, V.; Liu, J.N.; Zhong, M.; Xu, Y.
Identification of a flexible loop region (297-313) of urokinase-type plasminogen activator, which helps determine its catalytic activity
J. Biol. Chem.
272
23818-23823
1997
Homo sapiens
Manually annotated by BRENDA team
Verner, E.; Katz, B.A.; Spencer, J.R.; Allen, D.; Hataye, J.; Hruzewicz, W.; Hui, H.C.; Kolesnikov, A.; Li, Y.; Luong, C.; Martelli, A.; Radika, K.; Rai, R.; She, M.; Shrader, W.; Sprengeler, P.A.; Trapp, S.; Wang, J.; Young, W.B.; Mackman, R.L.
Development of serine protease inhibitors displaying a multicentered short 2.3 ANG hydrogen bond binding mode: inhibitors of urokinase-type plasminogen activator and factor Xa
J. Med. Chem.
44
2753-2771
2001
Homo sapiens
Manually annotated by BRENDA team
Yang, S.Q.; Craik, C.S.
Engineering bidentate macromolecular inhibitors for trypsin and urokinase-type plasminogen activator
J. Mol. Biol.
279
1001-1011
1998
Homo sapiens
Manually annotated by BRENDA team
Zeslawska, E.; Jacob, U.; Schweinitz, A.; Coombs, G.; Bode, W.; Madison, E.
Crystals of urokinase type plasminogen activator complexes reveal the binding mode of peptidomimetic inhibitors
J. Mol. Biol.
328
109-118
2003
Homo sapiens
Manually annotated by BRENDA team
Law, B.; Hsiao, J.K.; Bugge, T.H.; Weissleder, R.; Tung, C.H.
Optical zymography for specific detection of urokinase plasminogen activator activity in biological samples
Anal. Biochem.
338
151-158
2005
Homo sapiens
Manually annotated by BRENDA team
Barber, C.G.; Dickinson, R.P.; Fish, P.V.
Selective urokinase-type plasminogen activator (uPA) inhibitors. Part 3: 1-Isoquinolinylguanidines
Bioorg. Med. Chem. Lett.
14
3227-3230
2004
Homo sapiens
Manually annotated by BRENDA team
Al-Ejeh, F.; Croucher, D.; Ranson, M.
Kinetic analysis of plasminogen activator inhibitor type-2: urokinase complex formation and subsequent internalization by carcinoma cell lines
Exp. Cell Res.
297
259-271
2004
Homo sapiens
Manually annotated by BRENDA team
Li, H.; Soria, C.; Griscelli, F.; Opolon, P.; Soria, J.; Yeh, P.; Legrand, C.; Vannier, J.P.; Belin, D.; Perricaudet, M.; Lu, H.
Amino-terminal fragment of urokinase inhibits tumor cell invasion in vitro and in vivo: respective contribution of the urokinase plasminogen activator receptor-dependent or -independent pathway
Hum. Gene Ther.
16
1157-1167
2005
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Gandhari, M.; Arens, N.; Majety, M.; Dorn-Beineke, A.; Hildenbrand, R.
Urokinase-type plasminogen activator induces proliferation in breast cancer cells
Int. J. Oncol.
28
1463-1470
2006
Homo sapiens
Manually annotated by BRENDA team
Schweinitz, A.; Steinmetzer, T.; Banke, I.J.; Arlt, M.J.; Sturzebecher, A.; Schuster, O.; Geissler, A.; Giersiefen, H.; Zeslawska, E.; Jacob, U.; Kruger, A.; Sturzebecher, J.
Design of novel and selective inhibitors of urokinase-type plasminogen activator with improved pharmacokinetic properties for use as antimetastatic agents
J. Biol. Chem.
279
33613-33622
2004
Homo sapiens (P00749), Homo sapiens
Manually annotated by BRENDA team
Madsen, M.A.; Deryugina, E.I.; Niessen, S.; Cravatt, B.F.; Quigley, J.P.
Activity-based protein profiling implicates urokinase activation as a key step in human fibrosarcoma intravasation
J. Biol. Chem.
281
15997-16005
2006
Homo sapiens
Manually annotated by BRENDA team
Gonzalez-Cuevas, J.; Bueno-Topete, M.; Armendariz-Borunda, J.
Urokinase plasminogen activator stimulates function of active forms of stromelysin and gelatinases (MMP-2 and MMP-9) in cirrhotic tissue
J. Gastroenterol. Hepatol.
21
1544-1554
2006
Homo sapiens
Manually annotated by BRENDA team
Joossens, J.; Van der Veken, P.; Lambeir, A.M.; Augustyns, K.; Haemers, A.
Development of irreversible diphenyl phosphonate inhibitors for urokinase plasminogen activator
J. Med. Chem.
47
2411-2413
2004
Homo sapiens
Manually annotated by BRENDA team
Zhao, G.; Yuan, C.; Bian, C.; Hou, X.; Shi, X.; Ye, X.; Huang, Z.; Huang, M.
Protein expression and preliminary crystallographic analysis of amino-terminal fragment of urokinase-type plasminogen activator
Protein Expr. Purif.
49
71-77
2006
Homo sapiens
Manually annotated by BRENDA team
Sun, Z.; Liu, J.N.
Mutagenesis at Pro309 of single-chain urokinase-type plasminogen activator alters its catalytic properties
Proteins
61
870-877
2005
Homo sapiens
Manually annotated by BRENDA team
Huai, Q.; Mazar, A.P.; Kuo, A.; Parry, G.C.; Shaw, D.E.; Callahan, J.; Li, Y.; Yuan, C.; Bian, C.; Chen, L.; Furie, B.; Furie, B.C.; Cines, D.B.; Huang, M.
Structure of human urokinase plasminogen activator in complex with its receptor
Science
311
656-659
2006
Homo sapiens
Manually annotated by BRENDA team
Van Leer, C.; Stutz, M.; Haeberli, A.; Geiser, T.
Urokinase plasminogen activator released by alveolar epithelial cells modulates alveolar epithelial repair in vitro
Thromb. Haemost.
94
1257-1264
2005
Homo sapiens
Manually annotated by BRENDA team
Andersen, L.M.; Wind, T.; Hansen, H.D.; Andreasen, P.A.
A cyclic peptidylic inhibitor of murine urokinase-type plasminogen activator: changing species specificity by substitution of a single residue
Biochem. J.
15
447-457
2008
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Sasajima, M.; Moriwaki, S.; Hotta, M.; Kitahara, T.; Takema, Y.
trans-3,4-Dimethyl-3-hydroxyflavanone, a hair growth enhancing active component, decreases active transforming growth factor beta2 (TGF-beta2) through control of urokinase-type plasminogen activator (uPA) on the surface of keratinocytes
Biol. Pharm. Bull.
31
449-453
2008
Homo sapiens
Manually annotated by BRENDA team
Kim, T.D.; Song, K.S.; Li, G.; Choi, H.; Park, H.D.; Lim, K.; Hwang, B.D.; Yoon, W.H.
Activity and expression of urokinase-type plasminogen activator and matrix metalloproteinases in human colorectal cancer
BMC Cancer
6
211
2006
Homo sapiens
Manually annotated by BRENDA team
Heynekamp, J.J.; Hunsaker, L.A.; Vander Jagt, T.A.; Deck, L.M.; Vander Jagt, D.L.
Uncharged isocoumarin-based inhibitors of urokinase-type plasminogen activator
BMC Chem. Biol.
6
1
2006
Homo sapiens
Manually annotated by BRENDA team
Kim, C.K.; Hong, S.H.; Joe, Y.A.; Shim, B.S.; Lee, S.K.; Hong, Y.K.
The recombinant kringle domain of urokinase plasminogen activator inhibits in vivo malignant glioma growth
Cancer Sci.
98
253-258
2007
Homo sapiens
Manually annotated by BRENDA team
Chu, S.C.; Yang, S.F.; Lue, K.H.; Hsieh, Y.S.; Li, T.J.; Lu, K.H.
Naproxen, meloxicam and methylprednisolone inhibit urokinase plasminogen activator and inhibitor and gelatinases expression during the early stage of osteoarthritis
Clin. Chim. Acta
387
90-96
2008
Homo sapiens
Manually annotated by BRENDA team
Skeldal, S.; Larsen, J.V.; Pedersen, K.E.; Petersen, H.H.; Egelund, R.; Christensen, A.; Jensen, J.K.; Gliemann, J.; Andreasen, P.A.
Binding areas of urokinase-type plasminogen activator-plasminogen activator inhibitor-1 complex for endocytosis receptors of the low-density lipoprotein receptor family, determined by site-directed mutagenesis
FEBS J.
273
5143-5159
2006
Homo sapiens
Manually annotated by BRENDA team
Crippa, M.P.
Urokinase-type plasminogen activator
Int. J. Biochem. Cell Biol.
39
690-694
2007
Homo sapiens
Manually annotated by BRENDA team
Stempien-Otero, A.; Plawman, A.; Meznarich, J.; Dyamenahalli, T.; Otsuka, G.; Dichek, D.A.
Mechanisms of cardiac fibrosis induced by urokinase plasminogen activator
J. Biol. Chem.
281
15345-15351
2006
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Al-Ayyoubi, M.; Schwartz, B.S.; Gettins, P.G.
Maspin binds to urokinase-type and tissue-type plasminogen activator through exosite-exosite interactions
J. Biol. Chem.
282
19502-19509
2007
Homo sapiens
Manually annotated by BRENDA team
Barinka, C.; Parry, G.; Callahan, J.; Shaw, D.E.; Kuo, A.; Bdeir, K.; Cines, D.B.; Mazar, A.; Lubkowski, J.
Structural basis of interaction between urokinase-type plasminogen activator and its receptor
J. Mol. Biol.
363
482-495
2006
Homo sapiens
Manually annotated by BRENDA team
Liu, Y.; Wang, C.; Yang, Y.; Hou, X.; Wang, J.
Pro-urokinase up-regulates the expression of urokinase-type plasminogen activator (u-PA) in human pulmonary arterial endothelial cells
Thromb. Res.
121
485-491
2008
Homo sapiens
Manually annotated by BRENDA team
Goscinski, M.A.; Suo, Z.H.; Nesland, J.M.; Chen, W.T.; Zakrzewska, M.; Wang, J.; Zhang, S.; Florenes, V.A.; Giercksky, K.E.
Seprase, dipeptidyl peptidase IV and urokinase-type plasminogen activator expression in dysplasia and invasive squamous cell carcinoma of the esophagus. A study of 229 cases from Anyang Tumor Hospital, Henan Province, China
Oncology
75
49-59
2008
Homo sapiens
Manually annotated by BRENDA team
Kenny, S.; Duval, C.; Sammut, S.J.; Steele, I.; Pritchard, D.M.; Atherton, J.C.; Argent, R.H.; Dimaline, R.; Dockray, G.J.; Varro, A.
Increased expression of the urokinase plasminogen activator system by Helicobacter pylori in gastric epithelial cells
Am. J. Physiol. Gastrointest. Liver Physiol.
295
G431-G441
2008
Homo sapiens
Manually annotated by BRENDA team
Fuhrman, B.; Khateeb, J.; Shiner, M.; Nitzan, O.; Karry, R.; Volkova, N.; Aviram, M.
Urokinase plasminogen activator upregulates paraoxonase 2 expression in macrophages via an NADPH oxidase-dependent mechanism
Arterioscler. Thromb. Vasc. Biol.
28
1361-1367
2008
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Veljkovic, D.K.; Rivard, G.E.; Diamandis, M.; Blavignac, J.; Cramer-Borde, E.M.; Hayward, C.P.
Increased expression of urokinase plasminogen activator in Quebec platelet disorder is linked to megakaryocyte differentiation
Blood
113
1535-1542
2009
Homo sapiens
Manually annotated by BRENDA team
Alfano, M.; Mariani, S.A.; Elia, C.; Pardi, R.; Blasi, F.; Poli, G.
Ligand-engaged urokinase-type plasminogen activator receptor and activation of the CD11b/CD18 integrin inhibit late events of HIV expression in monocytic cells
Blood
113
1699-1709
2009
Homo sapiens
Manually annotated by BRENDA team
Herszenyi, L.; Farinati, F.; Cardin, R.; Istvan, G.; Molnar, L.D.; Hritz, I.; De Paoli, M.; Plebani, M.; Tulassay, Z.
Tumor marker utility and prognostic relevance of cathepsin B, cathepsin L, urokinase-type plasminogen activator, plasminogen activator inhibitor type-1, CEA and CA 19-9 in colorectal cancer
BMC Cancer
8
194
2008
Homo sapiens
Manually annotated by BRENDA team
Miyake, K.; Shimada, M.; Nishioka, M.; Sugimoto, K.; Batmunkh, E.; Uto, Y.; Nagasawa, H.; Hori, H.
Downregulation of matrix metalloprotease-9 and urokinase plasminogen activator by TX-1877 results in decreased tumor growth and metastasis on xenograft model of rectal cancer
Cancer Chemother. Pharmacol.
64
885-892
2009
Homo sapiens
Manually annotated by BRENDA team
Brezillon, N.M.; DaSilva, L.; LHote, D.; Bernex, F.; Piquet, J.; Binart, N.; Morosan, S.; Kremsdorf, D.
Rescue of fertility in homozygous mice for the urokinase plasminogen activator transgene by the transplantation of mouse hepatocytes
Cell Transplant.
17
803-812
2008
Homo sapiens
Manually annotated by BRENDA team
Bin Hafeez, B.; Adhami, V.M.; Asim, M.; Siddiqui, I.A.; Bhat, K.M.; Zhong, W.; Saleem, M.; Din, M.; Setaluri, V.; Mukhtar, H.
Targeted knockdown of Notch1 inhibits invasion of human prostate cancer cells concomitant with inhibition of matrix metalloproteinase-9 and urokinase plasminogen activator
Clin. Cancer Res.
15
452-459
2009
Homo sapiens
Manually annotated by BRENDA team
Fevang, B.; Eugen-Olsen, J.; Yndestad, A.; Brosstad, F.; Beiske, K.; Aukrust, P.; Froland, S.S.
Enhanced levels of urokinase plasminogen activator and its soluble receptor in common variable immunodeficiency
Clin. Immunol.
131
438-446
2009
Homo sapiens
Manually annotated by BRENDA team
Jin, T.; Bokarewa, M.; Zhu, Y.; Tarkowski, A.
Staphylokinase reduces plasmin formation by endogenous plasminogen activators
Eur. J. Haematol.
81
8-17
2008
Homo sapiens
Manually annotated by BRENDA team
Lee, K.H.; Kim, J.R.
Reactive oxygen species regulate the generation of urokinase plasminogen activator in human hepatoma cells via MAPK pathways after treatment with hepatocyte growth factor
Exp. Mol. Med.
41
180-188
2009
Homo sapiens
Manually annotated by BRENDA team
Kowal, K.; Zukowski, S.; Moniuszko, M.; Bodzenta-?ukaszyk, A.
Plasminogen activator inhibitor-1 (PAI-1) and urokinase plasminogen activator (uPA) in sputum of allergic asthma patients
Folia Histochem. Cytobiol.
46
193-198
2008
Homo sapiens
Manually annotated by BRENDA team
Biermann, J.C.; Holzscheiter, L.; Kotzsch, M.; Luther, T.; Kiechle-Bahat, M.; Sweep, F.C.; Span, P.N.; Schmitt, M.; Magdolen, V.
Quantitative RT-PCR assays for the determination of urokinase-type plasminogen activator and plasminogen activator inhibitor type 1 mRNA in primary tumor tissue of breast cancer patients: comparison to antigen quantification by ELISA
Int. J. Mol. Med.
21
251-259
2008
Homo sapiens
Manually annotated by BRENDA team
Cheng, C.Y.; Hsieh, H.L.; Sun, C.C.; Lin, C.C.; Luo, S.F.; Yang, C.M.
IL-1 beta induces urokinase-plasminogen activator expression and cell migration through PKC alpha, JNK1/2, and NF-kappaB in A549 cells
J. Cell. Physiol.
219
183-193
2009
Homo sapiens
Manually annotated by BRENDA team
Bayliss, M.A.; Venn, R.F.; Edgington, A.M.; Webster, R.; Walker, D.K.
Determination of a potent urokinase-type plasminogen activator, UK-356,202, in plasma at pg/mL levels using column-switching HPLC and fluorescence detection
J. Chromatogr. B
877
121-126
2009
Homo sapiens
Manually annotated by BRENDA team
Karthikeyan, C.; Moorthy, N.S.; Trivedi, P.
QSAR study of substituted 2-pyridinyl guanidines as selective urokinase-type plasminogen activator (uPA) inhibitors
J. Enzyme Inhib. Med. Chem.
24
6-13
2009
Homo sapiens
Manually annotated by BRENDA team
Hashizume, H.; Kamio, N.; Nakao, S.; Matsushima, K.; Sugiya, H.
Protein kinase C synergistically stimulates tumor necrosis factor-alpha-induced secretion of urokinase-type plasminogen activator in human dental pulp cells
J. Physiol. Sci.
58
83-86
2008
Homo sapiens
Manually annotated by BRENDA team
Dong, Z.; Saliganan, A.D.; Meng, H.; Nabha, S.M.; Sabbota, A.L.; Sheng, S.; Bonfil, R.D.; Cher, M.L.
Prostate cancer cell-derived urokinase-type plasminogen activator contributes to intraosseous tumor growth and bone turnover
Neoplasia
10
439-449
2008
Homo sapiens
Manually annotated by BRENDA team
Naruse, K.; Lash, G.E.; Bulmer, J.N.; Innes, B.A.; Otun, H.A.; Searle, R.F.; Robson, S.C.
The urokinase plasminogen activator (uPA) system in uterine natural killer cells in the placental bed during early pregnancy
Placenta
30
398-404
2009
Homo sapiens
Manually annotated by BRENDA team
Gutova, M.; Najbauer, J.; Frank, R.T.; Kendall, S.E.; Gevorgyan, A.; Metz, M.Z.; Guevorkian, M.; Edmiston, M.; Zhao, D.; Glackin, C.A.; Kim, S.U.; Aboody, K.S.
Urokinase plasminogen activator and urokinase plasminogen activator receptor mediate human stem cell tropism to malignant solid tumors
Stem Cells
26
1406-1413
2008
Homo sapiens
Manually annotated by BRENDA team
Zhou, H.; Wu, X.; Lu, X.; Chen, G.; Ye, X.; Huang, J.
Evaluation of plasma urokinase-type plasminogen activator and urokinase-type plasminogen-activator receptor in patients with acute and chronic hepatitis B
Thromb. Res.
123
537-542
2009
Homo sapiens
Manually annotated by BRENDA team
Lee, K.H.; Choi, E.Y.; Hyun, M.S.; Eun, J.R.; Jang, B.I.; Kim, T.N.; Lee, H.J.; Lee, D.S.; Yun, S.S.; Kim, H.J.; Kim, J.H.; Kim, J.R.
Cellular mechanisms of hepatocyte growth factor-mediated urokinase plasminogen activator secretion by MAPK signaling in hepatocellular carcinoma
Tumori
94
523-530
2008
Homo sapiens
Manually annotated by BRENDA team
Radha, K.S.; Madhyastha, H.K.; Nakajima, Y.; Omura, S.; Maruyama, M.
Emodin upregulates urokinase plasminogen activator, plasminogen activator inhibitor-1 and promotes wound healing in human fibroblasts
Vascul. Pharmacol.
48
184-190
2008
Homo sapiens
Manually annotated by BRENDA team
Uchiba, M.; Imamura, T.; Hata, H.; Tatetsu, H.; Yonemura, Y.; Ueda, M.; Wada, Y.; Mitsuya, H.; Ando, Y.
Excessive fibrinolysis in AL-amyloidosis is induced by urokinae-type plasminogen activator from bone marrow plasma cells
Amyloid
16
89-93
2009
Homo sapiens
Manually annotated by BRENDA team
Gao, Q.; Fu, G.; Huang, G.; Lian, X.; Yu, J.; Yang, T.
Relationship between urokinase plasminogen activator receptor (uPAR) and the invasion of human prenatal hair follicle
Arch. Dermatol. Res.
302
409-418
2009
Homo sapiens
Manually annotated by BRENDA team
Yang, H.; Choi, H.J.; Park, S.H.; Kim, J.S.; Moon, Y.
Macrophage inhibitory cytokine-1 (MIC-1) and subsequent urokinase-type plasminogen activator mediate cell death responses by ribotoxic anisomycin in HCT-116 colon cancer cells
Biochem. Pharmacol.
78
1205-1213
2009
Homo sapiens
Manually annotated by BRENDA team
Boetkjaer, K.A.; Byszuk, A.A.; Andersen, L.M.; Christensen, A.; Andreasen, P.A.; Blouse, G.E.
Nonproteolytic induction of catalytic activity into the single-chain form of urokinase-type plasminogen activator by dipeptides
Biochemistry
48
9606-9617
2009
Homo sapiens
Manually annotated by BRENDA team
West, C.W.; Adler, M.; Arnaiz, D.; Chen, D.; Chu, K.; Gualtieri, G.; Ho, E.; Huwe, C.; Light, D.; Phillips, G.; Pulk, R.; Sukovich, D.; Whitlow, M.; Yuan, S.; Bryant, J.
Identification of orally bioavailable, non-amidine inhibitors of urokinase plasminogen activator (uPA)
Bioorg. Med. Chem. Lett.
19
5712-5715
2009
Homo sapiens
Manually annotated by BRENDA team
Zhu, Y.; Cheng, Z.; Dai, H.; Hu, L.
The relationship between urokinase plasminogen activator/plasminogen activator inhibitor type-1 expression in myoma/myometrium and mechanism of uterine artery occlusion by laparoscopy for uterine myoma treatment
Blood Coagul. Fibrinolysis
20
565-570
2009
Homo sapiens
Manually annotated by BRENDA team
Ulisse, S.; Baldini, E.; Mottolese, M.; Sentinelli, S.; Gargiulo, P.; Brancato, V.; Sorrenti, S.; Di Benedetto, A.; De Antoni, E.; DArmiento, M.
Increased expression of urokinase plasminogen activator and its cognate receptor in human seminomas
BMC Cancer
10
151
2010
Homo sapiens
Manually annotated by BRENDA team
Stewart, C.E.; Sayers, I.
Characterisation of urokinase plasminogen activator receptor variants in human airway and peripheral cells
BMC Mol. Biol.
10
75
2009
Homo sapiens
Manually annotated by BRENDA team
Killeen, S.D.; Wang, J.H.; Andrews, E.J.; Redmond, H.P.
Bacterial endotoxin enhances colorectal cancer cell adhesion and invasion through TLR-4 and NF-kappaB-dependent activation of the urokinase plasminogen activator system
Br. J. Cancer
100
1589-1602
2009
Homo sapiens
Manually annotated by BRENDA team
Tkachuk, V.A.; Plekhanova, O.S.; Parfyonova, Y.V.
Regulation of arterial remodeling and angiogenesis by urokinase-type plasminogen activator
Can. J. Physiol. Pharmacol.
87
231-251
2009
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Ports, M.O.; Nagle, R.B.; Pond, G.D.; Cress, A.E.
Extracellular engagement of alpha6 integrin inhibited urokinase-type plasminogen activator-mediated cleavage and delayed human prostate bone metastasis
Cancer Res.
69
5007-5014
2009
Homo sapiens
Manually annotated by BRENDA team
Shih, Y.W.; Lee, Y.C.; Wu, P.F.; Lee, Y.B.; Chiang, T.A.
Plumbagin inhibits invasion and migration of liver cancer HepG2 cells by decreasing productions of matrix metalloproteinase-2 and urokinase-plasminogen activator
Hepatol. Res.
39
998-1009
2009
Homo sapiens
Manually annotated by BRENDA team
Minoo, P.; Baker, K.; Baumhoer, D.; Terracciano, L.; Lugli, A.; Zlobec, I.
Urokinase-type plasminogen activator is a marker of aggressive phenotype and an independent prognostic factor in mismatch repair-proficient colorectal cancer
Hum. Pathol.
41
70-78
2010
Homo sapiens
Manually annotated by BRENDA team
Bae, K.B.; Jeong, Y.J.; Won, H.J.; Hong, K.H.; Choi, I.W.; Seo, S.K.; Park, S.G.
A human monoclonal antibody scFv to urokinase plasminogen activator
Hybridoma
29
147-152
2010
Homo sapiens
Manually annotated by BRENDA team
Xue, A.; Xue, M.; Jackson, C.; Smith, R.C.
Suppression of urokinase plasminogen activator receptor inhibits proliferation and migration of pancreatic adenocarcinoma cells via regulation of ERK/p38 signaling
Int. J. Biochem. Cell Biol.
41
1731-1738
2009
Homo sapiens
Manually annotated by BRENDA team
Zhou, H.; Tang, Y.; Liang, X.; Yang, X.; Yang, J.; Zhu, G.; Zheng, M.; Zhang, C.
RNAi targeting urokinase-type plasminogen activator receptor inhibits metastasis and progression of oral squamous cell carcinoma in vivo
Int. J. Cancer
125
453-462
2009
Homo sapiens
Manually annotated by BRENDA team
Villar, V.; Koci?, J.; Santibanez, J.F.
Spred2 inhibits TGF-beta1-induced urokinase type plasminogen activator expression, cell motility and epithelial mesenchymal transition
Int. J. Cancer
127
77-85
2010
Homo sapiens
Manually annotated by BRENDA team
Dmello, V.; Singh, S.; Wu, Y.; Birge, R.B.
The urokinase plasminogen activator receptor promotes efferocytosis of apoptotic cells
J. Biol. Chem.
284
17030-17038
2009
Homo sapiens
Manually annotated by BRENDA team
Cheng, X.; Shen, Z.; Yin, L.; Lu, S.H.; Cui, Y.
ECRG2 regulates cell migration/invasion through urokinase-type plasmin activator receptor (uPAR)/beta1 integrin pathway
J. Biol. Chem.
284
30897-30906
2009
Homo sapiens
Manually annotated by BRENDA team
Nieves, E.C.; Manchanda, N.
A cleavage-resistant urokinase plasminogen activator receptor exhibits dysregulated cell-surface clearance
J. Biol. Chem.
285
12595-12603
2010
Homo sapiens
Manually annotated by BRENDA team
Nagase, K.; Kobayashi, H.; Yoshikawa, E.; Kurita, N.
Ab initio molecular orbital calculations on specific interactions between urokinase-type plasminogen activator and its receptor
J. Mol. Graph. Model.
28
46-53
2009
Homo sapiens
Manually annotated by BRENDA team
Humphries, J.; Gossage, J.A.; Modarai, B.; Burnand, K.G.; Sisson, T.H.; Murdoch, C.; Smith, A.
Monocyte urokinase-type plasminogen activator up-regulation reduces thrombus size in a model of venous thrombosis
J. Vasc. Surg.
50
1127-1134
2009
Homo sapiens
Manually annotated by BRENDA team
Young, N.; Pearl, D.K.; Van Brocklyn, J.R.
Sphingosine-1-phosphate regulates glioblastoma cell invasiveness through the urokinase plasminogen activator system and CCN1/Cyr61
Mol. Cancer Res.
7
23-32
2009
Homo sapiens
Manually annotated by BRENDA team
Obermajer, N.; Doljak, B.; Kos, J.
Cytokeratin 8 ectoplasmic domain binds urokinase-type plasminogen activator to breast tumor cells and modulates their adhesion, growth and invasiveness
Mol. Cancer
8
88
2009
Homo sapiens
Manually annotated by BRENDA team
Iyer, A.M.; Zurolo, E.; Boer, K.; Baayen, J.C.; Giangaspero, F.; Arcella, A.; Di Gennaro, G.C.; Esposito, V.; Spliet, W.G.; van Rijen, P.C.; Troost, D.; Gorter, J.A.; Aronica, E.
Tissue plasminogen activator and urokinase plasminogen activator in human epileptogenic pathologies
Neuroscience
167
929-945
2010
Homo sapiens
Manually annotated by BRENDA team
Armstrong, A.F.; Lemon, J.A.; Czorny, S.K.; Singh, G.; Valliant, J.F.
Evaluation of single amino acid chelate derivatives and regioselective radiolabelling of a cyclic peptide for the urokinase plasminogen activator receptor
Nucl. Med. Biol.
36
907-917
2009
Homo sapiens
Manually annotated by BRENDA team
Li, X.F.; Yan, P.J.; Shao, Z.M.
Downregulation of miR-193b contributes to enhance urokinase-type plasminogen activator (uPA) expression and tumor progression and invasion in human breast cancer
Oncogene
28
3937-3948
2009
Homo sapiens
Manually annotated by BRENDA team
Sandra, D.; Radha, M.; Harishkumar, M.; Yuichi, N.; Sayuri, O.; Masugi, M.
Downregulation of urokinase-type plasminogen activator and plasminogen activator inhibitor-1 by grape seed proanthocyanidin extract
Phytomedicine
17
42-46
2010
Homo sapiens
Manually annotated by BRENDA team
Sgier, D.; Zuberbuehler, K.; Pfaffen, S.; Neri, D.
Isolation and characterization of an inhibitory human monoclonal antibody specific to the urokinase-type plasminogen activator, uPA
Protein Eng. Des. Sel.
23
261-269
2010
Homo sapiens
Manually annotated by BRENDA team
Odaka, T.; Kobayashi, K.; Takahashi, K.; Nakamura, H.; Matsuoka, T.
Effect of prostaglandin E2 on urokinase-type plasminogen activator production by human lung fibroblasts
Scand. J. Clin. Lab. Invest.
69
225-233
2009
Homo sapiens
Manually annotated by BRENDA team
Kumano, M.; Miyake, H.; Muramaki, M.; Furukawa, J.; Takenaka, A.; Fujisawa, M.
Expression of urokinase-type plasminogen activator system in prostate cancer: correlation with clinicopathological outcomes in patients undergoing radical prostatectomy
Urol. Oncol.
27
180-186
2009
Homo sapiens
Manually annotated by BRENDA team
Nassar, T.; Yarovoi, S.; Fanne, R.; Waked, O.; Allen, T.; Idell, S.; Cines, D.; Higazi, A.
Urokinase plasminogen activator regulates pulmonary arterial contractility and vascular permeability in mice
Am. J. Respir. Cell Mol. Biol.
45
1015-1021
2011
Homo sapiens
Manually annotated by BRENDA team
Beaufort, N.; Seweryn, P.; de Bentzmann, S.; Tang, A.; Kellermann, J.; Grebenchtchikov, N.; Schmitt, M.; Sommerhoff, C.P.; Pidard, D.; Magdolen, V.
Activation of human pro-urokinase by unrelated proteases secreted by Pseudomonas aeruginosa
Biochem. J.
428
473-482
2010
Homo sapiens
Manually annotated by BRENDA team
Botkjaer, K.A.; Fogh, S.; Bekes, E.C.; Chen, Z.; Blouse, G.E.; Jensen, J.M.; Mortensen, K.K.; Huang, M.; Deryugina, E.; Quigley, J.P.; Declerck, P.J.; Andreasen, P.A.
Targeting the autolysis loop of urokinase-type plasminogen activator with conformation-specific monoclonal antibodies
Biochem. J.
438
39-51
2011
Homo sapiens
Manually annotated by BRENDA team
Venkatraman, L.; Li, H.; Dewey Jr., C.; White, J.; Bhowmick, S.; Yu, H.; Tucker-Kellogg, L.
Steady states and dynamics of urokinase-mediated plasmin activation in silico and in vitro
Biophys. J.
101
1825-1834
2011
Homo sapiens
Manually annotated by BRENDA team
Uchino, R.; Madhyastha, R.; Madhyastha, H.; Dhungana, S.; Nakajima, Y.; Omura, S.; Maruyama, M.
NFkappaB-dependent regulation of urokinase plasminogen activator by proanthocyanidin-rich grape seed extract: effect on invasion by prostate cancer cells
Blood Coagul. Fibrinolysis
21
528-533
2010
Homo sapiens
Manually annotated by BRENDA team
Makarova, A.M.; Lebedeva, T.V.; Nassar, T.; Higazi, A.A.; Xue, J.; Carinato, M.E.; Bdeir, K.; Cines, D.B.; Stepanova, V.
Urokinase-type plasminogen activator (uPA) induces pulmonary microvascular endothelial permeability through low density lipoprotein receptor-related protein (LRP)-dependent activation of endothelial nitric-oxide synthase
J. Biol. Chem.
286
23044-23053
2011
Homo sapiens
Manually annotated by BRENDA team
Lin, Z.; Jiang, L.; Yuan, C.; Jensen, J.K.; Zhang, X.; Luo, Z.; Furie, B.C.; Furie, B.; Andreasen, P.A.; Huang, M.
Structural basis for recognition of urokinase-type plasminogen activator by plasminogen activator inhibitor-1
J. Biol. Chem.
286
7027-7032
2011
Homo sapiens (P00749)
Manually annotated by BRENDA team
Schroetzlmair, F.; Kopitz, C.; Halbgewachs, B.; Lu, F.; Alguel, H.; Bruenner, N.; Gaensbacher, B.; Krueger, A.
Tissue inhibitor of metalloproteinases-1-induced scattered liver metastasis is mediated by host-derived urokinase-type plasminogen activator
J. Cell. Mol. Med.
14
2760-2770
2010
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Markowska, A.; Bruzgo, I.; Midura-Nowaczek, K.
Synthesis and activity of amides of tripeptides as potential urokinase inhibitors
J. Enzyme Inhib. Med. Chem.
25
139-142
2010
Homo sapiens
Manually annotated by BRENDA team
Chao, S.C.; Hu, D.N.; Yang, P.Y.; Lin, C.Y.; Yang, S.F.
Overexpression of urokinase-type plasminogen activator in pterygia and pterygium fibroblasts
Mol. Vis.
17
23-31
2011
Homo sapiens
Manually annotated by BRENDA team
Matsunoshita, Y.; Ijiri, K.; Ishidou, Y.; Nagano, S.; Yamamoto, T.; Nagao, H.; Komiya, S.; Setoguchi, T.
Suppression of osteosarcoma cell invasion by chemotherapy is mediated by urokinase plasminogen activator activity via up-regulation of EGR1
PLoS ONE
6
e16234
2011
Homo sapiens
Manually annotated by BRENDA team
Graziano, F.; Elia, C.; Laudanna, C.; Poli, G.; Alfano, M.
Urokinase plasminogen activator inhibits HIV virion release from macrophage-differentiated chronically infected cells via activation of RhoA and PKCepsilon
PLoS ONE
6
e23674
2011
Homo sapiens
Manually annotated by BRENDA team
Paland, N.; Aharoni, S.; Fuhrman, B.
Urokinase-type plasminogen activator (uPA) modulates monocyte-to-macrophage differentiation and prevents Ox-LDL-induced macrophage apoptosis
Atherosclerosis
231
29-38
2013
Mus musculus, Homo sapiens (P00749), Mus musculus C57BL/6
Manually annotated by BRENDA team
Chulsky, S.; Paland, N.; Lazarovich, A.; Fuhrman, B.
Urokinase-type plasminogen activator (uPA) decreases hepatic SR-BI expression and impairs HDL-mediated reverse cholesterol transport
Atherosclerosis
233
11-18
2014
Homo sapiens
Manually annotated by BRENDA team
Paland, N.; Gamliel-Lazarovich, A.; Coleman, R.; Fuhrman, B.
Urokinase-type plasminogen activator (uPA) stimulates triglyceride synthesis in Huh7 hepatoma cells via p38-dependent upregulation of DGAT2
Atherosclerosis
237
200-207
2014
Mus musculus, Homo sapiens (P00749), Mus musculus C57BL/6
Manually annotated by BRENDA team
Krstic, J.; Obradovic, H.; Jaukovic, A.; Okic-Dordevic, I.; Trivanovic, D.; Kukolj, T.; Mojsilovic, S.; Ilic, V.; Santibanez, J.F.; Bugarski, D.
Urokinase type plasminogen activator mediates interleukin-17-induced peripheral blood mesenchymal stem cell motility and transendothelial migration
Biochim. Biophys. Acta
1853
431-444
2015
Homo sapiens (P00749)
Manually annotated by BRENDA team
Massey, A.P.; Harley, W.R.; Pasupuleti, N.; Gorin, F.A.; Nantz, M.H.
2-Amidino analogs of glycine-amiloride conjugates: inhibitors of urokinase-type plasminogen activator
Bioorg. Med. Chem. Lett.
22
2635-2639
2012
Homo sapiens (P00749), Homo sapiens
Manually annotated by BRENDA team
Venkatraj, M.; Messagie, J.; Joossens, J.; Lambeir, A.M.; Haemers, A.; Van der Veken, P.; Augustyns, K.
Synthesis and evaluation of non-basic inhibitors of urokinase-type plasminogen activator (uPA)
Bioorg. Med. Chem.
20
1557-1568
2012
Homo sapiens (P00749)
Manually annotated by BRENDA team
Jiang, L.; Zhao, B.; Xu, P.; Soerensen, H.P.; Jensen, J.K.; Christensen, A.; Hosseini, M.; Nielsen, N.C.; Jensen, K.J.; Andreasen, P.A.; Huang, M.
Distinctive binding modes and inhibitory mechanisms of two peptidic inhibitors of urokinase-type plasminogen activator with isomeric P1 residues
Int. J. Biochem. Cell Biol.
62
88-92
2015
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Ji, H.L.; Zhao, R.; Komissarov, A.A.; Chang, Y.; Liu, Y.; Matthay, M.A.
Proteolytic regulation of epithelial sodium channels by urokinase plasminogen activator: cutting edge and cleavage sites
J. Biol. Chem.
290
5241-5255
2015
Homo sapiens
Manually annotated by BRENDA team
Al-Shaer, M.A.; Khanfar, M.A.; Taha, M.O.
Discovery of novel urokinase plasminogen activator (uPA) inhibitors using ligand-based modeling and virtual screening followed by in vitro analysis
J. Mol. Model.
20
2080
2014
Homo sapiens (P00749)
Manually annotated by BRENDA team
Asuthkar, S.; Stepanova, V.; Lebedeva, T.; Holterman, A.L.; Estes, N.; Cines, D.B.; Rao, J.S.; Gondi, C.S.
Multifunctional roles of urokinase plasminogen activator (uPA) in cancer stemness and chemoresistance of pancreatic cancer
Mol. Biol. Cell
24
2620-2632
2013
Homo sapiens (P00749)
Manually annotated by BRENDA team
Zha, X.; Diaz, R.; Franco, J.J.; Sanchez, V.F.; Fasoli, E.; Barletta, G.; Carvajal, A.; Bansal, V.
Inhibitors of urokinase type plasminogen activator and cytostatic activity from crude plants extracts
Molecules
18
8945-8958
2013
Homo sapiens (P00749), Homo sapiens
Manually annotated by BRENDA team
Sanderson-Smith, M.L.; Zhang, Y.; Ly, D.; Donahue, D.; Hollands, A.; Nizet, V.; Ranson, M.; Ploplis, V.A.; Walker, M.J.; Castellino, F.J.
A key role for the urokinase plasminogen activator (uPA) in invasive Group A streptococcal infection
PLoS Pathog.
9
e1003469
2013
Homo sapiens (P00749), Homo sapiens
Manually annotated by BRENDA team
Jendroszek, A.; Madsen, J.; Chana-Munoz, A.; Dupont, D.; Christensen, A.; Panitz, F.; Fuechtbauer, E.; Lovell, S.; Jensen, J.
Biochemical and structural analyses suggest that plasminogen activators coevolved with their cognate protein substrates and inhibitors
J. Biol. Chem.
294
3794-3805
2019
Homo sapiens (P00749), Homo sapiens
Manually annotated by BRENDA team