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ABZ-Ile-Arg-Ala-Arg-Ser-Ala-Ala-Tyr(3-NO2)-NH2 + H2O
ABZ-Ile-Arg-Ala-Arg + Ser-Ala-Ala-Tyr(3-NO2)-NH2
-
-
-
?
ABZ-Ile-Arg-Ala-Arg-Ser-Ala-Gly-Tyr(3-NO2)-NH2 + H2O
ABZ-Ile-Arg-Ala-Arg + Ser-Ala-Gly-Tyr(3-NO2)-NH2
-
-
-
?
ABZ-Ile-Arg-Ala-Arg-Ser-Ala-Ser-Tyr(3-NO2)-NH2 + H2O
ABZ-Ile-Arg-Ala-Arg + Ser-Ala-Ser-Tyr(3-NO2)-NH2
-
-
-
?
alphaEbeta7integrin + H2O
?
-
-
-
?
Boc-Gln-Ala-Arg-4-nitroanilide + H2O
Boc-Gln-Ala-Arg + 4-nitroaniline
-
-
-
?
Boc-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
Boc-Gln-Ala-Arg + 7-amino-4-methylcoumarin
fluorogenic substrate
-
-
?
Boc-QAR-Amc + H2O
?
matriptase-2 mediates efficient cleavage of artificial peptides corresponding to cleavage sites located in the proteins filaggrin, CUB-domain-containing protein 1 (CDCP1), and alphaE beta7 integrin
-
-
?
CUB-domain-containing protein 1 + H2O
?
-
-
-
?
fetuin-A + H2O
?
a liver-derived alpha2-Heremans-Schmid glycoprotein from plasma, processing into a two-chain form, cleavage sites are Arg and Lys residues in the 40 amino acid sequence of the linker connceting the two peptides
-
-
?
Fibrinogen + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
-
-
?
filaggrin + H2O
?
-
-
-
?
hemojuvelin (furin site) + H2O
?
-
-
-
?
matriptase-2 + H2O
?
autocatalysis
-
-
?
N2-t-butyloxycarbonyl-QNR-7-amido-4-methylcoumarin + H2O
?
matriptase-2 mediates efficient cleavage of artificial peptides corresponding to cleavage sites located in the proteins filaggrin, CUB-domain-containing protein 1 (CDCP1), and alphaE beta7 integrin
-
-
?
proform matriptase + H2O
mature matriptase
matriptase is expressed as a zymogen and is autocatalytically processed and activated through cleavage at Arg614 within the RQAR614-VVGG activation sequence
-
-
?
proform matriptase-2 + H2O
mature matriptase
matriptase-2 is expressed as zymogen form and undergoes autocatalysis at Arg576 within the PSSR576-IVGG sequence located in the consensus activation site of its pro-domain
-
-
?
TMPRSS6 + H2O
?
autocleavage site: PSSR/IVGG
-
-
?
Type I collagen + H2O
?
-
-
-
?
(DY-681)-Gly-Arg-Gln-Ser-Arg-Ala-Ile-Lys (DY-681)-NH + H2O
?
-
synthetic substrate, peptide sequence is derived from one of the preferred matriptase cleavage sequences, P4(Arg/Lys)-P3(Xxx)-P2(Ser)-P1(Arg)-P10(Ala), where Xxx is a nonbasic amino acid
-
-
?
acid-sensing ion channel 1 + H2O
?
-
the matriptase recognition sites Arg-145, Lys-185, and Lys-384 are identified in the specific substrate acid-sensing ion channel 1
-
-
?
alphaEbeta7 integrin + H2O
?
-
-
-
-
?
amyloid precursor protein + H2O
?
-
-
-
-
?
Arg-Xaa-Ser-Arg-Ala + H2O
Arg-Xaa-Ser + Arg-Ala
-
X: non-basic amino acid, good substrate
-
?
benzoyl-L-arginine-4-methylcoumaryl-7-amide + H2O
benzoyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-Gln-Ala-Arg-4-nitroanilide + H2O
Boc-Gln-Ala-Arg + 4-nitroaniline
-
-
-
?
Boc-Glu-Ala-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Boc-Glu-Ala-Arg-7-amido-4-methylcoumarin + H2O
Boc-Glu-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-QAR-Amc + H2O
?
-
-
-
?
butyloxycarbonyl-L-Gln-L-Ala-L-Arg-4-nitroanilide + H2O
butyloxycarbonyl-L-Gln-L-Ala-L-Arg + 4-nitroaniline
-
-
-
-
?
EpCAM + H2O
?
-
i.e. epithelial cell adhesion molecule CD326
-
-
?
epidermal growth factor receptor + H2O
EGFR135 + EGFR110
filaggrin + H2O
?
-
-
-
-
?
G-protein-coupled protease-activated receptor-2 + H2O
?
-
-
-
-
?
Glu-Gly-Arg-p-nitroanilide + H2O
?
-
substrate activity assay
-
-
?
growth factor macrophage-stimulating protein 1 + H2O
?
-
-
-
-
?
hemojuvelin + H2O
?
-
-
-
-
?
hepatocyte growth factor + H2O
?
-
-
?
hepatocyte growth factor + H2O
activated hepatocyte growth factor + ?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
HGF/SF + H2O
?
-
i.e. hepatocyte growth factor/scatter factor, growth factor
-
-
?
Ile-Pro-Arg-p-nitroanilide + H2O
Ile-Pro + Arg-p-nitroanilide
-
-
-
?
influenza A H1 virus hemagglutinin + H2O
?
the soluble form of the protease is able to specifically cleave hemagglutinins from H1 virus, but not from H2 and H3 viruses, in a broad pH range
-
-
?
insulin growth factor binding protein-related protein-1 + H2O
?
-
cleaved by the soluble form of active matripase
-
-
?
insulin-like growth factor binding protein related protein-1
?
insulin-like growth factor binding protein-related protein-1 + H2O
?
insulin-like growth factor binding-related protein-1 + H2O
?
-
-
-
-
?
Lys-Xaa-Ser-Arg-Ala + H2O
Lys-Xaa-Ser + Arg-Ala
-
X: non-basic amino acid, good substrate
-
?
matriptase + H2O
?
-
-
-
-
?
matrix metalloprotease-3 + H2O
?
methyl-sulfonyl-D-cyclo-hexyltyrosyl-glycyl-L-arginine-4-nitroanilide + H2O
?
-
-
-
?
MSP-1 + H2O
?
-
i.e. macrophage-stimulating protein 1, a growth factor
-
-
?
N-Ala-Ala-Ala-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
N-succinyl-Ala-Phe-Lys-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
N-succinyl-Ala-Phe-Lys-7-amido-4-methylcoumarin + H2O
N-succinyl-Ala-Phe-Lys + 7-amino-4-methylcoumarin
-
-
?
N-succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
N-tert-butoxy-carbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin
N-tert-butoxy-carbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-benzyl-Asp-Pro-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-benzyl-Asp-Pro-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-benzyl-Glu-Gly-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-benzyl-Glu-Gly-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-gamma-benzyl-Glu-Ala-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
N-tert-butoxycarbonyl-gamma-benzyl-Glu-Ala-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-gamma-benzyl-Glu-Ala-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-gamma-benzyl-Glu-Gly-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-gamma-benzyl-Glu-Gly-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg 7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
N-tert-butoxycarbonyl-Gly-Lys-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gly-Lys-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Leu-Arg-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Leu-Gly-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Leu-Gly-Arg + 7-amino-4-methylcoumarin
N-tert-butoxycarbonyl-Leu-Ser-Thr-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Leu-Ser-Thr-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
-
?
plasminogen + H2O
?
-
-
?
pro matrix metalloproteinase 1 + H2O
?
-
matriptase activates pro-matrix metalloproteinase-1 and processes pro-matrix metalloproteinase-3 to its fully active form
-
-
?
pro matrix metalloproteinase 3 + H2O
?
-
matriptase activates pro-matrix metalloproteinase-1 and processes pro-matrix metalloproteinase-3 to its fully active form
-
-
?
pro-form GPI-anchored serine protease prostasin + H2O
mature GPI-anchored serine protease prostasin + ?
pro-form influenza hemagglutinin H1 + H2O
mature influenza hemagglutinin H1 + ?
pro-form influenza hemagglutinin H2 + H2O
mature influenza hemagglutinin H2 + ?
subtype H2N2
-
-
?
pro-form influenza hemagglutinin H3 + H2O
mature influenza hemagglutinin H3 + ?
subtype H3N2
-
-
?
pro-form matriptase + H2O
mature matriptase + ?
autocatalytic activation
-
-
?
pro-hepatocyte growth factor + H2O
?
-
-
-
-
?
pro-hepatocyte growth factor/scatter factor + H2O
?
pro-HGF + H2O
?
-
matriptase is an efficient activator of hepatocyte growth factor
-
-
?
pro-urokinase plasminogen activator + H2O
?
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
pro-urokinase-type plasminogen activator + H2O
?
-
-
-
-
?
profilaggrin + H2O
?
-
-
-
-
?
profilaggrin + H2O
filaggrin + propeptide of filaggrin
proform epithelial sodium channel + H2O
mature epithelial sodium channel + ?
-
-
-
-
?
proform G protein-coupled protease activated receptor-2 + H2O
mature G protein-coupled protease activated receptor-2 + ?
-
-
-
-
?
proform prostasin + H2O
mature prostasin + ?
-
-
-
-
?
prostasin + H2O
activated prostasin + ?
prostatin + H2O
?
-
-
-
-
?
protease activated receptor 2 + H2O
?
-
-
-
-
?
protease-activated receptor-2
?
protease-activated receptor-2 + H2O
?
-
-
-
-
?
proteinase-activated receptor 2 + H2O
?
-
-
-
-
?
RAARVVGG + H2O
RAAR + VVGG
-
-
-
-
?
RLARVVGG + H2O
RLAR + VVGG
-
-
-
-
?
RQARAVGG + H2O
RQAR + AVGG
-
-
-
-
?
RQARQVGG + H2O
RQAR + QVGG
-
-
-
-
?
RQARVVGG + H2O
RQAR + VVGG
-
-
-
-
?
RQARYVGG + H2O
RQAR + YVGG
-
-
-
-
?
RQLRVVGG + H2O
RQLR + VVGG
-
-
-
-
?
RQRRVVGG + H2O
RQRR + VVGG
-
-
-
-
?
RQYRVVGG + H2O
RQYR + VVGG
-
-
-
-
?
RRARVVGG + H2O
RRAR + VVGG
-
-
-
-
?
RYARVVGG + H2O
RYAR + VVGG
-
-
-
-
?
serine protease uPA + H2O
?
-
-
-
-
?
SIMA135 + H2O
?
-
-
-
-
?
single-chain urokinase-type plaminogen activator + H2O
?
-
is activated by matriptase
-
?
stromelysin + H2O
?
-
MMP-3
-
-
?
stromelysin + H2O
activated stromelysin + propeptide of stromelysin
succinyl-Ala-Phe-Lys-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Phe-Lys + 7-amino-4-methylcoumarin
-
-
?
t-butoxycarbonyl-L-Gln-L-Ala-L-Arg-7-amido-4-methylcoumarin + H2O
t-butoxycarbonyl-L-Gln-L-Ala-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
enzymatic activity assay
-
-
?
urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
pro-uPA activation on THP-1 cells
-
-
?
VPEKQTRGL + H2O
?
influenza hemagglutinin H3 cleavage site peptide mimic
-
-
?
Xaa-Arg-Ser-Arg-Ala + H2O
Xaa-Arg-Ser + Arg-Ala
-
X: non-basic amino acid, good substrate
-
?
Xaa-Lys-Ser-Arg-Ala + H2O
Xaa-Lys-Ser + Arg-Ala
-
X: non-basic amino acid, good substrate
-
?
additional information
?
-
hemojuvelin + H2O
?
-
-
-
?
hemojuvelin + H2O
?
inactivation
-
-
?
hemojuvelin + H2O
?
a glycosylphosphatidylinositol-linked membrane protein. inactivation
-
-
?
hemojuvelin + H2O
?
bone morphogenetic protein co-receptor
-
-
?
collagen type IV + H2O
?
-
-
-
-
?
collagen type IV + H2O
?
-
involved in ECM degradation/remodeling
-
-
?
epidermal growth factor receptor + H2O
EGFR135 + EGFR110
-
-
fragments of 135 and 110 kDa, EGFR110 is constitutively active, while EGFR135 is inactive in terms of tyrosine phosphorylation
-
?
epidermal growth factor receptor + H2O
EGFR135 + EGFR110
-
the epidermal growth factor receptor, EGFR is proteolytically cleaved in the N-terminal extracellular domain by the matriptase-prostasin serine protease cascade in cultured epithelial cells
fragments of 135 and 110 kDa, no longer responsive to EGF stimulation
-
?
Fibronectin + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
-
involved in adhesion and migration/invasiveness
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
involved in ECM degradation/remodeling
-
-
?
hepatocyte growth factor + H2O
activated hepatocyte growth factor + ?
-
-
-
-
?
hepatocyte growth factor + H2O
activated hepatocyte growth factor + ?
-
proteolytic activation of hepatocyte growth factor/scatter factor, physiological function, overview
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
-
-
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
-
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
-
activation
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
-
seven proteases are involved in the activation of HGF/SF, involved in cell proliferation and adhesion, ECM degradation/remodeling, and migration/invasiveness, overview
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
the enzyme is involved in tumor progression and metastasis
-
-
?
IGFBP-rP1 + H2O
?
-
-
-
-
?
IGFBP-rP1 + H2O
?
-
an adhesion factor
-
-
?
IGFBP-rP1 + H2O
?
-
involved in involved in cell proliferation and adhesion
-
-
?
insulin-like growth factor binding protein related protein-1
?
-
IGFBP-rP1
-
-
?
insulin-like growth factor binding protein related protein-1
?
IGFBP-rP1
-
-
?
insulin-like growth factor binding protein-related protein-1 + H2O
?
-
activation
-
-
?
insulin-like growth factor binding protein-related protein-1 + H2O
?
-
proteolytical cleavage on the cell surface of a a single-chain IGFB-rP1 to a two-chain form, consisting of a 25 kDa chain and an 8 kDa chain, changing its biological in modulation of cellular adhesion and growth in an IGF/insulin-dependent or independent manner, as well as tumor-suppressive activity, the soluble form of active matriptase cleaves IGFBP-rP1 but HAI-1 or some other inhibitors block its activity in culture medium, overview
-
-
?
insulin-like growth factor binding protein-related protein-1 + H2O
?
-
i.e. IGFBP-rP1
-
-
?
insulin-like growth factor binding protein-related protein-1 + H2O
?
-
i.e. IGFBP-rP1 or angiomodulin or mac25
-
-
?
Laminin + H2O
?
-
-
-
-
?
Laminin + H2O
?
-
involved in adhesion and migration/invasiveness
-
-
?
matrix metalloprotease-3 + H2O
?
-
-
-
-
?
matrix metalloprotease-3 + H2O
?
-
activation
-
-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Leu-Gly-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Leu-Gly-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Leu-Gly-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Leu-Gly-Arg + 7-amino-4-methylcoumarin
-
-
?
PAR-2 + H2O
?
-
-
-
-
?
PAR-2 + H2O
?
-
G-protein coupled receptor
-
-
?
PAR-2 + H2O
?
-
involved in involved in cell adhesion
-
-
?
pro-form GPI-anchored serine protease prostasin + H2O
mature GPI-anchored serine protease prostasin + ?
activation
-
-
?
pro-form GPI-anchored serine protease prostasin + H2O
mature GPI-anchored serine protease prostasin + ?
activation, prostasin is also a regulator of the epidermal sodium channel like matriptase
-
-
?
pro-form influenza hemagglutinin H1 + H2O
mature influenza hemagglutinin H1 + ?
-
-
-
?
pro-form influenza hemagglutinin H1 + H2O
mature influenza hemagglutinin H1 + ?
preferred subtype H1N1
-
-
?
pro-hepatocyte growth factor/scatter factor + H2O
?
-
pro-HGF/SF
-
-
?
pro-hepatocyte growth factor/scatter factor + H2O
?
pro-HGF/SF
-
-
?
pro-uPA + H2O
?
-
-
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
-
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
activation
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
activation at the cell surface, where uPA and matriptase co-localize, involved in cell proliferation and adhesion, ECM degradation/remodeling, and migration/invasiveness
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
the enzyme is involved in tumor progression and metastasis
-
-
?
profilaggrin + H2O
filaggrin + propeptide of filaggrin
-
-
-
-
?
profilaggrin + H2O
filaggrin + propeptide of filaggrin
-
involved in terminal epithelial cell differentiation, mechanism of enzyme access for direct cleavage in vivo, overview
-
-
?
prostasin + H2O
?
-
-
-
-
?
prostasin + H2O
?
-
-
-
?
prostasin + H2O
?
-
a serine protease
-
-
?
prostasin + H2O
activated prostasin + ?
-
proteolytic activation by matriptase, when expressed without matriptase, prostasin remains in the zymogen form and no prostasin-PN-1 complex is formed, overview
-
-
?
prostasin + H2O
activated prostasin + ?
-
proteolytic activation by matriptase
-
-
?
protease-activated receptor-2
?
-
PAR2
-
-
?
protease-activated receptor-2
?
PAR2
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stromelysin + H2O
activated stromelysin + propeptide of stromelysin
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activation
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stromelysin + H2O
activated stromelysin + propeptide of stromelysin
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i.e. MMP-3 or matrix metalloproteinase-3, recombinant human substrate, activation
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trask + H2O
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trask + H2O
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a transmembrane glycoprotein
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trask + H2O
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i.e. CDCP1 or SIMA 135, a transmembrane glycoprotein
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VEGFR-2 + H2O
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VEGFR-2 + H2O
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i.e. vascular endothelial growth factor receptor 2, a growth factor receptor
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additional information
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the optimized peptide substrate sequence is Ile-Arg-Ala-Arg-Ser-Ala-Gly
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additional information
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the optimized peptide substrate sequence is Ile-Arg-Ala-Arg-Ser-Ala-Gly
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additional information
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substrate specificity, overview
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additional information
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cleaves synthetic substrates with arginine or lysine as their P1 sites and prefers small side chain amino acids, such as Ala and Gly, at P2 sites
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additional information
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cleaves synthetic substrates with arginine or lysine as their P1 sites and prefers small side chain amino acids, such as Ala and Gly, at P2 sites
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additional information
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preferred amino acid residues: at P4 position: Lys and Arg, at P3 position: basic residues and Glu, at P2 position: Gly, Ser and Phe
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additional information
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degrades extracellular matrix
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additional information
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degrades extracellular matrix
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additional information
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degrades extracellular matrix
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additional information
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degrades extracellular matrix
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additional information
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degrades extracellular matrix
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additional information
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degrades extracellular matrix
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additional information
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degrades extracellular matrix, matriptase-binding protein is a Kunitz-type serine protease inhibitor
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?
additional information
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degrades extracellular matrix, matriptase-binding protein is a Kunitz-type serine protease inhibitor
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additional information
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initiator of matrix-degrading protein cascade, activates hepatocyte growth factor scattering factor
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additional information
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initiator of matrix-degrading protein cascade, activates hepatocyte growth factor scattering factor
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additional information
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involved in multiple aspects of tumor progression and cancer invasion
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additional information
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enzyme regulation and deregulation in cancer, overview, matriptase is involved in cancer initiation and progression, it not only facilitates cellular invasiveness but may also activate oncogenic pathways, overview
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additional information
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matriptase blockade could potentially modulate tumorigenesis and metastasis in vivo
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additional information
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matriptase cleaves and activates proteins implicated in the progression of cancer
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additional information
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matriptase expression is correlated with tumor progression in epithelium-derived cancer cells
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additional information
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matriptase has an essential physiological role in profilaggrin processing, corneocyte maturation, and lipid matrix formation associated with terminal differentiation of the oral epithelium and the epidermis, and is also critical for hair follicle growth, matriptase and HAI expression are frequently dysregulated in human cancer, and matriptase expression, that is unopposed by HAI-1, potently promotes carcinogenesis and metastatic dissemination in animal models, matriptase dramatically increases apoptosis of immature thymocytes in the thymus, leading to thymocyte depletion, physiological functions of matriptase, the enzyme is involved in epithelial carcinogenesis, detailed overview
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additional information
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matriptase is a type II transmembrane serine protease and highly regulated in leukocytes, and correlates with the presence of active uPA on their surface, it is up-regulated in a variety of cancers and correlates closely with disease progression, it acts as initiator of protease cascades/signaling pathways, overview
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additional information
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matriptase promotes tumor growth and angiogenesis by enhancing extracellular matrix degradation in tumor cell microenvironments, overview
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additional information
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matriptase-1 enhances breast tumor growth and invasion and correlates with poor prognosis for breast cancer patients, while matriptase-2 shows the opposite effects, overview
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additional information
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matriptase-1 enhances breast tumor growth and invasion and correlates with poor prognosis for breast cancer patients, while matriptase-2 shows the opposite effects, overview
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additional information
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matriptase-2 inhibits breast tumor growth and invasion and correlates with favorable prognosis for breast cancer patients, while matriptase-1 shows the opposite effects, overview
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additional information
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matriptase-2 inhibits breast tumor growth and invasion and correlates with favorable prognosis for breast cancer patients, while matriptase-1 shows the opposite effects, overview
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additional information
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mutation in gene ST14 causes autosomal recessive ichthyosis with hypotrichosis syndrome, characterized by congenital ichthyosis associated with abnormal hair, overview
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additional information
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physiological functions, overview, MT-SP1 is a type II transmembrane serine protease implicated in a range of cancers including those of the breast, cervix, ovaries, prostate, colon and gastrointestinal tract, MT-SP1 plays a role in embryologic development
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additional information
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physiological regulatory mechanisms, overview, matriptase is involved in cancer invasion and metastasis by serving as a membrane activator directly on cancer cell surfaces to recruit and activate urokinase type plasminogen activator, MMP-3, hepatocyte growth factor, and insulin-like growth factor binding protein-related protein-1, all of which are important in various aspects of cancers, including extracellular matrix degradation, adhesion, cellular motility and tumor vascularization
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additional information
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reduced matriptase activity is associated with incomplete terminal differentiation of epidermis, epidermal appendages, oral epithelium, and, likely, other epithelial structures, matriptase activity must be tightly controlled in epithelial tissues by transcriptional and posttranslational mechanisms, as matriptase dysregulation can cause embryonic demise as well as malignant transformation
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additional information
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the G827R mutation in patients with autosomal recessive ichthyosis with hypotrichosis leads to the expression of an inactive protease
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additional information
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matriptase binds cytosolic proteins to regulate enzymatic activity and cellular distribution of the protease
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additional information
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matriptase performs autoactivation
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additional information
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R/KXSR-/-A is the cleavage sequence of matriptase
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additional information
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the enzyme is a type II transmembrane serine protease
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additional information
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the enzyme performs autoproteolysis
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additional information
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matriptase does not cleave acid-sensing ion channel 2
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additional information
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the P1 residue for MT-SP1 substrates is either arginine or lysine
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additional information
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matriptase has an autocatalytic domain, RQAR. At physiological pH, matriptase is capable of cleaving both the H1 (IQSR-/-GLFG) and H3 (KQTR-/-GLFG) consensus cleavage sequences, whereas no cleavage is observed with the H2 (IESRGLFG) consensus sequence. RQRR-/-VVGG is the optimal cleavage sequence of matriptase
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additional information
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matriptase has an autocatalytic domain, RQAR. At physiological pH, matriptase is capable of cleaving both the H1 (IQSR-/-GLFG) and H3 (KQTR-/-GLFG) consensus cleavage sequences, whereas no cleavage is observed with the H2 (IESRGLFG) consensus sequence. RQRR-/-VVGG is the optimal cleavage sequence of matriptase
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additional information
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the enzyme shows low rate cleavage of the A/Japan/305/57 (H2) peptide mimic (VPQIESRGL) compared to that for the H1 consensus
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1-[(4S)-4-amino-5-(1,3-benzothiazol-2-yl)-5-oxopentyl]guanidine
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2-(L-alanyl-L-arginyl)-1,3-benzothiazole
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hepatocyte activation inhibitor 1
HAI-1, inhibition of matriptase
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hepatocyte growth factor activator inhibitor type 2
HAI-2
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KNAR
more selective for matriptase compared to matriptase-2
L-arginyl-L-glutaminyl-N-[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-hydroxypentan-2-yl]-L-alaninamide
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L-arginyl-N1-[(2S)-1-[[(2R)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
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L-arginyl-N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
L-arginyl-N1-[(2S)-1-[[(2S)-6-amino-1-(1,3-benzothiazol-2-yl)-1-oxohexan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
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LWWR
2-fold selectivity for matriptase-2 against matriptase
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
inhibitor modeling in the wild-type enzyme active site, overview
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
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N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
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N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
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N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
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RNPR
more selective for matriptase compared to matriptase-2
WCYR
more selective for matriptase compared to matriptase-2
WRER
more selective for matriptase compared to matriptase-2
YYVR
13times more selective for matriptase-2 than matriptase
(1r,4r)-4-amino-N-(3,5-bis(4-carbamimidoylphenoxy)phenyl)cyclohexanecarboxamide
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(1r,4r)-4-aminocyclohexyl 3,5-bis(4-carbamimidoylphenoxy)benzoate
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(2R)-1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-2-carboxylic acid
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(2S)-1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-2-carboxylic acid
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1-(2-aminoethyl)-N-(3,5-bis(4-carbamimidoylphenoxy)phenyl)piperidine-4-carboxamide
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1-(3,5-bis(4-carbamimidoylphenoxy)benzoyl)piperidine-4-carboxylic acid
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1-(3-aminopropanoyl)-N-(3,5-bis(4-carbamimidoylphenoxy)phenyl)piperidine-4-carboxamide
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1-(N-[[3-(b-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-3-carboxamide
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1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-4-carboxamide
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2-Nas-Phe(3-Am)-4-(2-guanidinoethyl)piperidide
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3,5-bis(4-carbamimidoylphenoxy)-N-((4-hydroxycyclohexyl)methyl)benzamide
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3,5-bis(4-carbamimidoylphenoxy)-N-(1-(2-hydroxyethyl)piperidin-4-yl)benzamide
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3,5-bis(4-carbamimidoylphenoxy)-N-(4-fluorophenyl)benzamide
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3,5-bis(4-carbamimidoylphenoxy)-N-(4-hydroxycyclohexyl)benzamide
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3,5-bis(4-carbamimidoylphenoxy)-N-(4-methylcyclohexyl)benzamide
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3,5-bis(4-carbamimidoylphenoxy)-N-(cyclohexylmethyl)benzamide
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3,5-bis(4-carbamimidoylphenoxy)-N-cyclohexylbenzamide
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3,5-bis(4-carbamimidoylphenoxy)benzamide
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3-(3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-ethylbiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl)benzenecarboximidamide
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inhibitor completely prevents matriptase zymogen activation in human adenocarcinoma cell lines AsPC-1 and BxPC-3. Pro-urokinase-type plasminogen activator activation is completely abolished by matriptase inhibition. Matriptase inhibitors reduce the phosphorylation of the HGF receptor/cMet and the overall cellular invasiveness of the human pancreatic adenocarcinoma cell line AsPC-1
3-[(2R)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
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3-[(2R)-3-[4-(2-carbamimidamidoethyl)piperidin-1-yl]-2-[(naphthalen-2-ylsulfonyl)amino]propyl]benzenecarboximidamide
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3-[(2S)-2-([[3-(4-aminobutyl)phenyl]sulfonyl]amino)-3-[4-(2-aminoethyl)piperidin-1-yl]-3-oxopropyl]benzenecarboximidamide
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3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(1H-indol-5-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
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3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(2-methylpyrimidin-4-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
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3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-aminopyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
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3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[4'-(1-methylethoxy)biphenyl-3-yl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
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3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[(biphenyl-3-ylsulfonyl)amino]-3-oxopropyl]benzenecarboximidamide
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3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[(naphthalen-2-ylsulfonyl)amino]-3-oxopropoxy]benzenecarboximidamide
higher cytotoxic effect, enzyme-bound structure, crystal structure analysis, overview
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[([3-[(3-aminopropyl)amino]phenyl]sulfonyl)amino]-3-oxopropyl]benzenecarboximidamide
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3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(2'-chlorobiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
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3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(3',4'-dimethoxybiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
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3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(3'-chlorobiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
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3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-chlorobiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
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3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-ethoxybiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
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3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-ethylbiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
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3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-methoxybiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
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3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4-cyclohexylphenyl)sulfonyl]amino]-3-oxopropoxy]benzenecarboximidamide
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3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-3-oxo-2-([[2,4,6-tri(propan-2-yl)phenyl]sulfonyl]amino)propoxy]benzenecarboximidamide
higher cytotoxic effect
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-3-oxo-2-[[(3-pyridin-3-ylphenyl)sulfonyl]amino]propyl]benzenecarboximidamide
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3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-3-oxo-2-[[(3-pyridin-4-ylphenyl)sulfonyl]amino]propyl]benzenecarboximidamide
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3-[(2S)-3-[4-(4-aminobutanoyl)piperidin-1-yl]-3-oxo-2-([[2,4,6-tri(propan-2-yl)phenyl]sulfonyl]amino)propoxy]benzenecarboximidamide
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3-[(2S)-3-[4-(b-alanyl)piperidin-1-yl]-3-oxo-2-([[2,4,6-tri(propan-2-yl)phenyl]sulfonyl]amino)propoxy]benzenecarboximidamide
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3-[(2S)-3-[4-(N-carbamimidoyl-b-alanyl)piperazin-1-yl]-3-oxo-2-([[2,4,6-tris(1-methylethyl)phenyl]sulfonyl]amino)propyl]benzenecarboximidamide
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3-[3-[4-(2-carbamimidamidoethyl)piperidin-1-yl]-2-[(naphthalen-2-ylsulfonyl)amino]-3-oxopropyl]benzenecarboximidamide
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4,4'-((5-(1,2,3,4-tetrahydroisoquinoline-2-carbonyl)-1,3-phenylene)bis(oxy))dibenzimidamide
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4,4'-((5-(4-(2-aminoethyl)piperidine-1-carbonyl)-1,3-phenylene)bis(oxy))dibenzimidamide
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4,4'-((5-(4-fluorophenylsulfonamido)-1,3-phenylene)bis(oxy))dibenzimidamide
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4,4'-((5-(decahydroquinoline-1-carbonyl)-1,3-phenylene)bis(oxy))dibenzimidamide
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4,4'-((5-(naphthalene-2-sulfonamido)-1,3-phenylene)bis(oxy))dibenzimidamide
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4,4'-[(3-[[(4-fluorophenyl)sulfonyl]amino]pyridine-2,6-diyl)bis(oxy)]dibenzenecarboximidamide
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4,4'-[(5-aminobenzene-1,3-diyl)bis(oxy)]dibenzenecarboximidamide
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4,4'-[benzene-1,4-diylbis(oxy)]dibenzenecarboximidamide
binding structure, overview
4-(1-[3-carbamimidoyl-N-[(3-pyrrolidin-1-ylphenyl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
-
4-(1-[3-carbamimidoyl-N-[(4'-ethoxybiphenyl-3-yl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
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-
4-(1-[3-carbamimidoyl-N-[(4'-ethylbiphenyl-3-yl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
4-(1-[N-[(4'-tert-butylbiphenyl-3-yl)sulfonyl]-3-carbamimidoyl-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
-
4-(2-aminoethyl)-benzenesulfonylfluoride hydrochloride
-
AEBSF
4-(2-aminoethyl)benzenesulfonyl fluoride hydrochloride
4-([1-[(2S)-3-(3-carbamimidoylphenyl)-2-([[2,4,6-tris(1-methylethyl)phenyl]sulfonyl]amino)propanoyl]piperidin-4-yl]carbonyl)piperidine-1-carboximidamide
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4-([1-[(2S)-3-(3-carbamimidoylphenyl)-2-[[(4-cyclohexylphenyl)sulfonyl]amino]propanoyl]piperidin-4-yl]carbonyl)piperidine-1-carboximidamide
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inhibitor completely prevents matriptase zymogen activation in human adenocarcinoma cell lines AsPC-1 and BxPC-3. Pro-urokinase-type plasminogen activator activation is completely abolished by matriptase inhibition. Matriptase inhibitor reduce the phosphorylation of the HGF receptor/cMet and the overall cellular invasiveness of the human pancreatic adenocarcinoma cell line AsPC-1
4-aminobenzamidine
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weak competitive inhibition, competition assay with antibody inhibitors, overview
4-aminocyclohexyl 3,5-bis(4-carbamimidoylphenoxy)benzoate
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4-[(2-[[(2S)-6-carbamimidamido-1-oxohexan-2-yl]amino]-2-oxoethyl)carbamoyl]-6-methoxy-6-oxo-4-[3-(prop-1-en-2-yl)benzyl]hexanoic acid
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4-[1-(3-carbamimidoyl-N-[[3-(1H-imidazol-1-yl)phenyl]sulfonyl]-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
4-[1-(3-carbamimidoyl-N-[[3-(2-oxopiperazin-1-yl)phenyl]sulfonyl]-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
4-[1-(3-carbamimidoyl-N-[[3-(2-oxopiperidin-1-yl)phenyl]sulfonyl]-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
4-[1-(3-carbamimidoyl-N-[[3-(6-oxopyridazin-1(6H)-yl)phenyl]sulfonyl]-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
4-[1-(N-[[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
4-[1-(N-[[3-(6-aminopyridin-3-yl)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
4-[1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
4-[1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]butanamide
-
-
4-[1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]butanoic acid
-
-
4-[4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazin-1-yl]-N-methyl-4-oxobutanamide
-
-
9-fluorenylmethyloxycarbonyl-GR-ketobenzothiazole
potent and selective inhibitor for matriptase over hepsin
alpha-1-antitrypsin
-
-
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alpha-2-Antiplasmin
-
-
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alpha1-antitrypsin
-
AAT
-
anti-matriptase LDL receptor domain 3-specific monoclonal antibodies
-
complete inhibition of enzyme activation
-
antisense-matripase
-
significantly reduces matripase protein expression by 70-80%, anti-tumoral activity on HRA cells intraperitoneal injected into nude mice
-
ARCTKSIPPICFPD
a mutant of sunflower trypsin inhibitor-18
benzyl 4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazine-1-carboxylate
benzylsulfonyl-D-arginyl-proline-(2-aminomethyl-5-chlorobenzyl)-amide bis(trifluoroacetate)
-
-
benzylsulfonyl-D-arginyl-proline-(4-amidinobenzyl)amide bis-(trifluoroacetate)
-
-
benzylsulfonyl-D-cyclohexylalanyl-proline-(2-aminomethyl-5-chlorobenzyl)amide
-
-
benzylsulfonyl-D-cyclohexylalanyl-proline-(4-amidinobenzyl)-amide
-
-
Bovine pancreatic trypsin inhibitor
-
BPTI
-
CJ-730
-
3-amidinophenylalanine-based inhibitor CJ-730, completely inhibits pro-HGF activation in PC3 cells
CVS-3983
a selective arginal-derived matriptase inhibitor
D-hTyr-Ala-4-amidinobenzylamide
compound has a 10fold reduced activity against thrombin and factor Xa
diisopropylfluorophosphate
-
complete inhibition at 5 mM
ethyl (3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)carbamate
-
ethyl 4-(3,5-bis(4-carbamimidoylphenoxy)benzamido)piperidine-1-carboxylate
-
ethyl 4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazine-1-carboxylate
-
-
GACTKSIPPICFPD
a mutant of sunflower trypsin inhibitor-17
GAVCPKILKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGACPKILKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGRCPKALKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGRCPKILKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCAKILKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPAILKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKALKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKIAKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKILAKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKILKACRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKILKKCRRDSDCPGACICRGAGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKILKKCRRDSDCPGACICRGNGACGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKILKKCRRDSDCPGACICRGNGYCASGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKILKKCRRDSDCPGACICRGNGYCGAGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKRLKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPRILKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GKCTKSIPPICFPD
a mutant of sunflower trypsin inhibitor-6
GRCAKSIPPICFPD
a mutant of sunflower trypsin inhibitor-16
GRCTASIPPICFPD
a mutant of sunflower trypsin inhibitor-15
GRCTKAIPPICFPD
a mutant of sunflower trypsin inhibitor-14
GRCTKSAPPICFPD
a mutant of sunflower trypsin inhibitor-13
GRCTKSAPPRCFPD
a mutant of sunflower trypsin inhibitor-1
GRCTKSIAPICFPD
a mutant of sunflower trypsin inhibitor-12
GRCTKSIPAICFPD
a mutant of sunflower trypsin inhibitor-11
GRCTKSIPPACFPD
a mutant of sunflower trypsin inhibitor-10
GRCTKSIPPDCFPD
a mutant of sunflower trypsin inhibitor-3
GRCTKSIPPGCFPD
a mutant of sunflower trypsin inhibitor-2
GRCTKSIPPICAPD
a mutant of sunflower trypsin inhibitor-9
GRCTKSIPPICFAD
a mutant of sunflower trypsin inhibitor-8
GRCTKSIPPICFPA
a mutant of sunflower trypsin inhibitor-7
GRCTKSIPPKCFPD
a mutant of sunflower trypsin inhibitor-0
GRCTKSIPPRCFPD
a mutant of sunflower trypsin inhibitor-1
GRCTKSRPPICFPD
a mutant of sunflower trypsin inhibitor-4
GRCTRSIPPICFPD
a mutant of sunflower trypsin inhibitor-5
HAI-1
-
inhibitor of matriptase in skin
hepatcyte growth factor activator inhibitor-1
-
in normal skin matriptase is complexed to hepatcyte growth factor activator inhibitor-1 wheras in squamous cell carcinoma the enzyme is present in an unassociated form
-
hepatocyte growth factor activator inhibitor
-
hepatocyte growth factor activator inhibitor 1
-
hepatocyte growth factor activator inhibitor-1
-
hepatocyte growth factor activator inhibitor-2
-
HAI-2
-
L-arginyl-N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
EC50 is 0.00564-0.0068 mM, the inhibitor contains a ketobenzothiazole serine trap designed based on matriptase's auto-catalytic domain (RQAR), it is a selective, slow, tight-binding inhibitor of matriptase that significantly reduces viral replication of H1N1 influenza virus, including the 2009 pandemic virus
methyl (2R)-1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-2-carboxylate
-
-
methyl (2S)-1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-2-carboxylate
-
-
methyl 4-[1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]butanoate
-
-
N-((1r,4r)-4-aminocyclohexyl)-3,5-bis((3-carbamimidoylbenzyl)oxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3,5-bis((4-carbamimidoylbenzyl)oxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3,5-bis(4-(aminomethyl)phenoxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-((3-carbamimidoylbenzyl)oxy)-5-(4-carbamimidoylphenoxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-((4-bromobenzyl)oxy)-5-(4-carbamimidoylphenoxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-((4-carbamimidoylbenzyl)oxy)-5-(4-carbamimidoylphenoxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-((6-aminopyridin-3-yl)oxy)-5-(4-carbamimidoylphenoxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-((6-bromopyridin-3-yl)methoxy)-5-(4-carbamimidoylphenoxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-(4-(3-aminopropanamido)phenoxy)-5-(4-carbamimidoylphenoxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-(4-(aminomethyl)phenoxy)-5-(4-carbamimidoylphenoxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-(4-aminophenoxy)-5-(4-carbamimidoylphenoxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-(4-carbamimidoylphenoxy)-5-((4-chlorobenzyl)oxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-(4-carbamimidoylphenoxy)-5-(4-carbamoylphenoxy)benzamide
-
N-(1-(3-aminopropyl)piperidin-4-yl)-3,5-bis(4-carbamimidoylphenoxy)benzamide
-
N-(2-aminoethyl)-1-(3-carbamimidoyl-N-[[2,4,6-tris(1-methylethyl)phenyl]sulfonyl]-L-phenylalanyl)piperidine-4-carboxamide
-
N-(3,5-bis(4-carbamimidoylphenoxy)phenyl)-1-(2-hydroxyethyl)piperidine-4-carboxamide
-
N-(3-[[(1R)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)ethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-(2-methylpiperidin-1-yl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-(4-methylpiperidin-1-yl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-oxo-2-piperazin-1-ylethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-oxo-2-piperidin-1-ylethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-[4-[4-(methylamino)-4-oxobutyl]piperidin-1-yl]-2-oxoethyl]sulfamoyl]phenyl)azetidine-3-carboxamide
-
-
N-(3-[[(1S)-1-[[4-(2-aminoethyl)piperidin-1-yl]carbonyl]-3-phenylpropyl]sulfamoyl]phenyl)-beta-alaninamide
-
N-(3-[[(1S)-1-[[4-(2-aminoethyl)piperidin-1-yl]carbonyl]-4-phenylbutyl]sulfamoyl]phenyl)-beta-alaninamide
-
N-(3-[[(1S)-2-(4-benzylpiperidin-1-yl)-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-3-hydroxypropanamide
-
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-b-alaninamide
-
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)azetidine-3-carboxamide
-
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)propanamide
-
N-(3-[[(1S)-2-[4-(2-carbamimidamidoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
N-(3-[[(2S)-1-[4-(2-aminoethyl)piperidin-1-yl]-3-(3-carbamimidoylphenyl)-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
-
inhibitor completely prevents matriptase zymogen activation in human adenocarcinoma cell lines AsPC-1 and BxPC-3. Pro-urokinase-type plasminogen activator activation is completely abolished by matriptase inhibition. Matriptase inhibitors reduce the phosphorylation of the HGF receptor/cMet and the overall cellular invasiveness of the human pancreatic adenocarcinoma cell line AsPC-1
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-oxo-1-(piperazin-1-yl)propan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
-
inhibitor completely prevents matriptase zymogen activation in human adenocarcinoma cell lines AsPC-1 and BxPC-3. Pro-urokinase-type plasminogen activator activation is completely abolished by matriptase inhibition. Matriptase inhibitors reduce the phosphorylation of the HGF receptor/cMet and the overall cellular invasiveness of the human pancreatic adenocarcinoma cell line AsPC-1
N-(4-aminocyclohexyl)-3,5-bis(4-carbamimidoylphenoxy)benzamide
-
N-(4-aminocyclohexyl)-O-(3-carbamimidoylphenyl)-N2-(naphthalen-2-ylsulfonyl)-L-serinamide
-
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
-
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
-
N-[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-[3-(aminomethyl)benzyl]-2-oxoethyl]-4'-methoxybiphenyl-3-sulfonamide
-
N-[3-([(1S)-1-(3-carbamimidoylbenzyl)-2-[4-(4-hydroxyphenyl)piperazin-1-yl]-2-oxoethyl]sulfamoyl)phenyl]-beta-alaninamide
-
-
N-[3-([(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-benzyl-2-oxoethyl]sulfamoyl)phenyl]-beta-alaninamide
-
N-[3-([(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-[3-(aminomethyl)benzyl]-2-oxoethyl]sulfamoyl)phenyl]-beta-alaninamide
-
N-[3-([(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-[4-(aminomethyl)benzyl]-2-oxoethyl]sulfamoyl)phenyl]-beta-alaninamide
-
N-[3-([1-[4-(2-aminoethyl)piperidin-1-yl]-3-(3-carbamimidoylphenyl)-1-oxopropan-2-yl]sulfamoyl)phenyl]-b-alaninamide
-
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
-
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
-
O-(3-carbamimidoylphenyl)-N-(4-methylcyclohexyl)-N2-(naphthalen-2-ylsulfonyl)-L-serinamide
-
plasminogen activator inhibitor I
-
-
-
R1K'4-eglin
-
different eglin c variants with differing inhibitory potential versus matriptase, construction, expression and purification of eglin c variants and screening for inhibitory potency, overview, R1K'4-eglin has the wild-type Pro45 at P1 position and Tyr49 at P4' position residues replaced with Arg and Lys, respectively, leads to the production of a selective, high affinity and proteolytically stable inhibitor of matriptase, molecular modeling of enzyme-inhibitor complex, overview
R1K4-eglin
-
wild type eglin c with Pro45 at P1 position and Tyr49 residues at P4 position replaced with Arg and Lys respectively, most potent, selective, high affinity and proteolytically stable inhibitor
R4R1-eglin
-
with substituted P42 and L45 for arginine residues, variants containing an Arg or Lys at position 49 instead of the original Tyr residue show enhanced inhibition
scFv antibody E2
-
competitive mechanism of inhibition of the scFv antibody enzyme inhibitors, which competes with substrate binding in the S1 site, the antibody binds to a number of residues flanking the active site, forming a unique three-dimensional binding epitope
-
scFv antibody S4
-
competitive mechanism of inhibition of the scFv antibody enzyme inhibitors, which competes with substrate binding in the S1 site, the antibody binds to a number of residues flanking the active site, forming a unique three-dimensional binding epitope
-
single chain variable fragment of antibodies
-
different variants
-
sulfated 3-amidinophenylalanine derivatives
deiverse variants, overview
-
sulfonylated 3-amidino-phenylalanine inhibitors
-
-
-
sunflower trypsin inhibitor
-
SFTI-1
-
sunflower trypsin inhibitor-1
sunflower trypsin inhibitor-2
-
SFTI-2
sunflower trypsin inhibitor-3
-
SFTI-3
L-arginyl-N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
-
L-arginyl-N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
docking of the inhibitor in the active site of matriptase, structure, overview
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
inhibitor completely prevents matriptase zymogen activation in human adenocarcinoma cell lines AsPC-1 and BxPC-3. Pro-urokinase-type plasminogen activator activation is completely abolished by matriptase inhibition. Matriptase inhibitors reduce the phosphorylation of the HGF receptor/cMet and the overall cellular invasiveness of the human pancreatic adenocarcinoma cell line AsPC-1
4-(1-[3-carbamimidoyl-N-[(4'-ethylbiphenyl-3-yl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
-
4-(1-[3-carbamimidoyl-N-[(4'-ethylbiphenyl-3-yl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
inhibitor completely prevents matriptase zymogen activation in human adenocarcinoma cell lines AsPC-1 and BxPC-3. Pro-urokinase-type plasminogen activator activation is completely abolished by matriptase inhibition. Matriptase inhibitors reduce the phosphorylation of the HGF receptor/cMet and the overall cellular invasiveness of the human pancreatic adenocarcinoma cell line AsPC-1
4-(2-aminoethyl)benzenesulfonyl fluoride hydrochloride
-
-
4-(2-aminoethyl)benzenesulfonyl fluoride hydrochloride
-
inhibition of IGFBP-rP1 processing
Aprotinin
-
-
Aprotinin
-
inhibition of IGFBP-rP1 processing
benzyl 4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazine-1-carboxylate
-
-
benzyl 4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazine-1-carboxylate
-
inhibitor completely prevents matriptase zymogen activation in human adenocarcinoma cell lines AsPC-1 and BxPC-3. Pro-urokinase-type plasminogen activator activation is completely abolished by matriptase inhibition. Matriptase inhibitors reduce the phosphorylation of the HGF receptor/cMet and the overall cellular invasiveness of the human pancreatic adenocarcinoma cell line AsPC-1
hepatocyte growth factor activator inhibitor
-
HAI-1
-
hepatocyte growth factor activator inhibitor
-
HAI-1, the cognate transmembrane inhibitor of the enzyme, which is coexpressed with matriptase in epithelium
-
hepatocyte growth factor activator inhibitor
HAI-1, conventional protease inhibitor
-
hepatocyte growth factor activator inhibitor
-
active protease is inhibited by, and forms complexes with, hepatocyte growth factor activator inhibitor (HAI-1)
-
hepatocyte growth factor activator inhibitor 1
-
following matriptase activation, the active enzyme is immediately inhibited by binding to hepatocyte growth factor activator inhibitor 1, resulting in stable matriptase-hepatocyte growth factor activator inhibitor 1 complexes that are rapidly secreted
-
hepatocyte growth factor activator inhibitor 1
-
HAI-1, a Kunitz-type inhibitor that functions both as a chaperone and a reversible inhibitor
-
hepatocyte growth factor activator inhibitor-1
-
-
-
hepatocyte growth factor activator inhibitor-1
i.e. HAI-1, binding is reversible and acid labile
-
hepatocyte growth factor activator inhibitor-1
-
HAI-1
-
hepatocyte growth factor activator inhibitor-1
HAI-1
-
hepatocyte growth factor activator inhibitor-1
-
HAI-1, a Kunitz-type transmembrane serine protease inhibitor, cognate inhibitor of matriptase with regulatory function, molecular mechanism of inhibition, domain structure of HAI-1, proteolytic processing during maturation, activation, and shedding, enzyme-inhibitor complex structure, overview, the level of HAI-1 expression seems to be an important factor in the regulation of matriptase zymogen activation
-
hepatocyte growth factor activator inhibitor-1
-
HAI-1, forms complexes wih the enzyme in vivo
-
hepatocyte growth factor activator inhibitor-1
-
HAI-1, without HAI-1 active matriptase may become unstable, leading to its degradation and low protein expression
-
hepatocyte growth factor activator inhibitor-1
-
is required for proper development of placenta, overview
-
hepatocyte growth factor activator inhibitor-1
-
activated matriptase is immediately inhibited by and forms complex with hepatocyte growth factor activator inhibitor-1
-
hexamidine
-
hexamidine
and its structural analogs
sunflower trypsin inhibitor-1
-
and several derivatives with different amino acid side chains, overview
sunflower trypsin inhibitor-1
-
SFTI-1, isolated from sunflower seeds
sunflower trypsin inhibitor-1
SFTI-1, GRCTKSIPPICFPD, the plant-derived cyclic peptide is a promising drug scaffold with potent matriptase inhibitory activity, three-dimensional structure of the inhibitor and the protease domain of matriptase, molecular modeling, overview
additional information
analysis of interaction of matriptase-2 with prototype low-molecular weight ligands using site-directed mutagenesis, kinetic analysis and molecular modeling, substrate/inhibitor-enzyme interactions, overview
-
additional information
analysis of interaction of matriptase-2 with prototype low-molecular weight ligands using site-directed mutagenesis, kinetic analysis and molecular modeling, substrate/inhibitor-enzyme interactions, overview
-
additional information
design and synthesis of potent, selective inhibitors of matriptase, overview. Design of a class of potent and selective peptidomimetic inhibitors of matriptase based on the P4-P1 (Arg-Gln-Ala-Arg) portion of the activation peptide of matriptase, to which is linked a C-terminal serine trap in the form of a ketobenzothiazole group. The ketobenzothiazole serine trap is selected to form a covalent and reversible bond with the catalytic serine residue of the enzyme. Importance of stereochemistry at the P1 position for inhibitory potency
-
additional information
peptide inhibitor docking study with matriptase and matriptase-2, overview
-
additional information
-
not inhibited by leupeptin, pepstatin and N-(R)-(2-(hydroxyaminocarbonyl)methyl)-4-methylpentanoyl-L-3-(2'-naphthyl)alaninyl-L-alanine 2-aminoethyl amide
-
additional information
-
wild type eglin c has no effect
-
additional information
-
autoinhibitory role of the LDLRA modules that may prevent premature activation of matriptase in the absence of appropriate activation stimuli
-
additional information
-
inhibition of matriptase activation in vitro and in vivo, overview
-
additional information
-
inhibitor design and synthesis, inhibitory potency and structure-activity relationships, overview, matriptase blockade could potentially modulate tumorigenesis and metastasis in vivo
-
additional information
-
inhibitor synthesis and validation, overview
-
additional information
-
no inhibition of IGFBP-rP1 processing by leupeptin, pepstatin, and N-(R)-(2-(hydroxyaminocarbonyl)methyl)-4-methylpentanoyl-l-3-(2'-naphthyl)alaninyl-l-alanine 2-aminoethyl amide, i.e. TAPI-1
-
additional information
controlled by a serpin complex, consisting of antithrombin III, alpha1-antitrypsin and alpha2-antiplasmin
-
additional information
-
controlled by a serpin complex, consisting of antithrombin III, alpha1-antitrypsin and alpha2-antiplasmin
-
additional information
-
the enzyme is competitively inhibited by the anti-MT-SP1 antibody FabE2
-
additional information
inhibitor design, synthesis of diverse 5-substituted phenylene1,3-bis(oxy) dibenzimidamide analogues, overview. Anaysis of cytotoxic effects of inhibitors
-
additional information
-
inhibitor design, synthesis of diverse 5-substituted phenylene1,3-bis(oxy) dibenzimidamide analogues, overview. Anaysis of cytotoxic effects of inhibitors
-
additional information
O-(3-carbamimidoylphenyl)-L-serine amides as matriptase inhibitors, overview. Analysis of cytotoxic effects of inhibitors
-
additional information
synthesis of high-affinity cyclic peptide matriptase inhibitors. An analogue of Momordica cochinchinensis trypsin inhibitor-II (MCoTI-II) is one of the most potent inhibitors of matriptase, structure-activity relationships of SFTI-1 and MCoTI-II, which is a structurally divergent trypsin inhibitor also containing a cyclic backbone
-
additional information
generation of monoclonal antibodies against mutant N164Q/R614A and use as inhibitors. Two antibodies are competitive inhibitors and able to block the activity of wild-type full-length matriptase in complex biological samples by binding near the active site
-
additional information
-
generation of monoclonal antibodies against mutant N164Q/R614A and use as inhibitors. Two antibodies are competitive inhibitors and able to block the activity of wild-type full-length matriptase in complex biological samples by binding near the active site
-
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Acidosis
Matriptase activation and shedding through PDGF-D-mediated extracellular acidosis.
Acidosis
Matriptase activation, an early cellular response to acidosis.
Adenocarcinoma
A novel biomarker for staging human prostate adenocarcinoma: overexpression of matriptase with concomitant loss of its inhibitor, hepatocyte growth factor activator inhibitor-1.
Adenocarcinoma
Decreased matriptase/HAI-1 ratio in advanced colorectal adenocarcinoma of Chinese patients.
Adenocarcinoma
Expression and prognostic value of matriptase in ovarian serous adenocarcinoma.
Adenocarcinoma
Increasing expression of serine protease matriptase in ovarian tumors: tissue microarray analysis of immunostaining score with clinicopathological parameters.
Adenocarcinoma
Matriptase activation and shedding with HAI-1 is induced by steroid sex hormones in human prostate cancer cells, but not in breast cancer cells.
Adenocarcinoma
Paradoxically enhanced immunoreactivity of hepatocyte growth factor activator inhibitor type 1 (HAI-1) in cancer cells at the invasion front.
Adenocarcinoma
Targeted HAI-2 deletion causes excessive proteolysis with prolonged active prostasin and depletion of HAI-1 monomer in intestinal but not epidermal epithelial cells.
Adenocarcinoma
The androgen-regulated type II serine protease TMPRSS2 is differentially expressed and mislocalized in prostate adenocarcinoma.
Adenocarcinoma
The novel serine protease tumor-associated differentially expressed gene-15 (matriptase/MT-SP1) is highly overexpressed in cervical carcinoma.
Adenocarcinoma
Use of IHC and newly designed matriptase inhibitors to elucidate the role of matriptase in pancreatic ductal adenocarcinoma.
Adenocarcinoma, Mucinous
Increasing expression of serine protease matriptase in ovarian tumors: tissue microarray analysis of immunostaining score with clinicopathological parameters.
Adenoma
Co-expression of matriptase and N-acetylglucosaminyltransferase V in thyroid cancer tissues--its possible role in prolonged stability in vivo by aberrant glycosylation.
Adenoma
The ratio of Matriptase/HAI-1 mRNA is higher in colorectal cancer adenomas and carcinomas than corresponding tissue from control individuals.
Anemia
A critical role for murine transferrin receptor 2 in erythropoiesis during iron restriction.
Anemia
A genome-wide meta-analysis yields 46 new loci associating with biomarkers of iron homeostasis.
Anemia
A mutation in the TMPRSS6 gene, encoding a transmembrane serine protease that suppresses hepcidin production, in familial iron deficiency anemia refractory to oral iron.
Anemia
A novel homozygous nonsense mutation (p.Y78*) in TMPRSS6 gene causing iron-refractory iron deficiency anemia (IRIDA) in two siblings.
Anemia
A novel mutation Gly603Arg of TMPRSS6 in a Korean female with iron-refractory iron deficiency anemia.
Anemia
A Novel mutation in the CUB sequence of matriptase-2 (Tmprss6) is implicated in iron-resistant iron deficiency anaemia (IRIDA).
Anemia
A novel mutation in the CUB sequence of matriptase-2 (TMPRSS6) is implicated in iron-resistant iron deficiency anaemia - response to Jaspers et al.
Anemia
A novel splice site mutation c.2278 (-1) G>C in the TMPRSS6 gene causes deletion of the substrate binding site of the serine protease resulting in refractory iron deficiency anaemia.
Anemia
A novel splicing mutation of TMPRSS6 in a Chinese child with iron-refractory iron deficiency anaemia.
Anemia
A novel tri-allelic mutation of TMPRSS6 in iron-refractory iron deficiency anaemia with response to glucocorticoid.
Anemia
A strong anti-inflammatory signature revealed by liver transcription profiling of Tmprss6-/- mice.
Anemia
An RNAi therapeutic targeting Tmprss6 decreases iron overload in Hfe(-/-) mice and ameliorates anemia and iron overload in murine ?-thalassemia intermedia.
Anemia
Anaemia, iron deficiency and a common polymorphism of iron-regulation, TMPRSS6 rs855791, in Rwandan children.
Anemia
Associations of Common Variants in HFE and TMPRSS6 Genes with Hepcidin-25 and Iron Status Parameters in Patients with End-Stage Renal Disease.
Anemia
Candidate gene sequencing of SLC11A2 and TMPRSS6 in a family with severe anaemia: common SNPs, rare haplotypes, no causative mutation.
Anemia
Combination therapy with a Tmprss6 RNAi-therapeutic and the oral iron chelator deferiprone additively diminishes secondary iron overload in a mouse model of ?-thalassemia intermedia.
Anemia
Cryptic splice site usage leading to truncated TMPRSS6 is responsible for Iron Refractory Iron Deficiency Anaemia (IRIDA) in an Italian Family.
Anemia
Deletion of TMPRSS6 attenuates the phenotype in a mouse model of ?-thalassemia.
Anemia
EPO-mediated reduction in Hamp expression in vivo corrects iron deficiency anaemia in TMPRSS6 deficiency.
Anemia
Evaluation of the level of selected iron-related proteins/receptors in the liver of rats during separate/combined vanadium and magnesium administration.
Anemia
Functional analysis of Matriptase-2 mutations and domains: Insights into the molecular basis of iron refractory iron deficiency anemia.
Anemia
Functional diversity of TMPRSS6 isoforms and variants expressed in hepatocellular carcinoma cell lines.
Anemia
Genetic analysis of TMPRSS6 gene in Saudi female patients with iron deficiency anemia.
Anemia
Genetic variability of TMPRSS6 and its association with iron deficiency anaemia.
Anemia
Global loss of Tfr2 with concomitant induced iron deficiency greatly ameliorates the phenotype of a murine thalassemia intermedia model.
Anemia
Haematologic data, iron parameters and molecular findings in two new cases of iron-refractory iron deficiency anaemia.
Anemia
Immunoassay for human serum hemojuvelin.
Anemia
Inter-ethnic differences in genetic variants within the transmembrane protease, serine 6 (TMPRSS6) gene associated with iron status indicators: a systematic review with meta-analyses.
Anemia
Iron and hepcidin: a story of recycling and balance.
Anemia
Iron deficiency anemia due to matriptase-2 inactivation is dependent upon the presence of functional Bmp6.
Anemia
Iron deficiency anemia refractory to iron preparations.
Anemia
Iron disorders of genetic origin: a changing world.
Anemia
Iron distribution in different tissues of homozygous Mask (msk/msk) mice and the effects of oral iron treatments.
Anemia
Iron Refractory Iron Deficiency Anaemia: A Rare Cause of Iron Deficiency Anaemia.
Anemia
Iron Refractory Iron Deficiency Anemia (IRIDA): A heterogeneous disease that is not always iron refractory.
Anemia
Iron Refractory Iron Deficiency Anemia Due to 374 Base Pairs Deletion in the TMPRSS6 Gene.
Anemia
Iron Refractory Iron Deficiency Anemia in Dizygotic Twins Due to a Novel TMPRSS6 Gene Mutation in Addition to Polymorphisms Associated With High Susceptibility to Develop Ferropenic Anemia.
Anemia
Iron refractory iron deficiency anemia.
Anemia
Iron refractory iron deficiency anemia: presentation with hyperferritinemia and response to oral iron therapy.
Anemia
Iron-refractory iron deficiency anemia (IRIDA) cases with 2 novel TMPRSS6 mutations.
Anemia
Iron-refractory iron deficiency anemia (IRIDA).
Anemia
Iron-refractory iron deficiency anemia: new molecular mechanisms.
Anemia
Is EPO therapy able to correct iron deficiency anaemia caused by matriptase-2 deficiency?
Anemia
Is the acronym IRIDA acceptable for slow responders to iron in the presence of TMPRSS6 mutations?
Anemia
Limiting hepatic Bmp-Smad signaling by matriptase-2 is required for erythropoietin-mediated hepcidin suppression in mice.
Anemia
Liver hemojuvelin protein levels in mice deficient in matriptase-2 (Tmprss6).
Anemia
Liver HFE protein content is posttranscriptionally decreased in iron-deficient mice and rats.
Anemia
Low Iron Promotes Megakaryocytic Commitment of Megakaryocytic-Erythroid Progenitors in Humans and Mice.
Anemia
Matriptase-2 (TMPRSS6): a proteolytic regulator of iron homeostasis.
Anemia
Matriptase-2 is essential for hepcidin repression during fetal life and postnatal development in mice to maintain iron homeostasis.
Anemia
Matriptase-2 mutations in iron-refractory iron deficiency anemia patients provide new insights into protease activation mechanisms.
Anemia
Matriptase-2: monitoring and inhibiting its proteolytic activity.
Anemia
Microcytic anaemia with low transferrin saturation, increased serum hepcidin and non-synonymous TMPRSS6 variants: not always iron-refractory iron deficiency anaemia.
Anemia
Mild iron deficiency does not ameliorate the phenotype of a murine erythropoietic protoporphyria model.
Anemia
Molecular mechanisms of the defective hepcidin inhibition in TMPRSS6 mutations associated with iron-refractory iron deficiency anemia.
Anemia
Mutations in TMPRSS6 cause iron-refractory iron deficiency anemia (IRIDA).
Anemia
N-glycosylation is required for matriptase-2 autoactivation and ectodomain shedding.
Anemia
Novel missense mutation in the TMPRSS6 gene in a Japanese female with iron-refractory iron deficiency anemia.
Anemia
Novel mutation in the TMPRSS6 gene with iron-refractory iron deficiency anemia.
Anemia
Novel TMPRSS6 mutations associated with iron-refractory iron deficiency anemia (IRIDA).
Anemia
Polymorphisms and mutations of human TMPRSS6 in iron deficiency anemia.
Anemia
Progress in iron metabolism research.
Anemia
Rapid, accurate detection of TMPRSS6 gene causative mutations with a high-resolution melting assay.
Anemia
Regulation of TMPRSS6 by BMP6 and iron in human cells and mice.
Anemia
Regulation of type II transmembrane serine proteinase TMPRSS6 by hypoxia-inducible factors: new link between hypoxia signalling & iron homeostasis.
Anemia
Responsiveness to oral iron and ascorbic acid in a patient with IRIDA.
Anemia
RNAi-mediated reduction of hepatic Tmprss6 diminishes anemia and secondary iron overload in a splenectomized mouse model of ?-thalassemia intermedia.
Anemia
Role of TMPRSS6 rs855791 (T > C) polymorphism in reproductive age women with iron deficiency anemia from Lahore, Pakistan.
Anemia
Severe microcytic anemia but increased erythropoiesis in mice lacking Hfe or Tfr2 and Tmprss6.
Anemia
SLN124, a GalNac-siRNA targeting transmembrane serine protease 6, in combination with deferiprone therapy reduces ineffective erythropoiesis and hepatic iron-overload in a mouse model of ?-thalassaemia.
Anemia
Systematic evaluation of paediatric cohort with iron refractory iron deficiency anaemia (IRIDA) phenotype reveals multiple TMPRSS6 gene variations.
Anemia
The role of TMPRSS6 and HFE variants in iron deficiency anemia in celiac disease.
Anemia
The role of TMPRSS6 gene variants in iron-related hematological parameters in Turkish patients with iron deficiency anemia.
Anemia
The role of TMPRSS6 polymorphisms in iron deficiency anemia partially responsive to oral iron treatment.
Anemia
The role of TMPRSS6/matriptase-2 in iron regulation and anemia.
Anemia
The serine protease matriptase-2 (TMPRSS6) inhibits hepcidin activation by cleaving membrane hemojuvelin.
Anemia
Tmprss6 is a genetic modifier of the Hfe-hemochromatosis phenotype in mice.
Anemia
TMPRSS6 rs855791 polymorphism and susceptibility to iron deficiency anaemia in non-dialysis chronic kidney disease patients in South Africa.
Anemia
TMPRSS6 rs855791 polymorphism influences the susceptibility to iron deficiency anemia in women at reproductive age.
Anemia
TMPRSS6 rs855791 Polymorphism Status in Children with Celiac Disease and Anemia.
Anemia
TMPRSS6, but not TF, TFR2 or BMP2 variants are associated with increased risk of iron-deficiency anemia.
Anemia
Two nonsense mutations in the TMPRSS6 gene in a patient with microcytic anemia and iron deficiency.
Anemia
Two novel mutations in TMPRSS6 associated with iron-refractory iron deficiency anemia in a mother and child.
Anemia
Two Novel TMPRSS6 Variants in a Compound Heterozygous Child With Iron Refractory Iron Deficiency Anemia (IRIDA).
Anemia
Very high frequency of TMPRSS6 gene variations in iron deficiency anaemia of patients with polyendocrine autoimmune syndromes: more than a casual association?
Anemia
[Iron deficiency anaemia due to a matriptase-2 mutation].
Anemia
[Iron deficiency and overload. Implications in oxidative stress and cardiovascular health]
Anemia
[Iron metabolism and iron-refractory iron deficiency anemia].
Anemia, Iron-Deficiency
A child with severe iron-deficiency anemia and a complex TMPRSS6 genotype.
Anemia, Iron-Deficiency
A genome-wide meta-analysis yields 46 new loci associating with biomarkers of iron homeostasis.
Anemia, Iron-Deficiency
A mutation in the TMPRSS6 gene, encoding a transmembrane serine protease that suppresses hepcidin production, in familial iron deficiency anemia refractory to oral iron.
Anemia, Iron-Deficiency
A novel homozygous nonsense mutation (p.Y78*) in TMPRSS6 gene causing iron-refractory iron deficiency anemia (IRIDA) in two siblings.
Anemia, Iron-Deficiency
A novel mutation Gly603Arg of TMPRSS6 in a Korean female with iron-refractory iron deficiency anemia.
Anemia, Iron-Deficiency
A Novel mutation in the CUB sequence of matriptase-2 (Tmprss6) is implicated in iron-resistant iron deficiency anaemia (IRIDA).
Anemia, Iron-Deficiency
A novel mutation in the CUB sequence of matriptase-2 (TMPRSS6) is implicated in iron-resistant iron deficiency anaemia - response to Jaspers et al.
Anemia, Iron-Deficiency
A novel splice site mutation c.2278 (-1) G>C in the TMPRSS6 gene causes deletion of the substrate binding site of the serine protease resulting in refractory iron deficiency anaemia.
Anemia, Iron-Deficiency
A novel splicing mutation of TMPRSS6 in a Chinese child with iron-refractory iron deficiency anaemia.
Anemia, Iron-Deficiency
A novel tri-allelic mutation of TMPRSS6 in iron-refractory iron deficiency anaemia with response to glucocorticoid.
Anemia, Iron-Deficiency
A strong anti-inflammatory signature revealed by liver transcription profiling of Tmprss6-/- mice.
Anemia, Iron-Deficiency
Candidate gene sequencing of SLC11A2 and TMPRSS6 in a family with severe anaemia: common SNPs, rare haplotypes, no causative mutation.
Anemia, Iron-Deficiency
Cryptic splice site usage leading to truncated TMPRSS6 is responsible for Iron Refractory Iron Deficiency Anaemia (IRIDA) in an Italian Family.
Anemia, Iron-Deficiency
EPO-mediated reduction in Hamp expression in vivo corrects iron deficiency anaemia in TMPRSS6 deficiency.
Anemia, Iron-Deficiency
Functional analysis of Matriptase-2 mutations and domains: Insights into the molecular basis of iron refractory iron deficiency anemia.
Anemia, Iron-Deficiency
Functional and clinical impact of novel TMPRSS6 variants in iron-refractory iron-deficiency anemia patients and genotype-phenotype studies.
Anemia, Iron-Deficiency
Functional diversity of TMPRSS6 isoforms and variants expressed in hepatocellular carcinoma cell lines.
Anemia, Iron-Deficiency
Genetic analysis of TMPRSS6 gene in Saudi female patients with iron deficiency anemia.
Anemia, Iron-Deficiency
Genetic variability of TMPRSS6 and its association with iron deficiency anaemia.
Anemia, Iron-Deficiency
Haematologic data, iron parameters and molecular findings in two new cases of iron-refractory iron deficiency anaemia.
Anemia, Iron-Deficiency
Immunoassay for human serum hemojuvelin.
Anemia, Iron-Deficiency
Inactive matriptase-2 mutants found in IRIDA patients still repress hepcidin in a transfection assay despite having lost their serine protease activity.
Anemia, Iron-Deficiency
Into the matrix: regulation of the iron regulatory hormone hepcidin by matriptase-2.
Anemia, Iron-Deficiency
Iron deficiency anemia due to matriptase-2 inactivation is dependent upon the presence of functional Bmp6.
Anemia, Iron-Deficiency
Iron deficiency anemia refractory to iron preparations.
Anemia, Iron-Deficiency
Iron disorders of genetic origin: a changing world.
Anemia, Iron-Deficiency
Iron distribution in different tissues of homozygous Mask (msk/msk) mice and the effects of oral iron treatments.
Anemia, Iron-Deficiency
Iron Refractory Iron Deficiency Anaemia: A Rare Cause of Iron Deficiency Anaemia.
Anemia, Iron-Deficiency
Iron Refractory Iron Deficiency Anemia (IRIDA): A heterogeneous disease that is not always iron refractory.
Anemia, Iron-Deficiency
Iron Refractory Iron Deficiency Anemia Due to 374 Base Pairs Deletion in the TMPRSS6 Gene.
Anemia, Iron-Deficiency
Iron Refractory Iron Deficiency Anemia in Dizygotic Twins Due to a Novel TMPRSS6 Gene Mutation in Addition to Polymorphisms Associated With High Susceptibility to Develop Ferropenic Anemia.
Anemia, Iron-Deficiency
Iron refractory iron deficiency anemia.
Anemia, Iron-Deficiency
Iron refractory iron deficiency anemia: presentation with hyperferritinemia and response to oral iron therapy.
Anemia, Iron-Deficiency
Iron-deficiency anemia secondary to mutations in genes controlling hepcidin.
Anemia, Iron-Deficiency
Iron-refractory iron deficiency anemia (IRIDA) cases with 2 novel TMPRSS6 mutations.
Anemia, Iron-Deficiency
Iron-refractory iron deficiency anemia (IRIDA).
Anemia, Iron-Deficiency
Is EPO therapy able to correct iron deficiency anaemia caused by matriptase-2 deficiency?
Anemia, Iron-Deficiency
Is the acronym IRIDA acceptable for slow responders to iron in the presence of TMPRSS6 mutations?
Anemia, Iron-Deficiency
Limiting hepatic Bmp-Smad signaling by matriptase-2 is required for erythropoietin-mediated hepcidin suppression in mice.
Anemia, Iron-Deficiency
Liver hemojuvelin protein levels in mice deficient in matriptase-2 (Tmprss6).
Anemia, Iron-Deficiency
Liver HFE protein content is posttranscriptionally decreased in iron-deficient mice and rats.
Anemia, Iron-Deficiency
Low Iron Promotes Megakaryocytic Commitment of Megakaryocytic-Erythroid Progenitors in Humans and Mice.
Anemia, Iron-Deficiency
Matriptase-2 (TMPRSS6): a proteolytic regulator of iron homeostasis.
Anemia, Iron-Deficiency
Matriptase-2 is essential for hepcidin repression during fetal life and postnatal development in mice to maintain iron homeostasis.
Anemia, Iron-Deficiency
Matriptase-2 mutations in iron-refractory iron deficiency anemia patients provide new insights into protease activation mechanisms.
Anemia, Iron-Deficiency
Matriptase-2: monitoring and inhibiting its proteolytic activity.
Anemia, Iron-Deficiency
Microcytic anaemia with low transferrin saturation, increased serum hepcidin and non-synonymous TMPRSS6 variants: not always iron-refractory iron deficiency anaemia.
Anemia, Iron-Deficiency
Molecular mechanisms of the defective hepcidin inhibition in TMPRSS6 mutations associated with iron-refractory iron deficiency anemia.
Anemia, Iron-Deficiency
Mutations in TMPRSS6 cause iron-refractory iron deficiency anemia (IRIDA).
Anemia, Iron-Deficiency
N-glycosylation is required for matriptase-2 autoactivation and ectodomain shedding.
Anemia, Iron-Deficiency
Novel missense mutation in the TMPRSS6 gene in a Japanese female with iron-refractory iron deficiency anemia.
Anemia, Iron-Deficiency
Novel mutation in the TMPRSS6 gene with iron-refractory iron deficiency anemia.
Anemia, Iron-Deficiency
Novel TMPRSS6 mutations associated with iron-refractory iron deficiency anemia (IRIDA).
Anemia, Iron-Deficiency
Polymorphisms and mutations of human TMPRSS6 in iron deficiency anemia.
Anemia, Iron-Deficiency
Progress in iron metabolism research.
Anemia, Iron-Deficiency
Rapid, accurate detection of TMPRSS6 gene causative mutations with a high-resolution melting assay.
Anemia, Iron-Deficiency
Regulation of TMPRSS6 by BMP6 and iron in human cells and mice.
Anemia, Iron-Deficiency
Regulation of type II transmembrane serine proteinase TMPRSS6 by hypoxia-inducible factors: new link between hypoxia signalling & iron homeostasis.
Anemia, Iron-Deficiency
Responsiveness to oral iron and ascorbic acid in a patient with IRIDA.
Anemia, Iron-Deficiency
Role of TMPRSS6 rs855791 (T > C) polymorphism in reproductive age women with iron deficiency anemia from Lahore, Pakistan.
Anemia, Iron-Deficiency
Systematic evaluation of paediatric cohort with iron refractory iron deficiency anaemia (IRIDA) phenotype reveals multiple TMPRSS6 gene variations.
Anemia, Iron-Deficiency
The role of TMPRSS6 and HFE variants in iron deficiency anemia in celiac disease.
Anemia, Iron-Deficiency
The role of TMPRSS6 gene variants in iron-related hematological parameters in Turkish patients with iron deficiency anemia.
Anemia, Iron-Deficiency
The role of TMPRSS6 polymorphisms in iron deficiency anemia partially responsive to oral iron treatment.
Anemia, Iron-Deficiency
The role of TMPRSS6/matriptase-2 in iron regulation and anemia.
Anemia, Iron-Deficiency
Tmprss6 is a genetic modifier of the Hfe-hemochromatosis phenotype in mice.
Anemia, Iron-Deficiency
TMPRSS6 rs855791 polymorphism and susceptibility to iron deficiency anaemia in non-dialysis chronic kidney disease patients in South Africa.
Anemia, Iron-Deficiency
TMPRSS6 rs855791 polymorphism influences the susceptibility to iron deficiency anemia in women at reproductive age.
Anemia, Iron-Deficiency
TMPRSS6, but not TF, TFR2 or BMP2 variants are associated with increased risk of iron-deficiency anemia.
Anemia, Iron-Deficiency
Two nonsense mutations in the TMPRSS6 gene in a patient with microcytic anemia and iron deficiency.
Anemia, Iron-Deficiency
Two novel mutations in the tmprss6 gene associated with iron-refractory iron-deficiency anaemia (irida) and partial expression in the heterozygous form.
Anemia, Iron-Deficiency
Two novel mutations in TMPRSS6 associated with iron-refractory iron deficiency anemia in a mother and child.
Anemia, Iron-Deficiency
Two Novel TMPRSS6 Variants in a Compound Heterozygous Child With Iron Refractory Iron Deficiency Anemia (IRIDA).
Anemia, Iron-Deficiency
Very high frequency of TMPRSS6 gene variations in iron deficiency anaemia of patients with polyendocrine autoimmune syndromes: more than a casual association?
Anemia, Iron-Deficiency
[Iron deficiency and overload. Implications in oxidative stress and cardiovascular health]
Anemia, Iron-Deficiency
[Iron metabolism and iron-refractory iron deficiency anemia].
beta-Thalassemia
Iron and hepcidin: a story of recycling and balance.
beta-Thalassemia
Modulating the selectivity of matriptase-2 inhibitors with unnatural amino acids.
Bile Duct Neoplasms
Overexpression of matriptase in tumor stroma is a poor prognostic indicator of extrahepatic bile duct cancer.
Breast Neoplasms
A novel serine protease SNC19 associated with human colorectal cancer.
Breast Neoplasms
Activated matriptase as a target to treat breast cancer with a drug conjugate.
Breast Neoplasms
An investigation of the relationship between TMPRSS6 gene expression, genetic variants and clinical findings in breast cancer.
Breast Neoplasms
Coexpression of beta1,6-N-acetylglucosaminyltransferase V glycoprotein substrates defines aggressive breast cancers with poor outcome.
Breast Neoplasms
Critical Adjuvant Influences on Preventive Anti-Metastasis Vaccine Using a Structural Epitope Derived from Membrane Type Protease PRSS14.
Breast Neoplasms
Deregulated activation of matriptase in breast cancer cells.
Breast Neoplasms
Design and synthesis of novel and potent inhibitors of the type II transmembrane serine protease, matriptase, based upon the sunflower trypsin inhibitor-1.
Breast Neoplasms
Differential subcellular localization renders HAI-2 a matriptase inhibitor in breast cancer cells but not in mammary epithelial cells.
Breast Neoplasms
Diversity of matriptase expression level and function in breast cancer.
Breast Neoplasms
Epithin/PRSS14 proteolytically regulates angiopoietin receptor Tie2 during transendothelial migration.
Breast Neoplasms
Expression of the serine protease, matriptase, in breast ductal carcinoma of Chinese women: correlation with clinicopathological parameters.
Breast Neoplasms
HAI-1 regulates activation and expression of matriptase, a membrane-bound serine protease.
Breast Neoplasms
Hepsin regulates TGF? signaling via fibronectin proteolysis.
Breast Neoplasms
Impact of suppression of tumorigenicity 14 (ST14)/serine protease 14 (prss14) expression analysis on the prognosis and management of estrogen receptor negative breast cancer.
Breast Neoplasms
Kempopeptin C, a Novel Marine-Derived Serine Protease Inhibitor Targeting Invasive Breast Cancer.
Breast Neoplasms
Matriptase activation and shedding with HAI-1 is induced by steroid sex hormones in human prostate cancer cells, but not in breast cancer cells.
Breast Neoplasms
Matriptase and HAI-1 are expressed by normal and malignant epithelial cells in vitro and in vivo.
Breast Neoplasms
Matriptase and survivin expression associated with tumor progression and malignant potential in breast cancer of Chinese women: tissue microarray analysis of immunostaining scores with clinicopathological parameters.
Breast Neoplasms
Matriptase-2 gene (TMPRSS6) variants associate with breast cancer survival, and reduced expression is related to triple-negative breast cancer.
Breast Neoplasms
Matriptase-2 inhibits breast tumor growth and invasion and correlates with favorable prognosis for breast cancer patients.
Breast Neoplasms
Matriptase-2 inhibits HECV motility and tubule formation in vitro and tumour angiogenesis in vivo.
Breast Neoplasms
N-Glycan Branching Affects the Subcellular Distribution of and Inhibition of Matriptase by HAI-2/Placental Bikunin.
Breast Neoplasms
N-terminal processing is essential for release of epithin, a mouse type II membrane serine protease.
Breast Neoplasms
Production of soluble matriptase by human cancer cell lines and cell surface activation of its zymogen by trypsin.
Breast Neoplasms
Proteolytic cleavages in the extracellular domain of receptor tyrosine kinases by membrane-associated serine proteases.
Breast Neoplasms
Purification and characterization of a complex containing matriptase and a Kunitz-type serine protease inhibitor from human milk.
Breast Neoplasms
Quantitation of membrane type serine protease 1 (MT-SP1) in transformed and normal cells.
Breast Neoplasms
Refinement of the 22q12-q13 Breast Cancer-Associated Region: Evidence of TMPRSS6 as a Candidate Gene in an Eastern Finnish Population.
Breast Neoplasms
ST14 gene variant and decreased matriptase protein expression predict poor breast cancer survival.
Breast Neoplasms
Strong expression association between matriptase and its substrate prostasin in breast cancer.
Breast Neoplasms
Targeting matriptase in breast cancer abrogates tumour progression via impairment of stromal-epithelial growth factor signalling.
Breast Neoplasms
The expression of a type II transmembrane serine protease (Seprase) in human gastric carcinoma.
Breast Neoplasms
The hepatocyte growth factor regulatory factors in human breast cancer.
Breast Neoplasms
The macrophage-stimulating protein pathway promotes metastasis in a mouse model for breast cancer and predicts poor prognosis in humans.
Breast Neoplasms
Tissue microarray analysis of hepatocyte growth factor/Met pathway components reveals a role for Met, matriptase, and hepatocyte growth factor activator inhibitor 1 in the progression of node-negative breast cancer.
Breast Neoplasms
Type II transmembrane serine protease gene variants associate with breast cancer.
Burkitt Lymphoma
Imbalanced matriptase pericellular proteolysis contributes to the pathogenesis of malignant B-cell lymphomas.
Carcinogenesis
c-Met-induced epithelial carcinogenesis is initiated by the serine protease matriptase.
Carcinogenesis
Cell Surface Human Airway Trypsin-Like Protease Is Lost During Squamous Cell Carcinogenesis.
Carcinogenesis
Co-localization of the channel activating protease prostasin/(CAP1/PRSS8) with its candidate activator, matriptase.
Carcinogenesis
Delineation of matriptase protein expression by enzymatic gene trapping suggests diverging roles in barrier function, hair formation, and squamous cell carcinogenesis.
Carcinogenesis
Deregulated matriptase causes ras-independent multistage carcinogenesis and promotes ras-mediated malignant transformation.
Carcinogenesis
Design and synthesis of novel and potent inhibitors of the type II transmembrane serine protease, matriptase, based upon the sunflower trypsin inhibitor-1.
Carcinogenesis
Differential expression of genes encoding proteins of the HGF/MET system in insulinomas.
Carcinogenesis
Entosis and apical cell extrusion constitute a tumor-suppressive mechanism downstream of Matriptase.
Carcinogenesis
Growth differentiation factor-15 upregulates interleukin-6 to promote tumorigenesis of prostate carcinoma PC-3 cells.
Carcinogenesis
HAI-2 stabilizes, inhibits and regulates SEA-cleavage-dependent secretory transport of matriptase.
Carcinogenesis
Hepatocyte growth factor activator inhibitor-1 (HAI-1) is essential for the integrity of basement membranes in the developing placental labyrinth.
Carcinogenesis
Hepatocyte growth factor activator inhibitor-1 has a complex subcellular itinerary.
Carcinogenesis
Imaging a functional tumorigenic biomarker in the transformed epithelium.
Carcinogenesis
Insights into the regulation of the matriptase-prostasin proteolytic system.
Carcinogenesis
Laminin-332 cleavage by matriptase alters motility parameters of prostate cancer cells.
Carcinogenesis
Matriptase activation and shedding through PDGF-D-mediated extracellular acidosis.
Carcinogenesis
Matriptase promotes inflammatory cell accumulation and progression of established epidermal tumors.
Carcinogenesis
Matriptase-2 inhibits breast tumor growth and invasion and correlates with favorable prognosis for breast cancer patients.
Carcinogenesis
Matriptase: potent proteolysis on the cell surface.
Carcinogenesis
Phenotypic analysis of mice lacking the Tmprss2-encoded protease.
Carcinogenesis
Protease-activated receptor-2 accelerates intestinal tumor formation through activation of nuclear factor-?B signaling and tumor angiogenesis in ApcMin/+ mice.
Carcinogenesis
ST14 gene variant and decreased matriptase protein expression predict poor breast cancer survival.
Carcinogenesis
Suppression of Tumorigenicity-14, encoding matriptase, is a critical suppressor of colitis and colitis-associated colon carcinogenesis.
Carcinogenesis
The androgen-regulated type II serine protease TMPRSS2 is differentially expressed and mislocalized in prostate adenocarcinoma.
Carcinogenesis
The level of claudin-7 is reduced as an early event in colorectal carcinogenesis.
Carcinogenesis
The ratio of Matriptase/HAI-1 mRNA is higher in colorectal cancer adenomas and carcinomas than corresponding tissue from control individuals.
Carcinogenesis
Tissue expression, protease specificity, and Kunitz domain functions of hepatocyte growth factor activator inhibitor-1B (HAI-1B), a new splice variant of HAI-1.
Carcinogenesis
TMPRSS13 promotes cell survival, invasion, and resistance to drug-induced apoptosis in colorectal cancer.
Carcinoma
A novel biomarker for staging human prostate adenocarcinoma: overexpression of matriptase with concomitant loss of its inhibitor, hepatocyte growth factor activator inhibitor-1.
Carcinoma
A role for membrane-type serine protease (MT-SP1) in intestinal epithelial turnover.
Carcinoma
Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease.
Carcinoma
c-Met-induced epithelial carcinogenesis is initiated by the serine protease matriptase.
Carcinoma
Clinical relevance of hepsin and hepatocyte growth factor activator inhibitor type 2 expression in renal cell carcinoma.
Carcinoma
Co-expression of matriptase and N-acetylglucosaminyltransferase V in thyroid cancer tissues--its possible role in prolonged stability in vivo by aberrant glycosylation.
Carcinoma
CVS-3983, a selective matriptase inhibitor, suppresses the growth of androgen independent prostate tumor xenografts.
Carcinoma
Delineation of matriptase protein expression by enzymatic gene trapping suggests diverging roles in barrier function, hair formation, and squamous cell carcinogenesis.
Carcinoma
Deregulated activation of matriptase in breast cancer cells.
Carcinoma
Deregulated matriptase activity in oral squamous cell carcinoma promotes the infiltration of cancer-associated fibroblasts by paracrine activation of protease-activated receptor 2.
Carcinoma
Deregulated matriptase causes ras-independent multistage carcinogenesis and promotes ras-mediated malignant transformation.
Carcinoma
DESC1, a novel tumor suppressor, sensitizes cells to apoptosis by down-regulating the EGFR/AKT pathway in esophageal squamous cell carcinoma.
Carcinoma
Differential subcellular localization renders HAI-2 a matriptase inhibitor in breast cancer cells but not in mammary epithelial cells.
Carcinoma
Down-regulation of matriptase by overexpression of bikunin attenuates cell invasion in prostate carcinoma cells.
Carcinoma
Downexpression of Matriptase-2 Correlates With Tumor Progression and Clinical Prognosis in Oral Squamous-Cell Carcinoma.
Carcinoma
Dysregulation of Type II Transmembrane Serine Proteases and Ligand-Dependent Activation of MET in Urological Cancers.
Carcinoma
Entosis and apical cell extrusion constitute a tumor-suppressive mechanism downstream of Matriptase.
Carcinoma
Evaluating the function of matriptase and N-acetylglucosaminyltransferase V in prostate cancer metastasis.
Carcinoma
Expression of EMMPRIN and matriptase in esophageal squamous cell carcinoma: correlation with clinicopathological parameters.
Carcinoma
Expression of matriptase correlates with tumour progression and clinical prognosis in oral squamous cell carcinoma.
Carcinoma
Expression of serine protease matriptase in renal cell carcinoma: correlation of tissue microarray immunohistochemical expression analysis results with clinicopathological parameters.
Carcinoma
Growth differentiation factor-15 upregulates interleukin-6 to promote tumorigenesis of prostate carcinoma PC-3 cells.
Carcinoma
Human Cancer Cells Retain Modest Levels of Enzymatically Active Matriptase Only in Extracellular Milieu following Induction of Zymogen Activation.
Carcinoma
In vitro inhibition of matriptase prevents invasive growth of cell lines of prostate and colon carcinoma.
Carcinoma
Increased expression of matriptase is associated with histopathologic grades of cervical neoplasia.
Carcinoma
Increasing expression of serine protease matriptase in ovarian tumors: tissue microarray analysis of immunostaining score with clinicopathological parameters.
Carcinoma
Matriptase activation and shedding with HAI-1 is induced by steroid sex hormones in human prostate cancer cells, but not in breast cancer cells.
Carcinoma
Matriptase activation of Gq drives epithelial disruption and inflammation via RSK and DUOX.
Carcinoma
Matriptase activation, an early cellular response to acidosis.
Carcinoma
Matriptase and HAI-1 are expressed by normal and malignant epithelial cells in vitro and in vivo.
Carcinoma
Matriptase and MET are prominently expressed at the site of bone metastasis in renal cell carcinoma: immunohistochemical analysis.
Carcinoma
Matriptase is inhibited by extravascular antithrombin in epithelial cells but not in most carcinoma cells.
Carcinoma
Mechanisms for the control of matriptase activity in the absence of sufficient HAI-1.
Carcinoma
Mouse DESC1 is located within a cluster of seven DESC1-like genes and encodes a type II transmembrane serine protease that forms serpin inhibitory complexes.
Carcinoma
Non-hematopoietic PAR-2 is essential for matriptase-driven pre-malignant progression and potentiation of ras-mediated squamous cell carcinogenesis.
Carcinoma
Ovarian carcinoma subtypes are different diseases: implications for biomarker studies.
Carcinoma
Overexpression of matriptase correlates with poor prognosis in esophageal squamous cell carcinoma.
Carcinoma
Pericellular activation of hepatocyte growth factor by the transmembrane serine proteases matriptase and hepsin, but not by the membrane-associated protease uPA.
Carcinoma
Probing the interaction mechanism of small molecule inhibitors with matriptase based on molecular dynamics simulation and free energy calculations.
Carcinoma
Production of soluble matriptase by human cancer cell lines and cell surface activation of its zymogen by trypsin.
Carcinoma
Protease degradomics: mass spectrometry discovery of protease substrates and the CLIP-CHIP, a dedicated DNA microarray of all human proteases and inhibitors.
Carcinoma
Purification from human milk of matriptase complexes with secreted serpins: mechanism for inhibition of matriptase other than HAI-1.
Carcinoma
Reverse biochemistry: use of macromolecular protease inhibitors to dissect complex biological processes and identify a membrane-type serine protease in epithelial cancer and normal tissue.
Carcinoma
Role of Matriptase and Proteinase-Activated Receptor-2 in Nonmelanoma Skin Cancer.
Carcinoma
Semiautomatic landmark-based two-dimensional-three-dimensional image fusion in living mice: correlation of near-infrared fluorescence imaging of Cy5.5-labeled antibodies with flat-panel volume computed tomography.
Carcinoma
The expression of a type II transmembrane serine protease (Seprase) in human gastric carcinoma.
Carcinoma
The novel serine protease tumor-associated differentially expressed gene-15 (matriptase/MT-SP1) is highly overexpressed in cervical carcinoma.
Carcinoma
The ratio of Matriptase/HAI-1 mRNA is higher in colorectal cancer adenomas and carcinomas than corresponding tissue from control individuals.
Carcinoma
Transmembrane serine protease TADG-15 (ST14/Matriptase/MT-SP1): expression and prognostic value in ovarian cancer.
Carcinoma
Zebrafish modeling reveals that SPINT1 regulates the aggressiveness of skin cutaneous melanoma and its crosstalk with tumor immune microenvironment.
Carcinoma, Basal Cell
Role of Matriptase and Proteinase-Activated Receptor-2 in Nonmelanoma Skin Cancer.
Carcinoma, Ductal
Expression of the serine protease, matriptase, in breast ductal carcinoma of Chinese women: correlation with clinicopathological parameters.
Carcinoma, Ductal
Matriptase and survivin expression associated with tumor progression and malignant potential in breast cancer of Chinese women: tissue microarray analysis of immunostaining scores with clinicopathological parameters.
Carcinoma, Endometrioid
Increasing expression of serine protease matriptase in ovarian tumors: tissue microarray analysis of immunostaining score with clinicopathological parameters.
Carcinoma, Hepatocellular
Functional diversity of TMPRSS6 isoforms and variants expressed in hepatocellular carcinoma cell lines.
Carcinoma, Hepatocellular
Increasing EMMPRIN and matriptase expression in hepatocellular carcinoma: tissue microarray analysis of immunohistochemical scores with clinicopathological parameters.
Carcinoma, Hepatocellular
Inflammation regulates TMPRSS6 expression via STAT5.
Carcinoma, Intraductal, Noninfiltrating
Expression of the serine protease, matriptase, in breast ductal carcinoma of Chinese women: correlation with clinicopathological parameters.
Carcinoma, Intraductal, Noninfiltrating
Matriptase and survivin expression associated with tumor progression and malignant potential in breast cancer of Chinese women: tissue microarray analysis of immunostaining scores with clinicopathological parameters.
Carcinoma, Ovarian Epithelial
Expression of the serine protease matriptase and its inhibitor HAI-1 in epithelial ovarian cancer: correlation with clinical outcome and tumor clinicopathological parameters.
Carcinoma, Papillary
Co-expression of matriptase and N-acetylglucosaminyltransferase V in thyroid cancer tissues--its possible role in prolonged stability in vivo by aberrant glycosylation.
Carcinoma, Renal Cell
Clinical relevance of hepsin and hepatocyte growth factor activator inhibitor type 2 expression in renal cell carcinoma.
Carcinoma, Renal Cell
Dysregulation of Type II Transmembrane Serine Proteases and Ligand-Dependent Activation of MET in Urological Cancers.
Carcinoma, Renal Cell
Expression of serine protease matriptase in renal cell carcinoma: correlation of tissue microarray immunohistochemical expression analysis results with clinicopathological parameters.
Carcinoma, Renal Cell
Matriptase and MET are prominently expressed at the site of bone metastasis in renal cell carcinoma: immunohistochemical analysis.
Carcinoma, Squamous Cell
c-Met-induced epithelial carcinogenesis is initiated by the serine protease matriptase.
Carcinoma, Squamous Cell
Delineation of matriptase protein expression by enzymatic gene trapping suggests diverging roles in barrier function, hair formation, and squamous cell carcinogenesis.
Carcinoma, Squamous Cell
Deregulated matriptase causes ras-independent multistage carcinogenesis and promotes ras-mediated malignant transformation.
Carcinoma, Squamous Cell
DESC1, a novel tumor suppressor, sensitizes cells to apoptosis by down-regulating the EGFR/AKT pathway in esophageal squamous cell carcinoma.
Carcinoma, Squamous Cell
Expression of EMMPRIN and matriptase in esophageal squamous cell carcinoma: correlation with clinicopathological parameters.
Carcinoma, Squamous Cell
Increased expression of matriptase is associated with histopathologic grades of cervical neoplasia.
Carcinoma, Squamous Cell
Mouse DESC1 is located within a cluster of seven DESC1-like genes and encodes a type II transmembrane serine protease that forms serpin inhibitory complexes.
Carcinoma, Squamous Cell
Role of Matriptase and Proteinase-Activated Receptor-2 in Nonmelanoma Skin Cancer.
Carcinoma, Squamous Cell
Zebrafish modeling reveals that SPINT1 regulates the aggressiveness of skin cutaneous melanoma and its crosstalk with tumor immune microenvironment.
Carcinoma, Transitional Cell
Increasing expression of serine protease matriptase in ovarian tumors: tissue microarray analysis of immunostaining score with clinicopathological parameters.
Celiac Disease
About TMPRSS6 rs855791 polymorphism, iron metabolism and celiac disease.
Celiac Disease
The role of TMPRSS6 and HFE variants in iron deficiency anemia in celiac disease.
Celiac Disease
TMPRSS6 rs855791 Polymorphism Status in Children with Celiac Disease and Anemia.
Colitis
Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis.
Colitis
Matriptase protects against experimental colitis and promotes intestinal barrier recovery.
Colitis
Suppression of Tumorigenicity-14, encoding matriptase, is a critical suppressor of colitis and colitis-associated colon carcinogenesis.
Colitis, Ulcerative
Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis.
Colitis, Ulcerative
Matriptase protects against experimental colitis and promotes intestinal barrier recovery.
Colonic Neoplasms
Discovery of novel 2-hydroxydiarylamide derivatives as TMPRSS4 inhibitors.
Colonic Neoplasms
Imaging a functional tumorigenic biomarker in the transformed epithelium.
Colonic Neoplasms
Quantitation of membrane type serine protease 1 (MT-SP1) in transformed and normal cells.
Colorectal Neoplasms
A novel serine protease SNC19 associated with human colorectal cancer.
Colorectal Neoplasms
The ratio of Matriptase/HAI-1 mRNA is higher in colorectal cancer adenomas and carcinomas than corresponding tissue from control individuals.
Colorectal Neoplasms
Zebrafish modeling reveals that SPINT1 regulates the aggressiveness of skin cutaneous melanoma and its crosstalk with tumor immune microenvironment.
Common Cold
Protease Inhibitors: Candidate Drugs to Inhibit Severe Acute Respiratory Syndrome Coronavirus 2 Replication.
Coronavirus Infections
Biochemical Characterization of Middle East Respiratory Syndrome Coronavirus Spike Protein Proteolytic Processing.
Coronavirus Infections
TMPRSS2 contributes to virus spread and immunopathology in the airways of murine models after coronavirus infection.
COVID-19
ACE2/ADAM17/TMPRSS2 Interplay May Be the Main Risk Factor for COVID-19.
COVID-19
Characteristics of Angiotensin I-converting enzyme 2, type II transmembrane serine protease 2 and 4 in tree shrew indicate it as a potential animal model for SARS-CoV-2 infection.
COVID-19
Sex, Hormones, Immune Functions, and Susceptibility to Coronavirus Disease 2019 (COVID-19)-Related Morbidity.
COVID-19
TMPRSS2 Correlated With Immune Infiltration Serves as a Prognostic Biomarker in Prostatic Adenocarcinoma: Implication for the COVID-2019.
Crohn Disease
Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis.
Crohn Disease
Matriptase protects against experimental colitis and promotes intestinal barrier recovery.
Cystic Fibrosis
Activity and inhibition of prostasin and matriptase on apical and basolateral surfaces of human airway epithelial cells.
Deafness
Mice deficient for the type II transmembrane serine protease, TMPRSS1/hepsin, exhibit profound hearing loss.
Deafness
Tmprss3, a transmembrane serine protease deficient in human DFNB8/10 deafness, is critical for cochlear hair cell survival at the onset of hearing.
Deafness
TMPRSS3, a type II transmembrane serine protease mutated in non-syndromic autosomal recessive deafness.
Dehydration
Activity and inhibition of prostasin and matriptase on apical and basolateral surfaces of human airway epithelial cells.
Diabetes Mellitus, Type 2
A Genome-Wide Association Study of IVGTT-Based Measures of First-Phase Insulin Secretion Refines the Underlying Physiology of Type 2 Diabetes Variants.
Diabetes Mellitus, Type 2
Association of TMPRSS6 polymorphisms with ferritin, hemoglobin, and type 2 diabetes risk in a Chinese Han population.
Diabetes, Gestational
Associations of TMPRSS6 Polymorphisms with Gestational Diabetes Mellitus in Chinese Han Pregnant Women: a Preliminary Cohort Study.
Dysgerminoma
Increasing expression of serine protease matriptase in ovarian tumors: tissue microarray analysis of immunostaining score with clinicopathological parameters.
Endodermal Sinus Tumor
Increasing expression of serine protease matriptase in ovarian tumors: tissue microarray analysis of immunostaining score with clinicopathological parameters.
Endometrial Hyperplasia
Expression of matriptase and clinical outcome of human endometrial cancer.
Endometrial Neoplasms
Expression of matriptase and clinical outcome of human endometrial cancer.
Endometrial Neoplasms
Regulation of matriptase and HAI-1 system, a novel therapeutic target in human endometrial cancer cells.
Esophageal Squamous Cell Carcinoma
Expression of EMMPRIN and matriptase in esophageal squamous cell carcinoma: correlation with clinicopathological parameters.
Esophageal Squamous Cell Carcinoma
Overexpression of matriptase correlates with poor prognosis in esophageal squamous cell carcinoma.
Fibroadenoma
Expression of the serine protease, matriptase, in breast ductal carcinoma of Chinese women: correlation with clinicopathological parameters.
Fibroadenoma
Matriptase and survivin expression associated with tumor progression and malignant potential in breast cancer of Chinese women: tissue microarray analysis of immunostaining scores with clinicopathological parameters.
Fibroma
Increasing expression of serine protease matriptase in ovarian tumors: tissue microarray analysis of immunostaining score with clinicopathological parameters.
Fibrosarcoma
Purification and characterization of a complex containing matriptase and a Kunitz-type serine protease inhibitor from human milk.
Gastritis, Atrophic
Iron deficiency anemia refractory to iron preparations.
Genetic Diseases, Inborn
Matriptase Expression and Zymogen Activation in Human Pilosebaceous Unit.
Genetic Diseases, Inborn
Mutation G827R in Matriptase Causing Autosomal Recessive Ichthyosis with Hypotrichosis Yields an Inactive Protease.
Genetic Diseases, Inborn
The role of TMPRSS6 polymorphisms in iron deficiency anemia partially responsive to oral iron treatment.
Genetic Diseases, Inborn
The spatiotemporal control of human matriptase action on its physiological substrates: a case against a direct role for matriptase proteolytic activity in profilaggrin processing and desquamation.
Genetic Diseases, Inborn
[Iron metabolism and iron-refractory iron deficiency anemia].
Glioma
Aberrations in the Iron Regulatory Gene Signature Are Associated with Decreased Survival in Diffuse Infiltrating Gliomas.
Glioma
Imaging of Fibroblast Activation Protein Alpha Expression in a Preclinical Mouse Model of Glioma Using Positron Emission Tomography.
Glioma
Proteolytic cleavage of human acid-sensing ion channel 1 by the serine protease matriptase.
Granulosa Cell Tumor
Increasing expression of serine protease matriptase in ovarian tumors: tissue microarray analysis of immunostaining score with clinicopathological parameters.
Hearing Loss
Defective Tmprss3-Associated Hair Cell Degeneration in Inner Ear Organoids.
Hearing Loss
Mice deficient for the type II transmembrane serine protease, TMPRSS1/hepsin, exhibit profound hearing loss.
Hearing Loss
Thyroxine treatments do not correct inner ear defects in tmprss1 mutant mice.
Hearing Loss
Tmprss3, a transmembrane serine protease deficient in human DFNB8/10 deafness, is critical for cochlear hair cell survival at the onset of hearing.
Hemochromatosis
Design and chemical syntheses of potent matriptase-2 inhibitors based on trypsin inhibitor SFTI-1 isolated from sunflower seeds.
Hemochromatosis
Effect of the A736V TMPRSS6 polymorphism on the penetrance and clinical expression of hereditary hemochromatosis.
Hemochromatosis
Genetic factors influencing hemoglobin levels in 15,567 blood donors: results from the Danish Blood Donor Study.
Hemochromatosis
Global loss of Tfr2 with concomitant induced iron deficiency greatly ameliorates the phenotype of a murine thalassemia intermedia model.
Hemochromatosis
Iron and hepcidin: a story of recycling and balance.
Hemochromatosis
Iron regulation by hepcidin.
Hemochromatosis
Modulating the selectivity of matriptase-2 inhibitors with unnatural amino acids.
Hemochromatosis
Phosphono Bisbenzguanidines as Irreversible Dipeptidomimetic Inhibitors and Activity-Based Probes of Matriptase-2.
Hemochromatosis
Progress in iron metabolism research.
Hemochromatosis
Reducing TMPRSS6 ameliorates hemochromatosis and ?-thalassemia in mice.
Hemochromatosis
SLN124, a GalNAc-siRNA Conjugate Targeting TMPRSS6, Efficiently Prevents Iron Overload in Hereditary Haemochromatosis Type 1.
Hemochromatosis
Tmprss6 is a genetic modifier of the Hfe-hemochromatosis phenotype in mice.
Hemophilia A
[Detection of the heterozygote carrier state and prenatal diagnosis of hemophilia A using DNA probes]
Hepatitis C, Chronic
Hepcidin in Iron Homeostasis: Diagnostic and Therapeutic Implications in Type 2 Diabetes Mellitus Patients.
Hyperferritinemia
Iron refractory iron deficiency anemia: presentation with hyperferritinemia and response to oral iron therapy.
Hypersensitivity
[Association of FokI rs2228570 and TMPRSS6 rs855791 polymorphisms with cow's milk protein allergy in children].
Hypohidrosis
A novel mutation in ST14 at a functionally significant amino acid residue expands the spectrum of ichthyosis-hypotrichosis syndrome.
Hypohidrosis
Matriptase Regulates Proliferation and Early, but Not Terminal, Differentiation of Human Keratinocytes.
Hypotrichosis
A novel mutation in ST14 at a functionally significant amino acid residue expands the spectrum of ichthyosis-hypotrichosis syndrome.
Hypotrichosis
Autosomal ichthyosis with hypotrichosis syndrome displays low matriptase proteolytic activity and is phenocopied in ST14 hypomorphic mice.
Hypotrichosis
Autosomal recessive ichthyosis with hypotrichosis caused by a mutation in ST14, encoding type II transmembrane serine protease matriptase.
Hypotrichosis
Autosomal recessive ichthyosis with hypotrichosis syndrome: further delineation of the phenotype.
Hypotrichosis
Ichthyosis, Follicular Atrophoderma, and Hypotrichosis Caused by Mutations in ST14 Is Associated with Impaired Profilaggrin Processing.
Hypotrichosis
Matriptase Regulates Proliferation and Early, but Not Terminal, Differentiation of Human Keratinocytes.
Hypotrichosis
Mutation G827R in Matriptase Causing Autosomal Recessive Ichthyosis with Hypotrichosis Yields an Inactive Protease.
Hypotrichosis
The matriptase-prostasin proteolytic cascade in epithelial development and pathology.
Ichthyosis
A novel mutation in ST14 at a functionally significant amino acid residue expands the spectrum of ichthyosis-hypotrichosis syndrome.
Ichthyosis
Autosomal ichthyosis with hypotrichosis syndrome displays low matriptase proteolytic activity and is phenocopied in ST14 hypomorphic mice.
Ichthyosis
Autosomal recessive ichthyosis with hypotrichosis caused by a mutation in ST14, encoding type II transmembrane serine protease matriptase.
Ichthyosis
Autosomal recessive ichthyosis with hypotrichosis syndrome: further delineation of the phenotype.
Ichthyosis
Genetic skin diseases related to desmosomes and corneodesmosomes.
Ichthyosis
Ichthyosis, Follicular Atrophoderma, and Hypotrichosis Caused by Mutations in ST14 Is Associated with Impaired Profilaggrin Processing.
Ichthyosis
Loss of Matriptase Suppression Underlies Spint1 Mutation-Associated Ichthyosis and Postnatal Lethality.
Ichthyosis
Matriptase Cleaves EpCAM and TROP2 in Keratinocytes, Destabilizing Both Proteins and Associated Claudins.
Ichthyosis
Matriptase Regulates Proliferation and Early, but Not Terminal, Differentiation of Human Keratinocytes.
Ichthyosis
Mutation G827R in Matriptase Causing Autosomal Recessive Ichthyosis with Hypotrichosis Yields an Inactive Protease.
Idiopathic Pulmonary Fibrosis
Matriptase, Protease-activated Receptor 2, and Idiopathic Pulmonary Fibrosis. Further Evidence for Signaling Pathway Redundancy in this Difficult-to-Treat Disease?
Infections
A phase I study of high dose camostat mesylate in healthy adults provides a rationale to repurpose the TMPRSS2 inhibitor for the treatment of COVID-19.
Infections
Cathepsins B and L activate Ebola but not Marburg virus glycoproteins for efficient entry into cell lines and macrophages independent of TMPRSS2 expression.
Infections
Hepcidin in Iron Homeostasis: Diagnostic and Therapeutic Implications in Type 2 Diabetes Mellitus Patients.
Infections
Matriptase activation connects tissue factor-dependent coagulation initiation to epithelial proteolysis and signaling.
Infections
Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Infection Mediated by the Transmembrane Serine Protease TMPRSS2.
Infections
The HIV-1 gp41 ectodomain is cleaved by matriptase to produce a chemotactic peptide that acts through FPR2.
Inflammatory Breast Neoplasms
Matriptase regulates c-Met mediated proliferation and invasion in inflammatory breast cancer.
Influenza, Human
Cleavage Activation of the Human-Adapted Influenza Virus Subtypes by Matriptase Reveals both Subtype and Strain Specificities.
Influenza, Human
DESC1 and MSPL activate influenza A viruses and emerging coronaviruses for host cell entry.
Influenza, Human
Evidence that TMPRSS2 activates the SARS-coronavirus spike-protein for membrane fusion and reduces viral control by the humoral immune response.
Influenza, Human
Identification of the first synthetic inhibitors of the type II transmembrane serine protease TMPRSS2 suitable for inhibition of influenza virus activation.
Influenza, Human
Matriptase proteolytically activates influenza virus and promotes multicycle replication in the human airway epithelium.
Influenza, Human
Matriptase, HAT, and TMPRSS2 activate the hemagglutinin of H9N2 influenza A viruses.
Influenza, Human
Non-human primate orthologues of TMPRSS2 cleave and activate the influenza virus hemagglutinin.
Influenza, Human
SPINT2 inhibits proteases involved in activation of both influenza viruses and metapneumoviruses.
Insulin Resistance
Matriptase-2 deficiency protects from obesity by modulating iron homeostasis.
Insulinoma
Differential expression of genes encoding proteins of the HGF/MET system in insulinomas.
Intestinal Failure
Matriptase drives early-onset intestinal failure in a mouse model of congenital tufting enteropathy.
Iron Deficiencies
Anaemia, iron deficiency and a common polymorphism of iron-regulation, TMPRSS6 rs855791, in Rwandan children.
Iron Deficiencies
Common TMPRSS6 mutations and iron, erythrocyte, and pica phenotypes in 48 women with iron deficiency or depletion.
Iron Deficiencies
Does TMPRSS6 RS855791 polymorphism contribute to iron deficiency in treated celiac disease?
Iron Deficiencies
Effect of Erythropoietin, Iron Deficiency and Iron Overload on Liver Matriptase-2 (TMPRSS6) Protein Content in Mice and Rats.
Iron Deficiencies
Fine tuning of hepcidin expression by positive and negative regulators.
Iron Deficiencies
Heeney MM, Guo D, De Falco L, et al. Normalizing hepcidin predicts TMPRSS6 mutation status in patients with chronic iron deficiency. Blood. 2018;132(4):448-452.
Iron Deficiencies
Iron deficiency anemia due to matriptase-2 inactivation is dependent upon the presence of functional Bmp6.
Iron Deficiencies
Iron homeostasis and nutritional iron deficiency.
Iron Deficiencies
Iron Refractory Iron Deficiency Anaemia: A Rare Cause of Iron Deficiency Anaemia.
Iron Deficiencies
Iron refractory iron deficiency anemia.
Iron Deficiencies
Iron-refractory iron deficiency anemia.
Iron Deficiencies
Iron-refractory iron deficiency anemia: new molecular mechanisms.
Iron Deficiencies
Low intracellular iron increases the stability of matriptase-2.
Iron Deficiencies
Matriptase-2 is essential for hepcidin repression during fetal life and postnatal development in mice to maintain iron homeostasis.
Iron Deficiencies
Matriptase-2 mutations in iron-refractory iron deficiency anemia patients provide new insights into protease activation mechanisms.
Iron Deficiencies
Mild iron deficiency does not ameliorate the phenotype of a murine erythropoietic protoporphyria model.
Iron Deficiencies
Normalizing hepcidin predicts TMPRSS6 mutation status in patients with chronic iron deficiency.
Iron Deficiencies
Polymorphisms and mutations of human TMPRSS6 in iron deficiency anemia.
Iron Deficiencies
Severe microcytic anemia but increased erythropoiesis in mice lacking Hfe or Tfr2 and Tmprss6.
Iron Deficiencies
Study the association of transmembrane serine protease 6 gene polymorphisms with iron deficiency status in Saudi Arabia.
Iron Deficiencies
Suppression of the hepcidin-encoding gene Hamp permits iron overload in mice lacking both hemojuvelin and matriptase-2/TMPRSS6.
Iron Deficiencies
The erythroid function of Transferrin Receptor 2 revealed by Tmprss6inactivation in different models of Transferrin Receptor 2 knock out mice.
Iron Deficiencies
The serine protease matriptase-2 (TMPRSS6) inhibits hepcidin activation by cleaving membrane hemojuvelin.
Iron Deficiencies
The serine protease TMPRSS6 is required to sense iron deficiency.
Iron Deficiencies
Tmprss6 is a genetic modifier of the Hfe-hemochromatosis phenotype in mice.
Iron Deficiencies
TMPRSS6, but not TF, TFR2 or BMP2 variants are associated with increased risk of iron-deficiency anemia.
Iron Deficiencies
Transferrin Receptor 1 Regulates Thermogenic Capacity and Cell Fate in Brown/Beige Adipocytes.
Iron Deficiencies
Two nonsense mutations in the TMPRSS6 gene in a patient with microcytic anemia and iron deficiency.
Iron Metabolism Disorders
A child with severe iron-deficiency anemia and a complex TMPRSS6 genotype.
Iron Metabolism Disorders
A novel homozygous nonsense mutation (p.Y78*) in TMPRSS6 gene causing iron-refractory iron deficiency anemia (IRIDA) in two siblings.
Iron Metabolism Disorders
Functional diversity of TMPRSS6 isoforms and variants expressed in hepatocellular carcinoma cell lines.
Iron Overload
3,1-Benzothiazines, 1,4-Benzodioxines and 1,4-Benzoxazines as Inhibitors of Matriptase-2: Outcome of a Focused Screening Approach.
Iron Overload
A genome-wide meta-analysis yields 46 new loci associating with biomarkers of iron homeostasis.
Iron Overload
A strong anti-inflammatory signature revealed by liver transcription profiling of Tmprss6-/- mice.
Iron Overload
An RNAi therapeutic targeting Tmprss6 decreases iron overload in Hfe(-/-) mice and ameliorates anemia and iron overload in murine ?-thalassemia intermedia.
Iron Overload
Combination therapy with a Tmprss6 RNAi-therapeutic and the oral iron chelator deferiprone additively diminishes secondary iron overload in a mouse model of ?-thalassemia intermedia.
Iron Overload
Deletion of TMPRSS6 attenuates the phenotype in a mouse model of ?-thalassemia.
Iron Overload
Design and chemical syntheses of potent matriptase-2 inhibitors based on trypsin inhibitor SFTI-1 isolated from sunflower seeds.
Iron Overload
Down-regulation of Bmp/Smad signaling by Tmprss6 is required for maintenance of systemic iron homeostasis.
Iron Overload
Effect of Erythropoietin, Iron Deficiency and Iron Overload on Liver Matriptase-2 (TMPRSS6) Protein Content in Mice and Rats.
Iron Overload
En Route to New Therapeutic Options for Iron Overload Diseases: Matriptase-2 as a Target for Kunitz-Type Inhibitors.
Iron Overload
Evaluation of bisbenzamidines as inhibitors for matriptase-2.
Iron Overload
Global loss of Tfr2 with concomitant induced iron deficiency greatly ameliorates the phenotype of a murine thalassemia intermedia model.
Iron Overload
Hepatocyte growth factor activator inhibitor type 2 (HAI-2) modulates hepcidin expression by inhibiting the cell surface protease matriptase-2.
Iron Overload
Identification of the first low-molecular-weight inhibitors of matriptase-2.
Iron Overload
Iron deficiency anemia due to matriptase-2 inactivation is dependent upon the presence of functional Bmp6.
Iron Overload
Matriptase-2: monitoring and inhibiting its proteolytic activity.
Iron Overload
Modulating the selectivity of matriptase-2 inhibitors with unnatural amino acids.
Iron Overload
Recent progress on inhibitors of the type II transmembrane serine proteases, hepsin, matriptase and matriptase-2.
Iron Overload
RNAi-mediated reduction of hepatic Tmprss6 diminishes anemia and secondary iron overload in a splenectomized mouse model of ?-thalassemia intermedia.
Iron Overload
SLN124, a GalNAc-siRNA Conjugate Targeting TMPRSS6, Efficiently Prevents Iron Overload in Hereditary Haemochromatosis Type 1.
Iron Overload
SLN124, a GalNac-siRNA targeting transmembrane serine protease 6, in combination with deferiprone therapy reduces ineffective erythropoiesis and hepatic iron-overload in a mouse model of ?-thalassaemia.
Iron Overload
Striking the target in iron overload disorders.
Iron Overload
The A736V TMPRSS6 polymorphism influences hepatic iron overload in nonalcoholic fatty liver disease.
Iron Overload
Tmprss6 is a genetic modifier of the Hfe-hemochromatosis phenotype in mice.
Iron Overload
[Iron deficiency and overload. Implications in oxidative stress and cardiovascular health]
Kidney Diseases
Proteolytic Cleavage of Podocin by Matriptase Exacerbates Podocyte Injury.
Kidney Failure, Chronic
Associations of Common Variants in HFE and TMPRSS6 Genes with Hepcidin-25 and Iron Status Parameters in Patients with End-Stage Renal Disease.
Leukemia
A novel serine protease SNC19 associated with human colorectal cancer.
Leukemia
Cloning and chromosomal mapping of a gene isolated from thymic stromal cells encoding a new mouse type II membrane serine protease, epithin, containing four LDL receptor modules and two CUB domains.
Leukemia, Lymphocytic, Chronic, B-Cell
Matriptase is highly upregulated in chronic lymphocytic leukemia and promotes cancer cell invasion.
Leukemia, Myeloid, Acute
[Expression and Clinical Significances of HGFA, Matriptase, HAI-1 and HAI-2 in Acute Myeloid Leukemia].
Leukemia, Myeloid, Acute
[Expression level and Clinical Significance of Serum SE-CAD and Matriptase in Patients with Acute Myeloid Leukemia].
Liver Cirrhosis
Evaluation of genome-wide loci of iron metabolism in hereditary hemochromatosis identifies PCSK7 as a host risk factor of liver cirrhosis.
Liver Diseases
The A736V TMPRSS6 polymorphism influences hepatic iron overload in nonalcoholic fatty liver disease.
Lung Injury
Membrane-anchored Serine Protease Matriptase is a Trigger of Pulmonary Fibrogenesis.
Lung Neoplasms
A novel serine protease SNC19 associated with human colorectal cancer.
Lung Neoplasms
Production of soluble matriptase by human cancer cell lines and cell surface activation of its zymogen by trypsin.
Lymphatic Metastasis
Expression and prognostic value of matriptase in ovarian serous adenocarcinoma.
Lymphatic Metastasis
Expression of matriptase and clinical outcome of human endometrial cancer.
Lymphatic Metastasis
Increased expression of matriptase is associated with histopathologic grades of cervical neoplasia.
Lymphoma
A Novel Antibody-Toxin Conjugate to Treat Mantle Cell Lymphoma.
Lymphoma
A novel serine protease SNC19 associated with human colorectal cancer.
Lymphoma
Imbalanced matriptase pericellular proteolysis contributes to the pathogenesis of malignant B-cell lymphomas.
Lymphoma, B-Cell
Imbalanced matriptase pericellular proteolysis contributes to the pathogenesis of malignant B-cell lymphomas.
Lymphoma, Follicular
Imbalanced matriptase pericellular proteolysis contributes to the pathogenesis of malignant B-cell lymphomas.
Lymphoma, Mantle-Cell
A Novel Antibody-Toxin Conjugate to Treat Mantle Cell Lymphoma.
matriptase deficiency
Decreased hemojuvelin protein levels in mask mice lacking matriptase-2-dependent proteolytic activity.
matriptase deficiency
EPO-mediated reduction in Hamp expression in vivo corrects iron deficiency anaemia in TMPRSS6 deficiency.
matriptase deficiency
Iron disorders of genetic origin: a changing world.
matriptase deficiency
Iron refractory iron deficiency anemia.
matriptase deficiency
Matriptase Regulates Proliferation and Early, but Not Terminal, Differentiation of Human Keratinocytes.
matriptase deficiency
Matriptase-2 deficiency protects from obesity by modulating iron homeostasis.
matriptase deficiency
The spatiotemporal control of human matriptase action on its physiological substrates: a case against a direct role for matriptase proteolytic activity in profilaggrin processing and desquamation.
matriptase deficiency
[Iron deficiency anaemia due to a matriptase-2 mutation].
Melanoma
A novel serine protease SNC19 associated with human colorectal cancer.
Melanoma
The expression of a type II transmembrane serine protease (Seprase) in human gastric carcinoma.
Mesothelioma, Malignant
Gene expression profiling identifies matriptase overexpression in malignant mesothelioma.
Milk Hypersensitivity
[Association of FokI rs2228570 and TMPRSS6 rs855791 polymorphisms with cow's milk protein allergy in children].
Neoplasm Metastasis
?-Ketobenzothiazole Serine Protease Inhibitors of Aberrant HGF/c-MET and MSP/RON Kinase Pathway Signaling in Cancer.
Neoplasm Metastasis
A Novel Antibody-Toxin Conjugate to Treat Mantle Cell Lymphoma.
Neoplasm Metastasis
Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease.
Neoplasm Metastasis
Addition of beta1-6 GlcNAc branching to the oligosaccharide attached to Asn 772 in the serine protease domain of matriptase plays a pivotal role in its stability and resistance against trypsin.
Neoplasm Metastasis
Androgen-Induced TMPRSS2 Activates Matriptase and Promotes Extracellular Matrix Degradation, Prostate Cancer Cell Invasion, Tumor Growth, and Metastasis.
Neoplasm Metastasis
Coordinate expression and functional profiling identify an extracellular proteolytic signaling pathway.
Neoplasm Metastasis
Curcumin-targeting Pericellular Serine Protease Matriptase Role in Suppression of Prostate Cancer Cell Invasion, Tumor Growth and Metastasis.
Neoplasm Metastasis
Decreasing the ratio of matriptase/HAI?1 by downregulation of matriptase as a potential adjuvant therapy in ovarian cancer.
Neoplasm Metastasis
Design and synthesis of novel and potent inhibitors of the type II transmembrane serine protease, matriptase, based upon the sunflower trypsin inhibitor-1.
Neoplasm Metastasis
Development of a Protease Biosensor Based on a Dimerization-Dependent Red Fluorescent Protein.
Neoplasm Metastasis
Differential expression of genes encoding proteins of the HGF/MET system in insulinomas.
Neoplasm Metastasis
Discovery of novel 2-hydroxydiarylamide derivatives as TMPRSS4 inhibitors.
Neoplasm Metastasis
Down-regulation of matriptase by overexpression of bikunin attenuates cell invasion in prostate carcinoma cells.
Neoplasm Metastasis
Downexpression of Matriptase-2 Correlates With Tumor Progression and Clinical Prognosis in Oral Squamous-Cell Carcinoma.
Neoplasm Metastasis
Dysregulated HAI-2 Plays an Important Role in Renal Cell Carcinoma Bone Metastasis through Ligand-Dependent MET Phosphorylation.
Neoplasm Metastasis
Evaluating the function of matriptase and N-acetylglucosaminyltransferase V in prostate cancer metastasis.
Neoplasm Metastasis
Expression and prognostic value of matriptase in ovarian serous adenocarcinoma.
Neoplasm Metastasis
Expression of hepatocyte growth factor activator inhibitor-1 (HAI-1) gene in prostate cancer: Clinical and biological significance.
Neoplasm Metastasis
Expression of matriptase and clinical outcome of human endometrial cancer.
Neoplasm Metastasis
Genetic upregulation of matriptase-2 reduces the aggressiveness of prostate cancer cells in vitro and in vivo and affects FAK and paxillin localisation.
Neoplasm Metastasis
HAI-2 suppresses the invasive growth and metastasis of prostate cancer through regulation of matriptase.
Neoplasm Metastasis
Hepsin activates pro-hepatocyte growth factor and is inhibited by hepatocyte growth factor activator inhibitor-1B (HAI-1B) and HAI-2.
Neoplasm Metastasis
Increased expression of matriptase is associated with histopathologic grades of cervical neoplasia.
Neoplasm Metastasis
Inhibition of cyclooxygenase-2-mediated matriptase activation contributes to the suppression of prostate cancer cell motility and metastasis.
Neoplasm Metastasis
Intramembrane proteolysis of an extracellular serine protease, epithin/PRSS14, enables its intracellular nuclear function.
Neoplasm Metastasis
Kempopeptin C, a Novel Marine-Derived Serine Protease Inhibitor Targeting Invasive Breast Cancer.
Neoplasm Metastasis
Matriptase and MET are prominently expressed at the site of bone metastasis in renal cell carcinoma: immunohistochemical analysis.
Neoplasm Metastasis
Secondary amides of sulfonylated 3-amidinophenylalanine. New potent and selective inhibitors of matriptase.
Neoplasm Metastasis
Shedding of epithin/PRSS14 is induced by TGF-? and mediated by tumor necrosis factor-? converting enzyme.
Neoplasm Metastasis
Soluble epithin/PRSS14 secreted from cancer cells contains active angiogenic potential.
Neoplasm Metastasis
Specifically targeting cancer proliferation and metastasis processes: the development of matriptase inhibitors.
Neoplasm Metastasis
Structure-based approach for the discovery of bis-benzamidines as novel inhibitors of matriptase.
Neoplasm Metastasis
Structure-based design, synthesis, and biological evaluation of Leu-Arg dipeptide analogs as novel hepsin inhibitors.
Neoplasm Metastasis
Structure-guided discovery of 1,3,5 tri-substituted benzenes as potent and selective matriptase inhibitors exhibiting in vivo antitumor efficacy.
Neoplasm Metastasis
Structure-guided discovery of 2-aryl/pyridin-2-yl-1H-indole derivatives as potent and selective hepsin inhibitors.
Neoplasm Metastasis
The androgen-regulated type II serine protease TMPRSS2 is differentially expressed and mislocalized in prostate adenocarcinoma.
Neoplasm Metastasis
The macrophage-stimulating protein pathway promotes metastasis in a mouse model for breast cancer and predicts poor prognosis in humans.
Neoplasm Metastasis
The novel serine protease tumor-associated differentially expressed gene-15 (matriptase/MT-SP1) is highly overexpressed in cervical carcinoma.
Neoplasm Metastasis
TMPRSS4 induces cancer stem cell-like properties in lung cancer cells and correlates with ALDH expression in NSCLC patients.
Neoplasm Metastasis
[Study on post-translational processing and active forms of the novel metastasis-associated protein SNC19]
Neoplasms
3-Cl-AHPC inhibits pro-HGF maturation by inducing matriptase/HAI-1 complex formation.
Neoplasms
?-Ketobenzothiazole Serine Protease Inhibitors of Aberrant HGF/c-MET and MSP/RON Kinase Pathway Signaling in Cancer.
Neoplasms
A nanometer-sized protease inhibitor for precise cancer diagnosis and treatment.
Neoplasms
A Novel Antibody-Toxin Conjugate to Treat Mantle Cell Lymphoma.
Neoplasms
A novel biomarker for staging human prostate adenocarcinoma: overexpression of matriptase with concomitant loss of its inhibitor, hepatocyte growth factor activator inhibitor-1.
Neoplasms
A novel serine protease SNC19 associated with human colorectal cancer.
Neoplasms
A pan-cancer analysis of alternative splicing events reveals novel tumor-associated splice variants of matriptase.
Neoplasms
A supramolecular nanocarrier for efficient cancer imaging and therapy by targeting at matriptase.
Neoplasms
Activated matriptase as a target to treat breast cancer with a drug conjugate.
Neoplasms
Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease.
Neoplasms
Addition of beta1-6 GlcNAc branching to the oligosaccharide attached to Asn 772 in the serine protease domain of matriptase plays a pivotal role in its stability and resistance against trypsin.
Neoplasms
An investigation of the relationship between TMPRSS6 gene expression, genetic variants and clinical findings in breast cancer.
Neoplasms
Androgen-Induced TMPRSS2 Activates Matriptase and Promotes Extracellular Matrix Degradation, Prostate Cancer Cell Invasion, Tumor Growth, and Metastasis.
Neoplasms
Bikunin target genes in ovarian cancer cells identified by microarray analysis.
Neoplasms
c-Met-induced epithelial carcinogenesis is initiated by the serine protease matriptase.
Neoplasms
Cell Surface Human Airway Trypsin-Like Protease Is Lost During Squamous Cell Carcinogenesis.
Neoplasms
Characterization of matriptase expression in normal human tissues.
Neoplasms
Clinical relevance of hepsin and hepatocyte growth factor activator inhibitor type 2 expression in renal cell carcinoma.
Neoplasms
Co-expression of matriptase and N-acetylglucosaminyltransferase V in thyroid cancer tissues--its possible role in prolonged stability in vivo by aberrant glycosylation.
Neoplasms
Co-localization of the channel activating protease prostasin/(CAP1/PRSS8) with its candidate activator, matriptase.
Neoplasms
Combinatorial optimization of cystine-knot peptides towards high-affinity inhibitors of human matriptase-1.
Neoplasms
Coordinate expression and functional profiling identify an extracellular proteolytic signaling pathway.
Neoplasms
Crystal structures of matriptase in complex with its inhibitor hepatocyte growth factor activator inhibitor-1.
Neoplasms
Curcumin-targeting Pericellular Serine Protease Matriptase Role in Suppression of Prostate Cancer Cell Invasion, Tumor Growth and Metastasis.
Neoplasms
CVS-3983, a selective matriptase inhibitor, suppresses the growth of androgen independent prostate tumor xenografts.
Neoplasms
Decreased matriptase/HAI-1 ratio in advanced colorectal adenocarcinoma of Chinese patients.
Neoplasms
Deregulated activation of matriptase in breast cancer cells.
Neoplasms
Deregulated matriptase causes ras-independent multistage carcinogenesis and promotes ras-mediated malignant transformation.
Neoplasms
Design and synthesis of potent, selective inhibitors of matriptase.
Neoplasms
Development of a Protease Biosensor Based on a Dimerization-Dependent Red Fluorescent Protein.
Neoplasms
Differential Tumorigenic Potential and Matriptase Activation between PDGF B versus PDGF D in Prostate Cancer.
Neoplasms
Discovery of O-(3-carbamimidoylphenyl)-l-serine amides as matriptase inhibitors using a fragment-linking approach.
Neoplasms
Discovery of Selective Matriptase and Hepsin Serine Protease Inhibitors: Useful Chemical Tools for Cancer Cell Biology.
Neoplasms
Diversity of matriptase expression level and function in breast cancer.
Neoplasms
Downexpression of Matriptase-2 Correlates With Tumor Progression and Clinical Prognosis in Oral Squamous-Cell Carcinoma.
Neoplasms
Dysregulation of Type II Transmembrane Serine Proteases and Ligand-Dependent Activation of MET in Urological Cancers.
Neoplasms
Engineering a potent inhibitor of matriptase from the natural hepatocyte growth factor activator inhibitor type-1 (HAI-1) protein.
Neoplasms
Epithin, a target of transforming growth factor-beta signaling, mediates epithelial-mesenchymal transition.
Neoplasms
Epithin/PRSS14 proteolytically regulates angiopoietin receptor Tie2 during transendothelial migration.
Neoplasms
Evaluating the function of matriptase and N-acetylglucosaminyltransferase V in prostate cancer metastasis.
Neoplasms
Expression and prognostic value of matriptase in ovarian serous adenocarcinoma.
Neoplasms
Expression of EMMPRIN and matriptase in esophageal squamous cell carcinoma: correlation with clinicopathological parameters.
Neoplasms
Expression of hepatocyte growth factor activator inhibitor-1 (HAI-1) gene in prostate cancer: Clinical and biological significance.
Neoplasms
Expression of matriptase and clinical outcome of human endometrial cancer.
Neoplasms
Expression of matriptase correlates with tumour progression and clinical prognosis in oral squamous cell carcinoma.
Neoplasms
Expression of serine protease matriptase in renal cell carcinoma: correlation of tissue microarray immunohistochemical expression analysis results with clinicopathological parameters.
Neoplasms
Expression of the serine protease matriptase and its inhibitor HAI-1 in epithelial ovarian cancer: correlation with clinical outcome and tumor clinicopathological parameters.
Neoplasms
Expression of the serine protease, matriptase, in breast ductal carcinoma of Chinese women: correlation with clinicopathological parameters.
Neoplasms
Function and clinical relevance of kallikrein-related peptidases and other serine proteases in gynecological cancers.
Neoplasms
Genetic reduction of matriptase-1 expression is associated with a reduction in the aggressive phenotype of prostate cancer cells in vitro and in vivo.
Neoplasms
Genetic upregulation of matriptase-2 reduces the aggressiveness of prostate cancer cells in vitro and in vivo and affects FAK and paxillin localisation.
Neoplasms
Gold nanoparticles based molecular beacons for in vitro and in vivo detection of the matriptase expression on tumor.
Neoplasms
HAI-2 stabilizes, inhibits and regulates SEA-cleavage-dependent secretory transport of matriptase.
Neoplasms
HAI-2 suppresses the invasive growth and metastasis of prostate cancer through regulation of matriptase.
Neoplasms
HATL5: A Cell Surface Serine Protease Differentially Expressed in Epithelial Cancers.
Neoplasms
Hepsin activates pro-hepatocyte growth factor and is inhibited by hepatocyte growth factor activator inhibitor-1B (HAI-1B) and HAI-2.
Neoplasms
High expression level of TMPRSS4 predicts adverse outcomes of colorectal cancer patients.
Neoplasms
High-affinity cyclic peptide matriptase inhibitors.
Neoplasms
Human Cancer Cells Retain Modest Levels of Enzymatically Active Matriptase Only in Extracellular Milieu following Induction of Zymogen Activation.
Neoplasms
Imaging a functional tumorigenic biomarker in the transformed epithelium.
Neoplasms
Imaging of Fibroblast Activation Protein Alpha Expression in a Preclinical Mouse Model of Glioma Using Positron Emission Tomography.
Neoplasms
Imbalanced matriptase pericellular proteolysis contributes to the pathogenesis of malignant B-cell lymphomas.
Neoplasms
Improving the species cross-reactivity of an antibody using computational design.
Neoplasms
Increased expression of matriptase is associated with histopathologic grades of cervical neoplasia.
Neoplasms
Increasing EMMPRIN and matriptase expression in hepatocellular carcinoma: tissue microarray analysis of immunohistochemical scores with clinicopathological parameters.
Neoplasms
Increasing expression of serine protease matriptase in ovarian tumors: tissue microarray analysis of immunostaining score with clinicopathological parameters.
Neoplasms
Inhibition of an active zymogen protease: the zymogen form of matriptase is regulated by HAI-1 and HAI-2.
Neoplasms
Inhibition of cyclooxygenase-2-mediated matriptase activation contributes to the suppression of prostate cancer cell motility and metastasis.
Neoplasms
Inhibition of human matriptase by eglin c variants.
Neoplasms
Inhibition of tumor invasion by genomic down-regulation of matriptase through suppression of activation of receptor-bound pro-urokinase.
Neoplasms
Inhibitors of HGFA, Matriptase, and Hepsin Serine Proteases: A Nonkinase Strategy to Block Cell Signaling in Cancer.
Neoplasms
Intramembrane proteolysis of an extracellular serine protease, epithin/PRSS14, enables its intracellular nuclear function.
Neoplasms
Kallikrein 5 Inhibition by the Lympho-Epithelial Kazal-Type Related Inhibitor Hinders Matriptase-Dependent Carcinogenesis.
Neoplasms
Kempopeptin C, a Novel Marine-Derived Serine Protease Inhibitor Targeting Invasive Breast Cancer.
Neoplasms
Knockdown of TMPRSS3, a Transmembrane Serine Protease, Inhibits the Proliferation, Migration, and Invasion in Human Nasopharyngeal Carcinoma Cells.
Neoplasms
Loss of the matriptase inhibitor HAI-2 during prostate cancer progression.
Neoplasms
Matriptase activates stromelysin (MMP-3) and promotes tumor growth and angiogenesis.
Neoplasms
Matriptase activation and shedding with HAI-1 is induced by steroid sex hormones in human prostate cancer cells, but not in breast cancer cells.
Neoplasms
Matriptase activation connects tissue factor-dependent coagulation initiation to epithelial proteolysis and signaling.
Neoplasms
Matriptase and HAI-1 are expressed by normal and malignant epithelial cells in vitro and in vivo.
Neoplasms
Matriptase and its putative role in cancer.
Neoplasms
Matriptase and survivin expression associated with tumor progression and malignant potential in breast cancer of Chinese women: tissue microarray analysis of immunostaining scores with clinicopathological parameters.
Neoplasms
Matriptase expression in the normal and neoplastic mast cells.
Neoplasms
Matriptase is highly upregulated in chronic lymphocytic leukemia and promotes cancer cell invasion.
Neoplasms
Matriptase Is Involved in ErbB-2-Induced Prostate Cancer Cell Invasion.
Neoplasms
Matriptase promotes inflammatory cell accumulation and progression of established epidermal tumors.
Neoplasms
Matriptase regulates c-Met mediated proliferation and invasion in inflammatory breast cancer.
Neoplasms
Matriptase-2 gene (TMPRSS6) variants associate with breast cancer survival, and reduced expression is related to triple-negative breast cancer.
Neoplasms
Matriptase-2 inhibits breast tumor growth and invasion and correlates with favorable prognosis for breast cancer patients.
Neoplasms
Matriptase-2 inhibits HECV motility and tubule formation in vitro and tumour angiogenesis in vivo.
Neoplasms
Matriptase-Induced Phosphorylation of MET is Significantly Associated with Poor Prognosis in Invasive Bladder Cancer; an Immunohistochemical Analysis.
Neoplasms
Matriptase: a culprit in cancer?
Neoplasms
Matriptase: potent proteolysis on the cell surface.
Neoplasms
Mechanisms for the control of matriptase activity in the absence of sufficient HAI-1.
Neoplasms
Mechanisms of hepatocyte growth factor activation in cancer tissues.
Neoplasms
Metabolism and distribution of two highly potent and selective peptidomimetic inhibitors of matriptase.
Neoplasms
MT-SP1 proteolysis and regulation of cell-microenvironment interactions.
Neoplasms
Ovarian tumor cells express a transmembrane serine protease: a potential candidate for early diagnosis and therapeutic intervention.
Neoplasms
Overexpression of matriptase correlates with poor prognosis in esophageal squamous cell carcinoma.
Neoplasms
Overexpression of matriptase in tumor stroma is a poor prognostic indicator of extrahepatic bile duct cancer.
Neoplasms
Pericellular activation of hepatocyte growth factor by the transmembrane serine proteases matriptase and hepsin, but not by the membrane-associated protease uPA.
Neoplasms
Polyserase-1/TMPRSS9 induces pro-tumor effects in pancreatic cancer cells by activation of pro-uPA.
Neoplasms
Potent and specific inhibition of the biological activity of the type-II transmembrane serine protease matriptase by the cyclic microprotein MCoTI-II.
Neoplasms
Probing the interaction mechanism of small molecule inhibitors with matriptase based on molecular dynamics simulation and free energy calculations.
Neoplasms
Production of soluble matriptase by human cancer cell lines and cell surface activation of its zymogen by trypsin.
Neoplasms
Prognostic value of TMPRSS4 expression in patients with breast cancer.
Neoplasms
Prostate specific antigen gene expression in androgen insensitive prostate carcinoma subculture cell line.
Neoplasms
Protease-activated receptor-2 accelerates intestinal tumor formation through activation of nuclear factor-?B signaling and tumor angiogenesis in ApcMin/+ mice.
Neoplasms
Protein expression of matriptase and its cognate inhibitor HAI-1 in human prostate cancer: a tissue microarray and automated quantitative analysis.
Neoplasms
Proteolytic activation of pro-macrophage-stimulating protein by hepsin.
Neoplasms
PRSS14/Epithin is induced in macrophages by the IFN-?/JAK/STAT pathway and mediates transendothelial migration.
Neoplasms
Rapid Assessment of Surface Markers on Cancer Cells Using Immuno-Magnetic Separation and Multi-frequency Impedance Cytometry for Targeted Therapy.
Neoplasms
Role of TMPRSS4 Modulation in Breast Cancer Cell Proliferation.
Neoplasms
Sampling the N-terminal proteome of human blood.
Neoplasms
Secondary amides of sulfonylated 3-amidinophenylalanine. New potent and selective inhibitors of matriptase.
Neoplasms
Shedding of epithin/PRSS14 is induced by TGF-? and mediated by tumor necrosis factor-? converting enzyme.
Neoplasms
Soluble epithin/PRSS14 secreted from cancer cells contains active angiogenic potential.
Neoplasms
Sp1 decoy transfected to carcinoma cells suppresses the expression of vascular endothelial growth factor, transforming growth factor beta1, and tissue factor and also cell growth and invasion activities.
Neoplasms
Specifically targeting cancer proliferation and metastasis processes: the development of matriptase inhibitors.
Neoplasms
SPINT2 Deregulation in Prostate Carcinoma.
Neoplasms
Structure-activity relationship studies of dipeptide-based hepsin inhibitors with Arg bioisosteres.
Neoplasms
Structure-based approach for the discovery of bis-benzamidines as novel inhibitors of matriptase.
Neoplasms
Structure-guided discovery of 1,3,5 tri-substituted benzenes as potent and selective matriptase inhibitors exhibiting in vivo antitumor efficacy.
Neoplasms
Targeting matriptase in breast cancer abrogates tumour progression via impairment of stromal-epithelial growth factor signalling.
Neoplasms
The androgen-regulated type II serine protease TMPRSS2 is differentially expressed and mislocalized in prostate adenocarcinoma.
Neoplasms
The expression of a type II transmembrane serine protease (Seprase) in human gastric carcinoma.
Neoplasms
THE IMPACT OF ALCOHOL ON PRO-METASTATIC N-GLYCOSYLATION IN PROSTATE CANCER.
Neoplasms
The influence of matriptase-2 on prostate cancer in vitro: A possible role for ?-catenin.
Neoplasms
The Kunitz Domain I of Hepatocyte Growth Factor Activator Inhibitor-2 Inhibits Matriptase Activity and Invasive Ability of Human Prostate Cancer Cells.
Neoplasms
The novel serine protease tumor-associated differentially expressed gene-15 (matriptase/MT-SP1) is highly overexpressed in cervical carcinoma.
Neoplasms
The role of TMPRSS6/matriptase-2 in iron regulation and anemia.
Neoplasms
The type II transmembrane serine protease matriptase-2--identification, structural features, enzymology, expression pattern and potential roles.
Neoplasms
The type II transmembrane serine protease, matriptase-2: Possible links to cancer?
Neoplasms
Time-domain in vivo near infrared fluorescence imaging for evaluation of matriptase as a potential target for the development of novel, inhibitor-based tumor therapies.
Neoplasms
TMPRSS13 promotes cell survival, invasion, and resistance to drug-induced apoptosis in colorectal cancer.
Neoplasms
TMPRSS2 Correlated With Immune Infiltration Serves as a Prognostic Biomarker in Prostatic Adenocarcinoma: Implication for the COVID-2019.
Neoplasms
TMPRSS4 correlates with colorectal cancer pathological stage and regulates cell proliferation and self-renewal ability.
Neoplasms
TMPRSS4 induces cancer cell invasion through pro-uPA processing.
Neoplasms
TMPRSS4 induces cancer stem cell-like properties in lung cancer cells and correlates with ALDH expression in NSCLC patients.
Neoplasms
TMPRSS4 induces invasion and epithelial-mesenchymal transition through upregulation of integrin alpha5 and its signaling pathways.
Neoplasms
TMPRSS4 induces invasion and proliferation of prostate cancer cells through induction of Slug and cyclin D1.
Neoplasms
TMPRSS4 is a type II transmembrane serine protease involved in cancer and viral infections.
Neoplasms
TMPRSS4 upregulates uPA gene expression through JNK signaling activation to induce cancer cell invasion.
Neoplasms
Transmembrane serine protease TADG-15 (ST14/Matriptase/MT-SP1): expression and prognostic value in ovarian cancer.
Neoplasms
Tumor detection by imaging proteolytic activity.
Neoplasms
Type II transmembrane serine protease (TTSP) deregulation in cancer.
Neoplasms
Type II transmembrane serine proteases as potential targets for cancer therapy.
Neoplasms
Use of IHC and newly designed matriptase inhibitors to elucidate the role of matriptase in pancreatic ductal adenocarcinoma.
Neoplasms
Zebrafish modeling reveals that SPINT1 regulates the aggressiveness of skin cutaneous melanoma and its crosstalk with tumor immune microenvironment.
Neoplasms
[Study on post-translational processing and active forms of the novel metastasis-associated protein SNC19]
Netherton Syndrome
Matriptase initiates activation of epidermal pro-kallikrein and disease onset in a mouse model of Netherton syndrome.
Netherton Syndrome
Toward the first class of suicide inhibitors of kallikreins involved in skin diseases.
Neural Tube Defects
Regulation of cell surface protease matriptase by HAI2 is essential for placental development, neural tube closure and embryonic survival in mice.
Neuroblastoma
Matriptase cleaves the amyloid-beta peptide 1-42 at Arg-5, Lys-16, and Lys-28.
Non-alcoholic Fatty Liver Disease
The A736V TMPRSS6 polymorphism influences hepatic iron overload in nonalcoholic fatty liver disease.
Obesity
Matriptase-2 deficiency protects from obesity by modulating iron homeostasis.
Osteoarthritis
Changing the selectivity profile - from substrate analog inhibitors of thrombin and factor Xa to potent matriptase inhibitors.
Osteoarthritis
Development of a Protease Biosensor Based on a Dimerization-Dependent Red Fluorescent Protein.
Osteoarthritis
Matriptase Induction of Metalloproteinase-Dependent Aggrecanolysis In Vitro and In Vivo: Promotion of Osteoarthritic Cartilage Damage by Multiple Mechanisms.
Osteoarthritis
Matriptase is a novel initiator of cartilage matrix degradation in osteoarthritis.
Osteoarthritis
Protease activated receptor 2 and matriptase expression in the joints of cats with and without osteoarthritis.
Ovarian Neoplasms
Decreasing the ratio of matriptase/HAI?1 by downregulation of matriptase as a potential adjuvant therapy in ovarian cancer.
Ovarian Neoplasms
Expression of hepatocyte growth factor activator inhibitors (HAI-1 and HAI-2) in ovarian cancer.
Ovarian Neoplasms
Expression of the serine protease matriptase and its inhibitor HAI-1 in epithelial ovarian cancer: correlation with clinical outcome and tumor clinicopathological parameters.
Ovarian Neoplasms
Increasing expression of serine protease matriptase in ovarian tumors: tissue microarray analysis of immunostaining score with clinicopathological parameters.
Ovarian Neoplasms
Inhibition of tumor invasion by genomic down-regulation of matriptase through suppression of activation of receptor-bound pro-urokinase.
Ovarian Neoplasms
Possible role of matriptase in the diagnosis of ovarian cancer.
Ovarian Neoplasms
Transmembrane serine protease TADG-15 (ST14/Matriptase/MT-SP1): expression and prognostic value in ovarian cancer.
Ovarian Neoplasms
[Expression and significance of matriptase in ovarian cancer cells with diverse metastatic potential].
Pancreatic Neoplasms
Use of IHC and newly designed matriptase inhibitors to elucidate the role of matriptase in pancreatic ductal adenocarcinoma.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Examination of HFE associations with childhood leukemia risk and extension to other iron regulatory genes.
Prostatic Hyperplasia
A novel biomarker for staging human prostate adenocarcinoma: overexpression of matriptase with concomitant loss of its inhibitor, hepatocyte growth factor activator inhibitor-1.
Prostatic Intraepithelial Neoplasia
A novel biomarker for staging human prostate adenocarcinoma: overexpression of matriptase with concomitant loss of its inhibitor, hepatocyte growth factor activator inhibitor-1.
Prostatic Neoplasms
A novel biomarker for staging human prostate adenocarcinoma: overexpression of matriptase with concomitant loss of its inhibitor, hepatocyte growth factor activator inhibitor-1.
Prostatic Neoplasms
Androgen receptor non-nuclear regulation of prostate cancer cell invasion mediated by Src and matriptase.
Prostatic Neoplasms
Androgen-Induced TMPRSS2 Activates Matriptase and Promotes Extracellular Matrix Degradation, Prostate Cancer Cell Invasion, Tumor Growth, and Metastasis.
Prostatic Neoplasms
Author Correction: The Kunitz Domain I of Hepatocyte Growth Factor Activator Inhibitor-2 Inhibits Matriptase Activity and Invasive Ability of Human Prostate Cancer Cells.
Prostatic Neoplasms
Curcumin-targeting Pericellular Serine Protease Matriptase Role in Suppression of Prostate Cancer Cell Invasion, Tumor Growth and Metastasis.
Prostatic Neoplasms
CVS-3983, a selective matriptase inhibitor, suppresses the growth of androgen independent prostate tumor xenografts.
Prostatic Neoplasms
Development of an Activatable Fluorescent Probe for Prostate Cancer Imaging.
Prostatic Neoplasms
Differential Tumorigenic Potential and Matriptase Activation between PDGF B versus PDGF D in Prostate Cancer.
Prostatic Neoplasms
Discovery of O-(3-carbamimidoylphenyl)-l-serine amides as matriptase inhibitors using a fragment-linking approach.
Prostatic Neoplasms
Down-regulation of matriptase by overexpression of bikunin attenuates cell invasion in prostate carcinoma cells.
Prostatic Neoplasms
Dynamic regulation of platelet-derived growth factor D (PDGF-D) activity and extracellular spatial distribution by matriptase-mediated proteolysis.
Prostatic Neoplasms
Evaluating the function of matriptase and N-acetylglucosaminyltransferase V in prostate cancer metastasis.
Prostatic Neoplasms
From in-silico to Experimental Validation: Tailoring Peptide Substrates for a Serine Protease.
Prostatic Neoplasms
Genetic reduction of matriptase-1 expression is associated with a reduction in the aggressive phenotype of prostate cancer cells in vitro and in vivo.
Prostatic Neoplasms
Genetic upregulation of matriptase-2 reduces the aggressiveness of prostate cancer cells in vitro and in vivo and affects FAK and paxillin localisation.
Prostatic Neoplasms
HAI-2 suppresses the invasive growth and metastasis of prostate cancer through regulation of matriptase.
Prostatic Neoplasms
Hepsin activates pro-hepatocyte growth factor and is inhibited by hepatocyte growth factor activator inhibitor-1B (HAI-1B) and HAI-2.
Prostatic Neoplasms
Hepsin inhibits CDK11p58 IRES activity by suppressing unr expression and eIF-2? phosphorylation in prostate cancer.
Prostatic Neoplasms
HEPSIN inhibits cell growth/invasion in prostate cancer cells.
Prostatic Neoplasms
HLA-A2-restricted Cytotoxic T Lymphocyte Epitopes from Human Hepsin as Novel Targets for Prostate Cancer Immunotherapy.
Prostatic Neoplasms
Identification and characterization of small-molecule inhibitors of hepsin.
Prostatic Neoplasms
Inhibition of cyclooxygenase-2-mediated matriptase activation contributes to the suppression of prostate cancer cell motility and metastasis.
Prostatic Neoplasms
Laminin-332 cleavage by matriptase alters motility parameters of prostate cancer cells.
Prostatic Neoplasms
Loss of the matriptase inhibitor HAI-2 during prostate cancer progression.
Prostatic Neoplasms
Matriptase activation and shedding with HAI-1 is induced by steroid sex hormones in human prostate cancer cells, but not in breast cancer cells.
Prostatic Neoplasms
Matriptase Is Involved in ErbB-2-Induced Prostate Cancer Cell Invasion.
Prostatic Neoplasms
Pro-urokinase-type plasminogen activator is a substrate for hepsin.
Prostatic Neoplasms
Protein expression of matriptase and its cognate inhibitor HAI-1 in human prostate cancer: a tissue microarray and automated quantitative analysis.
Prostatic Neoplasms
Structure-activity relationship studies of dipeptide-based hepsin inhibitors with Arg bioisosteres.
Prostatic Neoplasms
Structure-based design, synthesis, and biological evaluation of Leu-Arg dipeptide analogs as novel hepsin inhibitors.
Prostatic Neoplasms
Structure-guided discovery of 2-aryl/pyridin-2-yl-1H-indole derivatives as potent and selective hepsin inhibitors.
Prostatic Neoplasms
The influence of matriptase-2 on prostate cancer in vitro: A possible role for ?-catenin.
Prostatic Neoplasms
The Kunitz Domain I of Hepatocyte Growth Factor Activator Inhibitor-2 Inhibits Matriptase Activity and Invasive Ability of Human Prostate Cancer Cells.
Prostatic Neoplasms
TMEFF2 shedding is regulated by oxidative stress and mediated by ADAMs and transmembrane serine proteases implicated in prostate cancer.
Pulmonary Fibrosis
Membrane-anchored Serine Protease Matriptase is a Trigger of Pulmonary Fibrogenesis.
Renal Insufficiency, Chronic
TMPRSS6 rs855791 polymorphism and susceptibility to iron deficiency anaemia in non-dialysis chronic kidney disease patients in South Africa.
Restless Legs Syndrome
Genetic factors influencing hemoglobin levels in 15,567 blood donors: results from the Danish Blood Donor Study.
Sarcoma
Matriptase and HAI-1 are expressed by normal and malignant epithelial cells in vitro and in vivo.
Severe Acute Respiratory Syndrome
A phase I study of high dose camostat mesylate in healthy adults provides a rationale to repurpose the TMPRSS2 inhibitor for the treatment of COVID-19.
Severe Acute Respiratory Syndrome
Sex, Hormones, Immune Functions, and Susceptibility to Coronavirus Disease 2019 (COVID-19)-Related Morbidity.
Severe Acute Respiratory Syndrome
Simultaneous treatment of human bronchial epithelial cells with serine and cysteine protease inhibitors prevents severe acute respiratory syndrome coronavirus entry.
Skin Diseases
Increased matriptase zymogen activation in inflammatory skin disorders.
Skin Diseases
Toward the first class of suicide inhibitors of kallikreins involved in skin diseases.
Skin Neoplasms
Role of Matriptase and Proteinase-Activated Receptor-2 in Nonmelanoma Skin Cancer.
Squamous Cell Carcinoma of Head and Neck
Deregulated matriptase activity in oral squamous cell carcinoma promotes the infiltration of cancer-associated fibroblasts by paracrine activation of protease-activated receptor 2.
Squamous Cell Carcinoma of Head and Neck
Expression of matriptase correlates with tumour progression and clinical prognosis in oral squamous cell carcinoma.
Stomach Neoplasms
A novel serine protease SNC19 associated with human colorectal cancer.
Stomach Neoplasms
Matriptase activates stromelysin (MMP-3) and promotes tumor growth and angiogenesis.
Stomach Neoplasms
Prometastatic effect of N-acetylglucosaminyltransferase V is due to modification and stabilization of active matriptase by adding beta 1-6 GlcNAc branching.
Stomach Neoplasms
TMPRSS4 promotes invasion, migration and metastasis of human tumor cells by facilitating an epithelial-mesenchymal transition.
Thalassemia
Design and chemical syntheses of potent matriptase-2 inhibitors based on trypsin inhibitor SFTI-1 isolated from sunflower seeds.
Thalassemia
Iron and hepcidin: a story of recycling and balance.
Thalassemia
The role of TMPRSS6 polymorphisms in iron deficiency anemia partially responsive to oral iron treatment.
Thalassemia
The V736A TMPRSS6 polymorphism influences liver iron concentration in nontransfusion-dependent thalassemias.
Thrombocytosis
Low Iron Promotes Megakaryocytic Commitment of Megakaryocytic-Erythroid Progenitors in Humans and Mice.
Thromboembolism
Design and synthesis of novel and potent inhibitors of the type II transmembrane serine protease, matriptase, based upon the sunflower trypsin inhibitor-1.
Thymoma
Epithin/PRSS14 proteolytically regulates angiopoietin receptor Tie2 during transendothelial migration.
Thymoma
Soluble epithin/PRSS14 secreted from cancer cells contains active angiogenic potential.
Thyroid Neoplasms
Co-expression of matriptase and N-acetylglucosaminyltransferase V in thyroid cancer tissues--its possible role in prolonged stability in vivo by aberrant glycosylation.
Triple Negative Breast Neoplasms
Matriptase-2 gene (TMPRSS6) variants associate with breast cancer survival, and reduced expression is related to triple-negative breast cancer.
Urinary Bladder Neoplasms
Expression of protease activating receptor-2 (PAR-2) is positively correlated with the recurrence of non-muscle invasive bladder cancer: an immunohistochemical analysis.
Urinary Bladder Neoplasms
Ibuprofen regulates the expression and function of membrane-associated serine proteases prostasin and matriptase.
Urinary Bladder Neoplasms
Matriptase-Induced Phosphorylation of MET is Significantly Associated with Poor Prognosis in Invasive Bladder Cancer; an Immunohistochemical Analysis.
Urologic Neoplasms
Dysregulation of Type II Transmembrane Serine Proteases and Ligand-Dependent Activation of MET in Urological Cancers.
Uterine Cervical Neoplasms
A novel serine protease SNC19 associated with human colorectal cancer.
Virus Diseases
TMPRSS4 is a type II transmembrane serine protease involved in cancer and viral infections.
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0.000457
1-[(4S)-4-amino-5-(1,3-benzothiazol-2-yl)-5-oxopentyl]guanidine
matriptase, pH and temperature not specified in the publication
0.0000014
2-(L-alanyl-L-arginyl)-1,3-benzothiazole
matriptase, pH and temperature not specified in the publication
0.0061
L-arginyl-L-glutaminyl-N-[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-hydroxypentan-2-yl]-L-alaninamide
matriptase, pH and temperature not specified in the publication
0.0000046
L-arginyl-N1-[(2S)-1-[[(2R)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
matriptase, pH and temperature not specified in the publication
0.000000011 - 0.0000033
L-arginyl-N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
0.0000095
L-arginyl-N1-[(2S)-1-[[(2S)-6-amino-1-(1,3-benzothiazol-2-yl)-1-oxohexan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
matriptase, pH and temperature not specified in the publication
0.000052 - 0.1
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
0.003 - 0.28
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
0.000000088
N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
matriptase, pH and temperature not specified in the publication
0.000046 - 0.03
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
0.0026 - 0.62
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
0.000003
(1r,4r)-4-amino-N-(3,5-bis(4-carbamimidoylphenoxy)phenyl)cyclohexanecarboxamide
pH 8.5, temperature not specified in the publication
0.000001
(1r,4r)-4-aminocyclohexyl 3,5-bis(4-carbamimidoylphenoxy)benzoate
pH 8.5, temperature not specified in the publication
0.00018
(2R)-1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-2-carboxylic acid
-
-
0.011
(2S)-1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-2-carboxylic acid
-
-
0.000018
1-(2-aminoethyl)-N-(3,5-bis(4-carbamimidoylphenoxy)phenyl)piperidine-4-carboxamide
pH 8.5, temperature not specified in the publication
0.000061
1-(3-aminopropanoyl)-N-(3,5-bis(4-carbamimidoylphenoxy)phenyl)piperidine-4-carboxamide
pH 8.5, temperature not specified in the publication
0.000031
1-(N-[[3-(b-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-3-carboxamide
-
-
0.000013
1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-4-carboxamide
-
-
0.00005
2-Nas-Phe(3-Am)-4-(2-guanidinoethyl)piperidide
pH 8.0, recombinant catalytic enzyme domain
0.001182
3,5-bis(4-carbamimidoylphenoxy)-N-((4-hydroxycyclohexyl)methyl)benzamide
pH 8.5, temperature not specified in the publication
0.000204
3,5-bis(4-carbamimidoylphenoxy)-N-(1-(2-hydroxyethyl)piperidin-4-yl)benzamide
pH 8.5, temperature not specified in the publication
0.000591
3,5-bis(4-carbamimidoylphenoxy)-N-(4-fluorophenyl)benzamide
pH 8.5, temperature not specified in the publication
0.000301
3,5-bis(4-carbamimidoylphenoxy)-N-(4-hydroxycyclohexyl)benzamide
pH 8.5, temperature not specified in the publication
0.00077
3,5-bis(4-carbamimidoylphenoxy)-N-(4-methylcyclohexyl)benzamide
pH 8.5, temperature not specified in the publication
0.000411
3,5-bis(4-carbamimidoylphenoxy)-N-(cyclohexylmethyl)benzamide
pH 8.5, temperature not specified in the publication
0.000592
3,5-bis(4-carbamimidoylphenoxy)-N-cyclohexylbenzamide
pH 8.5, temperature not specified in the publication
0.00162
3,5-bis(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.0000025
3-(3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-ethylbiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl)benzenecarboximidamide
-
-
0.000046
3-[(2R)-3-[4-(2-carbamimidamidoethyl)piperidin-1-yl]-2-[(naphthalen-2-ylsulfonyl)amino]propyl]benzenecarboximidamide
-
-
0.000001
3-[(2S)-2-([[3-(4-aminobutyl)phenyl]sulfonyl]amino)-3-[4-(2-aminoethyl)piperidin-1-yl]-3-oxopropyl]benzenecarboximidamide
-
0.000013
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(1H-indol-5-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
0.000028
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(2-methylpyrimidin-4-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
0.00000008 - 0.0000001
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
0.0000016
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-aminopyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
0.000012
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[4'-(1-methylethoxy)biphenyl-3-yl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
0.00011
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[(biphenyl-3-ylsulfonyl)amino]-3-oxopropyl]benzenecarboximidamide
-
0.0003
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[(naphthalen-2-ylsulfonyl)amino]-3-oxopropoxy]benzenecarboximidamide
pH and temperature not specified in the publication
0.0000067
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[([3-[(3-aminopropyl)amino]phenyl]sulfonyl)amino]-3-oxopropyl]benzenecarboximidamide
-
0.000029
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(2'-chlorobiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
0.0000054
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(3',4'-dimethoxybiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
0.000091
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(3'-chlorobiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
0.000026
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-chlorobiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
0.000006
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-ethoxybiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
0.0000025
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-ethylbiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
0.000007
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-methoxybiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
0.0003
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4-cyclohexylphenyl)sulfonyl]amino]-3-oxopropoxy]benzenecarboximidamide
pH and temperature not specified in the publication
0.0001
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-3-oxo-2-([[2,4,6-tri(propan-2-yl)phenyl]sulfonyl]amino)propoxy]benzenecarboximidamide
pH and temperature not specified in the publication
0.000047
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-3-oxo-2-[[(3-pyridin-3-ylphenyl)sulfonyl]amino]propyl]benzenecarboximidamide
-
0.00006
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-3-oxo-2-[[(3-pyridin-4-ylphenyl)sulfonyl]amino]propyl]benzenecarboximidamide
-
0.0015
3-[(2S)-3-[4-(4-aminobutanoyl)piperidin-1-yl]-3-oxo-2-([[2,4,6-tri(propan-2-yl)phenyl]sulfonyl]amino)propoxy]benzenecarboximidamide
pH and temperature not specified in the publication
0.0017
3-[(2S)-3-[4-(b-alanyl)piperidin-1-yl]-3-oxo-2-([[2,4,6-tri(propan-2-yl)phenyl]sulfonyl]amino)propoxy]benzenecarboximidamide
pH and temperature not specified in the publication
0.000082
3-[(2S)-3-[4-(N-carbamimidoyl-b-alanyl)piperazin-1-yl]-3-oxo-2-([[2,4,6-tris(1-methylethyl)phenyl]sulfonyl]amino)propyl]benzenecarboximidamide
pH 8.0, recombinant catalytic enzyme domain
0.00073
4,4'-((5-(1,2,3,4-tetrahydroisoquinoline-2-carbonyl)-1,3-phenylene)bis(oxy))dibenzimidamide
pH 8.5, temperature not specified in the publication
0.000094
4,4'-((5-(4-(2-aminoethyl)piperidine-1-carbonyl)-1,3-phenylene)bis(oxy))dibenzimidamide
pH 8.5, temperature not specified in the publication
0.00198
4,4'-((5-(4-fluorophenylsulfonamido)-1,3-phenylene)bis(oxy))dibenzimidamide
pH 8.5, temperature not specified in the publication
0.000305
4,4'-((5-(decahydroquinoline-1-carbonyl)-1,3-phenylene)bis(oxy))dibenzimidamide
pH 8.5, temperature not specified in the publication
0.00179
4,4'-((5-(naphthalene-2-sulfonamido)-1,3-phenylene)bis(oxy))dibenzimidamide
pH 8.5, temperature not specified in the publication
0.000218
4,4'-[(3-[[(4-fluorophenyl)sulfonyl]amino]pyridine-2,6-diyl)bis(oxy)]dibenzenecarboximidamide
pH 8.5, temperature not specified in the publication
0.00106
4,4'-[(5-aminobenzene-1,3-diyl)bis(oxy)]dibenzenecarboximidamide
pH 8.5, temperature not specified in the publication
0.000177
4-(1-[3-carbamimidoyl-N-[(3-pyrrolidin-1-ylphenyl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
-
0.000028
4-(1-[3-carbamimidoyl-N-[(4'-ethoxybiphenyl-3-yl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
-
0.000024 - 0.0000245
4-(1-[3-carbamimidoyl-N-[(4'-ethylbiphenyl-3-yl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
0.000087
4-(1-[N-[(4'-tert-butylbiphenyl-3-yl)sulfonyl]-3-carbamimidoyl-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
-
0.000014
4-([1-[(2S)-3-(3-carbamimidoylphenyl)-2-([[2,4,6-tris(1-methylethyl)phenyl]sulfonyl]amino)propanoyl]piperidin-4-yl]carbonyl)piperidine-1-carboximidamide
pH 8.0, recombinant catalytic enzyme domain
0.000026
4-([1-[(2S)-3-(3-carbamimidoylphenyl)-2-[[(4-cyclohexylphenyl)sulfonyl]amino]propanoyl]piperidin-4-yl]carbonyl)piperidine-1-carboximidamide
-
-
0.0288
4-aminobenzamidine
-
-
0.000545
4-aminocyclohexyl 3,5-bis(4-carbamimidoylphenoxy)benzoate
pH 8.5, temperature not specified in the publication
0.2
4-[1-(3-carbamimidoyl-N-[[3-(1H-imidazol-1-yl)phenyl]sulfonyl]-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
0.000024
4-[1-(3-carbamimidoyl-N-[[3-(2-oxopiperazin-1-yl)phenyl]sulfonyl]-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
0.00003
4-[1-(3-carbamimidoyl-N-[[3-(2-oxopiperidin-1-yl)phenyl]sulfonyl]-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
0.000098
4-[1-(3-carbamimidoyl-N-[[3-(6-oxopyridazin-1(6H)-yl)phenyl]sulfonyl]-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
0.00000043
4-[1-(N-[[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
0.00001
4-[1-(N-[[3-(6-aminopyridin-3-yl)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
0.0000063
4-[1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
0.000012
4-[1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]butanamide
-
-
0.000255
4-[1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]butanoic acid
-
-
0.000053
4-[4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazin-1-yl]-N-methyl-4-oxobutanamide
-
-
0.00000013
9-fluorenylmethyloxycarbonyl-GR-ketobenzothiazole
pH not specified in the publication, temperature not specified in the publication
0.000005 - 0.000013
Aprotinin
0.00019
ARCTKSIPPICFPD
pH 7,6, 37°C
0.0000061 - 0.0000075
benzyl 4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazine-1-carboxylate
0.00022 - 0.01
benzylsulfonyl-D-arginyl-proline-(2-aminomethyl-5-chlorobenzyl)-amide bis(trifluoroacetate)
0.000055 - 0.00019
benzylsulfonyl-D-arginyl-proline-(4-amidinobenzyl)amide bis-(trifluoroacetate)
0.0021 - 0.01
benzylsulfonyl-D-cyclohexylalanyl-proline-(2-aminomethyl-5-chlorobenzyl)amide
0.00029 - 0.00077
benzylsulfonyl-D-cyclohexylalanyl-proline-(4-amidinobenzyl)-amide
0.0000000497
Bovine pancreatic trypsin inhibitor
-
-
-
0.00004
CJ-730
-
3-amidinophenylalanine-based inhibitor CJ-730
0.000026
D-hTyr-Ala-4-amidinobenzylamide
pH 8.0, temperature not specified in the publication
0.000041
ethyl (3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)carbamate
-
0.00185
ethyl 4-(3,5-bis(4-carbamimidoylphenoxy)benzamido)piperidine-1-carboxylate
pH 8.5, temperature not specified in the publication
0.000065
ethyl 4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazine-1-carboxylate
-
-
0.01
GACTKSIPPICFPD
pH 7,6, 37°C
0.00018
GAVCPKILKKCRRDSDCPGACICRGNGYCGSGSD
pH 7,6, 37°C
0.0000023
GGACPKILKKCRRDSDCPGACICRGNGYCGSGSD
pH 7,6, 37°C
0.0000035
GGRCPKALKKCRRDSDCPGACICRGNGYCGSGSD
pH 7,6, 37°C
0.00000029
GGRCPKILKKCRRDSDCPGACICRGNGYCGSGSD
pH 7,6, 37°C
0.000039
GGVCAKILKKCRRDSDCPGACICRGNGYCGSGSD
pH 7,6, 37°C
0.01
GGVCPAILKKCRRDSDCPGACICRGNGYCGSGSD
above, pH 7,6, 37°C
0.0000098
GGVCPKALKKCRRDSDCPGACICRGNGYCGSGSD
pH 7,6, 37°C
0.000012
GGVCPKIAKKCRRDSDCPGACICRGNGYCGSGSD
pH 7,6, 37°C
0.000076
GGVCPKILAKCRRDSDCPGACICRGNGYCGSGSD
pH 7,6, 37°C
0.0000041
GGVCPKILKACRRDSDCPGACICRGNGYCGSGSD
pH 7,6, 37°C
0.000012
GGVCPKILKKCRRDSDCPGACICRGAGYCGSGSD
pH 7,6, 37°C
0.000011
GGVCPKILKKCRRDSDCPGACICRGNGACGSGSD
pH 7,6, 37°C
0.0000037
GGVCPKILKKCRRDSDCPGACICRGNGYCASGSD
pH 7,6, 37°C
0.000098
GGVCPKILKKCRRDSDCPGACICRGNGYCGAGSD
pH 7,6, 37°C
0.00011
GGVCPKRLKKCRRDSDCPGACICRGNGYCGSGSD
pH 7,6, 37°C
0.000039
GGVCPRILKKCRRDSDCPGACICRGNGYCGSGSD
pH 7,6, 37°C
0.0012
GKCTKSIPPICFPD
pH 7,6, 37°C
0.0015
GRCAKSIPPICFPD
pH 7,6, 37°C
0.01
GRCTASIPPICFPD
above, pH 7,6, 37°C
0.0016
GRCTKAIPPICFPD
pH 7,6, 37°C
0.000084
GRCTKSAPPICFPD
pH 7,6, 37°C
0.000051
GRCTKSAPPRCFPD
pH 7,6, 37°C
0.000027
GRCTKSIAPICFPD
pH 7,6, 37°C
0.00037
GRCTKSIPAICFPD
pH 7,6, 37°C
0.000073
GRCTKSIPPACFPD
pH 7,6, 37°C
0.01
GRCTKSIPPDCFPD
pH 7,6, 37°C
0.0037
GRCTKSIPPGCFPD
pH 7,6, 37°C
0.00032
GRCTKSIPPICAPD
pH 7,6, 37°C
0.00024
GRCTKSIPPICFAD
pH 7,6, 37°C
0.0015
GRCTKSIPPICFPA
pH 7,6, 37°C
0.0002
GRCTKSIPPICFPD
pH 7,6, 37°C
0.00004
GRCTKSIPPKCFPD
pH 7,6, 37°C
0.0000064
GRCTKSIPPRCFPD
pH 7,6, 37°C
0.0045
GRCTKSRPPICFPD
pH 7,6, 37°C
0.00031
GRCTRSIPPICFPD
pH 7,6, 37°C
0.000924
hexamidine
pH 8.5
0.0019 - 0.0041
leupeptin
0.0001
methyl (2R)-1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-2-carboxylate
-
-
0.0024
methyl (2S)-1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-2-carboxylate
-
-
0.0000061
methyl 4-[1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]butanoate
-
-
0.000003
N-((1r,4r)-4-aminocyclohexyl)-3,5-bis((3-carbamimidoylbenzyl)oxy)benzamide
pH 8.5, temperature not specified in the publication
0.000023
N-((1r,4r)-4-aminocyclohexyl)-3,5-bis((4-carbamimidoylbenzyl)oxy)benzamide
pH 8.5, temperature not specified in the publication
0.001698
N-((1r,4r)-4-aminocyclohexyl)-3,5-bis(4-(aminomethyl)phenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.000006
N-((1r,4r)-4-aminocyclohexyl)-3-((3-carbamimidoylbenzyl)oxy)-5-(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.00026
N-((1r,4r)-4-aminocyclohexyl)-3-((4-bromobenzyl)oxy)-5-(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.00001
N-((1r,4r)-4-aminocyclohexyl)-3-((4-carbamimidoylbenzyl)oxy)-5-(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.00203
N-((1r,4r)-4-aminocyclohexyl)-3-((6-aminopyridin-3-yl)oxy)-5-(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.000793
N-((1r,4r)-4-aminocyclohexyl)-3-((6-bromopyridin-3-yl)methoxy)-5-(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.000116
N-((1r,4r)-4-aminocyclohexyl)-3-(4-(3-aminopropanamido)phenoxy)-5-(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.00004
N-((1r,4r)-4-aminocyclohexyl)-3-(4-(aminomethyl)phenoxy)-5-(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.00113
N-((1r,4r)-4-aminocyclohexyl)-3-(4-aminophenoxy)-5-(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.00047
N-((1r,4r)-4-aminocyclohexyl)-3-(4-carbamimidoylphenoxy)-5-((4-chlorobenzyl)oxy)benzamide
pH 8.5, temperature not specified in the publication
0.000824
N-((1r,4r)-4-aminocyclohexyl)-3-(4-carbamimidoylphenoxy)-5-(4-carbamoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.000141
N-(1-(3-aminopropyl)piperidin-4-yl)-3,5-bis(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.000026
N-(2-aminoethyl)-1-(3-carbamimidoyl-N-[[2,4,6-tris(1-methylethyl)phenyl]sulfonyl]-L-phenylalanyl)piperidine-4-carboxamide
pH 8.0, recombinant catalytic enzyme domain
0.000018
N-(3,5-bis(4-carbamimidoylphenoxy)phenyl)-1-(2-hydroxyethyl)piperidine-4-carboxamide
pH 8.5, temperature not specified in the publication
0.0000067
N-(3-[[(1R)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)ethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.00047
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-(2-methylpiperidin-1-yl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.000053
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-(4-methylpiperidin-1-yl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.000037
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-oxo-2-piperazin-1-ylethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.000033
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-oxo-2-piperidin-1-ylethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.000016
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-[4-[4-(methylamino)-4-oxobutyl]piperidin-1-yl]-2-oxoethyl]sulfamoyl]phenyl)azetidine-3-carboxamide
-
-
1
N-(3-[[(1S)-1-[[4-(2-aminoethyl)piperidin-1-yl]carbonyl]-3-phenylpropyl]sulfamoyl]phenyl)-beta-alaninamide
larger than 1
1
N-(3-[[(1S)-1-[[4-(2-aminoethyl)piperidin-1-yl]carbonyl]-4-phenylbutyl]sulfamoyl]phenyl)-beta-alaninamide
larger than 1
0.000017
N-(3-[[(1S)-2-(4-benzylpiperidin-1-yl)-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.00012
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-3-hydroxypropanamide
-
0.0000066
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-b-alaninamide
pH 8.0, recombinant catalytic enzyme domain
0.0000038
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
0.000003
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)azetidine-3-carboxamide
-
0.00018
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)propanamide
-
0.0000018
N-(3-[[(1S)-2-[4-(2-carbamimidamidoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.0000038
N-(3-[[(2S)-1-[4-(2-aminoethyl)piperidin-1-yl]-3-(3-carbamimidoylphenyl)-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.000036
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-oxo-1-(piperazin-1-yl)propan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.00001
N-(4-aminocyclohexyl)-3,5-bis(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.0037
N-(4-aminocyclohexyl)-O-(3-carbamimidoylphenyl)-N2-(naphthalen-2-ylsulfonyl)-L-serinamide
pH and temperature not specified in the publication
0.00077
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C
0.0021
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C
0.000145
N-[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-[3-(aminomethyl)benzyl]-2-oxoethyl]-4'-methoxybiphenyl-3-sulfonamide
-
0.00015
N-[3-([(1S)-1-(3-carbamimidoylbenzyl)-2-[4-(4-hydroxyphenyl)piperazin-1-yl]-2-oxoethyl]sulfamoyl)phenyl]-beta-alaninamide
-
-
0.01
N-[3-([(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-benzyl-2-oxoethyl]sulfamoyl)phenyl]-beta-alaninamide
-
0.000056
N-[3-([(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-[3-(aminomethyl)benzyl]-2-oxoethyl]sulfamoyl)phenyl]-beta-alaninamide
-
0.0028
N-[3-([(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-[4-(aminomethyl)benzyl]-2-oxoethyl]sulfamoyl)phenyl]-beta-alaninamide
-
0.000055
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C
0.00022
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C
0.000004
R1K'4-eglin
-
pH 9.0, recombinant His-tagged amino acids 596-855 of matriptase
0.0000000123
scFv antibody E2
-
-
-
0.0000000704
scFv antibody S4
-
-
-
0.0000067 - 0.000046
sulfonylated 3-amidino-phenylalanines
-
-
-
0.00000092
sunflower trypsin inhibitor
-
-
-
0.00000092 - 0.0001
sunflower trypsin inhibitor-1
0.000025
sunflower trypsin inhibitor-2
-
-
0.0000025
sunflower trypsin inhibitor-3
-
-
additional information
additional information
-
0.000000011
L-arginyl-N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
matriptase, pH and temperature not specified in the publication
0.0000033
L-arginyl-N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
matriptase-2, pH and temperature not specified in the publication
0.000052
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant H665F
0.00021
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S
0.00029
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged wild-type enzyme
0.015
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant L785S
0.02
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S/L785S
0.02
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y
0.1
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y/A757S/L785S
0.003
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant H665F
0.037
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged wild-type enzyme
0.075
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S
0.2
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y
0.2
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y/A757S/L785S
0.22
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant L785S
0.28
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S/L785S
0.000046
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant H665F
0.00016
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S
0.00019
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged wild-type enzyme
0.0012
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant L785S
0.0016
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S/L785S
0.02
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y
0.03
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y/A757S/L785S
0.0026
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant H665F
0.03
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged wild-type enzyme
0.054
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant L785S
0.069
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S
0.2
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y
0.2
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y/A757S/L785S
0.62
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S/L785S
0.00000008
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
0.0000001
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
-
0.000024
4-(1-[3-carbamimidoyl-N-[(4'-ethylbiphenyl-3-yl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
-
0.0000245
4-(1-[3-carbamimidoyl-N-[(4'-ethylbiphenyl-3-yl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
-
0.000005
Aprotinin
-
matriptase-2 in conditioned medium of HEK-MT2 cells, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.0000098
Aprotinin
-
recombinant human matriptase, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.000013
Aprotinin
-
purified matriptase-2, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.0000061
benzyl 4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazine-1-carboxylate
-
-
0.0000075
benzyl 4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazine-1-carboxylate
-
-
0.00022
benzylsulfonyl-D-arginyl-proline-(2-aminomethyl-5-chlorobenzyl)-amide bis(trifluoroacetate)
-
recombinant human matriptase, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.01
benzylsulfonyl-D-arginyl-proline-(2-aminomethyl-5-chlorobenzyl)-amide bis(trifluoroacetate)
-
Ki above 0.01 mM, matriptase-2 in conditioned medium of HEK-MT2 cells, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.01
benzylsulfonyl-D-arginyl-proline-(2-aminomethyl-5-chlorobenzyl)-amide bis(trifluoroacetate)
-
Ki above 0.01 mM, purified matriptase-2, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.000055
benzylsulfonyl-D-arginyl-proline-(4-amidinobenzyl)amide bis-(trifluoroacetate)
-
recombinant human matriptase, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.00017
benzylsulfonyl-D-arginyl-proline-(4-amidinobenzyl)amide bis-(trifluoroacetate)
-
purified matriptase-2, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.00019
benzylsulfonyl-D-arginyl-proline-(4-amidinobenzyl)amide bis-(trifluoroacetate)
-
matriptase-2 in conditioned medium of HEK-MT2 cells, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.0021
benzylsulfonyl-D-cyclohexylalanyl-proline-(2-aminomethyl-5-chlorobenzyl)amide
-
recombinant human matriptase, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.01
benzylsulfonyl-D-cyclohexylalanyl-proline-(2-aminomethyl-5-chlorobenzyl)amide
-
Ki above 0.01 mM, matriptase-2 in conditioned medium of HEK-MT2 cells, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.01
benzylsulfonyl-D-cyclohexylalanyl-proline-(2-aminomethyl-5-chlorobenzyl)amide
-
Ki above 0.01 mM, purified matriptase-2, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.00029
benzylsulfonyl-D-cyclohexylalanyl-proline-(4-amidinobenzyl)-amide
-
matriptase-2 in conditioned medium of HEK-MT2 cells, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.00046
benzylsulfonyl-D-cyclohexylalanyl-proline-(4-amidinobenzyl)-amide
-
purified enzyme, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.00077
benzylsulfonyl-D-cyclohexylalanyl-proline-(4-amidinobenzyl)-amide
-
recombinant human matriptase, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.0019
leupeptin
-
recombinant human matriptase, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.0024
leupeptin
-
matriptase-2 in conditioned medium of HEK-MT2 cells, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.0041
leupeptin
-
purified matriptase-2, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.00000092
sunflower trypsin inhibitor-1
-
-
0.0001
sunflower trypsin inhibitor-1
-
-
additional information
additional information
-
-
additional information
additional information
-
inhibition kinetics with antobodies E2 and S4 and point mutants thereof, overview
-
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Sun, J.; Pons, J.; Craik, C.S.
Potent and selective inhibition of membrane-type serine protease 1 by human single-chain antibodies
Biochemistry
42
892-900
2003
Homo sapiens
brenda
Benaud, C.; Dickson, R.B.; Lin, C.Y.
Regulation of the activity of matriptase on epithelial cell surfaces by a blood-derived factor
Eur. J. Biochem.
268
1439-1447
2001
Homo sapiens (Q9Y5Y6), Homo sapiens
brenda
Lin, C.Y.; Anders, J.; Johnson, M.; Sang, Q.A.; Dickson, R.B.
Molecular cloning of cDNA for matriptase, a matrix-degrading serine protease with trypsin-like activity
J. Biol. Chem.
274
18231-18236
1999
Homo sapiens (Q9Y5Y6), Homo sapiens
brenda
Lin, C.Y.; Anders, J.; Johnson, M.; Dickson, R.B.
Purification and characterization of a complex containing matriptase and a Kunitz-type serine protease inhibitor from human milk
J. Biol. Chem.
274
18237-18242
1999
Homo sapiens
brenda
Takeuchi, T.; Harris, J.L.; Huang, W.; Yan, K.W.; Coughlin, S.R.; Craik, C.S.
Cellular localization of membrane-type serine protease 1 and identification of protease-activated receptor-2 and single-chain urokinase-type plasminogen activator as substrates
J. Biol. Chem.
275
26333-26342
2000
Homo sapiens
brenda
Lee, S.L.; Dickson, R.B.; Lin, C.Y.
Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease
J. Biol. Chem.
275
36720-36725
2000
Homo sapiens (Q9Y5Y6), Homo sapiens
brenda
Benaud, C.; Oberst, M.; Hobson, J.P.; Spiegel, S.; Dickson, R.B.; Lin, C.Y.
Sphingosine 1-phosphate, present in serum-derived lipoproteins, activates matriptase
J. Biol. Chem.
277
10539-10546
2002
Homo sapiens
brenda
Friedrich, R.; Fuentes-Prior, P.; Ong, E.; Coombs, G.; Hunter, M.; Oehler, R.; Pierson, D.; Gonzalez, R.; Huber, R.; Bode, W.; Madison, E.L.
Catalytic domain structures of MT-SP1/matriptase, a matrix-degrading transmembrane serine proteinase
J. Biol. Chem.
277
2160-2168
2002
Homo sapiens
brenda
Oberst, M.D.; Williams, C.A.; Dickson, R.B.; Johnson, M.D.; Lin, C.Y.
The activation of matriptase requires its noncatalytic domains, serine protease domain, and its cognate inhibitor
J. Biol. Chem.
278
26773-26779
2003
Homo sapiens
brenda
Enyedy, I.J.; Lee, S.L.; Kuo, A.H.; Dickson, R.B.; Lin, C.Y.; Wang, S.
Structure-based approach for the discovery of bis-benzamidines as novel inhibitors of matriptase
J. Med. Chem.
44
1349-1355
2001
Homo sapiens (Q9Y5Y6)
brenda
Szabo, R.; Netzel-Arnett, S.; Hobson, J.P.; Antalis, T.M.; Bugge, T.H.
Matriptase-3 is a novel phylogenetically preserved membrane-anchored serine protease with broad serpin reactivity
Biochem. J.
290
231-242
2005
Homo sapiens, Mus musculus
-
brenda
Oberst, M.D.; Chen, L.L.; Kiyomiya, K.; Williams, C.A.; Lee, M.; Johnson, M.D.; Dickson, R.B.; Lin, C.
HAI-1 regulates activation and expression of matriptase, a membrane-bound serine protease
Am. J. Physiol.
289
C462-C470
2005
Homo sapiens
brenda
Ahmed, S.; Jin, X.; Yagi, M.; Yasuda, C.; Sato, Y.; Higashi, S.; Lin, C.Y.; Dickson, R.B.; Miyazaki, K.
Identification of membrane-bound serine proteinase matriptase as processing enzyme of insulin-like growth factor binding protein-related protein-1 (IGFBP-rP1/angiomodulin/mac25)
FEBS J.
273
615-627
2006
Homo sapiens
brenda
Desilets, A.; Longpre, J.M.; Beaulieu, M.E.; Leduc, R.
Inhibition of human matriptase by eglin c variants
FEBS Lett.
580
2227-2232
2006
Homo sapiens
brenda
Ihara, S.; Miyoshi, E.; Nakahara, S.; Sakiyama, H.; Ihara, H.; Akinaga, A.; Honke, K.; Dickson, R.B.; Lin, C.; Taniguchi, N.
Addition of beta1-6 GlcNAc branching to the oligosaccharide attached to Asn 772 in the serine protease domain of matriptase plays a pivotal role in its stability and resistance against trypsin
Glycobiology
14
139-146
2004
Homo sapiens
brenda
Ito, Y.; Akinaga, A.; Yamanaka, K.; Nakagawa, T.; Kondo, A.; Dickson, R.B.; Lin, C.Y.; Miyauchi, A.; Taniguchi, N.; Miyoshi, E.
Co-expression of matriptase and N-acetylglucosaminyltransferase V in thyroid cancer tissues - its possible role in prolonged stability in vivo by aberrant glycosylation
Glycobiology
16
368-374
2006
Homo sapiens
brenda
Suzuki, M.; Kobayashi, H.; Kanayama, N.; Saga, Y.; Suzuki, M.; Lin, C.Y.; Dickson, R.B.; Terao, T.
Inhibition of tumor invasion by genomic down-regulation of matriptase through suppression of activation of receptor-bound pro-urokinase
J. Biol. Chem.
279
14899-14908
2004
Homo sapiens
brenda
Jin, X.; Hirosaki, T.; Lin, C.Y.; Dickson, R.B.; Higashi, S.; Kitamura, H.; Miyazaki, K.
Production of soluble matriptase by human cancer cell lines and cell surface activation of its zymogen by trypsin
J. Cell. Biochem.
95
632-647
2005
Homo sapiens
brenda
Zeng, L.; Cao, J.; Zhang, X.
Expression of serine protease SNC19/matriptase and its inhibitor hepatocyte growth factor activator inhibitor type 1 in normal and malignant tissues of gastrointestinal tract
World J. Gastroenterol.
11
6202-6207
2005
Homo sapiens
brenda
Basel-Vanagaite, L.; Attia, R.; Ishida-Yamamoto, A.; Rainshtein, L.; Ben Amitai, D.; Lurie, R.; Pasmanik-Chor, M.; Indelman, M.; Zvulunov, A.; Saban, S.; Magal, N.; Sprecher, E.; Shohat, M.
Autosomal recessive ichthyosis with hypotrichosis caused by a mutation in ST14, encoding type II transmembrane serine protease matriptase
Am. J. Hum. Genet.
80
467-477
2007
Homo sapiens (Q9Y5Y6)
brenda
Lee, M.; Tseng, I.; Wang, Y.; Kiyomiya, K.; Johnson, M.D.; Dickson, R.B.; Lin, C.
Autoactivation of matriptase in vitro: requirement for biomembrane and LDL receptor domain
Am. J. Physiol. Cell Physiol.
293
C95-C105
2007
Homo sapiens
brenda
Qiu, D.; Owen, K.; Gray, K.; Bass, R.; Ellis, V.
Roles and regulation of membrane-associated serine proteases
Biochem. Soc. Trans.
35
583-587
2007
Homo sapiens, Mus musculus
brenda
Chen, M.; Chen, L.M.; Lin, C.Y.; Chai, K.X.
The epidermal growth factor receptor (EGFR) is proteolytically modified by the Matriptase-Prostasin serine protease cascade in cultured epithelial cells
Biochim. Biophys. Acta
1783
896-903
2007
Homo sapiens
brenda
Jin, X.; Yagi, M.; Akiyama, N.; Hirosaki, T.; Higashi, S.; Lin, C.Y.; Dickson, R.B.; Kitamura, H.; Miyazaki, K.
Matriptase activates stromelysin (MMP-3) and promotes tumor growth and angiogenesis
Cancer Sci.
97
1327-1334
2006
Homo sapiens
brenda
Uhland, K.
Matriptase and its putative role in cancer
Cell. Mol. Life Sci.
63
2968-2978
2006
Homo sapiens, Mus musculus
brenda
Parr, C.; Sanders, A.J.; Davies, G.; Martin, T.; Lane, J.; Mason, M.D.; Mansel, R.E.; Jiang, W.G.
Matriptase-2 inhibits breast tumor growth and invasion and correlates with favorable prognosis for breast cancer patients
Clin. Cancer Res.
13
3568-3576
2007
Homo sapiens, Homo sapiens (Q9Y5Y6)
brenda
Cheng, M.F.; Jin, J.S.; Wu, H.W.; Chiang, P.C.; Sheu, L.F.; Lee, H.S.
Matriptase expression in the normal and neoplastic mast cells
Eur. J. Dermatol.
17
375-380
2007
Homo sapiens
brenda
Bugge, T.H.; List, K.; Szabo, R.
Matriptase-dependent cell surface proteolysis in epithelial development and pathogenesis
Front. Biosci.
12
5060-5070
2007
Homo sapiens, Mus musculus
brenda
Darragh, M.R.; Bhatt, A.S.; Craik, C.S.
MT-SP1 proteolysis and regulation of cell-microenvironment interactions
Front. Biosci.
13
528-539
2008
Homo sapiens, Mus musculus
brenda
Ramsay, A.J.; Reid, J.C.; Velasco, G.; Quigley, J.P.; Hooper, J.D.
The type II transmembrane serine protease matriptase-2 - identification, structural features, enzymology, expression pattern and potential roles
Front. Biosci.
13
569-579
2008
Bos taurus, Canis lupus familiaris, Homo sapiens, Macaca mulatta, Rattus norvegicus, Mus musculus (Q9DBI0)
brenda
Lin, C.Y.; Tseng, I.C.; Chou, F.P.; Su, S.F.; Chen, Y.W.; Johnson, M.D.; Dickson, R.B.
Zymogen activation, inhibition, and ectodomain shedding of matriptase
Front. Biosci.
13
621-635
2008
Homo sapiens
brenda
Jin, J.S.; Cheng, T.F.; Tsai, W.C.; Sheu, L.F.; Chiang, H.; Yu, C.P.
Expression of the serine protease, matriptase, in breast ductal carcinoma of Chinese women: correlation with clinicopathological parameters
Histol. Histopathol.
22
305-309
2007
Homo sapiens
brenda
Desilets, A.; Beliveau, F.; Vandal, G.; McDuff, F.O.; Lavigne, P.; Leduc, R.
Mutation G827R in matriptase causing autosomal recessive Ichthyosis with hypotrichosis yields an inactive protease
J. Biol. Chem.
283
10535-10542
2008
Homo sapiens
brenda
Steinmetzer, T.; Schweinitz, A.; Stuerzebecher, A.; Doennecke, D.; Uhland, K.; Schuster, O.; Steinmetzer, P.; Mueller, F.; Friedrich, R.; Than, M.E.; Bode, W.; Stuerzebecher, J.
Secondary amides of sulfonylated 3-amidinophenylalanine. New potent and selective inhibitors of matriptase
J. Med. Chem.
49
4116-4126
2006
Homo sapiens (Q9Y5Y6)
brenda
Li, P.; Jiang, S.; Lee, S.L.; Lin, C.Y.; Johnson, M.D.; Dickson, R.B.; Michejda, C.J.; Roller, P.P.
Design and synthesis of novel and potent inhibitors of the type II transmembrane serine protease, matriptase, based upon the sunflower trypsin inhibitor-1
J. Med. Chem.
50
5976-5983
2007
Homo sapiens
brenda
Farady, C.J.; Sun, J.; Darragh, M.R.; Miller, S.M.; Craik, C.S.
The mechanism of inhibition of antibody-based inhibitors of membrane-type serine protease 1 (MT-SP1)
J. Mol. Biol.
369
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2007
Homo sapiens
brenda
List, K.; Bugge, T.H.; Szabo, R.
Matriptase: potent proteolysis on the cell surface
Mol. Med.
12
1-7
2006
Homo sapiens
brenda
Jiang, S.; Li, P.; Lee, S.L.; Lin, C.Y.; Long, Y.Q.; Johnson, M.D.; Dickson, R.B.; Roller, P.P.
Design and synthesis of redox stable analogues of sunflower trypsin inhibitors (SFTI-1) on solid support, potent inhibitors of matriptase
Org. Lett.
9
9-12
2007
Homo sapiens
brenda
Tsui, K.H.; Chang, P.L.; Feng, T.H.; Chung, L.C.; Sung, H.C.; Juang, H.H.
Evaluating the function of matriptase and N-acetylglucosaminyltransferase V in prostate cancer metastasis
Anticancer Res.
28
1993-1999
2008
Homo sapiens
brenda
Tseng, I.C.; Chou, F.P.; Su, S.F.; Oberst, M.; Madayiputhiya, N.; Lee, M.S.; Wang, J.K.; Sloane, D.E.; Johnson, M.; Lin, C.Y.
Purification from human milk of matriptase complexes with secreted serpins: mechanism for inhibition of matriptase other than HAI-1
Am. J. Physiol. Cell Physiol.
295
C423-C431
2008
Homo sapiens (Q9Y5Y6), Homo sapiens
brenda
Janciauskiene, S.; Nita, I.; Subramaniyam, D.; Li, Q.; Lancaster, J.R.; Matalon, S.
Alpha1-antitrypsin inhibits the activity of the matriptase catalytic domain in vitro
Am. J. Respir. Cell Mol. Biol.
39
631-637
2008
Homo sapiens
brenda
Schweinitz, A.; Doennecke, D.; Ludwig, A.; Steinmetzer, P.; Schulze, A.; Kotthaus, J.; Wein, S.; Clement, B.; Steinmetzer, T.
Incorporation of neutral C-terminal residues in 3-amidinophenylalanine-derived matriptase inhibitors
Bioorg. Med. Chem. Lett.
19
1960-1965
2009
Homo sapiens
brenda
Steinmetzer, T.; Doennecke, D.; Korsonewski, M.; Neuwirth, C.; Steinmetzer, P.; Schulze, A.; Saupe, S.M.; Schweinitz, A.
Modification of the N-terminal sulfonyl residue in 3-amidinophenylalanine-based matriptase inhibitors
Bioorg. Med. Chem. Lett.
19
67-73
2009
Homo sapiens (Q9Y5Y6)
brenda
Silvestri, L.; Pagani, A.; Nai, A.; De Domenico, I.; Kaplan, J.; Camaschella, C.
The serine protease matriptase-2 (TMPRSS6) inhibits hepcidin activation by cleaving membrane hemojuvelin
Cell Metab.
8
502-511
2008
Homo sapiens, Mus musculus
brenda
Beliveau, F.; Desilets, A.; Leduc, R.
Probing the substrate specificities of matriptase, matriptase-2, hepsin and DESC1 with internally quenched fluorescent peptides
FEBS J.
276
2213-2226
2009
Homo sapiens
brenda
List, K.
Matriptase: a culprit in cancer?
Future Oncol.
5
97-104
2009
Homo sapiens, Mus musculus
brenda
Szabo, R.; Hobson, J.P.; List, K.; Molinolo, A.; Lin, C.Y.; Bugge, T.H.
Potent inhibition and global co-localization implicate the transmembrane Kunitz-type serine protease inhibitor hepatocyte growth factor activator inhibitor-2 in the regulation of epithelial matriptase activity
J. Biol. Chem.
283
29495-29504
2008
Homo sapiens, Mus musculus
brenda
Sanders, A.J.; Parr, C.; Martin, T.A.; Lane, J.; Mason, M.D.; Jiang, W.G.
Genetic upregulation of matriptase-2 reduces the aggressiveness of prostate cancer cells in vitro and in vivo and affects FAK and paxillin localisation
J. Cell. Physiol.
216
780-789
2008
Homo sapiens
brenda
Lee, P.
Role of matriptase-2 (TMPRSS6) in iron metabolism
Acta Haematol.
122
87-96
2009
Mus musculus, Homo sapiens (Q8IU80)
brenda
Wang, J.; Lee, M.; Tseng, I.; Chou, F.; Chen, Y.; Fulton, A.; Lee, H.; Chen, G.; Johnson, M.; Lin, C.
Polarized epithelial cells secrete matriptase as a consequence of zymogen activation and HAI-1-mediated inhibition
Am. J. Physiol. Cell Physiol.
297
459-470
2009
Homo sapiens
brenda
Milner, J.M.; Patel, A.; Davidson, R.K.; Swingler, T.E.; Desilets, A.; Young, D.A.; Kelso, E.B.; Donell, S.T.; Cawston, T.E.; Clark, I.M.; Ferrell, W.R.; Plevin, R.; Lockhart, J.C.; Leduc, R.; Rowan, A.D.
Matriptase is a novel initiator of cartilage matrix degradation in osteoarthritis
Arthritis Rheum.
62
1955-1966
2010
Homo sapiens
brenda
Owen, K.A.; Qiu, D.; Alves, J.; Schumacher, A.M.; Kilpatrick, L.M.; Li, J.; Harris, J.L.; Ellis, V.
Pericellular activation of hepatocyte growth factor by the transmembrane serine proteases matriptase and hepsin, but not by the membrane-associated protease uPA
Biochem. J.
426
219-228
2010
Homo sapiens
brenda
Ramsay, A.J.; Quesada, V.; Sanchez, M.; Garabaya, C.; Sarda, M.P.; Baiget, M.; Remacha, A.; Velasco, G.; Lopez-Otin, C.
Matriptase-2 mutations in iron-refractory iron deficiency anemia patients provide new insights into protease activation mechanisms
Hum. Mol. Genet.
18
3673-3683
2009
Homo sapiens
brenda
Napp, J.; Dullin, C.; Mueller, F.; Uhland, K.; Petri, J.B.; van de Locht, A.; Steinmetzer, T.; Alves, F.
Time-domain in vivo near infrared fluorescence imaging for evaluation of matriptase as a potential target for the development of novel, inhibitor-based tumour therapies
Int. J. Cancer
127
1958-1974
2010
Homo sapiens
brenda
Uhland, K.; Siphos, B.; Arkona, C.; Schuster, M.; Petri, B.; Steinmetzer, P.; Mueller, F.; Schweinitz, A.; Steinmetzer, T.; Van De Locht, A.
Use of IHC and newly designed matriptase inhibitors to elucidate the role of matriptase in pancreatic ductal adenocarcinoma
Int. J. Oncol.
35
347-357
2009
Homo sapiens
brenda
Tseng, I.C.; Xu, H.; Chou, F.P.; Li, G.; Vazzano, A.P.; Kao, J.P.; Johnson, M.D.; Lin, C.Y.
Matriptase activation, an early cellular response to acidosis
J. Biol. Chem.
285
3261-3270
2010
Homo sapiens
brenda
Bocheva, G.; Rattenholl, A.; Kempkes, C.; Goerge, T.; Lin, C.Y.; DAndrea, M.R.; Staender, S.; Steinhoff, M.
Role of matriptase and proteinase-activated receptor-2 in nonmelanoma skin cancer
J. Invest. Dermatol.
129
1816-1823
2009
Homo sapiens
brenda
Ganesan, R.; Eigenbrot, C.; Kirchhofer, D.
Structural and mechanistic insight into how antibodies inhibit serine proteases
Biochem. J.
430
179-189
2010
Homo sapiens
brenda
Clark, E.B.; Jovov, B.; Rooj, A.K.; Fuller, C.M.; Benos, D.J.
Proteolytic cleavage of human acid-sensing ion channel 1 by the serine protease matriptase
J. Biol. Chem.
285
27130-27143
2010
Homo sapiens
brenda
Beliveau, F.; Brule, C.; Desilets, A.; Zimmerman, B.; Laporte, S.A.; Lavoie, C.L.; Leduc, R.
Essential role of endocytosis of the type II transmembrane serine protease TMPRSS6 in regulating its functionality
J. Biol. Chem.
286
29035-29043
2011
Homo sapiens
brenda
Bergum, C.; Zoratti, G.; Boerner, J.; List, K.
Strong expression association between matriptase and its substrate prostasin in breast cancer
J. Cell. Physiol.
227
1604-1609
2012
Homo sapiens, Homo sapiens (Q9Y5Y6)
brenda
Sisay, M.T.; Steinmetzer, T.; Stirnberg, M.; Maurer, E.; Hammami, M.; Bajorath, J.; Guetschow, M.
Identification of the first low-molecular-weight inhibitors of matriptase-2
J. Med. Chem.
53
5523-5535
2010
Homo sapiens
brenda
Colombo, E.; Dsilets, A.; Duchne, D.; Chagnon, F.; Najmanovich, R.; Leduc, R.; Marsault E.
Design and synthesis of potent, selective inhibitors of matriptase
ACS Med. Chem. Lett.
3
530-534
2012
Homo sapiens (Q8IU80)
brenda
Wysocka, M.; Gruba, N.; Miecznikowska, A.; Popow-Stellmaszyk, J.; Guetschow, M.; Stirnberg, M.; Furtmann, N.; Bajorath, J.; Lesner, A.; Rolka, K.
Substrate specificity of human matriptase-2
Biochimie
97
121-127
2014
Homo sapiens (Q8IU80), Homo sapiens
brenda
Stirnberg, M.; Maurer, E.; Arenz, K.; Babler, A.; Jahnen-Dechent, W.; Guetschow, M.
Cell surface serine protease matriptase-2 suppresses fetuin-A/AHSG-mediated induction of hepcidin
Biol. Chem.
396
81-93
2015
Homo sapiens (Q8IU80)
brenda
Goswami, R.; Wohlfahrt, G.; Mukherjee, S.; Ghadiyaram, C.; Nagaraj, J.; Satyam, L.K.; Subbarao, K.; Gopinath, S.; Krishnamurthy, N.R.; Subramanya, H.S.; Ramachandra, M.
Discovery of O-(3-carbamimidoylphenyl)-l-serine amides as matriptase inhibitors using a fragment-linking approach
Bioorg. Med. Chem. Lett.
25
616-620
2015
Homo sapiens (Q9Y5Y6)
brenda
Goswami, R.; Mukherjee, S.; Ghadiyaram, C.; Wohlfahrt, G.; Sistla, R.K.; Nagaraj, J.; Satyam, L.K.; Subbarao, K.; Palakurthy, R.K.; Gopinath, S.; Krishnamurthy, N.R.; Ikonen, T.; Moilanen, A.; Subramanya, H.S.; Kallio, P.; Ramachandra, M.
Structure-guided discovery of 1,3,5 tri-substituted benzenes as potent and selective matriptase inhibitors exhibiting in vivo antitumor efficacy
Bioorg. Med. Chem.
22
3187-3203
2014
Homo sapiens (Q9Y5Y6), Homo sapiens
brenda
Maurer, E.; Sisay, M.; Stirnberg, M.; Steinmetzer, T.; Bajorath, J.; Guetschow, M.
Insights into matriptase-2 substrate binding and inhibition mechanisms by analyzing active-site-mutated variants
ChemMedChem
7
68-72
2012
Homo sapiens (Q8IU80), Homo sapiens (Q9Y5Y6)
brenda
Buzza, M.S.; Martin, E.W.; Driesbaugh, K.H.; Desilets, A.; Leduc, R.; Antalis, T.M.
Prostasin is required for matriptase activation in intestinal epithelial cells to regulate closure of the paracellular pathway
J. Biol. Chem.
288
10328-10337
2013
Homo sapiens
brenda
Quimbar, P.; Malik, U.; Sommerhoff, C.P.; Kaas, Q.; Chan, L.Y.; Huang, Y.H.; Grundhuber, M.; Dunse, K.; Craik, D.J.; Anderson, M.A.; Daly, N.L.
High-affinity cyclic peptide matriptase inhibitors
J. Biol. Chem.
288
13885-13896
2013
Homo sapiens (Q9Y5Y6)
brenda
Zhao, N.; Nizzi, C.P.; Anderson, S.A.; Wang, J.; Ueno, A.; Tsukamoto, H.; Eisenstein, R.S.; Enns, C.A.; Zhang, A.S.
Low intracellular iron increases the stability of matriptase-2
J. Biol. Chem.
290
4432-4446
2015
Homo sapiens (Q8IU80)
brenda
Duchene, D.; Colombo, E.; Desilets, A.; Boudreault, P.L.; Leduc, R.; Marsault, E.; Najmanovich, R.
Analysis of subpocket selectivity and identification of potent selective inhibitors for matriptase and matriptase-2
J. Med. Chem.
57
10198-10204
2014
Homo sapiens (Q8IU80)
brenda
Hamilton, B.S.; Gludish, D.W.; Whittaker, G.R.
Cleavage activation of the human-adapted influenza virus subtypes by matriptase reveals both subtype and strain specificities
J. Virol.
86
10579-10586
2012
Homo sapiens (Q9Y5Y6)
brenda
Beaulieu, A.; Gravel, E.; Cloutier, A.; Marois, I.; Colombo, E.; Desilets, A.; Verreault, C.; Leduc, R.; Marsault, E.; Richter, M.V.
Matriptase proteolytically activates influenza virus and promotes multicycle replication in the human airway epithelium
J. Virol.
87
4237-4251
2013
Homo sapiens (Q9Y5Y6), Homo sapiens
brenda
Chai, A.C.; Robinson, A.L.; Chai, K.X.; Chen, L.M.
Ibuprofen regulates the expression and function of membrane-associated serine proteases prostasin and matriptase
BMC Cancer
15
1025
2015
Homo sapiens
brenda
Chen, L.M.; Chai, K.X.
Matriptase cleaves the amyloid-beta peptide 1-42 at Arg-5, Lys-16, and Lys-28
BMC Res. Notes
12
005
2019
Homo sapiens
brenda
Tamberg, T.; Hong, Z.; De Schepper, D.; Skovbjerg, S.; Dupont, D.M.; Vitved, L.; Schar, C.R.; Skjoedt, K.; Vogel, L.K.; Jensen, J.K.
Blocking the proteolytic activity of zymogen matriptase with antibody-based inhibitors
J. Biol. Chem.
294
314-326
2019
Homo sapiens (Q9Y5Y6), Homo sapiens
brenda
Wu, C.J.; Feng, X.; Lu, M.; Morimura, S.; Udey, M.C.
Matriptase-mediated cleavage of EpCAM destabilizes claudins and dysregulates intestinal epithelial homeostasis
J. Clin. Invest.
127
623-634
2017
Homo sapiens
brenda
Maiwald, A.; Hammami, M.; Wagner, S.; Heine, A.; Klebe, G.; Steinmetzer, T.
Changing the selectivity profile - from substrate analog inhibitors of thrombin and factor Xa to potent matriptase inhibitors
J. Enzyme Inhib. Med. Chem.
31
89-97
2016
Homo sapiens (Q9Y5Y6)
brenda
Damalanka, V.C.; Han, Z.; Karmakar, P.; ODonoghue, A.J.; La Greca, F.; Kim, T.; Pant, S.M.; Helander, J.; Klefstroem, J.; Craik, C.S.; Janetka, J.W.
Discovery of selective matriptase and hepsin serine protease inhibitors useful chemical tools for cancer cell biology
J. Med. Chem.
62
480-490
2019
Homo sapiens (Q9Y5Y6)
brenda
Lai, Y.J.; Chang, H.H.; Lai, H.; Xu, Y.; Shiao, F.; Huang, N.; Li, L.; Lee, M.S.; Johnson, M.D.; Wang, J.K.; Lin, C.Y.
N-Glycan branching affects the subcellular distribution of and inhibition of matriptase by HAI-2/placental bikunin
PLoS ONE
10
e0132163
2015
Homo sapiens
brenda
Lee, S.P.; Kao, C.Y.; Chang, S.C.; Chiu, Y.L.; Chen, Y.J.; Chen, M.G.; Chang, C.C.; Lin, Y.W.; Chiang, C.P.; Wang, J.K.; Lin, C.Y.; Johnson, M.D.
Tissue distribution and subcellular localizations determine in vivo functional relationship among prostasin, matriptase, HAI-1, and HAI-2 in human skin
PLoS ONE
13
e0192632
2018
Homo sapiens
brenda