+ |
MMP14 | down-regulates quantity by destabilization
cleavage
|
FGG |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263618 |
Ile105 |
ESSKPNMiDAATLKS |
in vitro |
|
pmid |
sentence |
10930399 |
Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII| We have now investigated the role of collagenase-2 (MMP-8), macrophage elastase (MMP-12), collagenase-3 (MMP-13), and membrane type 1-matrix metalloproteinase (MT1-MMP, MMP-14) in the degradation of fibrinogen and Factor XII of the plasma clotting system.|MMP-14 27YVATRDN g-chain| 105XDAATLKSR g-chain | 92LTYNPDES g-chain |105LTTNIXEXL a-chain|433LVTSKGDKE a-chain| 117FXSANNRD a-chain |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263617 |
Leu92 |
QLIKAIQlTYNPDES |
in vitro |
|
pmid |
sentence |
10930399 |
Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII| We have now investigated the role of collagenase-2 (MMP-8), macrophage elastase (MMP-12), collagenase-3 (MMP-13), and membrane type 1-matrix metalloproteinase (MT1-MMP, MMP-14) in the degradation of fibrinogen and Factor XII of the plasma clotting system.|MMP-14 27YVATRDN g-chain| 105XDAATLKSR g-chain | 92LTYNPDES g-chain |105LTTNIXEXL a-chain|433LVTSKGDKE a-chain| 117FXSANNRD a-chain |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263616 |
Tyr27 |
LSSTCVAyVATRDNC |
in vitro |
|
pmid |
sentence |
10930399 |
Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII| We have now investigated the role of collagenase-2 (MMP-8), macrophage elastase (MMP-12), collagenase-3 (MMP-13), and membrane type 1-matrix metalloproteinase (MT1-MMP, MMP-14) in the degradation of fibrinogen and Factor XII of the plasma clotting system.|MMP-14 27YVATRDN g-chain| 105XDAATLKSR g-chain | 92LTYNPDES g-chain |105LTTNIXEXL a-chain|433LVTSKGDKE a-chain| 117FXSANNRD a-chain |
|
Publications: |
3 |
Organism: |
In Vitro |
+ |
MMP13 | down-regulates quantity by destabilization
cleavage
|
FGG |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263614 |
Tyr27 |
LSSTCVAyVATRDNC |
in vitro |
|
pmid |
sentence |
10930399 |
Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII| We have now investigated the role of collagenase-2 (MMP-8), macrophage elastase (MMP-12), collagenase-3 (MMP-13), and membrane type 1-matrix metalloproteinase (MT1-MMP, MMP-14) in the degradation of fibrinogen and Factor XII of the plasma clotting system.|MMP-13 27YVATRDN g-chain| 20ADSGEGD a-chain| 124RNSVDXLNXN b-chain| 442LRTGKEKV a-chain |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
FGG | form complex
binding
|
Fibrinogen |
0.75 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263393 |
|
|
in vitro |
|
pmid |
sentence |
25427968 |
Fibrinogen is a plasma glycoprotein mainly synthesised by hepatocytes and circulating as a 340-kDa hexamer consisting of two sets of three different polypeptide chains (Aalpha, Bbeta, and gamma, encoded by the FGA, FGB, and FGG gene, respectively). |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
FGG | down-regulates activity
binding
|
FN1 |
0.534 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251970 |
|
|
Homo sapiens |
|
pmid |
sentence |
2243140 |
Fibrinogen y-chain carboxyterminal (GQQHHLGGAKQAGDV) peptides inhibit fibrinogen, fibronectin (Fn), vitronectin, and von Willebrand factor (vWF) binding to the platelet glycoprotein Ilb-Illa complex (GP lIbII1a). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FGG | down-regulates activity
binding
|
VWF |
0.478 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251968 |
|
|
Homo sapiens |
|
pmid |
sentence |
2243140 |
Fibrinogen y-chain carboxyterminal (GQQHHLGGAKQAGDV) peptides inhibit fibrinogen, fibronectin (Fn), vitronectin, and von Willebrand factor (vWF) binding to the platelet glycoprotein Ilb-Illa complex (GP lIbII1a). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AIIB/b3 integrin | up-regulates activity
binding
|
FGG |
0.546 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253360 |
|
|
Homo sapiens |
Blood Platelet |
pmid |
sentence |
16418530 |
In response to agonist stimulation, the αIIbβ3 integrin on platelets is converted to an active conformation that binds fibrinogen and mediates platelet aggregation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FGG | down-regulates activity
binding
|
VTN |
0.431 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251969 |
|
|
Homo sapiens |
|
pmid |
sentence |
2243140 |
Fibrinogen y-chain carboxyterminal (GQQHHLGGAKQAGDV) peptides inhibit fibrinogen, fibronectin (Fn), vitronectin, and von Willebrand factor (vWF) binding to the platelet glycoprotein Ilb-Illa complex (GP lIbII1a). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FGG | up-regulates
|
Platelet_aggregation |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253373 |
|
|
|
|
pmid |
sentence |
16418530 |
In response to agonist stimulation, the αIIbβ3 integrin on platelets is converted to an active conformation that binds fibrinogen and mediates platelet aggregation. |
|
Publications: |
1 |