+ |
Factor FVIIa:TF | down-regulates activity
cleavage
|
F5 |
0.496 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263645 |
Arg1046 |
HHAPLSPrTFHPLRS |
in vitro |
|
pmid |
sentence |
10026263 |
Factor VIIa/tissue factor generates a form of factor V with unchanged specific activity, resistance to activation by thrombin, and increased sensitivity to activated protein C| In this study, we found that TF/VIIa was able to cleave multiple peptide bonds in the coagulation cofactor, factor V. SDS-PAGE analysis and sequencing indicated the factor V was cleaved at Arg679, Arg709, Arg1018, and Arg1192 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263648 |
Arg1220 |
LSPELIQrNLSPALG |
in vitro |
|
pmid |
sentence |
10026263 |
Thrombin is considered the physiological activator of factor V and is the most potent activator, catalyzing the cleavage of three peptide bonds at Arg709, Arg1018, and Arg1545 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263647 |
Arg707 |
ESTVMATrKMHDRLE |
in vitro |
|
pmid |
sentence |
10026263 |
Thrombin is considered the physiological activator of factor V and is the most potent activator, catalyzing the cleavage of three peptide bonds at Arg709, Arg1018, and Arg1545 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263646 |
Arg737 |
LAAALGIrSFRNSSL |
in vitro |
|
pmid |
sentence |
10026263 |
Thrombin is considered the physiological activator of factor V and is the most potent activator, catalyzing the cleavage of three peptide bonds at Arg709, Arg1018, and Arg1545 |
|
Publications: |
4 |
Organism: |
In Vitro |
+ |
Factor FVIIa:TF | up-regulates activity
cleavage
|
F7 |
0.932 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263521 |
Arg212 |
NASKPQGrIVGGKVC |
Homo sapiens |
|
pmid |
sentence |
12524220 |
The factor VII zymogen is cleaved at arginine 152 by a variety of proteases, including thrombin, factor IXa, factor Xa, and factor VIIa–tissue factor to produce the serine protease factor VIIa. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Blood Plasma |
+ |
Factor FVIIa:TF | down-regulates activity
cleavage
|
F8 |
0.468 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263643 |
Arg355 |
CPEEPQLrMKNNEEA |
in vitro |
|
pmid |
sentence |
10350471 |
N-Terminal sequencing along with time courses of proteolysis indicated that VIIa-TF/PL cleaved factor VIII first at R740, followed by concomitant cleavage at R336 and R372. |hus, heavy chain cleavage of factor VIII by VIIa-TF/PL produces an inactive factor VIII cofactor no longer capable of activation by thrombin. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263642 |
Arg391 |
SPSFIQIrSVAKKHP |
in vitro |
|
pmid |
sentence |
10350471 |
N-Terminal sequencing along with time courses of proteolysis indicated that VIIa-TF/PL cleaved factor VIII first at R740, followed by concomitant cleavage at R336 and R372. |hus, heavy chain cleavage of factor VIII by VIIa-TF/PL produces an inactive factor VIII cofactor no longer capable of activation by thrombin. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263644 |
Arg759 |
KNNAIEPrSFSQNSR |
in vitro |
|
pmid |
sentence |
10350471 |
N-Terminal sequencing along with time courses of proteolysis indicated that VIIa-TF/PL cleaved factor VIII first at R740, followed by concomitant cleavage at R336 and R372. |hus, heavy chain cleavage of factor VIII by VIIa-TF/PL produces an inactive factor VIII cofactor no longer capable of activation by thrombin. |
|
Publications: |
3 |
Organism: |
In Vitro |
+ |
Factor FVIIa:TF | up-regulates activity
binding
|
F10 |
0.638 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263543 |
|
|
Homo sapiens |
|
pmid |
sentence |
32665005 |
During vascular injury, TF is exposed to the blood, where it functions as a cofactor for the circulating zymogen factor VII (FVII). This TF:FVIIa complex can then bind and activate either factor IX (FIX) or factor X (FX), triggering a cascade that generates fibrin and activates platelets, resulting in a hemostatic plug at the site of injury. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Blood Plasma |
+ |
F7 | form complex
binding
|
Factor FVIIa:TF |
0.932 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263555 |
|
|
Homo sapiens |
|
pmid |
sentence |
32665005 |
During vascular injury, TF is exposed to the blood, where it functions as a cofactor for the circulating zymogen factor VII (FVII). This TF:FVIIa complex can then bind and activate either factor IX (FIX) or factor X (FX), triggering a cascade that generates fibrin and activates platelets, resulting in a hemostatic plug at the site of injury. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Blood Plasma |
+ |
Factor FVIIa:TF | up-regulates activity
binding
|
F9 |
0.583 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263542 |
|
|
Homo sapiens |
|
pmid |
sentence |
32665005 |
During vascular injury, TF is exposed to the blood, where it functions as a cofactor for the circulating zymogen factor VII (FVII). This TF:FVIIa complex can then bind and activate either factor IX (FIX) or factor X (FX), triggering a cascade that generates fibrin and activates platelets, resulting in a hemostatic plug at the site of injury. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Blood Plasma |
+ |
F3 | form complex
binding
|
Factor FVIIa:TF |
0.932 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263556 |
|
|
Homo sapiens |
|
pmid |
sentence |
32665005 |
During vascular injury, TF is exposed to the blood, where it functions as a cofactor for the circulating zymogen factor VII (FVII). This TF:FVIIa complex can then bind and activate either factor IX (FIX) or factor X (FX), triggering a cascade that generates fibrin and activates platelets, resulting in a hemostatic plug at the site of injury. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Blood Plasma |