+ |
MMP12 | down-regulates quantity by destabilization
cleavage
|
FGA |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263622 |
Ala20 |
VVGTAWTaDSGEGDF |
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. |Fibrinogen was subjected to MMP-cleavage, and the resulting fragments were isolated. The amino acid sequences were determined by automated Edman degradation.|MMP-12 20ADSGEGD a-chain| 540FVSETESRG a-chain|433LVTSKGDK a-chain |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263624 |
Leu433 |
REYHTEKlVTSKGDK |
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. |Fibrinogen was subjected to MMP-cleavage, and the resulting fragments were isolated. The amino acid sequences were determined by automated Edman degradation.|MMP-12 20ADSGEGD a-chain| 540FVSETESRG a-chain|433LVTSKGDK a-chain |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263623 |
Phe540 |
FSPMLGEfVSETESR |
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. |Fibrinogen was subjected to MMP-cleavage, and the resulting fragments were isolated. The amino acid sequences were determined by automated Edman degradation.|MMP-12 20ADSGEGD a-chain| 540FVSETESRG a-chain|433LVTSKGDK a-chain |
|
Publications: |
3 |
Organism: |
In Vitro |
+ |
MMP8 | down-regulates quantity by destabilization
cleavage
|
FGA |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263625 |
Ala20 |
VVGTAWTaDSGEGDF |
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. |Fibrinogen was subjected to MMP-cleavage, and the resulting fragments were isolated. The amino acid sequences were determined by automated Edman degradation.|MMP-8 20ADSGEGD a-chain | 442LRTGKEKV a-chain |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263626 |
Leu442 |
TSKGDKElRTGKEKV |
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. |Fibrinogen was subjected to MMP-cleavage, and the resulting fragments were isolated. The amino acid sequences were determined by automated Edman degradation.|MMP-8 20ADSGEGD a-chain | 442LRTGKEKV a-chain |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
MMP13 | down-regulates quantity by destabilization
cleavage
|
FGA |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263612 |
Ala20 |
VVGTAWTaDSGEGDF |
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 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263613 |
Leu442 |
TSKGDKElRTGKEKV |
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: |
2 |
Organism: |
In Vitro |
+ |
MMP14 | down-regulates quantity by destabilization
cleavage
|
FGA |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263619 |
Leu105 |
NNKDSHSlTTNIMEI |
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-263620 |
Leu433 |
REYHTEKlVTSKGDK |
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-263621 |
Phe117 |
MEILRGDfSSANNRD |
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 |
+ |
FGA | form complex
binding
|
Fibrinogen |
0.759 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263392 |
|
|
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 |
+ |
FGA | up-regulates
binding
|
ITGAX |
0.36 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-31320 |
|
|
Homo sapiens |
|
pmid |
sentence |
7679388 |
To map the binding sites for four distinct ligands for mac-l: ic3b, fibrinogen, icam-1. __the i domain on the ot chain of mac-1 is an important recognition site for all four ligands. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AIIB/b3 integrin | up-regulates activity
binding
|
FGA |
0.562 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253359 |
|
|
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 |
+ |
FGA | up-regulates
|
Platelet_aggregation |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253372 |
|
|
|
|
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 |