+ |
COL4A4 | up-regulates activity
binding
|
A2/b1 integrin |
0.432 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253245 |
|
|
Homo sapiens |
K-562 Cell |
pmid |
sentence |
12123670 |
We have developed a cell-free assay for binding of solubilized beta1 integrins to their physiologically relevant ligands using an electrochemiluminescent detection method|Binding was clearly optimal for the presumed physiological ligands, i.e., collagen IV for a1b1, collagen I for a2b1, VCAM-Ig for a4b1, fibronectin (the 120-kDa cell attachment fragment was used) for a5b1, and laminin for a6b1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
COL4A4 | up-regulates activity
binding
|
A1/b1 integrin |
0.435 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272350 |
|
|
|
|
pmid |
sentence |
35267698 |
Integrins constitute a major group of receptors for extracellular matrix components, including collagens.|Among the four types, the signaling mechanism of α1β1 and α2β1 integrins has especially been reported. These integrins bind to both collagen types I and IV; however, their affinities differ: α1β1 has a higher affinity for collagen type IV, while α2β1 preferentially binds to collagen type I [13,23]. |
|
Publications: |
1 |
+ |
COL4A4 | up-regulates
|
ECM_synthesis |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254668 |
|
|
Homo sapiens |
|
pmid |
sentence |
12778132 |
Type IV collagen is the most abundant Type IV collagen is the most abundant constituent of the BM…All of the type IV collagen in mammals is derived from six genetically distinct alpha-chain polypeptides (alpha1-alpha6) |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PXDN | up-regulates quantity by stabilization
catalytic activity
|
COL4A4 |
0.259 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265250 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
29305973 |
Peroxidasin (PXDN), an ECM protein with peroxidase activity, is integral to basement membrane consolidation through catalysis of sulfilimine bonds in collagen IV. PXDN has been shown to form dityrosine crosslinks and also catalyses sulfilimine bonds, in the presence of hypohalous acids, to connect collagen IV protomers, which are an integral component of the basement membrane |
|
Publications: |
1 |
Organism: |
Homo Sapiens |