+ |
a7/b1 integrin | up-regulates
|
Cell_adhesion |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269007 |
|
|
Homo sapiens |
|
pmid |
sentence |
25388208 |
Integrin-mediated cell adhesion is important for development, immune responses, hemostasis and wound healing. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Laminin-1 | up-regulates activity
binding
|
a7/b1 integrin |
0.539 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253257 |
|
|
|
|
pmid |
sentence |
1839357 |
By using specific proteolytically derived fragments of laminin, it was determined that the alpha 7 beta 1 complex binds selectively to the E8 region, which represents part of the long arm of laminin. |
|
Publications: |
1 |
+ |
ITGA7 | form complex
binding
|
a7/b1 integrin |
0.764 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-241508 |
|
|
Homo sapiens |
Myoblast, Skeletal Muscle Fiber |
pmid |
sentence |
10199978 |
The alpha7beta1 integrin is a laminin receptor on the surface of skeletal myoblasts and myofibers. Alternative forms of both the alpha7 and beta1 chains are expressed in a developmentally regulated fashion during myogenesis. These different alpha7beta1 isoforms localize at specific sites on myofibers and appear to have distinct functions in skeletal muscle. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TGFBI | up-regulates activity
binding
|
a7/b1 integrin |
0.417 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253266 |
|
|
|
|
pmid |
sentence |
26387839 |
BIGH3 binds molecules of the ECM, including fibronectin, laminin and different collagens ( Hashimoto et al., 1997 ; Hanssen et al., 2003) and serves as a ligand for several integrins|BIGH3 has been shown to interact with α3β1, αvβ3, αvβ5, α1β1, α6β4 and α7β1 integrin heterodimers |
|
Publications: |
1 |
+ |
CIB2 | up-regulates activity
binding
|
a7/b1 integrin |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269668 |
|
|
Homo sapiens |
|
pmid |
sentence |
35408910 |
So far, two integrins have been found to interact with CIB2: αIIbβ3 is expressed by platelets and megakaryocytes and, apparently, a common target for all CIB family members, at odds with α7Bβ1D, which seems to be CIB2-specific and is expressed in skeletal muscles. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
a7/b1 integrin | down-regulates activity
|
A5/b1 integrin |
0.747 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253251 |
|
|
|
|
pmid |
sentence |
9925758 |
These data indicate that alpha7 expression leads to the functional down regulation of alpha5beta1 integrin by decreasing ligand binding affinity and surface expression. In conclusion, the data reported establish the existence of a negative cooperativity between alpha7 and alpha5 integrins that may be important in determining functional regulation of integrins during myogenic differentiation. |
|
Publications: |
1 |
+ |
ITGB1 | form complex
binding
|
a7/b1 integrin |
0.764 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-241512 |
|
|
Homo sapiens |
Myoblast, Skeletal Muscle Fiber |
pmid |
sentence |
10199978 |
The alpha7beta1 integrin is a laminin receptor on the surface of skeletal myoblasts and myofibers. Alternative forms of both the alpha7 and beta1 chains are expressed in a developmentally regulated fashion during myogenesis. These different alpha7beta1 isoforms localize at specific sites on myofibers and appear to have distinct functions in skeletal muscle. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |