| + |
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 |
| + |
LAMA1 | form complex 
binding
|
Laminin-1 |
0.549 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253232 |
|
|
|
|
| pmid |
sentence |
| 7496033 |
Laminin-1 is an extracellular matrix protein composed of three polypeptide chains that are designated alpha 1, beta 1, and gamma 1. |
|
| Publications: |
1 |
| + |
LAMC1 | form complex
binding
|
Laminin-1 |
0.601 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253234 |
|
|
|
|
| pmid |
sentence |
| 7496033 |
Laminin-1 is an extracellular matrix protein composed of three polypeptide chains that are designated alpha 1, beta 1, and gamma 1. |
|
| Publications: |
1 |
| + |
LAMB1 | form complex
binding
|
Laminin-1 |
0.613 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253233 |
|
|
|
|
| pmid |
sentence |
| 7496033 |
Laminin-1 is an extracellular matrix protein composed of three polypeptide chains that are designated alpha 1, beta 1, and gamma 1. |
|
| Publications: |
1 |
| + |
Laminin-1 | up-regulates activity
binding
|
A6/b1 integrin |
0.537 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253256 |
|
|
|
|
| pmid |
sentence |
| 2351695 |
In combination, the anti-alpha 1- and anti-alpha 6-specific antibodies completely inhibited JAR cell attachment to LN and fragment E1. Thus, the alpha 1/beta 1 and alpha 6/beta 1 integrin heterodimers each function as LN receptors and act together to mediate the interactions of human JAR choriocarcinoma cells with LN. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253221 |
|
|
|
|
| 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: |
2 |
| + |
Laminin-1 | up-regulates activity
binding
|
A6/b4 integrin |
0.505 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258998 |
|
|
Homo sapiens |
Epithelial Cell |
| pmid |
sentence |
| 24184828 |
Integrin α6β4 is a laminin receptor that is mainly expressed in the basal layer of epithelial tissues. The β4-integrin is unique because of its long cytoplasmic tail, which interacts with the intermediate filament network rather than actin. This interaction contributes to the ability of α6β4 to maintain the integrity of tissues normally exposed to shear stress. α6β4 integrin assembles its own signalling platform. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Laminin-1 | up-regulates activity
binding
|
A1/b1 integrin |
0.539 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253254 |
|
|
|
|
| pmid |
sentence |
| 9361014 |
Using integrin-specific antibodies, recognition sites for the alpha1beta1 and alpha2beta1 integrins were identified in the short arms of both laminin alpha1- and alpha2-chain isoforms. Comparisons with a beta-alpha chimeric short arm protein possessing beta1-chain domain VI further localized these activities to alpha-chain domain VI. |
|
| Publications: |
1 |
| + |
Laminin-1 | up-regulates activity
binding
|
A2/b1 integrin |
0.527 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253255 |
|
|
|
|
| pmid |
sentence |
| 9361014 |
Using integrin-specific antibodies, recognition sites for the alpha1beta1 and alpha2beta1 integrins were identified in the short arms of both laminin alpha1- and alpha2-chain isoforms. Comparisons with a beta-alpha chimeric short arm protein possessing beta1-chain domain VI further localized these activities to alpha-chain domain VI. |
|
| Publications: |
1 |
3.0
Laminin-1
CPX-1770