| + |
ITGAL | up-regulates activity 
binding
|
AKAP9 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260304 |
|
|
Homo sapiens |
HUT-78 Cell |
| pmid |
sentence |
| 16339516 |
However, association of CG-NAP/AKAP450 was signifi-cantly enhanced at 37°C in LFA-1-activated cells triggered toundergo motility. Taken together, our findings provide the first definitiveevidence that the protein CG-NAP/AKAP450 is a key scaffoldingcomponent of the multimolecular complex assembled in T cellsupon LFA cross-linking and is functionally indispensable for cellpolarity and migration induced by this integrin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SRC | down-regulates activity 
phosphorylation
|
ITGAL |
0.405 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254741 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25624455 |
PTKs of the JAK and SRC families have a regulatory role in LFA-1 affinity triggering, with JAKs showing a positive role (3), whereas SRCs possibly have a negative role. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JAK2 | up-regulates activity
phosphorylation
|
ITGAL |
0.273 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254739 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25624455 |
PTKs of the JAK and SRC families have a regulatory role in LFA-1 affinity triggering, with JAKs showing a positive role (3), whereas SRCs possibly have a negative role. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SELE | up-regulates 
|
ITGAL |
0.423 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255968 |
|
|
Homo sapiens |
Neutrophil |
| pmid |
sentence |
| 23994464 |
This deceleration is due to the expression of E-selectins on the inflamed endothelium which provides increased number of binding sites for PSGL-1 and also triggers an intermediate-affinity conformational state of the beta2-integrin LFA-1 on neutrophils. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRG | down-regulates activity 
|
ITGAL |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254736 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25624455 |
PTPRG activation inhibits chemoattractantinduced LFA-1 affinity triggering and mediated adhesion in human primary monocytes. we show that PTPRG is a novel negative regulator of LFA-1 high-affinity-state triggering and mediated arrest by chemoattractants in human primary monocytes. Notably, PTKs of the JAK and SRC families have a regulatory role in LFA-1 affinity triggering, with JAKs showing a positive role (3), whereas SRCs possibly have a negative role (37). In our context, SRC appears inhibited by PTPRG activation (Table I), thus making it unlikely that the antiadhesive effect of PTPRG is mediated by SRC activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ITGAL | up-regulates
binding
|
ICAM1 |
0.919 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255040 |
|
|
Homo sapiens |
Neutrophil |
| pmid |
sentence |
| 23994464 |
This leads to further neutrophil-endothelial cell interactions through the binding of LFA-1 to its endothelial counterreceptor ICAM-1 during the slow rolling phase |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ITGAL | form complex 
binding
|
AL/b2 integrin |
0.911 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253189 |
|
|
|
|
| pmid |
sentence |
| 16988024 |
Integrins are one of the major families of cell adhesion receptors (Humphries, 2000; Hynes, 2002). All integrins are non-covalently-linked, heterodimeric molecules containing an α and a β subunit. Both subunits are type I transmembrane proteins, containing large extracellular domains and mostly short cytoplasmic domains (Springer and Wang, 2004; Arnaout et al., 2005). Mammalian genomes contain 18 α subunit and 8 β subunit genes, and to date 24 different α,β combinations have been identified at the protein level. Although some subunits only appear in a single heterodimer, twelve integrins contain the β1 subunit, and five contain αV. |
|
| Publications: |
1 |
3.0
ITGAL
- 
- 