IndraLab

Statements

EGFR phosphorylates PLCG1 on Y783. 20 / 20
1 1 16 1 | 1
hprd
No evidence text available
16497976
hprd
No evidence text available
8657103
hprd
No evidence text available
8657103
biopax:phosphositeplus
No evidence text available
hprd
No evidence text available
7682059
hprd
No evidence text available
20068231
hprd
No evidence text available
7682059
hprd
No evidence text available
20068231
signor
"In contrast, egf-induced tyrosine phosphorylation of plc-gamma 1 was rather small, indicating that tyrosine phosphorylation of plc-gamma 1 is not proportional to changes in plc activity. These results suggest that autophosphorylation of theegfr may induce a conformational change of its kinase domain which enhances its kinase activity with exogenous substrates and may induce association with phospholipase c-gamma by increasing its affinity to a domain containing tyr-771."
9176240
hprd
No evidence text available
1689310
hprd
No evidence text available
17016520
reach
"According to a current model of Poulin et al. [8] the EGFR phosphorylates PLCgamma1 on Y783 and two minor sites, Y771 and Y1253."
17561374
hprd
No evidence text available
17016520
hprd
No evidence text available
17389395
phosphoelm
No evidence text available
1689310
hprd
No evidence text available
8885868
hprd
No evidence text available
17389395
hprd
No evidence text available
1689310
hprd
No evidence text available
16497976
hprd
No evidence text available
8885868