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G3BP1 — RASA1

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: G3BP1 — RASA1 (physical association, affinity chromatography technology) Gallouzi et al., Mol Cell Biol 1998*
• IRef Hprd Interaction: G3BP1 — RASA1 (in vitro) Gallouzi et al., Mol Cell Biol 1998*
• IRef Hprd Interaction: G3BP1 — RASA1 (in vivo) Gallouzi et al., Mol Cell Biol 1998*
• IRef Ophid Interaction: G3BP1 — RASA1 (aggregation, interologs mapping) Brown et al., Bioinformatics 2005

Text-mined interactions from Literome

Barnes et al., Cancer Res 2002 (Breast Neoplasms) : In addition, HRG stimulation of breast cancer cells promoted phosphorylation of G3BP and increased the association of G3BP with GTPase activating protein , both of which are essential for G3BP activity
Garaigorta et al., J Virol 2012 : Finally, in short hairpin RNA ( shRNA ) knockdown experiments, we found that the stress granule proteins T-cell restricted intracellular antigen 1 ( TIA-1 ), TIA1 related protein (TIAR), and RasGAP-SH3 domain binding protein 1 ( G3BP1 ) are required for efficient HCV RNA and protein accumulation at early time points in the infection and that G3BP1 and TIA-1 are required for intracellular and extracellular infectious virus production late in the infection, suggesting that they are required for virus assembly