Structural basis for specificity of GRB2-SH2 revealed by a novel ligand binding mode
- 1 July 1996
- journal article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 3 (7) , 586-589
- https://doi.org/10.1038/nsb0796-586
Abstract
No abstract availableThis publication has 34 references indexed in Scilit:
- Human Sos1: a Guanine Nucleotide Exchange Factor for Ras that Binds to GRB2Science, 1993
- Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factorCell, 1993
- Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformationNature, 1993
- Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signallingNature, 1993
- The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1Nature, 1993
- SH2 domains recognize specific phosphopeptide sequencesPublished by Elsevier ,1993
- Cloning of ASH, a ubiquitous protein composed of one Src homology region (SH) 2 and two SH3 domains, from human and rat cDNA libraries.Proceedings of the National Academy of Sciences, 1992
- The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signalingCell, 1992
- Receptor tyrosine kinasesThe FASEB Journal, 1992
- Oncogenes and signal transductionCell, 1991