SH2 domains: elements that control protein interactions during signal transduction
- PMID: 1781020
- DOI: 10.1016/0968-0004(91)90175-u
SH2 domains: elements that control protein interactions during signal transduction
Similar articles
-
Direct interaction of v-Src with the focal adhesion kinase mediated by the Src SH2 domain.Mol Biol Cell. 1994 Apr;5(4):413-21. doi: 10.1091/mbc.5.4.413. Mol Biol Cell. 1994. PMID: 8054685 Free PMC article.
-
Tyrosine phosphorylation of vav proto-oncogene product containing SH2 domain and transcription factor motifs.Nature. 1992 Mar 5;356(6364):71-4. doi: 10.1038/356071a0. Nature. 1992. PMID: 1531699
-
Src kinase tyrosine phosphorylates PTP1C, a protein tyrosine phosphatase containing Src homology-2 domains that down-regulates cell proliferation.Biochem Biophys Res Commun. 1994 Oct 28;204(2):874-81. doi: 10.1006/bbrc.1994.2541. Biochem Biophys Res Commun. 1994. PMID: 7980555
-
A direct signaling pathway through tyrosine kinase activation of SH2 domain-containing transcription factors.J Leukoc Biol. 1995 Apr;57(4):529-35. doi: 10.1002/jlb.57.4.529. J Leukoc Biol. 1995. PMID: 7722410 Review.
-
Membrane interactions of pp60v-src: a model for myristylated tyrosine protein kinases.Oncogene. 1990 Oct;5(10):1437-44. Oncogene. 1990. PMID: 2250906 Review. No abstract available.
Cited by
-
SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange.Mol Cell Biol. 1993 Mar;13(3):1449-55. doi: 10.1128/mcb.13.3.1449-1455.1993. Mol Cell Biol. 1993. PMID: 7680095 Free PMC article.
-
Common elements in interleukin 4 and insulin signaling pathways in factor-dependent hematopoietic cells.Proc Natl Acad Sci U S A. 1993 May 1;90(9):4032-6. doi: 10.1073/pnas.90.9.4032. Proc Natl Acad Sci U S A. 1993. PMID: 7683417 Free PMC article.
-
Interaction of the p85 subunit of PI 3-kinase and its N-terminal SH2 domain with a PDGF receptor phosphorylation site: structural features and analysis of conformational changes.EMBO J. 1992 Dec;11(12):4261-72. doi: 10.1002/j.1460-2075.1992.tb05524.x. EMBO J. 1992. PMID: 1330535 Free PMC article.
-
Phosphotyrosine recognition domains: the typical, the atypical and the versatile.Cell Commun Signal. 2012 Nov 7;10(1):32. doi: 10.1186/1478-811X-10-32. Cell Commun Signal. 2012. PMID: 23134684 Free PMC article.
-
The SH2 and SH3 domain-containing Nck protein is oncogenic and a common target for phosphorylation by different surface receptors.Mol Cell Biol. 1992 Dec;12(12):5824-33. doi: 10.1128/mcb.12.12.5824-5833.1992. Mol Cell Biol. 1992. PMID: 1333047 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Other Literature Sources