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234 related items for PubMed ID: 1531699
1. Tyrosine phosphorylation of vav proto-oncogene product containing SH2 domain and transcription factor motifs. Margolis B, Hu P, Katzav S, Li W, Oliver JM, Ullrich A, Weiss A, Schlessinger J. Nature; 1992 Mar 05; 356(6364):71-4. PubMed ID: 1531699 [Abstract] [Full Text] [Related]
2. Product of vav proto-oncogene defines a new class of tyrosine protein kinase substrates. Bustelo XR, Ledbetter JA, Barbacid M. Nature; 1992 Mar 05; 356(6364):68-71. PubMed ID: 1311423 [Abstract] [Full Text] [Related]
3. Single point mutations in the SH2 domain impair the transforming potential of vav and fail to activate proto-vav. Katzav S. Oncogene; 1993 Jul 05; 8(7):1757-63. PubMed ID: 8510922 [Abstract] [Full Text] [Related]
4. Insulin-like growth factor-1 induces rapid tyrosine phosphorylation of the vav proto-oncogene product. Uddin S, Yetter A, Katzav S, Hofmann C, White MF, Platanias LC. Exp Hematol; 1996 Apr 05; 24(5):622-7. PubMed ID: 8605967 [Abstract] [Full Text] [Related]
5. Vav binds to several SH2/SH3 containing proteins in activated lymphocytes. Ramos-Morales F, Druker BJ, Fischer S. Oncogene; 1994 Jul 05; 9(7):1917-23. PubMed ID: 8208538 [Abstract] [Full Text] [Related]
6. Tyrosine phosphorylation and activation of Vav GTP/GDP exchange activity in antigen receptor-triggered B cells. Gulbins E, Langlet C, Baier G, Bonnefoy-Berard N, Herbert E, Altman A, Coggeshall KM. J Immunol; 1994 Mar 01; 152(5):2123-9. PubMed ID: 8133029 [Abstract] [Full Text] [Related]
9. Mutagenic analysis of Vav reveals that an intact SH3 domain is required for transformation. Groysman M, Nagano M, Shaanan B, Katzav S. Oncogene; 1998 Sep 24; 17(12):1597-606. PubMed ID: 9794237 [Abstract] [Full Text] [Related]
15. Autophosphorylation mutants of the EGF-receptor signal through auxiliary mechanisms involving SH2 domain proteins. Li N, Schlessinger J, Margolis B. Oncogene; 1994 Dec 15; 9(12):3457-65. PubMed ID: 7970705 [Abstract] [Full Text] [Related]
16. The protein tyrosine kinase ZAP-70 can associate with the SH2 domain of proto-Vav. Katzav S, Sutherland M, Packham G, Yi T, Weiss A. J Biol Chem; 1994 Dec 23; 269(51):32579-85. PubMed ID: 7798261 [Abstract] [Full Text] [Related]
18. The SH2 and SH3 domain-containing Nck protein is oncogenic and a common target for phosphorylation by different surface receptors. Li W, Hu P, Skolnik EY, Ullrich A, Schlessinger J. Mol Cell Biol; 1992 Dec 23; 12(12):5824-33. PubMed ID: 1333047 [Abstract] [Full Text] [Related]
19. Vav family proteins couple to diverse cell surface receptors. Moores SL, Selfors LM, Fredericks J, Breit T, Fujikawa K, Alt FW, Brugge JS, Swat W. Mol Cell Biol; 2000 Sep 23; 20(17):6364-73. PubMed ID: 10938113 [Abstract] [Full Text] [Related]
20. Functional and physical interactions of Syk family kinases with the Vav proto-oncogene product. Deckert M, Tartare-Deckert S, Couture C, Mustelin T, Altman A. Immunity; 1996 Dec 23; 5(6):591-604. PubMed ID: 8986718 [Abstract] [Full Text] [Related] Page: [Next] [New Search]