Member database | CDD |
CDD type | domain |
Short name | C1_VAV1 |
Set | C1 |
Description
References
2.Vav1: an oncogene that regulates specific transcriptional activation of T cells. Katzav S. Blood 103, 2443-51, (2004). View articlePMID: 14592821
3.Structure and function of vav. Romero F, Fischer S. Cell. Signal. 8, 545-53, (1996). View articlePMID: 9115846
4.The role of Vav proteins in B cell responses. Turner M. Adv. Exp. Med. Biol. 512, 29-34, (2002). PMID: 12405184
5.Recognition and activation of Rho GTPases by Vav1 and Vav2 guanine nucleotide exchange factors. Heo J, Thapar R, Campbell SL. Biochemistry 44, 6573-85, (2005). View articlePMID: 15850391
6.CD28 costimulation: a source of Vav-1 for TCR signaling with the help of SLP-76? Michel F, Acuto O. Sci. STKE 2002, pe35, (2002). View articlePMID: 12165654
7.An active form of Vav1 induces migration of mammary epithelial cells by stimulating secretion of an epidermal growth factor receptor ligand. Wilsbacher JL, Moores SL, Brugge JS. Cell Commun Signal 4, 5, (2006). PMID: 16709244
8.VAV1: a new target in pancreatic cancer? Denicola G, Tuveson DA. Cancer Biol Ther 4, 509-11, (2005). PMID: 15970675
9.Vav-family proteins in T-cell signalling. Tybulewicz VL. Curr. Opin. Immunol. 17, 267-74, (2005). View articlePMID: 15886116
10.Vav1: a key signal transducer downstream of the TCR. Tybulewicz VL, Ardouin L, Prisco A, Reynolds LF. Immunol. Rev. 192, 42-52, (2003). View articlePMID: 12670394
11.Acidic region tyrosines provide access points for allosteric activation of the autoinhibited Vav1 Dbl homology domain. Amarasinghe GK, Rosen MK. Biochemistry 44, 15257-68, (2005). View articlePMID: 16285729
12.Structural basis of guanine nucleotide exchange mediated by the T-cell essential Vav1. Chrencik JE, Brooun A, Zhang H, Mathews II, Hura GL, Foster SA, Perry JJ, Streiff M, Ramage P, Widmer H, Bokoch GM, Tainer JA, Weckbecker G, Kuhn P. J. Mol. Biol. 380, 828-43, (2008). View articlePMID: 18589439
13.Vav1: a hematopoietic signal transduction molecule involved in human malignancies. Katzav S. Int. J. Biochem. Cell Biol. 41, 1245-8, (2009). View articlePMID: 19100858
14.Tyrosine residues at the carboxyl terminus of Vav1 play an important role in regulation of its biological activity. Lazer G, Pe'er L, Farago M, Machida K, Mayer BJ, Katzav S. J Biol Chem 285, 23075-85, (2010). PMID: 20457609
15.Structural and energetic mechanisms of cooperative autoinhibition and activation of Vav1. Yu B, Martins IR, Li P, Amarasinghe GK, Umetani J, Fernandez-Zapico ME, Billadeau DD, Machius M, Tomchick DR, Rosen MK. Cell 140, 246-56, (2010). View articlePMID: 20141838
16.The association of Sam68 with Vav1 contributes to tumorigenesis. Lazer G, Pe'er L, Schapira V, Richard S, Katzav S. Cell. Signal. 19, 2479-86, (2007). View articlePMID: 17855053
17.Vav proteins, masters of the world of cytoskeleton organization. Hornstein I, Alcover A, Katzav S. Cell. Signal. 16, 1-11, (2004). View articlePMID: 14607270
18.Flesh and blood: the story of Vav1, a gene that signals in hematopoietic cells but can be transforming in human malignancies. Katzav S. Cancer Lett. 255, 241-54, (2007). View articlePMID: 17590270
19.Crucial structural role for the PH and C1 domains of the Vav1 exchange factor. Rapley J, Tybulewicz VL, Rittinger K. EMBO Rep. 9, 655-61, (2008). View articlePMID: 18511940