Research Topics
Genomes and Genes | Y ZhengSummaryAffiliation: University of Tennessee Country: USA Publications
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Publications
Dbl family guanine nucleotide exchange factorsY Zheng
Dept of Molecular Sciences, University of Tennessee Health Science Center, Memphis, TN 38163, USA
Trends Biochem Sci 26:724-32. 2001..The detailed pictures of their autoregulation, agonist-controlled activation and mechanism of interaction with Rho GTPase substrates, have begun to emerge...
Autoinhibition mechanism of proto-DblF Bi
Department of Molecular Sciences, University of Tennessee Health Science Center, Memphis, Tennessee 38163, USA
Mol Cell Biol 21:1463-74. 2001....
Regulation of RhoA GTP hydrolysis by the GTPase-activating proteins p190, p50RhoGAP, Bcr, and 3BP-1B Zhang
Department of Biochemistry, University of Tennessee, Memphis, Tennessee 38163, USA
Biochemistry 37:5249-57. 1998....
Trp(56) of rac1 specifies interaction with a subset of guanine nucleotide exchange factorsY Gao
Department of Molecular Sciences, University of Tennessee Health Science Center, Memphis, TN 38163, USA
J Biol Chem 276:47530-41. 2001....
Interaction of Rac1 with GTPase-activating proteins and putative effectors. A comparison with Cdc42 and RhoAB Zhang
Department of Biochemistry, University of Tennessee, Memphis, Tennessee 38163, USA
J Biol Chem 273:8776-82. 1998....
Structural determinants required for the interaction between Rho GTPase and the GTPase-activating domain of p190R Li
Department of Biochemistry, University of Tennessee, Memphis, Tennessee 38163, USA
J Biol Chem 272:32830-5. 1997....
Oligomerization of DH domain is essential for Dbl-induced transformationK Zhu
Department of Molecular Sciences, University of Tennessee Health Science Center, Memphis, Tennessee 38163, USA
Mol Cell Biol 21:425-37. 2001....
A built-in arginine finger triggers the self-stimulatory GTPase-activating activity of rho family GTPasesB Zhang
Department of Biochemistry, University of Tennessee, Memphis, Tennessee 38163, USA
J Biol Chem 274:2609-12. 1999..cerevisiae CDC42 led to phenotypes consistent with down-regulated CDC42 function. Thus, specific Rho family GTPases may utilize a built-in arginine finger, in addition to RhoGAPs, for negative regulation...
Identification of Rho GTPase-dependent sites in the Dbl homology domain of oncogenic Dbl that are required for transformationK Zhu
Department of Biochemistry, University of Tennessee, Memphis, Tennessee 38163, USA
J Biol Chem 275:25993-6001. 2000....
Negative regulation of Rho family GTPases Cdc42 and Rac2 by homodimer formationB Zhang
Department of Biochemistry, University of Tennessee, Memphis, Tennessee 38163, USA
J Biol Chem 273:25728-33. 1998....
Oligomerization of Rac1 gtpase mediated by the carboxyl-terminal polybasic domainB Zhang
Department of Molecular Sciences, University of Tennessee Health Science Center, Memphis, Tennessee 38163, USA
J Biol Chem 276:8958-67. 2001....
Rac1 and extracellularly regulated kinase activation are sufficient for E1A-dependent cooperative transformation of primary epithelial cells, but progression can only be modulated by E1A or Rac1R S Fischer
Department of Microbiology and Immunology, University of Tennessee Health Science Center, Memphis 38163, USA
Cell Growth Differ 9:209-21. 1998..Thus, hypertransformation is not the result of extracellularly regulated kinase differences but can be effected by perturbations in Rac1 signals, as well as E1A 12S COOH-terminal mutants...
Characterization of the interactions between the small GTPase Cdc42 and its GTPase-activating proteins and putative effectors. Comparison of kinetic properties of Cdc42 binding to the Cdc42-interactive domainsB Zhang
Department of Biochemistry, University of Tennessee, Memphis, Tennessee 38163, USA
J Biol Chem 272:21999-2007. 1997....
The faciogenital dysplasia gene product FGD1 functions as a Cdc42Hs-specific guanine-nucleotide exchange factorY Zheng
Department of Biochemistry, University of Tennessee, Memphis, Tennessee 38163, USA
J Biol Chem 271:33169-72. 1996..Hence, our results indicate that FGD1, through its DH and PH domains, acts as a Cdc42Hs-specific guanine-nucleotide exchange factor and suggest that the Cdc42Hs GTPase may have a role in mammalian development...
