RAS2/YNL098C Literature Guide Help

Other names published for RAS2: CTN5, CYR3, GLC5, TSL7, YNL098C

RAS2 - Techniques and Reagents (17)

ReferenceOther Genes Addressed
Spira F, et al.  (2012) Patchwork organization of the yeast plasma membrane into numerous coexisting domains.LID - 10.1038/ncb2487 [doi] Nat Cell Biol ()
Manandhar SP, et al.  (2010) Chemical inhibition of CaaX protease activity disrupts yeast Ras localization. Yeast 27(6):327-43
Papanayotou I, et al.  (2010) Protein aggregation induced during glass bead lysis of yeast. Yeast 27(10):801-16
Vinnakota KC, et al.  (2010) Analysis of the diffusion of Ras2 in Saccharomyces cerevisiae using fluorescence recovery after photobleaching. Phys Biol 7(2):026011
Budde C, et al.  (2006) Purification and characterization of recombinant protein acyltransferases. Methods 40(2):143-50
Shibasaki S, et al.  (2006) Detection of protein-protein interactions by a combination of a novel cytoplasmic membrane targeting system of recombinant proteins and fluorescence resonance energy transfer. Appl Microbiol Biotechnol 70(4):451-7
Anderson JL, et al.  (2005) Purification, functional reconstitution, and characterization of the Saccharomyces cerevisiae isoprenylcysteine carboxylmethyltransferase Ste14p. J Biol Chem 280(8):7336-45
Bidlingmaier S and Snyder M  (2002) Large-scale identification of genes important for apical growth in Saccharomyces cerevisiae by directed allele replacement technology (DART) screening. Funct Integr Genomics 1(6):345-56
Blazquez MA, et al.  (1994) Use of Yarrowia lipolytica hexokinase for the quantitative determination of trehalose 6-phosphate. FEMS Microbiol Lett 121(2):223-7
Haney SA and Broach JR  (1994) Cdc25p, the guanine nucleotide exchange factor for the Ras proteins of Saccharomyces cerevisiae, promotes exchange by stabilizing Ras in a nucleotide-free state. J Biol Chem 269(24):16541-8
Jacquet E, et al.  (1994) Properties of the catalytic domain of CDC25, a Saccharomyces cerevisiae GDP/GTP exchange factor: comparison of its activity on full-length and C-terminal truncated RAS2 proteins. Biochem Biophys Res Commun 199(2):497-503
Kuroda Y, et al.  (1993) The effect of posttranslational modifications on the interaction of Ras2 with adenylyl cyclase. Science 259(5095):683-6
Mitchell DA, et al.  (1993) Vectors for the inducible overexpression of glutathione S-transferase fusion proteins in yeast. Yeast 9(7):715-22
Suzuki N, et al.  (1993) Antibody mimicking the action of RAS proteins on yeast adenylyl cyclase: implication for RAS-effector interaction. Mol Cell Biol 13(2):769-74
Verrotti AC, et al.  (1992) RAS residues that are distant from the GDP binding site play a critical role in dissociation factor-stimulated release of GDP. EMBO J 11(8):2855-62
Broek D, et al.  (1985) Differential activation of yeast adenylate cyclase by wild-type and mutant RAS proteins. Cell 41(3):763-9
Tamanoi F, et al.  (1984) A product of yeast RAS2 gene is a guanine nucleotide binding protein. Proc Natl Acad Sci U S A 81(22):6924-8