CDC19/YAL038W Literature Guide Help

Other names published for CDC19: PYK1, pyruvate kinase CDC19, YAL038W

CDC19 - Protein Processing/Modification/Regulation (33)

ReferenceOther Genes Addressed
Bluemlein K, et al.  (2012) Pyruvate kinase is a dosage-dependent regulator of cellular amino acid homeostasis. Oncotarget 3(11):1356-69
Gomez-Pastor R, et al.  (2012) Engineered Trx2p industrial yeast strain protects glycolysis and fermentation proteins from oxidative carbonylation during biomass propagation. Microb Cell Fact 11(1):4
Lesur A, et al.  (2012) Peptides quantification by liquid chromatography with matrix-assisted laser desorption/ionization and selected reaction monitoring detection. J Proteome Res 11(10):4972-82
Oliveira AP, et al.  (2012) Regulation of yeast central metabolism by enzyme phosphorylation. Mol Syst Biol 8():623
Tamarit J, et al.  (2012) Analysis of oxidative stress-induced protein carbonylation using fluorescent hydrazides. J Proteomics 75(12):3778-88
Xu YF, et al.  (2012) Regulation of yeast pyruvate kinase by ultrasensitive allostery independent of phosphorylation. Mol Cell 48(1):52-62
Helbig AO, et al.  (2011) The diversity of protein turnover and abundance under nitrogen-limited steady-state conditions in Saccharomyces cerevisiae. Mol Biosyst 7(12):3316-26
Fendt SM, et al.  (2010) Tradeoff between enzyme and metabolite efficiency maintains metabolic homeostasis upon perturbations in enzyme capacity. Mol Syst Biol 6():356
Galello F, et al.  (2010) Characterization of substrates that have a differential effect on Saccharomyces cerevisiae protein kinase A holoenzyme activation. J Biol Chem 285(39):29770-9
Helbig AO, et al.  (2010) Perturbation of the yeast N-acetyltransferase NatB induces elevation of protein phosphorylation levels. BMC Genomics 11(1):685
Irazusta V, et al.  (2010) Yeast frataxin mutants display decreased superoxide dismutase activity crucial to promote protein oxidative damage. Free Radic Biol Med 48(3):411-420
Kim JH, et al.  (2010) Dynamics of protein damage in yeast frataxin mutant exposed to oxidative stress. OMICS 14(6):689-99
Kim JH, et al.  (2010) Oxidative stress studies in yeast with a frataxin mutant: a proteomics perspective. J Proteome Res 9(2):730-6
Zi L, et al.  (2010) [Impact of distillage recycling on the glycolysis key enzymes, stress response metabolites and intracelluler components of the self-flocculating yeast]. Sheng Wu Gong Cheng Xue Bao 26(7):1019-24
Lin FM, et al.  (2009) Comparative proteomic analysis of tolerance and adaptation of ethanologenic Saccharomyces cerevisiae to furfural, a lignocellulosic inhibitory compound. Appl Environ Microbiol 75(11):3765-76
McDonagh B, et al.  (2009) Shotgun redox proteomics identifies specifically modified cysteines in key metabolic enzymes under oxidative stress in Saccharomyces cerevisiae. J Proteomics 72(4):677-89
Irazusta V, et al.  (2008) Major targets of iron-induced protein oxidative damage in frataxin-deficient yeasts are magnesium-binding proteins. Free Radic Biol Med 44(9):1712-1723
Lee RE, et al.  (2008) A non-death role of the yeast metacaspase: Yca1p alters cell cycle dynamics. PLoS ONE 3(8):e2956
Rinaldi J, et al.  (2008) A novel activating effect of the regulatory subunit of protein kinase A on catalytic subunit activity. Arch Biochem Biophys 480(2):95-103
Minard KI, et al.  (2007) Changes in disulfide bond content of proteins in a yeast strain lacking major sources of NADPH. Free Radic Biol Med 42(1):106-17
Molin M, et al.  (2007) Dihydroxyacetone-induced death is accompanied by advanced glycation endproduct formation in selected proteins of Saccharomyces cerevisiae and Caenorhabditis elegans. Proteomics 7(20):3764-74
Xie H, et al.  (2007) Preparative peptide isoelectric focusing as a tool for improving the identification of lysine-acetylated peptides from complex mixtures. J Proteome Res 6(5):2019-26
Portela P, et al.  (2006) Characterization of yeast pyruvate kinase 1 as a protein kinase A substrate, and specificity of the phosphorylation site sequence in the whole protein. Biochem J 396(1):117-26
Dephoure N, et al.  (2005) Combining chemical genetics and proteomics to identify protein kinase substrates. Proc Natl Acad Sci U S A 102(50):17940-5
Gruhler A, et al.  (2005) Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway. Mol Cell Proteomics 4(3):310-27
Kus B, et al.  (2005) A high throughput screen to identify substrates for the ubiquitin ligase Rsp5. J Biol Chem 280(33):29470-8
Zhou W, et al.  (2004) Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses. J Biol Chem 279(31):32262-8
Portela P, et al.  (2002) In vivo and in vitro phosphorylation of two isoforms of yeast pyruvate kinase by protein kinase A. J Biol Chem 277(34):30477-87
Cytrynska M, et al.  (2001) Saccharomyces cerevisiae pyruvate kinase Pyk1 is PKA phosphorylation substrate in vitro. FEMS Microbiol Lett 203(2):223-7
Nilsson A, et al.  (2001) The catabolic capacity of Saccharomyces cerevisiae is preserved to a higher extent during carbon compared to nitrogen starvation. Yeast 18(15):1371-81