ENO2/YHR174W Literature Guide Help

Other names published for ENO2: enolase, phosphopyruvate hydratase ENO2, YHR174W

ENO2 - Primary Literature (55)

Results: 1 - 30 of 55 records
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ReferenceOther Genes Addressed
Bang SY, et al.  (2013) Candidate target genes for the Saccharomyces cerevisiae transcription factor, Yap2. Folia Microbiol (Praha) ()
Miura N, et al.  (2012) Tracing putative trafficking of the glycolytic enzyme enolase via SNARE-driven unconventional secretion. Eukaryot Cell 11(8):1075-82
Kim KH, et al.  (2011) Effect of Saccharomyces cerevisiae ret1-1 mutation on glycosylation and localization of the secretome. Mol Cells 31(2):151-8
Fendt SM, et al.  (2010) Tradeoff between enzyme and metabolite efficiency maintains metabolic homeostasis upon perturbations in enzyme capacity. Mol Syst Biol 6():356
Ohlmeier S, et al.  (2010) Protein phosphorylation in mitochondria - A study on fermentative and respiratory growth of Saccharomyces cerevisiae. Electrophoresis 31(17):2869-81
Wiederhold E, et al.  (2009) The yeast vacuolar membrane proteome. Mol Cell Proteomics 8(2):380-92
Xie H, et al.  (2009) Characterization of protein impurities and site-specific modifications using peptide mapping with liquid chromatography and data independent acquisition mass spectrometry. Anal Chem 81(14):5699-708
Gomes RA, et al.  (2008) Protein glycation in vivo: functional and structural effects on yeast enolase. Biochem J 416(3):317-26
Pal-Bhowmick I, et al.  (2007) Differential susceptibility of Plasmodium falciparum versus yeast and mammalian enolases to dissociation into active monomers. FEBS J 274(8):1932-45
Sarry JE, et al.  (2007) Analysis of the vacuolar luminal proteome of Saccharomyces cerevisiae. FEBS J 274(16):4287-305
Brandina I, et al.  (2006) Enolase takes part in a macromolecular complex associated to mitochondria in yeast. Biochim Biophys Acta 1757(9-10):1217-1228
Decker BL and Wickner WT  (2006) Enolase activates homotypic vacuole fusion and protein transport to the vacuole in yeast. J Biol Chem 281(20):14523-8
Gomes RA, et al.  (2006) Yeast protein glycation in vivo by methylglyoxal. FEBS J 273(23):5273-87
Lopez-Villar E, et al.  (2006) Genetic and proteomic evidences support the localization of yeast enolase in the cell surface. Proteomics 6 Suppl 1:S107-18
Byrne KP and Wolfe KH  (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
De D, et al.  (2005) Inactive enzymatic mutant proteins (phosphoglycerate mutase and enolase) as sugar binders for ribulose-1,5-bisphosphate regeneration reactors. Microb Cell Fact 4(1):5
Boel G, et al.  (2004) Is 2-phosphoglycerate-dependent automodification of bacterial enolases implicated in their export? J Mol Biol 337(2):485-96
Kornblatt MJ, et al.  (2004) Use of hydrostatic pressure to produce 'native' monomers of yeast enolase. Eur J Biochem 271(19):3897-904
Hannaert V, et al.  (2003) Kinetic characterization, structure modelling studies and crystallization of Trypanosoma brucei enolase. Eur J Biochem 270(15):3205-13
Salusjarvi L, et al.  (2003) Proteome analysis of recombinant xylose-fermenting Saccharomyces cerevisiae. Yeast 20(4):295-314
Sims PA, et al.  (2003) Reverse protonation is the key to general acid-base catalysis in enolase. Biochemistry 42(27):8298-306
Larsen MR, et al.  (2001) Characterization of differently processed forms of enolase 2 from Saccharomyces cerevisiae by two-dimensional gel electrophoresis and mass spectrometry. Electrophoresis 22(3):566-75
Poyner RR, et al.  (2001) Role of metal ions in catalysis by enolase: an ordered kinetic mechanism for a single substrate enzyme. Biochemistry 40(27):8009-17
Peter Smits H, et al.  (2000) Simultaneous overexpression of enzymes of the lower part of glycolysis can enhance the fermentative capacity of Saccharomyces cerevisiae. Yeast 16(14):1325-34
Vinarov DA and Nowak T  (1999) Role of His159 in yeast enolase catalysis. Biochemistry 38(37):12138-49
Vinarov DA and Nowak T  (1998) pH dependence of the reaction catalyzed by yeast Mg-enolase. Biochemistry 37(43):15238-46
Larsen TM, et al.  (1996) A carboxylate oxygen of the substrate bridges the magnesium ions at the active site of enolase: structure of the yeast enzyme complexed with the equilibrium mixture of 2-phosphoglycerate and phosphoenolpyruvate at 1.8 A resolution. Biochemistry 35(14):4349-58
Poyner RR, et al.  (1996) Toward identification of acid/base catalysts in the active site of enolase: comparison of the properties of K345A, E168Q, and E211Q variants. Biochemistry 35(5):1692-9
Reed GH, et al.  (1996) Structural and mechanistic studies of enolase. Curr Opin Struct Biol 6(6):736-43
Carmen AA, et al.  (1995) Transcriptional regulation by an upstream repression sequence from the yeast enolase gene ENO1. Yeast 11(11):1031-43
Results: 1 - 30 of 55 records
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