PGK1/YCR012W Literature Guide Help

Other names published for PGK1: phosphoglycerate kinase, YCR012W

PGK1 - Function/Process (57)

Results: 1 - 30 of 57 records
   1  2 
ReferenceOther Genes Addressed
Lee SH, et al.  (2011) Global organization of protein complexome in the yeast Saccharomyces cerevisiae. BMC Syst Biol 5(1):126
Ma M and Liu LZ  (2010) Quantitative transcription dynamic analysis reveals candidate genes and key regulators for ethanol tolerance in Saccharomyces cerevisiae. BMC Microbiol 10():169
Hurth C, et al.  (2007) Enzymatic activity of immobilized yeast phosphoglycerate kinase. Biosens Bioelectron 22(11):2449-55
Magherini F, et al.  (2007) Protein expression profiles in Saccharomyces cerevisiae during apoptosis induced by H(2)O(2). Proteomics 7(9):1434-45
Osvath S, et al.  (2005) Asymmetric effect of domain interactions on the kinetics of folding in yeast phosphoglycerate kinase. Protein Sci 14(6):1609-16
Varga A, et al.  (2005) Correlation between conformational stability of the ternary enzyme-substrate complex and domain closure of 3-phosphoglycerate kinase. FEBS J 272(8):1867-85
Merritt J, et al.  (2003) Parallel competition analysis of Saccharomyces cerevisiae strains differing by a single base using polymerase colonies. Nucleic Acids Res 31(15):e84
Pearce AK, et al.  (2001) Pyruvate kinase (Pyk1) levels influence both the rate and direction of carbon flux in yeast under fermentative conditions. Microbiology 147(Pt 2):391-401
Van Hoek P, et al.  (2001) Human acylphosphatase cannot replace phosphoglycerate kinase in Saccharomyces cerevisiae. Antonie Van Leeuwenhoek 80(1):11-7
Collinet B, et al.  (2000) Functionally accepted insertions of proteins within protein domains. J Biol Chem 275(23):17428-33
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
McHarg J, et al.  (1999) Site-directed mutagenesis of proline 204 in the 'hinge' region of yeast phosphoglycerate kinase. Eur J Biochem 259(3):939-45
Williams SP, et al.  (1997) 19F NMR measurements of the rotational mobility of proteins in vivo. Biophys J 72(1):490-8
Cheung CW and Mas MT  (1996) Substrate-induced conformational changes in yeast 3-phosphoglycerate kinase monitored by fluorescence of single tryptophan probes. Protein Sci 5(6):1144-9
Pappu KM and Serpersu EH  (1994) Proton NMR studies of a large protein. pH, substrate titrations, and NOESY experiments with perdeuterated yeast phosphoglycerate kinase containing [1H]histidine residues. J Magn Reson B 105(2):157-66
Barber MD, et al.  (1993) Site-directed mutagenesis of yeast phosphoglycerate kinase. Arginines 65, 121 and 168. FEBS Lett 320(3):193-7
Cioni P, et al.  (1993) Tryptophan phosphorescence as a monitor of the solution structure of phosphoglycerate kinase from yeast. Biophys Chem 46(1):47-55
Gast K, et al.  (1992) Application of dynamic light scattering to studies of protein folding kinetics. Eur Biophys J 21(5):357-62
Missiakas D, et al.  (1992) Kinetic studies of the refolding of yeast phosphoglycerate kinase: comparison with the isolated engineered domains. Protein Sci 1(11):1485-93
Sherman MA, et al.  (1992) Characterization of the structure and properties of the His 62-->Ala and Arg 38-->Ala mutants of yeast phosphoglycerate kinase: an investigation of the catalytic and activatory sites by site-directed mutagenesis and NMR. Protein Sci 1(6):752-60
Vlasova II and Kuprin SP  (1992) [Evaluation of distances in yeast phosphoglycerate kinase molecules using saturation effect ESR spectra at 77 K] Biofizika 37(5):927-34
Walker PA, et al.  (1992) Characterisation of yeast phosphoglycerate kinase modified by mutagenesis at residue 21. Eur J Biochem 207(1):29-37
Desmadril M, et al.  (1991) Conformational changes in yeast phosphoglycerate kinase upon ligand binding: fluorescence of a linked probe and chemical reactivity of genetically introduced cysteinyl residues. Proteins 10(4):315-24
Graham HC and Williams RJ  (1991) The roles of ADP2- and Mg2+ in control steps of phosphoglycerate kinase. Eur J Biochem 197(1):81-91
LaDine JR and Cross RL  (1991) The adenine nucleotide-binding site on yeast 3-phosphoglycerate kinase. Affinity labeling of Lys-131 by pyridoxal 5'-diphospho-5'-adenosine. J Biol Chem 266(11):7194-8
Varley PG, et al.  (1991) Resolution of the fluorescence of the buried tryptophan in yeast 3-phosphoglycerate kinase using succinimide. Biochim Biophys Acta 1077(1):19-24
Ballery N, et al.  (1990) Introduction of internal cysteines as conformational probes in yeast phosphoglycerate kinase. Protein Eng 3(3):199-204
Fairbrother WJ, et al.  (1990) An NMR study of anion binding to yeast phosphoglycerate kinase. Eur J Biochem 190(1):161-9
Fairbrother WJ, et al.  (1990) The roles of ATP4- and Mg2+ in control steps of phosphoglycerate kinase. Eur J Biochem 190(2):407-14
Sherman MA, et al.  (1990) Probing the role of arginines and histidines in the catalytic function and activation of yeast 3-phosphoglycerate kinase by site-directed mutagenesis. J Biol Chem 265(18):10659-65
Results: 1 - 30 of 57 records
   1  2