PGK1/YCR012W Literature Guide Help

Other names published for PGK1: phosphoglycerate kinase, YCR012W

PGK1 - Protein Sequence Features (50)

ReferenceOther Genes Addressed
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Rosenkranz T, et al.  (2011) Native and Unfolded States of Phosphoglycerate Kinase Studied by Single-Molecule FRET. Chemphyschem 12(3):704-10
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Balog E, et al.  (2007) The influence of interdomain interactions on the intradomain motions in yeast phosphoglycerate kinase: a molecular dynamics study. Biophys J 92(5):1709-16
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
Kotsikorou E, et al.  (2006) Bisphosphonate inhibition of phosphoglycerate kinase: quantitative structure-activity relationship and pharmacophore modeling investigation. J Med Chem 49(23):6692-703
Osvath S, et al.  (2006) Domain interactions direct misfolding and amyloid formation of yeast phosphoglycerate kinase. Proteins 62(4):909-17
de Almeida JR, et al.  (2005) Molecular characterization of the 3-phosphoglycerate kinase gene (PGK1) from the methylotrophic yeast Pichia pastoris. Yeast 22(9):725-37
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
Osvath S and Gruebele M  (2003) Proline can have opposite effects on fast and slow protein folding phases. Biophys J 85(2):1215-22
Tougard P, et al.  (2002) Structure of a circularly permuted phosphoglycerate kinase. Acta Crystallogr D Biol Crystallogr 58(Pt 12):2018-23
Collinet B, et al.  (2001) Role of loops in the folding and stability of yeast phosphoglycerate kinase. Eur J Biochem 268(19):5107-18
Damaschun G, et al.  (1999) Proteins can adopt totally different folded conformations. J Mol Biol 291(3):715-25
Norbeck J and Blomberg A  (1997) Two-dimensional electrophoretic separation of yeast proteins using a non-linear wide range (pH 3-10) immobilized pH gradient in the first dimension; reproducibility and evidence for isoelectric focusing of alkaline (pI > 7) proteins. Yeast 13(16):1519-34
Sherman MA, et al.  (1997) An engineered amino-terminal domain of yeast phosphoglycerate kinase with native-like structure. Protein Sci 6(4):882-91
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
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
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
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
Graham HC, et al.  (1991) A proton-NMR study of a site-directed mutation (His388----Glu) in the interdomain region of yeast phosphoglycerate kinase. Implications for domain movement. Eur J Biochem 196(2):261-9
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
Semisotnov GV, et al.  (1991) Refolding kinetics of pig muscle and yeast 3-phosphoglycerate kinases and of their proteolytic fragments. Eur J Biochem 202(3):1083-9
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