PGK1/YCR012W Literature Guide Help

Other names published for PGK1: phosphoglycerate kinase, YCR012W

PGK1 - Protein/Nucleic Acid Structure (59)

Results: 1 - 30 of 59 records
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ReferenceOther Genes Addressed
Genereaux J, et al.  (2012) Genetic evidence links the ASTRA protein chaperone component Tti2 to the SAGA transcription factor Tra1. Genetics 191(3):765-80
Smolin N, et al.  (2012) Functional domain motions in proteins on the ~1-100 ns timescale: comparison of neutron spin-echo spectroscopy of phosphoglycerate kinase with molecular-dynamics simulation. Biophys J 102(5):1108-17
Dhar A, et al.  (2011) Protein stability and folding kinetics in the nucleus and endoplasmic reticulum of eucaryotic cells. Biophys J 101(2):421-30
Rosenkranz T, et al.  (2011) Native and Unfolded States of Phosphoglycerate Kinase Studied by Single-Molecule FRET. Chemphyschem 12(3):704-10
Agocs G, et al.  (2010) Recovery of functional enzyme from amyloid fibrils. FEBS Lett 584(6):1139-42
Dhar A, et al.  (2010) Structure, function, and folding of phosphoglycerate kinase are strongly perturbed by macromolecular crowding. Proc Natl Acad Sci U S A 107(41):17586-91
Gloor GB, et al.  (2010) Functionally compensating coevolving positions are neither homoplasic nor conserved in clades. Mol Biol Evol 27(5):1181-91
Inoue R, et al.  (2010) Large domain fluctuations on 50-ns timescale enable catalytic activity in phosphoglycerate kinase. Biophys J 99(7):2309-17
Ijeoma O, et al.  (2008) Thermodynamic analysis of the nondenaturational conformational change of baker's yeast phosphoglycerate kinase at 24 degrees C. Arch Biochem Biophys 478(2):206-11
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
Young TA, et al.  (2007) Comparison of proteolytic susceptibility in phosphoglycerate kinases from yeast and E. coli: modulation of conformational ensembles without altering structure or stability. J Mol Biol 368(5):1438-47
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
Osvath S, et al.  (2006) Hierarchic finite level energy landscape model: to describe the refolding kinetics of phosphoglycerate kinase. J Biol Chem 281(34):24375-80
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
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
Brodsky AS and Silver PA  (2000) Pre-mRNA processing factors are required for nuclear export. RNA 6(12):1737-49
Collinet B, et al.  (2000) Functionally accepted insertions of proteins within protein domains. J Biol Chem 275(23):17428-33
Receveur V, et al.  (2000) Role of hydrophobic interactions in yeast phosphoglycerate kinase stability. Proteins 38(2):226-38
Damaschun G, et al.  (1999) Proteins can adopt totally different folded conformations. J Mol Biol 291(3):715-25
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
Raghunathan V, et al.  (1999) Structural characterization of manganese(II)-nucleotide complexes bound to yeast 3-phosphoglycerate kinase: 13C relaxation measurements using [U-13C]ATP and [U-13C]ADP. Biochemistry 38(47):15597-605
Sabelko J, et al.  (1999) Observation of strange kinetics in protein folding. Proc Natl Acad Sci U S A 96(11):6031-6
Sherman MA, et al.  (1997) An engineered amino-terminal domain of yeast phosphoglycerate kinase with native-like structure. Protein Sci 6(4):882-91
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
Pecorari F, et al.  (1996) Occurrence of transient multimeric species during the refolding of a monomeric protein. J Biol Chem 271(9):5270-6
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
Results: 1 - 30 of 59 records
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