PGK1/YCR012W Literature Guide Help

Other names published for PGK1: phosphoglycerate kinase, YCR012W

PGK1 - Techniques and Reagents (32)

ReferenceOther Genes Addressed
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Welter E, et al.  (2010) Quantification of nonselective bulk autophagy in S. cerevisiae using Pgk1-GFP. Autophagy 6(6):794-7
Birkaya B, et al.  (2009) Role of the cell wall integrity and filamentous growth mitogen-activated protein kinase pathways in cell wall remodeling during filamentous growth. Eukaryot Cell 8(8):1118-33
Stahlberg A, et al.  (2008) Multiway real-time PCR gene expression profiling in yeast Saccharomyces cerevisiae reveals altered transcriptional response of ADH-genes to glucose stimuli. BMC Genomics 9:170
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Tagwerker C, et al.  (2006) A tandem affinity tag for two-step purification under fully denaturing conditions: application in ubiquitin profiling and protein complex identification combined with in vivocross-linking. Mol Cell Proteomics 5(4):737-48
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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
Plant EP, et al.  (2004) A programmed -1 ribosomal frameshift signal can function as a cis-acting mRNA destabilizing element. Nucleic Acids Res 32(2):784-90
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
Gellissen G and Hollenberg CP  (1997) Application of yeasts in gene expression studies: a comparison of Saccharomyces cerevisiae, Hansenula polymorpha and Kluyveromyces lactis -- a review. Gene 190(1):87-97
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
Lu M, et al.  (1996) Ucon-benzoyl dextran aqueous two-phase systems: protein purification with phase component recycling. J Chromatogr B Biomed Appl 680(1-2):65-70
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
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
Dryden DT and Pain RH  (1989) Assignment of the heterogeneous static and time-resolved tryptophan fluorescence of 3-phosphoglycerate kinase. Biochim Biophys Acta 997(3):313-21
Minard P, et al.  (1989) Efficient expression and characterization of isolated structural domains of yeast phosphoglycerate kinase generated by site-directed mutagenesis. Protein Eng 3(1):55-60
Tamura JK, et al.  (1986) Affinity labeling of nucleotide-binding sites on kinases and dehydrogenases by pyridoxal 5'-diphospho-5'-adenosine. J Biol Chem 261(9):4126-33
Hitzeman RA, et al.  (1980) Isolation and characterization of the yeast 3-phosphoglycerokinase gene (PGK) by an immunological screening technique. J Biol Chem 255(24):12073-80