PGK1/YCR012W Literature Guide Help

Other names published for PGK1: phosphoglycerate kinase, YCR012W

PGK1 - Protein-protein Interactions (12)

ReferenceOther Genes Addressed
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
Agocs G, et al.  (2010) Recovery of functional enzyme from amyloid fibrils. FEBS Lett 584(6):1139-42
Phan VT, et al.  (2010) The RasGAP proteins Ira2 and neurofibromin are negatively regulated by Gpb1 in yeast and ETEA in humans. Mol Cell Biol 30(9):2264-79
Nevzglyadova OV, et al.  (2009) Prion-associated proteins in yeast: comparative analysis of isogenic [PSI(+)] and [psi(-)] strains. Yeast 26(11):611-31
Wang Y, et al.  (2007) Characterization of proteins associated with polyglutamine aggregates: a novel approach towards isolation of aggregates from protein conformation disorders. Prion 1(2):128-35
Osvath S, et al.  (2006) Domain interactions direct misfolding and amyloid formation of yeast phosphoglycerate kinase. Proteins 62(4):909-17
Modler AJ, et al.  (2003) Assembly of amyloid protofibrils via critical oligomers--a novel pathway of amyloid formation. J Mol Biol 325(1):135-48
Belghazi M, et al.  (2001) Analysis of protein sequences and protein complexes by matrix-assisted laser desorption/ionization mass spectrometry. Proteomics 1(8):946-54
Damaschun G, et al.  (1999) Proteins can adopt totally different folded conformations. J Mol Biol 291(3):715-25
Pecorari F, et al.  (1996) Occurrence of transient multimeric species during the refolding of a monomeric protein. J Biol Chem 271(9):5270-6
Fairbrother WJ, et al.  (1989) Nuclear magnetic resonance studies of isolated structural domains of yeast phosphoglycerate kinase. Protein Eng 3(1):5-11
Ashmarina LI, et al.  (1985) Yeast glyceraldehyde-3-phosphate dehydrogenase. Evidence that subunit cooperativity in catalysis can be controlled by the formation of a complex with phosphoglycerate kinase. Eur J Biochem 149(1):67-72