TDH3/YGR192C Literature Guide Help

Other names published for TDH3: GLD1, HSP35, HSP36, SSS2, GPD, GAPDH, glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) TDH3, YGR192C

TDH3 - Protein-protein Interactions (18)

ReferenceOther Genes Addressed
Lee PY, et al.  (2011) The S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase 2 is reduced by interaction with glutathione peroxidase 3 in Saccharomyces cerevisiae. Mol Cells 31(3):255-9
Huang KY, et al.  (2009) Micropreparative fractionation of the complexome by blue native continuous elution electrophoresis. Proteomics 9(9):2494-502
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.  (2009) Abnormal proteins can form aggresome in yeast: aggresome-targeting signals and components of the machinery. FASEB J 23(2):451-63
Huthmacher C, et al.  (2008) A computational analysis of protein interactions in metabolic networks reveals novel enzyme pairs potentially involved in metabolic channeling. J Theor Biol 252(3):456-64
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
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
Roberts TM, et al.  (2006) Slx4 regulates DNA damage checkpoint-dependent phosphorylation of the BRCT domain protein Rtt107/Esc4. Mol Biol Cell 17(1):539-48
Serva S and Nagy PD  (2006) Proteomics analysis of the tombusvirus replicase: Hsp70 molecular chaperone is associated with the replicase and enhances viral RNA replication. J Virol 80(5):2162-9
Waingeh VF, et al.  (2006) Glycolytic enzyme interactions with yeast and skeletal muscle F-actin. Biophys J 90(4):1371-84
Liu W, et al.  (2002) Interaction of the GTS1 gene product with glyceraldehyde- 3-phosphate dehydrogenase 1 required for the maintenance of the metabolic oscillations of the yeast Saccharomyces cerevisiae. Eur J Biochem 269(14):3560-9
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
Buu A, et al.  (1995) The glyceraldehyde-3-phosphate dehydrogenase binds in vitro to the SH3 domain of Saccharomyces cerevisiae Cdc25p. C R Acad Sci III 318(6):665-9
Barnes G, et al.  (1992) Yeast proteins associated with microtubules in vitro and in vivo. Mol Biol Cell 3(1):29-47
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
McAlister L and Holland MJ  (1985) Differential expression of the three yeast glyceraldehyde-3-phosphate dehydrogenase genes. J Biol Chem 260(28):15019-27
Ashmarina LI, et al.  (1981) Immobilized D-glyceraldehyde-3-phosphate dehydrogenase can exist as a trimer. FEBS Lett 128(1):22-6
Nagradova NK, et al.  (1980) Glyceraldehyde-3-phosphate dehydrogenase: the role of subunit interactions in enzyme functioning. Adv Enzyme Regul 19:171-204