The S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase 2 is reduced by interaction with glutathione peroxidase 3 in saccharomyces cerevisiae

Molecules and Cells

Volumn 31, Issue 3, 2011, Pages 255-259

  Lee, Phil Young ^a,b   Bae, Kwang Hee ^a   Jeong, Dae Gwin ^a   Chi, Seung Wook ^a   Moon, Jeong Hee ^a   Kang, Seongman ^b   Cho, Sayeon ^c   Lee, Sang Chul ^a   Park, Byoung Chul ^a   Park, Sung Goo ^a  

^a Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

^b Korea University   (South Korea)

^c Chung Ang University   (South Korea)

Author keywords

Apoptosis; GAPDH; Glutathione peroxidase 3; Nitosylation; NO stress

Indexed keywords

GLUTATHIONE PEROXIDASE 3; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE 2; NITRIC OXIDE; OXIDOREDUCTASE; UNCLASSIFIED DRUG;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL PROTECTION; CELL VIABILITY; CHEMICAL MODIFICATION; ENZYME ACTIVITY; ENZYME ANALYSIS; FUNGAL STRAIN; FUNGUS CULTURE; GLYCOLYSIS; HOMEOSTASIS; IMMUNOPRECIPITATION; IN VITRO STUDY; IN VIVO STUDY; NONHUMAN; OXIDATIVE STRESS; PROTEIN EXPRESSION; PROTEIN INTERACTION; PROTEOMICS; S NITROSYLATION; SACCHAROMYCES CEREVISIAE;

CATALYTIC DOMAIN; CELL PROLIFERATION; ENZYME ASSAYS; GENE DELETION; GLUTATHIONE PEROXIDASE; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE (PHOSPHORYLATING); NITRIC OXIDE; OXIDATIVE STRESS; PROTEIN BINDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN PROCESSING, POST-TRANSLATIONAL; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

SACCHAROMYCES CEREVISIAE;

EID: 79959976468     PISSN: 10168478     EISSN: 02191032     Source Type: Journal    
DOI: 10.1007/s10059-011-0029-3     Document Type: Article

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