GAPDH Is Conformationally and Functionally Altered in Association with Oxidative Stress in Mouse Models of Amyotrophic Lateral Sclerosis

Journal of Molecular Biology

Volumn 382, Issue 5, 2008, Pages 1195-1210

  Pierce, Anson ^a   Mirzaei, Hamid ^b   Muller, Florian ^a   De Waal, Eric ^c   Taylor, Alexander B ^c   Leonard, Shanique ^c   Van Remmen, Holly ^a,c,d   Regnier, Fred ^b   Richardson, Arlan ^a,c,d   Chaudhuri, Asish ^c,d  

^a Mays Cancer Center at UT Health San Antonio   (United States)

^b PURDUE UNIVERSITY   (United States)

^c UNIVERSITY OF TEXAS HEALTH SCIENCE CENTER AT SAN ANTONIO   (United States)

^d SOUTH TEXAS VETERANS HEALTH CARE SYSTEM   (United States)

Author keywords

amyotrophic lateral sclerosis; BisANS; GAPDH; protein oxidation; protein unfolding

Indexed keywords

CREATINE KINASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; LYSINE; SERINE; THREONINE; TYROSINE;

AMYOTROPHIC LATERAL SCLEROSIS; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DISEASE MODEL; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME METABOLISM; ENZYME STRUCTURE; EXPERIMENTAL MOUSE; FEMALE; LIQUID CHROMATOGRAPHY; MALE; MOUSE; NONHUMAN; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN FUNCTION; SKELETAL MUSCLE; TANDEM MASS SPECTROMETRY;

MUS;

EID: 51349108171     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.07.088     Document Type: Article

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