Identification of a misfolded region in superoxide dismutase 1 that is exposed in amyotrophic lateral sclerosis

Journal of Biological Chemistry

Volumn 289, Issue 41, 2014, Pages 28527-28538

  Rotunno, Melissa S ^a   Auclair, Jared R ^b   Maniatis, Stephanie ^a   Shaffer, Scott A ^a   Agar, Jeffrey ^b   Bosco, Daryl A ^a  

^a UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

^b NORTHEASTERN UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CONFORMATIONS; CROSSLINKING; MASS SPECTROMETRY; NEURODEGENERATIVE DISEASES; OXYGEN; ZINC;

AMYOTROPHIC LATERAL SCLEROSIS; CHEMICAL CROSS-LINKING; CU ,ZN SUPEROXIDE DISMUTASE; PATHOGENIC CONFORMATION; POST-TRANSLATIONAL MODIFICATIONS; SITE DIRECTED MUTAGENESIS; SUPER OXIDE DISMUTASE; THERAPEUTIC STRATEGY;

EPITOPES;

COPPER ZINC SUPEROXIDE DISMUTASE; EPITOPE; ISOENZYME; MONOCLONAL ANTIBODY; PROTEIN BINDING; RECOMBINANT PROTEIN; SUPEROXIDE DISMUTASE;

AMYOTROPHIC LATERAL SCLEROSIS; ANIMAL CELL; ARTICLE; CELL ACTIVATION; CONTROLLED STUDY; CROSS LINKING; EMBRYO; MASS SPECTROMETRY; METALLATION; MICROGLIA; MOUSE; NONHUMAN; OXIDATION; PROTEIN CONFORMATION; PROTEIN LOCALIZATION; PROTEIN MISFOLDING; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; ANIMAL; BIOSYNTHESIS; CHEMISTRY; CYTOLOGY; DRUG EFFECTS; ESCHERICHIA COLI; GENE EXPRESSION; GENETICS; HUMAN; HYBRIDOMA; IMMUNOLOGY; ISOLATION AND PURIFICATION; METABOLISM; MUTATION; OXIDATION REDUCTION REACTION; PATHOLOGY; PRIMARY CELL CULTURE; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SPINAL CORD; TOXICITY;

AMYOTROPHIC LATERAL SCLEROSIS; ANIMALS; ANTIBODIES, MONOCLONAL; EPITOPES; ESCHERICHIA COLI; GENE EXPRESSION; HUMANS; HYBRIDOMAS; ISOENZYMES; MICE; MICROGLIA; MUTAGENESIS, SITE-DIRECTED; MUTATION; OXIDATION-REDUCTION; PRIMARY CELL CULTURE; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SPINAL CORD; SUPEROXIDE DISMUTASE;

EID: 84907606030     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.581801     Document Type: Article

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