Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis

Proceedings of the National Academy of Sciences of the United States of America

Volumn 102, Issue 30, 2005, Pages 10516-10521

  Rodriguez, Jorge A ^a   Shaw, Bryan Francis ^a   Durazo, Armando ^a   Sohn, Se Hui ^a   Doucette, Peter A ^a   Nersissian, Aram M ^a   Faull, Kym F ^a   Eggers, Daryl K ^b   Tiwari, Ashutosh ^c   Hayward, Lawrence J ^c   Valentine, Joan Selverstone ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b SAN JOSE STATE UNIVERSITY   (United States)

^c UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

Author keywords

Differential scanning calorimetry; Hydrogen deuterium exchange; Neurodegenerative disease; Protein aggregation; Protein stability

Indexed keywords

APOPROTEIN; COPPER ZINC SUPEROXIDE DISMUTASE; DEUTERIUM; HYDROGEN; MUTANT PROTEIN;

AMYOTROPHIC LATERAL SCLEROSIS; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DIFFERENTIAL SCANNING CALORIMETRY; MASS SPECTROMETRY; MELTING POINT; METAL BINDING; METALLATION; NONHUMAN; PATHOGENESIS; PRIORITY JOURNAL; PROTEIN STABILITY;

AMINO ACID SUBSTITUTION; AMYOTROPHIC LATERAL SCLEROSIS; CALORIMETRY, DIFFERENTIAL SCANNING; DEUTERIUM EXCHANGE MEASUREMENT; HUMANS; MASS SPECTROMETRY; METALS; MUTATION; SUPEROXIDE DISMUTASE; TRANSITION TEMPERATURE;

EID: 23044431627     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0502515102     Document Type: Article

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