Structural similarity of wild-type and ALS-mutant superoxide dismutase-1 fibrils using limited proteolysis and atomic force microscopy

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

Volumn 110, Issue 27, 2013, Pages 10934-10939

  Chan, Pik K ^a   Chattopadhyay, Madhuri ^a   Sharma, Shivani ^a   Souda, Puneet ^a   Gralla, Edith Butler ^a   Borchelt, David R ^b   Whitelegge, Julian P ^a   Valentine, Joan Selverstone ^a,c  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF FLORIDA COLLEGE OF MEDICINE   (United States)

^c Ewha Womans University   (South Korea)

Author keywords

Aggregation; Mass spectrometry; Neurodegeneration; Protein misfolding

Indexed keywords

AMYLOID; CHYMOTRYPSIN; COPPER ZINC SUPEROXIDE DISMUTASE; PRONASE; PROTEINASE; TRYPSIN;

ACETYLATION; AMINO TERMINAL SEQUENCE; AMYOTROPHIC LATERAL SCLEROSIS; ARTICLE; ATOMIC FORCE MICROSCOPY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN DEGRADATION;

AGGREGATION; MASS SPECTROMETRY; NEURODEGENERATION; PROTEIN MISFOLDING;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMYLOID; AMYOTROPHIC LATERAL SCLEROSIS; HUMANS; MICROSCOPY, ATOMIC FORCE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTANT PROTEINS; PROTEOLYSIS; SUPEROXIDE DISMUTASE;

EID: 84879734853     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1309613110     Document Type: Article

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