A multistage pathway for human prion protein aggregation in vitro: From multimeric seeds to β-oligomers and nonfibrillar structures

Journal of the American Chemical Society

Volumn 133, Issue 22, 2011, Pages 8586-8593

  Cho, Kang R ^a,b   Huang, Yu ^b   Yu, Shuiliang ^c   Yin, Shaoman ^c   Plomp, Marco ^a   Qiu, S Roger ^a   Lakshminarayanan, Rajamani ^d,f   Moradian Oldak, Janet ^d   Sy, Man Sun ^c   De Yoreo, James J ^a,e  

^a LAWRENCE LIVERMORE NATIONAL LABORATORY   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c CASE WESTERN RESERVE UNIVERSITY   (United States)

^d UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

^e LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

^f SINGAPORE EYE RESEARCH INSTITUTE   (Singapore)

Author keywords

[No Author keywords available]

Indexed keywords

AFM; AGGREGATION MECHANISM; CREUTZFELDT-JAKOB DISEASE; DIRECT INTERACTIONS; FORMATION PATHWAYS; HUMAN PRION PROTEIN; IN-VITRO; INSERTION MUTANTS; MULTIMERIC; NEUROLOGICAL DISEASE; PRION DISEASE; PROTEIN AGGREGATION; WILD TYPES;

MONOMERS; NEURODEGENERATIVE DISEASES; PROTEINS; SEED;

OLIGOMERS;

MONOMER; OCTAPEPTIDE; OLIGOMER; PRION PROTEIN; RECOMBINANT PROTEIN;

ARTICLE; ATOMIC FORCE MICROSCOPY; BETA SHEET; CREUTZFELDT JAKOB DISEASE; DENATURATION; IN VITRO STUDY; MOLECULAR MECHANICS; OLIGOMERIZATION; PARTICLE SIZE; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN INTERACTION; SOLUBILITY; THERMODYNAMICS; WILD TYPE;

HUMANS; MICROSCOPY, ATOMIC FORCE; MODELS, BIOLOGICAL; MUTATION; OLIGOPEPTIDES; PARTICLE SIZE; PRIONS;

EID: 79957999075     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja1117446     Document Type: Article

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