Normal-repeat-length polyglutamine peptides accelerate aggregation nucleation and cytotoxicity of expanded polyglutamine proteins

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

Volumn 103, Issue 39, 2006, Pages 14367-14372

  Slepko, Natalia ^a   Bhattacharyya, Anusri M ^b   Jackson, George R ^c   Steffan, Joan S ^a   Marsh, J Lawrence ^d   Thompson, Leslie Michels ^a   Wetzel, Ronald ^b,e  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF TENNESSEE GRADUATE SCHOOL OF MEDICINE   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

^d UNIVERSITY OF CALIFORNIA   (United States)

^e UNIVERSITY OF PITTSBURGH SCHOOL OF MEDICINE   (United States)

Author keywords

Amyloid; Drosophila; Elongation kinetics; Huntington's disease; In vitro

Indexed keywords

PEPTIDE DERIVATIVE; POLYGLUTAMINE;

ANIMAL CELL; ARTICLE; CELL NUCLEUS; CONTROLLED STUDY; CYTOTOXICITY; DROSOPHILA; EXON; GENE SEQUENCE; HUNTINGTON CHOREA; KINETICS; NERVE DEGENERATION; NEUROTOXICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN EXPRESSION;

ANIMALS; CELL DEATH; DROSOPHILA MELANOGASTER; EYE; HUMANS; KINETICS; MODELS, ANIMAL; NEURODEGENERATIVE DISEASES; PEPTIDES; PROTEIN STRUCTURE, QUATERNARY; PROTEINS; REPETITIVE SEQUENCES, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 33749266887     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0602348103     Document Type: Article

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