Small N-terminal mutant huntingtin fragments, but not wild type, are mainly present in monomeric form: Implications for pathogenesis

Experimental Neurology

Volumn 199, Issue 2, 2006, Pages 257-264

  Cong, Shu Yan ^a,b   Pepers, Barry A ^a   Roos, Raymund A C ^a   van Ommen, Gert Jan B ^a,c   Dorsman, Josephine C ^a,c,d  

^a LEIDEN UNIVERSITY MEDICAL CENTER   (Netherlands)

^b CHINA MEDICAL UNIVERSITY   (China)

^c LEIDEN UNIVERSITY   (Netherlands)

^d VU UNIVERSITY MEDICAL CENTER   (Netherlands)

Author keywords

Huntington's disease; Molecular pathogenesis; N terminal fragments of huntingtin; Native property

Indexed keywords

CASPASE; HUNTINGTIN; MONOMER; MUTANT PROTEIN; POLYGLUTAMINE;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; COMPLEX FORMATION; HUNTINGTON CHOREA; MOLECULAR WEIGHT; MUTANT; NONHUMAN; PATHOGENESIS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEGRADATION; PROTEIN INTERACTION; RAT; WILD TYPE;

ANIMALS; BLOTTING, WESTERN; CHROMATOGRAPHY, GEL; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GENE EXPRESSION; GREEN FLUORESCENT PROTEINS; HUMANS; HUNTINGTON DISEASE; MOLECULAR WEIGHT; MUTAGENESIS; NERVE TISSUE PROTEINS; NUCLEAR PROTEINS; PC12 CELLS; PEPTIDE FRAGMENTS; PEPTIDES; RATS; TIME FACTORS; TRANSFECTION;

EID: 33745256182     PISSN: 00144886     EISSN: 10902430     Source Type: Journal    
DOI: 10.1016/j.expneurol.2005.11.008     Document Type: Article

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