Expanded polyglutamine-containing N-terminal huntingtin fragments are entirely degraded by mammalian proteasomes

Journal of Biological Chemistry

Volumn 288, Issue 38, 2013, Pages 27068-27084

  Juenemann, Katrin ^a   Schipper Krom, Sabine ^a   Wiemhoefer, Anne ^a   Kloss, Alexander ^b   Sanz, Alicia Sanz ^a   Reits, Eric A J ^a  

^a UNIVERSITY OF AMSTERDAM   (Netherlands)

^b CHARITÉ UNIVERSITÄTSMEDIZIN BERLIN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CLEAVAGE PRODUCTS; INCLUSION BODIES; INHIBITORY EFFECT; INTRACELLULAR DEGRADATION; NEURODEGENERATION; NEURONAL CELL; POLYGLUTAMINE (POLYQ); PROTEASOMAL DEGRADATION;

MAMMALS;

PROTEINS;

HUNTINGTIN; POLYGLUTAMINE; PROTEASOME;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; EMBRYO; EXON; IN VITRO STUDY; MOUSE; NERVE CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN TARGETING;

AGGREGATION; AUTOPHAGY; HUNTINGTON DISEASE; POLYGLUTAMINE; PROTEASOME;

ANIMALS; CELL LINE; HUMANS; MICE; MICE, KNOCKOUT; NERVE TISSUE PROTEINS; NUCLEAR PROTEINS; PEPTIDES; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEOLYSIS; REPETITIVE SEQUENCES, AMINO ACID;

EID: 84884567375     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.486076     Document Type: Article

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