Molecular interaction between the chaperone Hsc70 and the N-terminal flank of huntingtin exon 1 modulates aggregation

Journal of Biological Chemistry

Volumn 290, Issue 5, 2015, Pages 2560-2576

  Monsellier, Elodie ^a   Redeker, Virginie ^a   Ruiz Arlandis, Gemma ^a   Bousset, Luc ^a   Melki, Ronald ^a  

^a CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; NEURODEGENERATIVE DISEASES;

AGGREGATION PROCESS; HUNTINGTON DISEASE; HUNTINGTON'S DISEASE; MOLECULAR CHAPERONES; POLYGLUTAMINE (POLYQ); RESIDUE LEVEL; SURFACE INTERFACES; THERAPEUTIC STRATEGY;

PROTEINS;

HEAT SHOCK COGNATE PROTEIN 70; HEAT SHOCK PROTEIN 40; HUNTINGTIN; HUNTINGTIN EXON 1; POLYGLUTAMINE; UNCLASSIFIED DRUG; CHAPERONE; HTT PROTEIN, HUMAN; NERVE PROTEIN; PEPTIDE; PROTEIN BINDING;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; DISEASE ASSOCIATION; HUMAN; HUNTINGTON CHOREA; IN VIVO STUDY; INHIBITION KINETICS; MASS SPECTROMETRY; MOLECULAR INTERACTION; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN CROSS LINKING; PROTEIN FUNCTION; PROTEIN INTERACTION; STRUCTURE ACTIVITY RELATION; EXON; GENETICS; METABOLISM;

EXONS; HSC70 HEAT-SHOCK PROTEINS; HUMANS; MASS SPECTROMETRY; MOLECULAR CHAPERONES; NERVE TISSUE PROTEINS; PEPTIDES; PROTEIN BINDING;

EID: 84921902920     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.603332     Document Type: Article

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