DNAJB6 is a peptide-binding chaperone which can suppress amyloid fibrillation of polyglutamine peptides at substoichiometric molar ratios

Cell Stress and Chaperones

Volumn 19, Issue 2, 2014, Pages 227-239

  Månsson, Cecilia ^a   Kakkar, Vaishali ^b   Monsellier, Elodie ^c   Sourigues, Yannick ^c   Härmark, Johan ^d   Kampinga, Harm H ^b   Melki, Ronald ^c   Emanuelsson, Cecilia ^a  

^a LUND UNIVERSITY   (Sweden)

^b UNIVERSITY MEDICAL CENTER GRONINGEN   (Netherlands)

^c CNRS   (France)

^d KAROLINSKA INSTITUTE   (Sweden)

Author keywords

Aggregation; Amyloid; DNAJ; Molecular chaperones; Polyglutamine

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMYLOID; CHAPERONE; DNAJB6 PROTEIN; NONSTOICHIOMETRIC COMPOUND; POLYGLUTAMINE; THIOFLAVINE; UNCLASSIFIED DRUG;

ARTICLE; HUMAN; IN VITRO STUDY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION;

AMINO ACID SEQUENCE; AMYLOID; HSP40 HEAT-SHOCK PROTEINS; HUMANS; LIGHT; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; NERVE TISSUE PROTEINS; PEPTIDES; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SCATTERING, RADIATION; SODIUM DODECYL SULFATE; SOLUBILITY;

EID: 84896094717     PISSN: 13558145     EISSN: 14661268     Source Type: Journal    
DOI: 10.1007/s12192-013-0448-5     Document Type: Article

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