The molecular mechanism of Hsp100 chaperone inhibition by the prion curing agent guanidinium chloride

Journal of Biological Chemistry

Volumn 288, Issue 10, 2013, Pages 7065-7076

  Zeymer, Cathleen ^a   Werbeck, Nicolas D ^a   Schlichting, Ilme ^a   Reinstein, Jochen ^a  

^a MAX PLANCK INSTITUTE FOR MEDICAL RESEARCH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC CYCLES; CURING AGENTS; GUANIDINIUM CHLORIDES; MOLECULAR MECHANISM; N-TERMINALS; NUCLEOTIDE BINDING; NUCLEOTIDE-BINDING DOMAIN;

BINDING ENERGY; CURING; NUCLEOTIDES;

CHLORINE COMPOUNDS;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; GLUTAMIC ACID; GUANIDINE; HEAT SHOCK PROTEIN 100; HEAT SHOCK PROTEIN 104; PROTEIN CLPB;

ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; INHIBITION KINETICS; MOLECULAR DYNAMICS; NUCLEOTIDE BINDING SITE; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN HYDROLYSIS; PROTEIN PROTEIN INTERACTION; PROTEIN UNFOLDING;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEINS; BIOCATALYSIS; CRYSTALLOGRAPHY, X-RAY; GUANIDINE; HEAT-SHOCK PROTEINS; HYDROLYSIS; KINETICS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MUTATION; NUCLEOTIDES; PRIONS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; THERMUS THERMOPHILUS;

EID: 84874818722     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.432583     Document Type: Article

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