Allosteric regulation of the Hsp90 dynamics and stability by client recruiter cochaperones: Protein structure network modeling

PLoS ONE

Volumn 9, Issue 1, 2014, Pages

  Blacklock, Kristin ^a,c   Verkhivker, Gennady M ^a,b  

^a CHAPMAN UNIVERSITY   (United States)

^b San Diego   (United States)

^c RUTGERS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHAPERONE; CHAPERONE REQUIRED FOR MLA12 RESISTANCE; CHAPERONE SUPPRESSOR OF G2 ALLELE OF SKP1; HEAT SHOCK PROTEIN 90; UNCLASSIFIED DRUG; PROTEIN BINDING; SACCHAROMYCES CEREVISIAE PROTEIN; COCHAPERONE; PROTEIN;

ALLOSTERISM; ARTICLE; CHEMICAL MUTAGENESIS; CONFORMATIONAL TRANSITION; ENZYME ACTIVITY; GLOBAL CHANGE; LID MOTIF; MOLECULAR DYNAMICS; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN MOTIF; PROTEIN STABILITY; PROTEIN STRUCTURE; RESIDUE ANALYSIS; SIGNAL TRANSDUCTION; CHEMISTRY; HUMAN; METABOLISM; MOLECULAR DOCKING; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE; CONTROLLED STUDY; DYNAMICS; MOTION; MUTAGENESIS;

ADENOSINE TRIPHOSPHATASES; ALLOSTERIC REGULATION; HSP90 HEAT-SHOCK PROTEINS; HUMANS; MOLECULAR CHAPERONES; MOLECULAR DOCKING SIMULATION; MOLECULAR DYNAMICS SIMULATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STABILITY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 84903215285     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0086547     Document Type: Article

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