The charged linker region is an important regulator of Hsp90 function

Journal of Biological Chemistry

Volumn 284, Issue 34, 2009, Pages 22559-22567

  Hainzl, Otmar ^a,b   Lapina, Maria Claribel ^a   Buchner, Johannes ^a   Richter, Klaus ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^b Sandoz Biopharmaceuticals   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ATP BINDING; ATP-ASE ACTIVITY; CONFORMATIONAL FLEXIBILITY; DELETION VARIANTS; DIMERIZATION DOMAIN; EUKARYOTIC ORGANISMS; IN-VITRO; IN-VIVO; LINKER REGION; LINKER SEQUENCE; MILD TEMPERATURES; MOLECULAR CHAPERONES; N-TERMINAL DOMAINS; N-TERMINALS; NON-VIABLE; TARGET PROTEINS;

PROTEINS;

ADENOSINE TRIPHOSPHATASE; CHAPERONE; HEAT SHOCK PROTEIN 90; PROTEIN P23;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DIMERIZATION; ENZYME ACTIVITY; IN VIVO STUDY; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; TEMPERATURE SENSITIVITY; YEAST;

ADENOSINE TRIPHOSPHATASES; AMINO ACID SEQUENCE; CIRCULAR DICHROISM; FLUORESCENCE RESONANCE ENERGY TRANSFER; HSP90 HEAT-SHOCK PROTEINS; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STABILITY; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE DELETION; STRUCTURE-ACTIVITY RELATIONSHIP; ULTRACENTRIFUGATION;

EUKARYOTA;

EID: 69249130057     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.031658     Document Type: Article

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