Structural environment dictates the biological significance of heme-responsive motifs and the role of Hsp90 in the activation of the heme activator protein Hap1

Molecular and Cellular Biology

Volumn 23, Issue 16, 2003, Pages 5857-5866

  Lee, Hee Chul ^a   Hon, Thomas ^a   Lan, Changgui ^a   Zhang, Li ^a  

^a NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 90; HEME; HEME ACTIVATOR PROTEIN 1; PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; MOLECULAR BIOLOGY; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; REGULATORY MECHANISM; SIGNAL TRANSDUCTION;

AMINO ACID MOTIFS; BETA-GALACTOSIDASE; BLOTTING, WESTERN; CARBON-OXYGEN LYASES; DIMERIZATION; DNA; DNA-(APURINIC OR APYRIMIDINIC SITE) LYASE; DOSE-RESPONSE RELATIONSHIP, DRUG; HEME; HSP90 HEAT-SHOCK PROTEINS; MODELS, BIOLOGICAL; MODELS, GENETIC; MUTATION; PLASMIDS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SIGNAL TRANSDUCTION;

EID: 0041630927     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.23.16.5857-5866.2003     Document Type: Article

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