The C-terminal half of heat shock protein 90 represents a second site for pharmacologic intervention in chaperone function

Current Cancer Drug Targets

Volumn 3, Issue 5, 2003, Pages 343-347

  Marcu, Monica G ^a   Neckers, Leonard M ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CHAPERONE; CHIMERIC PROTEIN; CISPLATIN; HEAT SHOCK PROTEIN 90; MOLYBDIC ACID; MUTANT PROTEIN; NOVOBIOCIN; NUCLEOTIDE BINDING PROTEIN; PROTEIN KINASE; STEROID RECEPTOR; TRANSCRIPTION FACTOR;

CANCER GROWTH; CANCER SURVIVAL; CARBOXY TERMINAL SEQUENCE; CELL PROTECTION; DRUG PROTEIN BINDING; DRUG TARGETING; HUMAN; MOLECULAR INTERACTION; MUTATION; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN STABILITY; PROTEIN STRUCTURE; REVIEW;

ADENOSINE TRIPHOSPHATASES; ANIMALS; ANTINEOPLASTIC AGENTS; ATP-BINDING CASSETTE TRANSPORTERS; HSP90 HEAT-SHOCK PROTEINS; HUMANS; MOLECULAR CHAPERONES;

EID: 0141708696     PISSN: 15680096     EISSN: None     Source Type: Journal    
DOI: 10.2174/1568009033481804     Document Type: Review

References (48)

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