Abstract
Heat shock protein (Hsp)90 is a chaperone with essential roles in maintaining transformation and in elevating the survival and growth potential of cancer cells. The recognition of Hsp90 as an important target in cancer therapy has prompted the identification, development and clinical translation of a large array of Hsp90 inhibitors. This review discusses the modalities that may interfere with this chaperone's function and describes the status of existing and emerging Hsp90 inhibitor classes.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Adenosine Triphosphate / antagonists & inhibitors
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Adenosine Triphosphate / metabolism
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Animals
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Antibodies, Monoclonal / therapeutic use
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Antineoplastic Agents / pharmacology
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Antineoplastic Agents / therapeutic use*
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Benzoquinones
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Binding, Competitive
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HSP90 Heat-Shock Proteins / antagonists & inhibitors*
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HSP90 Heat-Shock Proteins / immunology
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HSP90 Heat-Shock Proteins / metabolism
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Humans
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Lactams, Macrocyclic / pharmacology
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Lactams, Macrocyclic / therapeutic use
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Molecular Structure
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Neoplasms / drug therapy*
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Neoplasms / metabolism
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Protein Conformation
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Protein-Tyrosine Kinases / antagonists & inhibitors
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Pyrimidines / therapeutic use
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Quinones / therapeutic use
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Triazoles / therapeutic use
Substances
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Antibodies, Monoclonal
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Antineoplastic Agents
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Benzoquinones
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HSP90 Heat-Shock Proteins
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Lactams, Macrocyclic
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Pyrazolotriazolopyrimidine
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Pyrimidines
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Quinones
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Triazoles
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17-(dimethylaminoethylamino)-17-demethoxygeldanamycin
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Adenosine Triphosphate
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Protein-Tyrosine Kinases