A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors.

Kamal, Adeela; Thao, Lia; Sensintaffar, John; Zhang, Lin; Boehm, Marcus F; Fritz, Lawrence C; Burrows, Francis J

Kamal, Adeela; Thao, Lia; Sensintaffar, John; Zhang, Lin; Boehm, Marcus F; Fritz, Lawrence C; Burrows, Francis J.

Affiliation

Kamal A; Conforma Therapeutics Corporation, 9393 Towne Centre Drive, Suite 240, San Diego, California 92121, USA.

Nature ; 425(6956): 407-10, 2003 Sep 25.

Article in En | MEDLINE | ID: mdl-14508491

Subject(s)

Antineoplastic Agents/metabolism; Antineoplastic Agents/pharmacology; HSP90 Heat-Shock Proteins/antagonists & inhibitors; HSP90 Heat-Shock Proteins/chemistry; Neoplasms/metabolism; Rifabutin/analogs & derivatives; Rifabutin/metabolism; Rifabutin/pharmacology; Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/metabolism; Benzoquinones; Cell Line; Cysteine Endopeptidases/metabolism; HSP90 Heat-Shock Proteins/metabolism; Humans; Inhibitory Concentration 50; Lactams, Macrocyclic; Multienzyme Complexes/metabolism; Neoplasms/drug therapy; Precipitin Tests; Proteasome Endopeptidase Complex; Protein Binding/drug effects; Protein Conformation; Substrate Specificity; Tumor Cells, Cultured

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Collection: 01-internacional Database: MEDLINE Main subject: Rifabutin / HSP90 Heat-Shock Proteins / Neoplasms / Antineoplastic Agents Limits: Humans Language: En Journal: Nature Year: 2003 Document type: Article Affiliation country: United States

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