E3 ubiquitin ligase Cullin-5 modulates multiple molecular and cellular responses to heat shock protein 90 inhibition in human cancer cells

TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin-RING ligase complexes

(2013) Ian R Kelsall et al.   EMBO JOURNAL

Ubiquitin ligases and beyond

(2012) Ivan Dikic et al.   BMC BIOLOGY

Quantitative Analysis of Hsp90-Client Interactions Reveals Principles of Substrate Recognition

(2012) Mikko Taipale et al.   CELL

Hsp90 Molecular Chaperone Inhibitors: Are We There Yet?

(2012) L. Neckers et al.   CLINICAL CANCER RESEARCH

Advances in the clinical development of heat shock protein 90 (Hsp90) inhibitors in cancers

(2011) Komal Jhaveri et al.   BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH

Structural assembly of cullin-RING ubiquitin ligase complexes

(2010) Erik S Zimmerman et al.   CURRENT OPINION IN STRUCTURAL BIOLOGY

BIIB021, an orally available, fully synthetic small-molecule inhibitor of the heat shock protein Hsp90

(2009) K. Lundgren et al.   MOLECULAR CANCER THERAPEUTICS

Regulation of Hsp90 client proteins by a Cullin5-RING E3 ubiquitin ligase

(2009) E. S. Ehrlich et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Silencing of HSP90 Cochaperone AHA1 Expression Decreases Client Protein Activation and Increases Cellular Sensitivity to the HSP90 Inhibitor 17-Allylamino-17-Demethoxygeldanamycin

(2008) J. L. Holmes et al.   CANCER RESEARCH

NVP-AUY922: A Novel Heat Shock Protein 90 Inhibitor Active against Xenograft Tumor Growth, Angiogenesis, and Metastasis

(2008) S. A. Eccles et al.   CANCER RESEARCH

Silencing the cochaperone CDC37 destabilizes kinase clients and sensitizes cancer cells to HSP90 inhibitors

(2008) J R Smith et al.   ONCOGENE

4,5-Diarylisoxazole Hsp90 Chaperone Inhibitors: Potential Therapeutic Agents for the Treatment of Cancer

(2007) Paul A. Brough et al.   JOURNAL OF MEDICINAL CHEMISTRY