Structure-Activity Relationships in Purine-Based Inhibitor Binding to HSP90 Isoforms
- 1 June 2004
- journal article
- research article
- Published by Elsevier BV in Cell Chemical Biology
- Vol. 11 (6), 775-785
- https://doi.org/10.1016/j.chembiol.2004.03.033
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- Structural and Functional Analysis of the Middle Segment of Hsp90: Implications for ATP Hydrolysis and Client Protein and Cochaperone InteractionsMolecular Cell, 2003
- Heat shock protein 90 as a molecular target for cancer therapeuticsCancer Cell, 2003
- EVIDENCE THAT THE NOVOBIOCIN-SENSITIVE ATP-BINDING SITE OF THE HEAT SHOCK PROTEIN 90 (HSP90) IS NECESSARY FOR ITS AUTOPHOSPHORYLATIONCell Biology International, 2002
- HSP90 as a new therapeutic target for cancer therapy: the story unfoldsExpert Opinion on Biological Therapy, 2002
- A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cellsCell Chemical Biology, 2001
- The Heat Shock Protein 90 Antagonist Novobiocin Interacts with a Previously Unrecognized ATP-binding Domain in the Carboxyl Terminus of the ChaperoneJournal of Biological Chemistry, 2000
- Structure and in vivo function of Hsp90Current Opinion in Structural Biology, 2000
- GHKL, an emergent ATPase/kinase superfamilyTrends in Biochemical Sciences, 2000
- Crystal Structure of an Hsp90–Geldanamycin Complex: Targeting of a Protein Chaperone by an Antitumor AgentCell, 1997
- An atypical topoisomerase II from archaea with implications for meiotic recombinationNature, 1997