The Hsp90 complex—a super-chaperone machine as a novel drug target
- 1 September 1998
- journal article
- review article
- Published by Elsevier in Biochemical Pharmacology
- Vol. 56 (6), 675-682
- https://doi.org/10.1016/s0006-2952(98)00120-8
Abstract
No abstract availableKeywords
This publication has 64 references indexed in Scilit:
- Stable transformation of an Arabidopsis cell suspension culture with firefly luciferase providing a cellular system for analysis of chaperone activity in vivo.Plant Cell, 1997
- An atypical topoisomerase II from archaea with implications for meiotic recombinationNature, 1997
- Interaction of Endoplasmic Reticulum Chaperone GRP94 with Peptide Substrates Is Adenine Nucleotide-independentPublished by Elsevier ,1997
- A Cyclophilin Function in Hsp90-Dependent Signal TransductionScience, 1996
- The Tetratricopeptide Repeat Domain of Protein Phosphatase 5 Mediates Binding to Glucocorticoid Receptor Heterocomplexes and Acts as a Dominant Negative MutantJournal of Biological Chemistry, 1996
- Role of the Protein Chaperone YDJ1 in Establishing Hsp90-Mediated Signal Transduction PathwaysScience, 1995
- Transient Interaction of Hsp90 with Early Unfolding Intermediates of Citrate SynthaseJournal of Biological Chemistry, 1995
- Hsp 90α and Hsp 90β Genes Are Present in the Zebrafish and Are Differentially Regulated in Developing EmbryosBiochemical and Biophysical Research Communications, 1994
- Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperonesTrends in Biochemical Sciences, 1994
- Crystal structure of an N-terminal fragment of the DNA gyrase B proteinNature, 1991