Identification of Conserved Residues Required for the Binding of a Tetratricopeptide Repeat Domain to Heat Shock Protein 90
Open Access
- 1 July 1999
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 274 (29) , 20060-20063
- https://doi.org/10.1074/jbc.274.29.20060
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- The Hsp90 complex—a super-chaperone machine as a novel drug targetBiochemical Pharmacology, 1998
- Protein Phosphatase 5 Is a Major Component of Glucocorticoid Receptor·hsp90 Complexes with Properties of an FK506-binding ImmunophilinJournal of Biological Chemistry, 1997
- Chaperones get in touch: the Hip-Hop connectionTrends in Biochemical Sciences, 1997
- Activation of protein phosphatase 5 by limited proteolysis or the binding of polyunsaturated fatty acids to the TPR domainFEBS Letters, 1997
- Chaperone Function of Hsp90-Associated ProteinsScience, 1996
- Molecular Chaperone Machines: Chaperone Activities of the Cyclophilin Cyp-40 and the Steroid Aporeceptor-Associated Protein p23Science, 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
- THE FUNCTION OF HEAT-SHOCK PROTEINS IN STRESS TOLERANCE: DEGRADATION AND REACTIVATION OF DAMAGED PROTEINSAnnual Review of Genetics, 1993
- Snap helix with knob and hole: Essential repeats in S. pombe nuclear protein nuc2 +Cell, 1990
- A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesisCell, 1990