Functional analysis of the hsp90-associated human peptidyl prolyl Cis/Trans isomerases FKBP51, FKBP52 and cyp40 1 1Edited by R. Huber
- 1 May 2001
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 308 (4) , 795-806
- https://doi.org/10.1006/jmbi.2001.4595
Abstract
No abstract availableKeywords
This publication has 67 references indexed in Scilit:
- Structure of TPR Domain–Peptide ComplexesCell, 2000
- Hsp90 & Co. – a holding for foldingTrends in Biochemical Sciences, 1999
- Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalystsCellular and Molecular Life Sciences, 1999
- Cyclophilin-40: evidence for a dimeric complex with hsp90Biochemical Journal, 1995
- The ability of the immunophilin FKBP59-HBI to interact with the 90-kDa heat shock protein is encoded by its tetratricopeptide repeat domain.Proceedings of the National Academy of Sciences, 1994
- Peptidyl‐Prolyl cis/trans Isomerases and Their EffectorsAngewandte Chemie International Edition in English, 1994
- Prolyl Isomerase: Enzymatic Catalysis of Slow Protein-Folding ReactionsAnnual Review of Biophysics, 1993
- Prolyl Isomerases: Role in Protein FoldingAdvances in Protein Chemistry, 1993
- Specific Intermediates in the Folding Reactions of Small Proteins and the Mechanism of Protein FoldingAnnual Review of Biochemistry, 1982
- Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residuesBiochemistry, 1975