Crystal Structure and Activity of Human p23, a Heat Shock Protein 90 Co-chaperone
Open Access
- 1 July 2000
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 275 (30) , 23045-23052
- https://doi.org/10.1074/jbc.m003410200
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- An unstructured C-terminal region of the hsp90 co-chaperone p23 is important for its chaperone function 1 1Edited by R. HuberJournal of Molecular Biology, 1999
- Steroid Receptor Interactions with Heat Shock Protein and Immunophilin ChaperonesEndocrine Reviews, 1997
- Molecular Chaperone Machines: Chaperone Activities of the Cyclophilin Cyp-40 and the Steroid Aporeceptor-Associated Protein p23Science, 1996
- Mammalian DNA cytosine‐5 methyltransferase interacts with p23 proteinFEBS Letters, 1996
- Protein Structure Comparison by Alignment of Distance MatricesJournal of Molecular Biology, 1993
- PROCHECK: a program to check the stereochemical quality of protein structuresJournal of Applied Crystallography, 1993
- Improved methods for building protein models in electron density maps and the location of errors in these modelsActa Crystallographica Section A Foundations of Crystallography, 1991
- Crystal structure of chaperone protein PapD reveals an immunoglobulin foldNature, 1989
- Ribbon models of macromoleculesJournal of Molecular Graphics, 1987
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresBiopolymers, 1983