A Domain in the N-terminal Part of Hsp26 is Essential for Chaperone Function and Oligomerization
- 27 August 2004
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 343 (2), 445-455
- https://doi.org/10.1016/j.jmb.2004.08.048
Abstract
No abstract availableKeywords
This publication has 48 references indexed in Scilit:
- Analysis of the Interaction of Small Heat Shock Proteins with Unfolding ProteinsJournal of Biological Chemistry, 2003
- Mechanism of Chaperone Function in Small Heat-shock ProteinsJournal of Biological Chemistry, 2003
- Monodisperse Hsp16.3 Nonamer Exhibits Dynamic Dissociation and Reassociation, with the Nonamer Dissociation Prerequisite for Chaperone-like ActivityJournal of Molecular Biology, 2002
- Chaperone Activity and Homo- and Hetero-oligomer Formation of Bacterial Small Heat Shock ProteinsJournal of Biological Chemistry, 2000
- The Dynamics of Hsp25 Quaternary StructureJournal of Biological Chemistry, 1999
- The small heat-shock protein, αb-crystallin, has a variable quaternary structureJournal of Molecular Biology, 1998
- Cloning, Expression, and Chaperone-like Activity of Human αA-CrystallinPublished by Elsevier BV ,1996
- A New Generation of the IMAGIC Image Processing SystemJournal of Structural Biology, 1996
- Junior chaperonesCurrent Biology, 1993
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982