Molecular Chaperones. Resurrection or Destruction?

Overview

Journal Curr Biol

Publisher Cell Press

Specialty Biology

Date 1995 May 1

PMID 7583086

Citations 4

Authors

A L Horwich

Affiliations

Soon will be listed here.

Abstract

Recent studies implicate Hsp104/Clp family chaperones in both protein disaggregation and protein degradation. How do these homologous ring-shaped complexes function in such different ways?

Citing Articles

Heat shock proteins in association with heat tolerance in grasses.

Xu Y, Zhan C, Huang B Int J Proteomics. 2011; 2011:529648.

PMID: 22084689 PMC: 3200123. DOI: 10.1155/2011/529648.

Regulated protein degradation in mitochondria.

Langer T, Neupert W Experientia. 1996; 52(12):1069-76.

PMID: 8988248 DOI: 10.1007/BF01952104.

Molecular chaperones and protein folding in plants.

Boston R, Viitanen P, Vierling E Plant Mol Biol. 1996; 32(1-2):191-222.

PMID: 8980480 DOI: 10.1007/BF00039383.

The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria.

Schmitt M, Neupert W, Langer T J Cell Biol. 1996; 134(6):1375-86.

PMID: 8830768 PMC: 2120990. DOI: 10.1083/jcb.134.6.1375.