Literature DB >> 8856967

Roles for hsp70 in protein translocation across membranes of organelles.

D M Cyr1, W Neupert.   

Abstract

The family of hsp70 molecular chaperones plays an essential and diverse role in cellular physiology. Hsp70 proteins appear to elicit their effects by interaction with polypeptides that present domains which exhibit non-native conformations at distinct stages during their life in the cell. Work pertaining to the functions of hsp70 proteins in driving protein translocation across membranes is reviewed herein. Hsp70 proteins function to deliver polypeptides to protein translocation channels, unfold polypeptides during transit across membranes and drive the translocation process. All these reactions are facilitated in an ATP-dependent reaction cycle with the assistance of different partner proteins that modulate the function of hsp70.

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Year:  1996        PMID: 8856967     DOI: 10.1007/978-3-0348-9088-5_3

Source DB:  PubMed          Journal:  EXS        ISSN: 1023-294X


  5 in total

Review 1.  Mechanisms for regulation of Hsp70 function by Hsp40.

Authors:  Chun-Yang Fan; Soojin Lee; Douglas M Cyr
Journal:  Cell Stress Chaperones       Date:  2003       Impact factor: 3.667

Review 2.  Approaches for probing the sequence space of substrates recognized by molecular chaperones.

Authors:  Pradeep Kota; Nikolay V Dokholyan
Journal:  Methods       Date:  2010-12-30       Impact factor: 3.608

3.  The unique chaperone operon of Thermotoga maritima: cloning and initial characterization of a functional Hsp70 and small heat shock protein.

Authors:  E T Michelini; G C Flynn
Journal:  J Bacteriol       Date:  1999-07       Impact factor: 3.490

Review 4.  Insights Into the Role of Mortalin in Alzheimer's Disease, Parkinson's Disease, and HIV-1-Associated Neurocognitive Disorders.

Authors:  Pankaj Seth
Journal:  Front Cell Dev Biol       Date:  2022-07-04

5.  Hsp70 and its molecular role in nervous system diseases.

Authors:  Giuseppina Turturici; Gabriella Sconzo; Fabiana Geraci
Journal:  Biochem Res Int       Date:  2011-02-24
  5 in total

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