Home LiteratureArticle Details
PMID: 1357791 Published · ppublish English Journal Article Review

The emergence of the chaperone machines.

Trends in biochemical sciences ·Vol. 17 ·No. 8 ·1992-08-00 ·Pages 295-9

Georgopoulos C

Abstract

To ensure proper polypeptide folding, oligomerization and transport, elaborate molecular 'chaperone machines' have evolved. These machines are usually composed of a major chaperone protein that binds promiscuously to nascent, unfolded, misfolded or aggregated polypeptides and a set of chaperone 'cohorts', whose function is to enhance efficiency and ensure recycling. These chaperone machines can function by themselves or synergistically to carry out their various tasks.

MeSH Terms
Bacterial Proteins/metabolism Chaperonins Heat-Shock Proteins/metabolism Homeostasis/genetics Protein Folding Protein Processing, Post-Translational Proteins
Chemicals
Bacterial Proteins Heat-Shock Proteins Proteins SecB protein, Bacteria Chaperonins
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Georgopoulos C
Département de Biochimie Médicale, Centre Médical Universitaire, Geneve, Switzerland.
Article Info
Journal
Trends in biochemical sciences
Abbr.
Trends Biochem Sci
ISSN
0968-0004
Published
1992-08-00
Pages
295-9
Language
English
Region
England
NLM ID
7610674
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com