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THE EMERGENCE OF THE CHAPERONE MACHINES
Author(s): GEORGOPOULOS C
Source: TRENDS IN BIOCHEMICAL SCIENCES    Volume: 17    Issue: 8    Pages: 295-299    Published: AUG 1992  
Times Cited: 221     References: 32     
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.
Document Type: Article
Language: English
Reprint Address: GEORGOPOULOS, C (reprint author), UNIV GENEVA, HLTH SCI CTR, DEPT BIOCHIM MED, 1 RUE MICHEL SERVET, CH-1211 GENEVA 4, SWITZERLAND
Publisher: ELSEVIER SCI LTD, THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD, OXON, ENGLAND OX5 1GB
Subject Category: Biochemistry & Molecular Biology
IDS Number: JH637
ISSN: 0968-0004
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