| The general concept of molecular chaperones. | |
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MedLine Citation:
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PMID: 8098529 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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This introductory article proposes a conceptual framework in which to consider the information that is emerging about the proteins called molecular chaperones, and suggests some definitions that may be useful in this new field of biochemistry. Molecular chaperones are currently defined in functional terms as a class of unrelated families of protein that assist the correct non-covalent assembly of other polypeptide-containing structures in vivo, but which are not components of these assembled structures when they are performing their normal biological functions. The term assembly in this definition embraces not only the folding of newly synthesized polypeptides and any association into oligomers that may occur, but also includes any changes in the degree of either folding or association that may take place when proteins carry out their functions, are transported across membranes, or are repaired or destroyed after stresses such as heat shock. Known molecular chaperones do not convey steric information essential for correct assembly, but appear to act by binding to interactive protein surfaces that are transiently exposed during various cellular processes; this binding inhibits incorrect interactions that may otherwise produce non-functional structures. Thus the concept of molecular chaperones does not contradict the principle of protein self-assembly, but qualifies it by suggesting that in vivo self-assembly requires assistance by other protein molecules. |
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Authors:
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R J Ellis |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Review |
Journal Detail:
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Title: Philosophical transactions of the Royal Society of London. Series B, Biological sciences Volume: 339 ISSN: 0962-8436 ISO Abbreviation: Philos. Trans. R. Soc. Lond., B, Biol. Sci. Publication Date: 1993 Mar |
Date Detail:
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Created Date: 1993-06-11 Completed Date: 1993-06-11 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 7503623 Medline TA: Philos Trans R Soc Lond B Biol Sci Country: ENGLAND |
Other Details:
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Languages: eng Pagination: 257-61 Citation Subset: IM |
Affiliation:
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Department of Biological Sciences, University of Warwick, Coventry, U.K. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Chaperonins Heat-Shock Proteins / metabolism Kinetics Protein Biosynthesis Protein Folding Proteins / metabolism* |
| Chemical | |
Reg. No./Substance:
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0/Heat-Shock Proteins; 0/Proteins; EC 3.6.1.-/Chaperonins |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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