| Molecular chaperones: heat-shock proteins, foldases, and matchmakers. | |
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MedLine Citation:
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PMID: 8035099 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The term molecular chaperone includes a large family of unrelated proteins that comprise both stress-inducible and constitutive molecules. In recent years, molecular chaperones or heat-shock proteins (Hsps) have emerged as fundamentally important topics in cell biology. Living organisms respond to stressful conditions, such as heat shock, by rapidly producing a relatively small class of specific proteins that function to stabilize cellular components against stress. Hsps or molecular chaperones function by preventing misfolding of newly synthesized proteins, escorting proteins targeted for other cellular compartments, and modulating or regulating proteins involved in cell growth and differentiation. Clearly these proteins are of enormous importance to cellular function but of even more importance in helping to fight disease. From heart tissue protection after coronary thrombosis to the regulation of tumor suppressor activity to the use of these molecules as new diagnostic and therapeutic agents, molecular chaperones offer scientists many potential rewards. This review provides an insider's peek at molecular chaperones--a most indispensable set of molecules for cell growth, survival, and regulation. |
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Authors:
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R M Wynn; J R Davie; R P Cox; D T Chuang |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.; Review |
Journal Detail:
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Title: The Journal of laboratory and clinical medicine Volume: 124 ISSN: 0022-2143 ISO Abbreviation: J. Lab. Clin. Med. Publication Date: 1994 Jul |
Date Detail:
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Created Date: 1994-08-16 Completed Date: 1994-08-16 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 0375375 Medline TA: J Lab Clin Med Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 31-6 Citation Subset: AIM; IM |
Affiliation:
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Department of Bioochemistry, University of Texas Southwestern Medical Center, Dallas 75235-9038. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Heat-Shock Proteins* / chemistry, metabolism Humans Molecular Weight Protein Folding* Protein Processing, Post-Translational* Research |
| Grant Support | |
ID/Acronym/Agency:
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5-P32 GM-08014/GM/NIGMS NIH HHS; DK-37373/DK/NIDDK NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Heat-Shock Proteins |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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