| The ubiquitin-proteasome system of Saccharomyces cerevisiae. | |
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MedLine Citation:
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PMID: 23028185 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Protein modifications provide cells with exquisite temporal and spatial control of protein function. Ubiquitin is among the most important modifiers, serving both to target hundreds of proteins for rapid degradation by the proteasome, and as a dynamic signaling agent that regulates the function of covalently bound proteins. The diverse effects of ubiquitylation reflect the assembly of structurally distinct ubiquitin chains on target proteins. The resulting ubiquitin code is interpreted by an extensive family of ubiquitin receptors. Here we review the components of this regulatory network and its effects throughout the cell. |
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Authors:
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Daniel Finley; Helle D Ulrich; Thomas Sommer; Peter Kaiser |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Review |
Journal Detail:
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Title: Genetics Volume: 192 ISSN: 1943-2631 ISO Abbreviation: Genetics Publication Date: 2012 Oct |
Date Detail:
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Created Date: 2012-10-02 Completed Date: 2013-04-09 Revised Date: 2013-04-16 |
Medline Journal Info:
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Nlm Unique ID: 0374636 Medline TA: Genetics Country: United States |
Other Details:
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Languages: eng Pagination: 319-60 Citation Subset: IM |
Affiliation:
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Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Adenosine Triphosphatases
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genetics,
metabolism Cell Cycle Proteins / genetics, metabolism Membrane Proteins / genetics, metabolism Proteasome Endopeptidase Complex / genetics*, ultrastructure Protein Processing, Post-Translational / genetics Protein Transport* Proteolysis Saccharomyces cerevisiae* / genetics, metabolism Substrate Specificity Ubiquitin* / genetics, physiology Ubiquitination / genetics |
| Grant Support | |
ID/Acronym/Agency:
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CA112560/CA/NCI NIH HHS; GM095526/GM/NIGMS NIH HHS; GM43601/GM/NIGMS NIH HHS; GM66164/GM/NIGMS NIH HHS; R37 GM043601/GM/NIGMS NIH HHS; //Cancer Research UK |
| Chemical | |
Reg. No./Substance:
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0/Cell Cycle Proteins; 0/Membrane Proteins; 0/Ubiquitin; EC 3.4.25.1/Proteasome Endopeptidase Complex; EC 3.6.1.-/Adenosine Triphosphatases; EC 3.6.1.-/CDC48 protein |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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