| The promiscuity of ARF interactions with the proteasome. | |
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MedLine Citation:
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PMID: 18805416 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The tumor suppressor ARF is one of the most important oncogenic stress sensors in mammalian cells. Its effect is exerted through the interaction with different cellular partners, often resulting in their functional inactivation. This review focuses on the role played by the proteasome in ARF regulation of protein turnover and the function of most of its interacting partners. Specific proteasome components appear to be involved in the regulation of ARF turnover, bringing to light a complex network of interactions between ARF and the proteasome. |
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Authors:
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Alessandra Pollice; Maria Vivo; Girolama La Mantia |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Review Date: 2008-09-19 |
Journal Detail:
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Title: FEBS letters Volume: 582 ISSN: 0014-5793 ISO Abbreviation: FEBS Lett. Publication Date: 2008 Oct |
Date Detail:
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Created Date: 2008-11-03 Completed Date: 2008-12-10 Revised Date: 2008-12-23 |
Medline Journal Info:
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Nlm Unique ID: 0155157 Medline TA: FEBS Lett Country: Netherlands |
Other Details:
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Languages: eng Pagination: 3257-62 Citation Subset: IM |
Affiliation:
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Department of Structural and Functional Biology, University of Naples Federico II, Naples, Italy. apollice@unina.it |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Humans Mice Proteasome Endopeptidase Complex / metabolism* Proteins / metabolism* Tumor Suppressor Protein p14ARF / metabolism* |
| Chemical | |
Reg. No./Substance:
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0/Proteins; 0/Tumor Suppressor Protein p14ARF; EC 3.4.25.1/Proteasome Endopeptidase Complex |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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