| Selectivity of the ubiquitin-binding modules. | |
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MedLine Citation:
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PMID: 22569095 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Ubiquitin-binding modules are constituents of cellular proteins that mediate the effects of ubiquitylation by making transient, non-covalent interactions with ubiquitin molecules. While some ubiquitin-binding modules bind single ubiquitin moieties, others are selective for specific ubiquitin chains of different linkage types and lengths. In recent years, functions of ubiquitin chains that are polymerized through their Lys or N-terminal Met (i.e. linear chains) residues have been linked to a variety of cellular processes. Selectivity of ubiquitin-binding modules for different ubiquitin chain types appears as a key to the distinct regulatory consequences during protein quality control pathways, receptor endocytosis, gene transcription, signaling via the NF-κB pathway, and autophagy. |
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Authors:
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Simin Rahighi; Ivan Dikic |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-5-5 |
Journal Detail:
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Title: FEBS letters Volume: - ISSN: 1873-3468 ISO Abbreviation: - Publication Date: 2012 May |
Date Detail:
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Created Date: 2012-5-9 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0155157 Medline TA: FEBS Lett Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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Copyright © 2012. Published by Elsevier B.V. |
Affiliation:
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Buchmann Institute for Molecular Life Sciences and Institute of Biochemistry II, Goethe University School of Medicine, Theodor-Stern-Kai 7, 60590 Frankfurt am Main, Germany. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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