| Finding the needles in the haystack: mapping constitutive proteolytic events in vivo. | |
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MedLine Citation:
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PMID: 17822382 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Our quest to understand the complex inner workings of the cell depends on the development of new technologies that allow the study of global regulatory events as they happen within their native cellular environment. Post-translational processing of proteins by proteases is one such regulatory process that can control many aspects of basic cell biology. In this issue of the Biochemical Journal, Timmer et al. describe a new proteomic approach that can be used to globally monitor constitutive proteolytic events in vivo. Using bacterial, human, yeast and mouse cells, the authors show that this methodology provides a comprehensive map of constitutive trimming events mediated by regulatory proteases such as methionine aminopeptidase. This study also identifies previously uncharacterized processing events that highlight potential novel regulatory mechanisms mediated by proteolysis. |
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Authors:
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Matthew Bogyo |
Publication Detail:
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Type: Comment; Journal Article |
Journal Detail:
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Title: The Biochemical journal Volume: 407 ISSN: 1470-8728 ISO Abbreviation: Biochem. J. Publication Date: 2007 Oct |
Date Detail:
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Created Date: 2007-09-07 Completed Date: 2007-11-06 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 2984726R Medline TA: Biochem J Country: England |
Other Details:
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Languages: eng Pagination: e1-2 Citation Subset: IM |
Affiliation:
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Department of Pathology and Department of Microbiology and Immunology, Stanford University School of Medicine, 300 Pasteur Drive, Stanford, CA 94305-5324, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Aminopeptidases
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metabolism Animals Humans Mice Peptide Hydrolases / metabolism* Peptide Mapping Peptides / analysis, chemistry, metabolism Proteome / analysis, metabolism Proteomics / methods* |
| Chemical | |
Reg. No./Substance:
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0/Peptides; 0/Proteome; EC 3.4.-/Peptide Hydrolases; EC 3.4.11.-/Aminopeptidases; EC 3.4.11.18/methionyl aminopeptidase |
| Comments/Corrections | |
Comment On:
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Biochem J. 2007 Oct 1;407(1):41-8
[PMID:
17650073
]
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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