| Facile synthesis and biological evaluation of a cell-permeable probe to detect redox-regulated proteins. | |
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MedLine Citation:
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PMID: 19081252 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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We have developed an improved synthesis for the cell-permeable, sulfenic acid probe DAz-1. Using DAz-1, we detect sulfenic acid modifications in the cell-cycle regulatory phosphatase Cdc25A. In addition, we show that DAz-1 has superior potency in cells compared to a biotinylated derivative. Collectively, these findings set the stage for the development of activity-based inhibitors of Cdc25 cell-cycle phosphatases, which are sensitive to the redox state of the active-site cysteine and demonstrate the advantage of bioorthogonal conjugation methods to detect protein sulfenic acids in cells. |
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Authors:
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Young Ho Seo; Kate S Carroll |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2008-11-24 |
Journal Detail:
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Title: Bioorganic & medicinal chemistry letters Volume: 19 ISSN: 1464-3405 ISO Abbreviation: Bioorg. Med. Chem. Lett. Publication Date: 2009 Jan |
Date Detail:
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Created Date: 2008-12-26 Completed Date: 2009-03-02 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9107377 Medline TA: Bioorg Med Chem Lett Country: England |
Other Details:
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Languages: eng Pagination: 356-9 Citation Subset: IM |
Affiliation:
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Life Sciences Institute, University of Michigan, 210 Washtenaw Ave. #4401, Ann Arbor, MI 48109-2216, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Hela Cells Humans Molecular Probes* Oxidation-Reduction Permeability cdc25 Phosphatases / metabolism* |
| Chemical | |
Reg. No./Substance:
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0/Molecular Probes; EC 3.1.3.48/cdc25 Phosphatases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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