| Design and synthesis of novel photoaffinity probes for study of the target proteins of oleanolic acid. | |
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MedLine Citation:
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PMID: 22204907 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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To explore the molecular mechanisms of oleanolic acid, two novel photoaffinity probes were synthesized based on the structure-activity relationship reported previously. Their potency were evaluated in an enzyme inhibition assay against rabbit muscle glycogen phosphorylase a (RMGPa), a known target protein of oleanolic acid. The inhibitory activity of probe 2 was only about two-fold less potent than the mother compound oleanolic acid. The photoaffinity labeling experiments were also performed and two proteins were specifically tagged by probe 2. The results suggest that the synthesized probes could be used as powerful tools to isolate and identify the target proteins of oleanolic acid. |
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Authors:
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Liying Zhang; Yingxia Zhang; Jizhe Dong; Jun Liu; Luyong Zhang; Hongbin Sun |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-12-7 |
Journal Detail:
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Title: Bioorganic & medicinal chemistry letters Volume: - ISSN: 1464-3405 ISO Abbreviation: - Publication Date: 2011 Dec |
Date Detail:
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Created Date: 2011-12-29 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9107377 Medline TA: Bioorg Med Chem Lett Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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Copyright © 2011 Elsevier Ltd. All rights reserved. |
Affiliation:
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Institute of Traditional Chinese Medicine, Chengde Medical College, Chengde 067000, China; State Key Laboratory of Natural Medicines, China Pharmaceutical University, Nanjing 210009, China. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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