English  |  正體中文  |  简体中文  |  Items with full text/Total items : 93288/109022 (86%)
Visitors : 613659      Online Users : 381
RC Version 6.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
Scope Tips:
  • please add "double quotation mark" for query phrases to get precise results
  • please goto advance search for comprehansive author search
  • Adv. Search
    HomeLoginUploadHelpAboutAdminister Goto mobile version

    Please use this identifier to cite or link to this item: http://asiair.asia.edu.tw/ir/handle/310904400/8644

    Title: Study of AMP-activated protein kinase agonists by structure-based drug designing
    Authors: Chang, Yea-Huey;Ho, Tin-Yun;Wu, Chieh-Hsi;Chen, Chien-Yu;Huang, Hung-Jin;Tsai, Fuu-Jen (4);Tsai, Chang-Hai;Chen, Calvin Yu-Chian
    Contributors: Department of Bioinformatics
    Keywords: Binding energy;Docking;Enzyme activity;Functional materials;Metabolism;Molecular structure;Proteins;Yeast;AMP-activated protein kinase;Bond interactions;Breast Cancer;Homology modeling;Molecular simulations;Protein kinase;Structure-based;Virtual Screening;X ray crystal structures
    Date: 2009
    Issue Date: 2010-04-07 21:21:13 (UTC+8)
    Publisher: Asia University
    Abstract: AMP-activated protein kinase (AMPK) is a metabolite- sensed protein kinase in various eukaryotes. The activated AMPK regulates important proteins which cause diabetes, obesity, metabolic aberrant, and also breast cancer. In this study, the yeast AMPK structure was used as a template to model the human AMPK structure. By homology modeling, the reliable AMPK structure was built, and the active binding site was defined corresponding to X-ray crystal structure of yeast AMPK By virtual screening the database., All the potent ligands had the H-bond interaction in the key residues, same as the control. Thus, we suggested the phenylamide derivates might be the potent AMPK agonists.
    Relation: Advanced Materials Research 79-82 :2187-2190
    Appears in Collections:[生物資訊與醫學工程學系 ] 期刊論文

    Files in This Item:

    File Description SizeFormat
    39.doc31KbMicrosoft Word406View/Open

    All items in ASIAIR are protected by copyright, with all rights reserved.

    DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - Feedback