國家衛生研究院 NHRI:Item 3990099045/5811
English  |  正體中文  |  简体中文  |  全文筆數/總筆數 : 12145/12927 (94%)
造訪人次 : 914793      線上人數 : 1409
RC Version 6.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
搜尋範圍 查詢小技巧:
  • 您可在西文檢索詞彙前後加上"雙引號",以獲取較精準的檢索結果
  • 若欲以作者姓名搜尋,建議至進階搜尋限定作者欄位,可獲得較完整資料
  • 進階搜尋
    主頁登入上傳說明關於NHRI管理 到手機版
    請使用永久網址來引用或連結此文件: http://ir.nhri.org.tw/handle/3990099045/5811


    題名: Alpha1-antitrypsin deficiency and conformational diseases
    其他題名: α1-抗胰蛋白酶缺乏症與蛋白質構型變異疾病
    作者: Chang, YP;Chang, WS;W. Chu, YH
    貢獻者: National Institute of Cancer Research
    摘要: Abnormal protein aggregation is responsible for numerous diseases such as Alzheimer’s disease, Parkinson’s disease and α1-antitrypsin deficiency (AATD). This category of diseases is now recognized as conformational diseases. α1-Antitrypsin is the archetype of the serine protease inhibitor (serpin) superfamily, and its physiological role is a suicide substrate toward its cognate enzyme neutrophil elastase. Through an unique conformational transition, the snared elastase is neutralized and the alveolar matrices in lungs are protected from destruction. However, dysfunctional mutations can result in a loss of inhibitory activity or allow spontaneous and inappropriate intermolecular polymerization ofα1-antitrypsin, ultimately leading to emphysema and cirrhosis. Insights of the mechanism of diseases offer a promising anti-protein polymerization strategy. Previous studies have shown that synthetic peptides can anneal to Zα1-antitrypsin and block polymerization. Most recently, we have developed a combinatorial approach for the discovery of anti-protein polymerization ligands, valuable for the design of therapeutic agents
    日期: 2005-09
    關聯: 化學. 2005 Sep;63(3):419-430.
    Link to: http://readopac1.ncl.edu.tw/nclJournal/search/detail.jsp?sysId=0005798517&dtdId=000040&search_type=detail&la=ch
    顯示於類別:[張文祥] 期刊論文

    文件中的檔案:

    檔案 描述 大小格式瀏覽次數
    NCA2011062102.pdf1005KbAdobe PDF523檢視/開啟


    在NHRI中所有的資料項目都受到原著作權保護.

    TAIR相關文章

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