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  • FHA Domain pThr Binding Specificity: It's All about Me
    [作者:Coquelle, N; Glover, JNM,期刊:Structure, 页码:1549-1550 , 文章类型: Editorial Material,,卷期:2010年18-12]
  • The FHA domain is a phospho-peptide binding module involved in a wide range of cellular pathways, with a striking specificity for phospho-threonine over phospho-serine binding partners. Biochemical, structural, and dynam...
  • Finding the Path in an RNA Folding Landscape
    [作者:Boodram, SN; Johnson, PE,期刊:Structure, 页码:1550-1551 , 文章类型: Editorial Material,,卷期:2010年18-12]
  • In this issue of Structure, Reymond et al. (2010) combine molecular and computational biology approaches to provide structural details for intermediates in the folding pathway of the hepatitis delta virus ribozyme.
  • Structural and Functional Analysis of Phosphothreonine-Dependent FHA Domain Interactions
    [作者:Pennell, S; Westcott, S; Ortiz-Lombardia, M; Patel, D; Li, JJ; Nott, TJ; Mohammed, D; Buxton, RS; Yaffe, MB; Verma, C; Smerdon, SJ,期刊:Structure, 页码:1587-1595 , 文章类型: Article,,卷期:2010年18-12]
  • FHA domains are well established as phospho-dependent binding modules mediating signal transduction in Ser/Thr kinase signaling networks in both eukaryotic and prokaryotic species. Although they are unique in binding exc...
  • Structural Diversity in Integrin/Talin Interactions
    [作者:Anthis, NJ; Wegener, KL; Critchley, DR; Campbell, ID,期刊:Structure, 页码:1654-1666 , 文章类型: Article,,卷期:2010年18-12]
  • The adhesion of integrins to the extracellular matrix is regulated by binding of the cytoskeletal protein talin to the cytoplasmic tail of the beta-integrin subunit. Structural studies of this interaction have hitherto l...