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通过分析肽识别结构域中的特异性景观揭示蛋白质相互作用的新方面。

Uncovering new aspects of protein interactions through analysis of specificity landscapes in peptide recognition domains.

机构信息

Swiss Institute of Bioinformatics, Quartier Sorge, Bâtiment Génopode, CH-1015 Lausanne, Switzerland.

出版信息

FEBS Lett. 2012 Aug 14;586(17):2764-72. doi: 10.1016/j.febslet.2012.03.054. Epub 2012 Apr 3.

Abstract

Protein interactions underlie all biological processes. An important class of protein interactions, often observed in signaling pathways, consists of peptide recognition domains binding short protein segments on the surface of their target proteins. Recent developments in experimental techniques have uncovered many such interactions and shed new lights on their specificity. To analyze these data, novel computational methods have been introduced that can accurately describe the specificity landscape of peptide recognition domains and predict new interactions. Combining large-scale analysis of binding specificity data with structure-based modeling can further reveal new biological insights into the molecular recognition events underlying signaling pathways.

摘要

蛋白质相互作用是所有生物过程的基础。一类重要的蛋白质相互作用,通常在信号通路中观察到,由肽识别结构域与靶蛋白表面的短蛋白片段结合组成。实验技术的最新发展揭示了许多这样的相互作用,并为其特异性提供了新的线索。为了分析这些数据,已经引入了新的计算方法,可以准确描述肽识别结构域的特异性景观,并预测新的相互作用。将结合特异性数据的大规模分析与基于结构的建模相结合,进一步揭示了信号通路中分子识别事件的新生物学见解。

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