AmyPro: a database of proteins with validated amyloidogenic regions.
AmyPro: a database of proteins with validated amyloidogenic regions.
复制标题
DOI：
10.1093/nar/gkx950
复制
发表时间：
2018-01-04
影响因子：
14.9
通讯作者：
Pancsa R
中科院分区：
文献类型：
--
作者：
Varadi M;De Baets G;Vranken WF;Tompa P;Pancsa R
可溶性功能性蛋白质可转化为不溶性淀粉样纤维，存款在各种组织。淀粉样蛋白形成是年龄相关性退行性疾病的标志。也许令人惊讶的是，淀粉样蛋白原纤维也可以是有益的，并且经常被利用来在生物体中发挥各种功能作用。在这里，我们介绍AmyPro，一个开放获取的数据库，提供了一个全面的，精心策划的收集验证淀粉样纤维形成蛋白从所有王国的生活分为广泛的功能类别（http：amypro.net）。特别是，AmyPro提供了实验验证的淀粉样蛋白生成序列区域的边界，蛋白质及其淀粉样蛋白状态的功能相关性的简短描述，用于研究淀粉样蛋白状态的实验技术列表，从UniProt转移的重要结构/功能/变异/突变数据，根据蛋白质状态分类的相关PDB结构列表，数据库交叉引用和文献参考。AmyPro通过结合朊病毒和功能性淀粉样蛋白以及致病性淀粉样蛋白，极大地改进了目前可用的类似资源，并允许用户针对整个已验证的淀粉样蛋白序列片段集合筛选其序列。通过进一步阐明淀粉样蛋白原纤维形成的顺序决定因素，我们希望AmyPro将促进新方法的发展，用于精确预测蛋白质内的淀粉样蛋白生成区域。
Soluble functional proteins may transform into insoluble amyloid fibrils that deposit in a variety of tissues. Amyloid formation is a hallmark of age-related degenerative disorders. Perhaps surprisingly, amyloid fibrils can also be beneficial and are frequently exploited for diverse functional roles in organisms. Here we introduce AmyPro, an open-access database providing a comprehensive, carefully curated collection of validated amyloid fibril-forming proteins from all kingdoms of life classified into broad functional categories (http://amypro.net). In particular, AmyPro provides the boundaries of experimentally validated amyloidogenic sequence regions, short descriptions of the functional relevance of the proteins and their amyloid state, a list of the experimental techniques applied to study the amyloid state, important structural/functional/variation/mutation data transferred from UniProt, a list of relevant PDB structures categorized according to protein states, database cross-references and literature references. AmyPro greatly improves on similar currently available resources by incorporating both prions and functional amyloids in addition to pathogenic amyloids, and allows users to screen their sequences against the entire collection of validated amyloidogenic sequence fragments. By enabling further elucidation of the sequential determinants of amyloid fibril formation, we hope AmyPro will enhance the development of new methods for the precise prediction of amyloidogenic regions within proteins.
登录
查看更多内容
DOI：
10.1126/science.1173155
发表时间：
2009-07-17
期刊：
Science (New York, N.Y.)
影响因子：
--
作者：
Maji SK;Perrin MH;Sawaya MR;Jessberger S;Vadodaria K;Rissman RA;Singru PS;Nilsson KP;Simon R;Schubert D;Eisenberg D;Rivier J;Sawchenko P;Vale W;Riek R
通讯作者：
Riek R
影响因子：
--
作者：
Otoo, Henry N.;Lee, Kyeng Gea;Lipke, Peter N.
通讯作者：
Lipke, Peter N.
影响因子：
5.8
作者：
Beerten, Jacinte;Van Durme, Joost;Schymkowitz, Joost
通讯作者：
Schymkowitz, Joost
影响因子：
3.7
作者：
Tsolis AC;Papandreou NC;Iconomidou VA;Hamodrakas SJ
通讯作者：
Hamodrakas SJ
DOI：
10.1073/pnas.0910560107
发表时间：
2010-02-02
影响因子：
11.1
作者：
Romero, Diego;Aguilar, Claudio;Kolter, Roberto
通讯作者：
Kolter, Roberto