MPact: the MIPS protein interaction resource on yeast.

MPact: the MIPS protein interaction resource on yeast.
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DOI:
10.1093/nar/gkj003
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发表时间:
2006-01-01
影响因子:
14.9
通讯作者:
Stümpflen V
Stümpflen V
中科院分区:
生物学2区
文献类型:
--
作者:
Güldener U;Münsterkötter M;Oesterheld M;Pagel P;Ruepp A;Mewes HW;Stümpflen V

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近年来,慕尼黑蛋白质序列信息中心(MIPS)酵母蛋白质-蛋白质相互作用(PPI)数据集已被用于蛋白质网络的许多分析,并因其质量和全面性而被称为金标准[H. Yu,N. M. Luscombe,H. X. Lu、X. Zhu,Y. Xia,J.D. Han,N. Bertin,S.钟,M。维达尔和M. Gerstein(2004)Genome Res.,14,1107-1118]。MPact和酵母蛋白定位目录提供了与酵母中蛋白质邻近性相关的信息。除了高通量数据的整合外,有关文献中PPI实验证据的信息由专家汇编,总计4300种不同的PPI连接酵母中的1500种蛋白质。由于交互数据是CYGD的补充部分,因此可以将数据交互映射到其他集成数据类型,例如功能分类目录[A]。Ruepp,A. Zollner,D.迈尔K. Albermann,J.哈尼,M.莫克雷斯岛泰特科大学居尔代纳湾曼豪普特,M. Münsterkötter和H. W. Mewes(2004)Nucleic Acids Res.,5539-5545)是可能的。一项对信号蛋白的调查和与KEGG途径数据的比较表明,基于这些手动注释的数据,只能在酵母中获得对这种功能网络复杂性的广泛概述。基于网络的PPI分析工具的实现允许蛋白质相互作用网络的分析和可视化,并促进了我们的策划数据与高通量数据集的整合。完整的数据集以及用户定义的子网络可以很容易地检索标准化的PSI-MI格式。资源可以通过访问。
In recent years, the Munich Information Center for Protein Sequences (MIPS) yeast protein–protein interaction (PPI) dataset has been used in numerous analyses of protein networks and has been called a gold standard because of its quality and comprehensiveness [H. Yu, N. M. Luscombe, H. X. Lu, X. Zhu, Y. Xia, J. D. Han, N. Bertin, S. Chung, M. Vidal and M. Gerstein (2004) Genome Res., 14, 1107–1118]. MPact and the yeast protein localization catalog provide information related to the proximity of proteins in yeast. Beside the integration of high-throughput data, information about experimental evidence for PPIs in the literature was compiled by experts adding up to 4300 distinct PPIs connecting 1500 proteins in yeast. As the interaction data is a complementary part of CYGD, interactive mapping of data on other integrated data types such as the functional classification catalog [A. Ruepp, A. Zollner, D. Maier, K. Albermann, J. Hani, M. Mokrejs, I. Tetko, U. Güldener, G. Mannhaupt, M. Münsterkötter and H. W. Mewes (2004) Nucleic Acids Res., 32, 5539–5545] is possible. A survey of signaling proteins and comparison with pathway data from KEGG demonstrates that based on these manually annotated data only an extensive overview of the complexity of this functional network can be obtained in yeast. The implementation of a web-based PPI-analysis tool allows analysis and visualization of protein interaction networks and facilitates integration of our curated data with high-throughput datasets. The complete dataset as well as user-defined sub-networks can be retrieved easily in the standardized PSI-MI format. The resource can be accessed through .
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