Cancer Research Center (CiC-IBMCC, CSIC/USAL/IBSAL), Consejo Superior de Investigaciones Científicas and University of Salamanca, Salamanca, Spain.
Center for Cancer Systems Biology, Department of Cancer Biology, Dana-Farber Cancer Institute and Department of Genetics, Harvard Medical School, Boston, MA, USA.
Database (Oxford). 2019 Jan 1;2019:baz005. doi: 10.1093/database/baz005.
The collection and integration of all the known protein-protein physical interactions within a proteome framework are critical to allow proper exploration of the protein interaction networks that drive biological processes in cells at molecular level. APID Interactomes is a public resource of biological data (http://apid.dep.usal.es) that provides a comprehensive and curated collection of protein interactomes' for more than 1100 organisms, including 30 species with more than 500 interactions, derived from the integration of experimentally detected protein-to-protein physical interactions (PPIs). We have performed an update of APID database including a redefinition of several key properties of the PPIs to provide a more precise data integration and to avoid false duplicated records. This includes the unification of all the PPIs from five primary databases of molecular interactions (BioGRID, DIP, HPRD, IntAct and MINT), plus the information from two original systematic sources of human data and from experimentally resolved 3D structures (i.e. PDBs, Protein Data Bank files, where more than two distinct proteins have been identified). Thus, APID provides PPIs reported in published research articles (with traceable PMIDs) and detected by valid experimental interaction methods that give evidences about such protein interactions (following the ontology and controlled vocabulary': www.ebi.ac.uk/ols/ontologies/mi; developed by HUPO PSI-MI'). Within this data mining framework, all interaction detection methods have been grouped into two main types: (i) binary' physical direct detection methods and (ii) indirect' methods. As a result of these redefinitions, APID provides unified protein interactomes including the specific experimental evidences' that support each PPI, indicating whether the interactions can be considered `binary' (i.e. supported by at least one binary detection method) or not.
在蛋白质组学框架内收集和整合所有已知的蛋白质-蛋白质物理相互作用对于适当探索驱动细胞内分子水平生物过程的蛋白质相互作用网络至关重要。APID Interactomes 是一个生物数据公共资源(http://apid.dep.usal.es),提供了超过 1100 种生物体的综合和精心整理的“蛋白质相互作用组”集合,包括 30 种具有超过 500 种相互作用的物种,这些物种源自实验检测到的蛋白质-蛋白质物理相互作用(PPIs)的整合。我们对 APID 数据库进行了更新,包括重新定义了几个 PPI 的关键属性,以提供更精确的数据集成并避免错误的重复记录。这包括统一来自五个主要分子相互作用数据库(BioGRID、DIP、HPRD、IntAct 和 MINT)的所有 PPI,加上来自两个原始人类数据系统来源和实验解析的 3D 结构(即 PDBs、蛋白质数据库文件,其中已鉴定出两个以上不同的蛋白质)的信息。因此,APID 提供了在已发表的研究文章中报告的(可追溯到 PMID 的)PPIs 和通过有效实验相互作用方法检测到的 PPI,这些方法提供了有关这些蛋白质相互作用的证据(遵循“本体论和受控词汇”:www.ebi.ac.uk/ols/ontologies/mi;由“HUPO PSI-MI”开发)。在这个数据挖掘框架内,所有的相互作用检测方法都被分为两种主要类型:(i)“二进制”物理直接检测方法和(ii)“间接”方法。由于这些重新定义,APID 提供了统一的蛋白质相互作用组,包括支持每个 PPI 的特定“实验证据”,表明相互作用是否可以被认为是“二进制”(即至少有一种二进制检测方法支持)或不是。