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Morph·D·Base has been developed to serve scientific research and education. It provides a platform for storing the detailed documentation of all material, methods, procedures, and concepts applied, together with the specific parameters, values, techniques, and instruments used during morphological data production. In other words, it's purpose is to provide a publicly available resource for recording and documenting morphological metadata. Moreover, it is also a repository for different types of media files that can be uploaded in order to serve as support and empirical substantiation of the results of morphological investigations. Our long-term perspective with Morph·D·Base is to provide an instrument that will enable a highly formalized and standardized way of generating morphological descriptions using a morphological ontology that will be based on the web ontology language (OWL - http://www.w3.org/TR/owl-features/). This, however, represents a project that is still in development.
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The goal of the Autophagy Database is to provide up-to-date relevant information including protein structure data to researchers of autophagy, and to disseminate important findings to a wider audience so that their ramifications can be appreciated. For this purpose, we strive to make the database to contain as much pertinent information as possible and to make the contents freely available in a user-friendly format.
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APID Interactomes is a database that provides a comprehensive collection of protein interactomes for more than 400 organisms based in the integration of known experimentally validated protein-protein physical interactions (PPIs). Construction of the interactomes is done with a methodological approach to report quality levels and coverage over the proteomes for each organism included. In this way, APID provides interactomes from specific organisms that in 25 cases have more than 500 proteins. As a whole APID includes a comprehensive compendium of 90,379 distinct proteins and 678,441 singular interactions. The analytical and integrative effort done in APID unifies PPIs from primary databases of molecular interactions (BIND, BioGRID, DIP, HPRD, IntAct, MINT) and also from experimentally resolved 3D structures (PDB) where more than two distinct proteins have been identified. In this way, 8,388 structures have been analyzed to find specific protein-protein interactions reported with details of their molecular interfaces. APID also includes a new data visualization web-tool that allows the construction of sub-interactomes using query lists of proteins of interest and the visual exploration of the corresponding networks, including an interactive selection of the properties of the interactions (i.e. the reliability of the "edges" in the network) and an interactive mapping of the functional environment of the proteins (i.e. the functional annotations of the "nodes" in the network).