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Found 10 result(s)

Peptidome

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Peptidome was a public repository that archived tandem mass spectrometry peptide and protein identification data generated by the scientific community. This repository is now offline and is in archival mode. All data may be obtained from the Peptidome FTP site. Due to budgetary constraints NCBI has discontinued the Peptidome Repository. All existing data and metadata files will continue to be made available from our ftp server a ftp://ftp.ncbi.nih.gov/pub/peptidome/ indefinitely. Those files are named according to their Peptidome accession number, allowing cited data to be identified and downloaded. All of the Peptidome studies have been made publicly available at the PRoteomics IDEntifications (PRIDE) database. A map of Peptidome to Pride accessions may be found at ftp://ftp.ncbi.nih.gov/pub/peptidome/peptidome-pride_map.txt. If you have any specific questions, please feel free to contact us at info@ncbi.nlm.nih.gov.

Human protein-protein interaction network database search

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<<<!!!<<< This repository is no longer available. >>>!!!>>> A human interactome map. The sequencing of the human genome has provided a surprisingly small number of genes, indicating that the complex organization of life is not reflected in the gene number but, rather, in the gene products – that is, in the proteins. These macromolecules regulate the vast majority of cellular processes by their ability to communicate with each other and to assemble into larger functional units. Therefore, the systematic analysis of protein-protein interactions is fundamental for the understanding of protein function, cellular processes and, ultimately, the complexity of life. Moreover, interactome maps are particularly needed to link new proteins to disease pathways and the identification of novel drug targets.

IMEx

The International Molecular Exchange Consortium

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The IMEx consortium is an international collaboration between a group of major public interaction data providers who have agreed to share curation effort and develop and work to a single set of curation rules when capturing data from both directly deposited interaction data or from publications in peer-reviewed journals, capture full details of an interaction in a “deep” curation model, perform a complete curation of all protein-protein interactions experimentally demonstrated within a publication, make these interaction available in a single search interface on a common website, provide the data in standards compliant download formats, make all IMEx records freely accessible under the Creative Commons Attribution License

UniProtKB

UniProtKnowledgebase

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The UniProt Knowledgebase (UniProtKB) is the central hub for the collection of functional information on proteins, with accurate, consistent and rich annotation. In addition to capturing the core data mandatory for each UniProtKB entry (mainly, the amino acid sequence, protein name or description, taxonomic data and citation information), as much annotation information as possible is added. This includes widely accepted biological ontologies, classifications and cross-references, and clear indications of the quality of annotation in the form of evidence attribution of experimental and computational data. The Universal Protein Resource (UniProt) is a comprehensive resource for protein sequence and annotation data. The UniProt databases are the UniProt Knowledgebase (UniProtKB), the UniProt Reference Clusters (UniRef), and the UniProt Archive (UniParc). The UniProt Metagenomic and Environmental Sequences (UniMES) database is a repository specifically developed for metagenomic and environmental data. The UniProt Knowledgebase,is an expertly and richly curated protein database, consisting of two sections called UniProtKB/Swiss-Prot and UniProtKB/TrEMBL.

PeptideAtlas

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The PeptideAtlas validates expressed proteins to provide eukaryotic genome data. Peptide Atlas provides data to advance biological discoveries in humans. The PeptideAtlas accepts proteomic data from high-throughput processes and encourages data submission.

Small Molecule Pathway Database

formerly: PathBank

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The Small Molecule Pathway Database (SMPDB) contains small molecule pathways found in humans, which are presented visually. All SMPDB pathways include information on the relevant organs, subcellular compartments, protein cofactors, protein locations, metabolite locations, chemical structures and protein quaternary structures. Accompanying data includes detailed descriptions and references, providing an overview of the pathway, condition or processes depicted in each diagram.

Worldwide Protein Data Bank

wwPDB

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The Protein Data Bank (PDB) is an archive of experimentally determined three-dimensional structures of biological macromolecules that serves a global community of researchers, educators, and students. The data contained in the archive include atomic coordinates, crystallographic structure factors and NMR experimental data. Aside from coordinates, each deposition also includes the names of molecules, primary and secondary structure information, sequence database references, where appropriate, and ligand and biological assembly information, details about data collection and structure solution, and bibliographic citations. The Worldwide Protein Data Bank (wwPDB) consists of organizations that act as deposition, data processing and distribution centers for PDB data. Members are: RCSB PDB (USA), PDBe (Europe) and PDBj (Japan), and BMRB (USA). The wwPDB's mission is to maintain a single PDB archive of macromolecular structural data that is freely and publicly available to the global community.

PDBj

Protein Data Bank Japan

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PDBj (Protein Data Bank Japan) provides a centralized PDB archive of macromolecular structures, integrated tools for data retrieval, visualization, and functional characterization. PDBj is supported by JST-NBDC and Osaka University.

OMICtools

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>>>!!!<<< OMICtools is no longer online >>>!!!<<< We founded OMICtools in 2012 with the vision to drive progress in life science. We wanted to empower life science practitioners all over the world to achieve breakthroughs by getting data to talk. While we made tremendous progress over the past three years, developing a bioinformatics database of software and dynamic protocols, attracting more than 1.5M visitors a year, we lacked the financial support we needed to continue. We certainly gave it our all. We'd like to thank everyone who believed in us and supported us on this journey: all our users, our community, our friends, families and employees (who we consider as our extended family!). omicX will probably shut down its operations within the next few weeks. The team and I remain firmly committed to our vision, particularly at this very difficult time. It is now, more than ever before, that researchers need access to a resource that pools collective scientific intelligence. We have accumulated an awful lot of experience which we are keen to share. If your institution would be interested in taking over our website and database, to provide researchers with continued access to the platform, or you simply want to stay in touch with the omicX team, contact us at contact@omictools.com or at carine.toutain@fhbx.eu.

Influenza Research Database

IRD

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<<<!!!<<< The migration of the data, tools, and services from the legacy IRD and ViPR applications to BV-BRC is now complete. All web traffic from the IRD and ViPR resources is also being forwarded to the BV-BRC home page https://www.re3data.org/repository/r3d100014100 >>>!!!>>>