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Found 9 result(s)

Physical mapping data at Canada's Michael Smith Genome Sciences Centre - Data

Physical Mapping Data Access

Subject(s)
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FPC Mapping data files from species that have been fingerprinted at Canada's Michael Smith Genome Sciences Centre (BCGSC).

Protein Lysine Modification Database

PLMD

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PLMD (Protein Lysine Modifications Database) is an online data resource specifically designed for protein lysine modifications (PLMs). The PLMD 3.0 database was extended and adapted from CPLA 1.0 (Compendium of Protein Lysine Acetylation) database and CPLM 2.0 (Compendium of Protein Lysine Modifications) database

National Parasite Resource Center

国家寄生虫资源库

Subject(s)
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From 2005 to 2008, with the support of the Ministry of Science and Technology (MOST), the construction of parasite germplasm repositories has spread to 20 conservation institutions in 15 provinces (cities) nationwide, with 3 physical exhibition halls; 3 live parasite conservation centers. A total of 1115 species/117814 pieces of parasitic germplasm resources of 23 orders in 11 phyla have been integrated into the physical library and database, including human parasites and vectors, animal parasites, plant nematodes, medical insects, trematodes, and parasitic snails, and the resources are combined with moderate distribution, medium- and long-term support, and off-site duplicates. The number of resources accounts for 39.27% of the national total. Through 10 years of accumulation, we have built the largest and only parasite species resource database in the field of parasites in China, and created a sharing platform of parasite germplasm resource center.

ConsensusPathDB

CPDB

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ConsensusPathDB integrates interaction networks in humans (and in the model organisms - yeast and mouse) including binary and complex protein-protein, genetic, metabolic, signaling, gene regulatory and drug-target interactions, as well as biochemical pathways. Data originate from public resources for interactions and interactions curated from the literature. The interaction data are integrated in a complementary manner to avoid redundancies.

MiCroKitS

formerly: MiCroKit

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During cell cycle, numerous proteins temporally and spatially localized in distinct sub-cellular regions including centrosome (spindle pole in budding yeast), kinetochore/centromere, cleavage furrow/midbody (related or homolog structures in plants and budding yeast called as phragmoplast and bud neck, respectively), telomere and spindle spatially and temporally. These sub-cellular regions play important roles in various biological processes. In this work, we have collected all proteins identified to be localized on kinetochore, centrosome, midbody, telomere and spindle from two fungi (S. cerevisiae and S. pombe) and five animals, including C. elegans, D. melanogaster, X. laevis, M. musculus and H. sapiens based on the rationale of "Seeing is believing" (Bloom K et al., 2005). Through ortholog searches, the proteins potentially localized at these sub-cellular regions were detected in 144 eukaryotes. Then the integrated and searchable database MiCroKiTS - Midbody, Centrosome, Kinetochore, Telomere and Spindle has been established.

European Zebrafish Resource Center

EZRC

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The EZRC at KIT houses the largest experimental fish facility in Europe with a capacity of more than 300,000 fish. Zebrafish stocks are maintained mostly as frozen sperm. Frequently requested lines are also kept alive as well as a selection of wildtype strains. Several thousand mutations in protein coding genes generated by TILLING in the Stemple lab of the Sanger Centre, Hinxton, UK and lines generated by ENU mutagenesis by the Nüsslein-Volhard lab in addition to transgenic lines and mutants generated by KIT groups or brought in through collaborations. We also accept submissions on an individual basis and ship fish upon request to PIs in Europe and elsewhere. EZRC also provides screening services and technologies such as imaging and high-throughput sequencing. Key areas include automation of embryo handling and automated image acquisition and processing. Our platform also involves the development of novel microscopy techniques (e.g. SPIM, DSLM, robotic macroscope) to permit high-resolution, real-time imaging in 4D. By association with the ComPlat platform, we can support also chemical screens and offer libraries with up to 20,000 compounds in total for external users. As another service to the community the EZRC provides plasmids (cDNAs, transgenes, Talen, Crispr/cas9) maintained by the Helmholtz repository of Bioparts (HERBI) to the scientific community. In addition the fish facility keeps a range of medaka stocks, maintained by the Loosli group.

MassBank Europe

MassBank

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Database of mass spectra of known, unknown and provisionally identified substances. MassBank is the first public repository of mass spectral data for sharing them among scientific research community. MassBank data are useful for the chemical identification and structure elucidation of chemical compounds detected by mass spectrometry.

STRING

Known and Predicted Protein-Protein Interactions

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STRING is a database of known and predicted protein interactions. The interactions include direct (physical) and indirect (functional) associations; they are derived from four sources: - Genomic Context - High-throughput Experiments - (Conserved) Coexpression - Previous Knowledge STRING quantitatively integrates interaction data from these sources for a large number of organisms, and transfers information between these organisms where applicable.

APID

Agile Protein Interactomes DataServer

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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).