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SciCrunch Registry is a curated repository of scientific resources, with a focus on biomedical resources, including tools, databases, and core facilities - visit SciCrunch to register your resource.

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http://dbserv2.informatik.uni-leipzig.de:8080/onex/

THIS RESOURCE IS NO LONGER IN SERVICE. Documented on September 6,2023. Web-based application that integrates versions of 16 life science ontologies including the Gene Ontology, NCI Thesaurus and selected OBO ontologies with data leading back to 2002 in a common repository to explore ontology changes. It allows to study and apply the evolution of these integrated ontologies on three different levels. It provides global ontology evolution statistics and ontology-specific evolution trends for concepts and relationships and it allows the migration of annotations in case a new ontology version was released

Proper citation: OnEx - Ontology Evolution Explorer (RRID:SCR_000602) Copy   


  • RRID:SCR_000667

    This resource has 1000+ mentions.

http://megasoftware.net/

Software integrated tool for conducting automatic and manual sequence alignment, inferring phylogenetic trees, mining web based databases, estimating rates of molecular evolution, and testing evolutionary hypotheses. Used for comparative analysis of DNA and protein sequences to infer molecular evolutionary patterns of genes, genomes, and species over time. MEGA version 4 expands on existing facilities for editing DNA sequence data from autosequencers, mining Web-databases, performing automatic and manual sequence alignment, analyzing sequence alignments to estimate evolutionary distances, inferring phylogenetic trees, and testing evolutionary hypotheses. MEGA version 6 enables inference of timetrees, as it implements RelTime method for estimating divergence times for all branching points in phylogeny.

Proper citation: MEGA (RRID:SCR_000667) Copy   


  • RRID:SCR_000810

http://www.bork.embl.de/j/

The main focus of this Computational Biology group is to predict function and to gain insights into evolution by comparative analysis of complex molecular data. The group currently works on three different scales: * genes and proteins, * protein networks and cellular processes, and * phenotypes and environments. They require both tool development and applications. Some selected projects include comparative gene, genome and metagenome analysis, mapping interactions to proteins and pathways as well as the study of temporal and spatial protein network aspects. All are geared towards the bridging of genotype and phenotype through a better understanding of molecular and cellular processes. The services - resources & tools, developed by Bork Group, are mainly designed and maintained for research & academic purposes. Most of services are published and documented in one or more papers. All our tools can be completely customized and integrated into your existing framework. This service is provided by the company biobyte solutions GmbH. Please visit their tools and services pages for full details and more information. Standard commercial licenses for our tools are also available through biobyte solutions GmbH. The group is partially associated with Max Delbr��ck Center for Molecular Medicine (MDC), Berlin.

Proper citation: EMBL - Bork Group (RRID:SCR_000810) Copy   


  • RRID:SCR_001139

http://www.abazyme.com/

Commercial antibody supplier that provides reagents such as immunoassay kits, antibodies, and proteins as well as custom services such as antigen preparation, sequencing and engineering.

Proper citation: Abazyme (RRID:SCR_001139) Copy   


  • RRID:SCR_001137

https://atlasantibodies.com/

An antibody supply company that provides reagents targeting all human proteins. Atlas Antibodies develops reagents and antibodies for mass-spectrometry-based quantitative proteomics as well. Their production and development is based on the Human Protein Atlas (HPA) project, which released a complete tissue-based map of human protein expression using antibodies.

Proper citation: Atlas Antibodies (RRID:SCR_001137) Copy   


  • RRID:SCR_014286

http://gpcr.usc.edu/#nogo

A protein family specific platform that works closely with the GPCR community to determine the high resolution structure and function of GPCRs. Structures are available in the glutamate, secretin, frizzled/TAS2, adhesion, and rhodopsin branches of the protein phylogenetic tree. Users can access a list of protein structure targets and completed protein structures.

Proper citation: GPCR Network (RRID:SCR_014286) Copy   


  • RRID:SCR_014322

    This resource has 5000+ mentions.

http://www.matrixscience.com/server.html

A software package and server used to identify and characterize proteins from primary sequence databases using mass spectrometry data. Mascot integrates peptide mass fingerprinting, sequence querying, and MS/MS ion searching in order to search for proteins in databases like SwissProt, NCBInr, EMBL EST divisions, contaminants, and cRAP. If a license is purchased, users may: search data sets that exceed the 1200 spectrum limit of the free version; set up automated, high throughput work; add and edit proteins and quantification methods; and search a preferred collection of sequence databases. The software package works with instruments from AB Sciex, Agilent, Bruker, Jeol, Shimadzu, Thermo Scientific, and Waters.

Proper citation: Mascot (RRID:SCR_014322) Copy   


  • RRID:SCR_014594

    This resource has 500+ mentions.

http://tools.thermofisher.com/content/sfs/manuals/Man-XCALI-97194-BioWorks-331-SP1-User-ManXCALI97194-B-EN.pdf

A a configurable software package for peptide and protein mass spectrometry analyses. It includes the SEQUEST search algorithm to identify separate proteins in complex mixtures, interactive navigation tools to filter and sort protein summaries, customized spectral plots, and chromatograms using the PEPMATCH and PEPMAP tools. This software also has batch processing capabilities to improve throughput by queuing up several files, and custom-build proprietary databases, index databases, and retrieve databases through a public server.

Proper citation: BioWorks (RRID:SCR_014594) Copy   


  • RRID:SCR_014631

    This resource has 100+ mentions.

http://fatcat.burnham.org/

Web server for flexible protein structure comparison. Structure alignment is formulated as the aligned fragment pairs chaining process allowing at most t twists, and the flexible structure alignment is transformed into a rigid structure alignment when t is forced to be 0., THIS RESOURCE IS NO LONGER IN SERVICE. Documented on September 16,2025.

Proper citation: FATCAT (RRID:SCR_014631) Copy   


  • RRID:SCR_014565

    This resource has 5000+ mentions.

http://www.gromacs.org

Software package created to perform molecular dynamics. Molecular dynamics package mainly designed for simulations of proteins, lipids, and nucleic acids. Can also be used for research on non-biological systems, such as polymers.

Proper citation: GROMACS (RRID:SCR_014565) Copy   


  • RRID:SCR_014878

    This resource has 10+ mentions.

http://www.molsoft.com/icm_browser.html

Molecular graphics environment which provides biologists and chemists with representations of proteins, DNA, RNA, and multiple sequence alignments. Users can build, annotate, and edit interactive views and slides of molecules. Users can also superimpose protein structures, search PDB, measure distanaces and angles, and view and make high resolution images of alignments.

Proper citation: ICM Browser (RRID:SCR_014878) Copy   


  • RRID:SCR_014914

    This resource has 10+ mentions.

http://www.bioclipse.net/

Open source downloadable application which contains a framework for managing and analyzing chemical compounds, as well as supports editing in 2D, processing large collections of molecules in tables, calculate various types of properties, and more cheminformatics functionality. This software also is used for the management and analysis of biological sequences (DNA, RNA, and protein), and relates the chemical structures and a target and then describes them using mathematical descriptors and models them using statistical methods. Bioclipse is equipped with a scripting language (Bioclipse Scripting Language or BSL) which can be used to automate tasks or create reusable snippets that can be shared with others,

Proper citation: Bioclipse (RRID:SCR_014914) Copy   


  • RRID:SCR_013082

    This resource has 100+ mentions.

https://bitbucket.org/nsegata/phylophlan/wiki/Home

Software pipeline for reconstructing highly accurate and resolved phylogenetic trees based on whole-genome sequence information. Pipeline is scalable to thousands of genomes and uses the most conserved 400 proteins for extracting the phylogenetic signal. PhyloPhlAn also implements taxonomic curation, estimation, and insertion operations., THIS RESOURCE IS NO LONGER IN SERVICE. Documented on September 16,2025.

Proper citation: PhyloPhlAn (RRID:SCR_013082) Copy   


  • RRID:SCR_013098

    This resource has 1+ mentions.

http://bioinfo.eie.polyu.edu.hk/mGoaSvmServer/mGOASVM.html

Data analysis service for the prediction of multi-label protein subcellular localization based on gene ontology and support vector machines. Web services are also available.

Proper citation: mGOASVM (RRID:SCR_013098) Copy   


  • RRID:SCR_013291

    This resource has 1000+ mentions.

https://github.com/macs3-project/MACS

Software Python package for identifying transcript factor binding sites. Used to evaluate significance of enriched ChIP regions. Improves spatial resolution of binding sites through combining information of both sequencing tag position and orientation. Can be used for ChIP-Seq data alone, or with control sample with increase of specificity.

Proper citation: MACS (RRID:SCR_013291) Copy   


http://genetics.bwh.harvard.edu/pph2/

Software tool which predicts possible impact of amino acid substitution on structure and function of human protein using straightforward physical and comparative considerations. PolyPhen-2 is new development of PolyPhen tool for annotating coding nonsynonymous SNPs.

Proper citation: PolyPhen: Polymorphism Phenotyping (RRID:SCR_013189) Copy   


http://xin.cz3.nus.edu.sg/group/admeap/admeap.asp

A database for facilitating the search for drug Absorption, Distribution, Metabolism, Excretion (ADME) associated proteins. It contains information about known drug ADME associated proteins, functions, similarities, substrates / ligands, tissue distributions, and other properties of the targets. Associated references are also included. Drug absorption, distribution, metabolism and excretion (ADME) often involve interaction of a drug with specific proteins. Knowledge about these ADME-associated proteins is important in facilitating the study of the molecular mechanism of disposition and individual response as well as therapeutic action of drugs. It is also useful in the development and testing of pharmacokinetics prediction tools. Several databases describing specific classes of ADME-associated proteins have appeared. A new database, ADME-associated proteins (ADME-AP), is introduced to provide comprehensive information about all classes of ADME-associated proteins described in the literature including physiological function of each protein, pharmacokinetic effect, ADME classification, direction and driving force of disposition, location and tissue distribution, substrates, synonyms, gene name and protein availability in other species. Cross-links to other databases are also provided to facilitate the access of information about the sequence, 3D structure, function, polymorphisms, genetic disorders, nomenclature, ligand binding properties and related literatures of each protein. ADME-AP currently contains entries for 321 proteins and 964 substrates. ADME Class Based on their respective role of pharmacokinetics, ADME-associated proteins can be classified into four categories: A: This Category includes proteins involved in the absorption or re-absorption of drugs into systemic system. D: This category includes proteins responsible for facilitating the distribution of drugs from the systemic system to the target sites or away from the target sites back to the systemic system. Certain plasma proteins and intracellular binding proteins may alter free drug concentration by acting as drug storage depot. These proteins thus play a regulatory role in drug distribution and they are thus included in Category D. Based on their role in drug distribution, proteins in this category can be further divided into three groups D1, D2, and D3. The first group D1 includes transporters capable of transporting chemicals across membranes of various tissue barriers from the systemic system into the target sites. Blood-brain barrier and placenta barrier are examples of tissue barrier. Proteins in the second group D2 are responsible for transporting drugs back into the systemic system. Proteins in the third group D3 mainly function as drug storage depot. These include ligand binding proteins in plasma and intracellular proteins. M: Proteins in category M are drug-metabolizing enzymes. These enzymes can be further divided into two separate groups M1 and M2, according to whether the corresponding enzymatic reaction is phase I or phase II. E: This category E includes proteins that enable the excretion or presystemic elimination of drugs. Some proteins belong to more than one category: e.g. P-glycoprotein both limits intestinal absorption and excludes drugs from the brain back to the blood. It thus belongs to both Category E and D. For those proteins capable of transporting natural substrates without literature report of interaction with a drug, a postfix potential is attached to their respective classification to indicate that their specific role in ADME is yet to be confirmed. Use of ADME-AP for commercial purposes is not allowed.

Proper citation: Drug ADME Associated Protein Database (RRID:SCR_013501) Copy   


http://opm.phar.umich.edu/

Database that provides a collection of transmembrane, monotopic and peripheral proteins from the Protein Data Bank whose spatial arrangements in the lipid bilayer have been calculated theoretically and compared with experimental data. The database allows analysis, sorting and searching of membrane proteins based on their structural classification, species, destination membrane, numbers of transmembrane segments and subunits, numbers of secondary structures and the calculated hydrophobic thickness or tilt angle with respect to the bilayer normal.

Proper citation: Orientations of Proteins in Membranes database (RRID:SCR_011961) Copy   


  • RRID:SCR_011970

    This resource has 1+ mentions.

http://www.umr6026.univ-rennes1.fr/english/home/research/basic/software/cobalten

A comprehensive database that gathers all prediction outputs concerning complete prokaryotic proteomes. It is a client-server application, with the server installed and staying at Biogenouest bioinformatics platform, keeping all needed pre-computed genomic data, while the CoBaltDB Client or GUI is a Java application which communicates with the server via web-services. The CoBaltDB Client needs to be downloaded on your computer.

Proper citation: CoBaltDB (RRID:SCR_011970) Copy   


  • RRID:SCR_012813

    This resource has 10000+ mentions.

http://sift.bii.a-star.edu.sg/

Data analysis service to predict whether an amino acid substitution affects protein function based on sequence homology and the physical properties of amino acids. SIFT can be applied to naturally occurring nonsynonymous polymorphisms and laboratory-induced missense mutations. (entry from Genetic Analysis Software) Web service is also available.

Proper citation: SIFT (RRID:SCR_012813) Copy   



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