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https://netbio.bgu.ac.il/labwebsite/software/responsenet/

WebServer that identifies high-probability signaling and regulatory paths that connect input data sets. The input includes two weighted lists of condition-related proteins and genes, such as a set of disease-associated proteins and a set of differentially expressed disease genes, and a molecular interaction network (i.e., interactome). The output is a sparse, high-probability interactome sub-network connecting the two sets that is biased toward signaling pathways. This sub-network exposes additional proteins that are potentially involved in the studied condition and their likely modes of action. Computationally, it is formulated as a minimum-cost flow optimization problem that is solved using linear programming.

Proper citation: ResponseNet (RRID:SCR_003176) Copy   

•   Source: SciCrunch Registry

http://www.jci-bioinfo.cn/iLoc-Animal

Data analysis service for predicting subcellular localization of animal proteins with single or multiple sites.

Proper citation: iLoc-Animal (RRID:SCR_003173) Copy   

•   Source: SciCrunch Registry

http://www.i3crb.fr/

Project to improve data and sample exchanges and to facilitate large scale analysis of data by improving interoperability of French Biological Resources Centres (BRC or biobanks) IT systems and biological databases. The work done in this project will be linked to other national (IBiSA, ANR, R��seau des Biobanques, Club 3C-R), European (BBMRI, ELIXIR) or international project (P3G). In the preliminary phase (2009-2010) I3-CRB has developed a directory of French Biological Resource Centres / Biobanks where one may register their French BRC or perform a search across all of them. Detail by overall data or kingdom is provided as well as many filtering options. Access to biological samples is provided by the participating BRC''''s. Biological Resources Centres (BRC or biobanks) collect annotated biological samples from various sources (human, animal, plant, bacteria...). The type of samples depends on the collection and the associated thematic (DNA, proteins, cells, tissues, blood, serum, organisms...). The aims of these centers are to collect, to store, to transform and to distribute the biological samples. They constitute a vital infrastructure for life science and health research. Goals of the French Biobanks/Biological Resource Centres: * List French biobanks and their biological collections * Improve sample exchanges * Improve the international visibility of the French biological collections MeSH terms have been integrated: Domains, diseases, and location of the disease (Anatomy). Collections/species are based on NCBI Taxonomy.

Proper citation: I3-CRB: Interoperable IT Infrastructure for Biological Resources Centres / Biobanks - France (RRID:SCR_006991) Copy   

•   Source: SciCrunch Registry

http://nmrresource.ucsd.edu/

Biomedical technology research center that develops new technology for NMR spectroscopy and makes it available to the biomedical research community for structure determination of proteins in biological supramolecular assemblies, such as membrane proteins or virus particles. The principal applications are to membrane-associated proteins; however, the approach is generally applicable to polypeptides that cannot be prepared in forms suitable for X-ray crystallography or multidimensional solution NMR spectroscopy. As a result, there are also applications to viruses and other biological systems. The principal instrumentation consists of high-field NMR spectrometers dedicated to high-resolution solid-state NMR spectroscopy. The spectrometers are capable of the full-range of multiple-resonance experiments on stationary and spinning samples; however, the major emphasis is on methods that utilize mechanically or magnetically oriented samples. Development encompasses preparation of samples, including: * Expression and purification of membrane proteins * Design and construction of instrumentation, especially probes * Implementation of new pulse sequences and other experimental protocols for solid-state NMR spectroscopy * Calculations for the processing of experimental data and protein structure determination from the orientational constraints derived from these data

Proper citation: UCSD Center for NMR Spectroscopy and Imaging of Proteins (RRID:SCR_001401) Copy   

•   Source: SciCrunch Registry

http://anya.igsb.anl.gov/Geneways/GeneWays.html

System for automatically extracting, analzying, visualizing and integrating molecular pathway data from the research literature. System focuses on interactions between molecular substances and actions, providing a graphical consensus view on the collected information. GeneWays is designed as open platform, allowing researchers to query, review and critique integrated information.

Proper citation: GeneWays (RRID:SCR_000572) Copy   

•   Source: SciCrunch Registry

http://www.glycosciences.de/glycocd/

Manually curated, comprehensive repository of clusters of differentiation (CDs) which are a) defined as distinct oligosaccharide sequences as part of either glycoproteins and/or glycosphingolipids and b) defined as proteins which have carbohydrate recognition sites (CRDs) or as carbohydrate binding lectins. The data base is generated by exhaustive search of literature and other online data banks related to carbohydrates and proteins. This data bank is the beginning of an effort to provide concise, relevant information of carbohydrate-related CDs in a user- friendly manner. For users convenience the data bank under menu browse of GlycoCD is arranged in two section namely carbohydrate recognition CDs (CRD CD) and glycan CD. The carbohydrate recognition CD part is the collection of proteins which recognize glycan structures by means of the CRDs. Glycan CD is the part in which CDs are summarized which characterize specific oligosaccharide structures. The GlycoCD databank has been developed with the aim to assist the immunologist, cell biologist as well as the clinician who wants to keep up with the present knowledge in this field of glycobiology.

Proper citation: Glyco-CD (RRID:SCR_001574) Copy   

•   Source: SciCrunch Registry

https://www.tamuk.edu/agriculture/institutes-and-other-units/nntrc/Products-Services.html

Center to provide global research, training, and resources that will lead to the discovery of medically important toxins found in venoms. The Viper Resource Center (VRC) is located in the Natural Toxins Research Center at Texas A&M University-Kingsville.

Proper citation: National Natural Toxins Research Center (RRID:SCR_002824) Copy   

•   Source: SciCrunch Registry

http://www.uniprot.org/program/Chordata

Data set of manually annotated chordata-specific proteins as well as those that are widely conserved. The program keeps existing human entries up-to-date and broadens the manual annotation to other vertebrate species, especially model organisms, including great apes, cow, mouse, rat, chicken, zebrafish, as well as Xenopus laevis and Xenopus tropicalis. A draft of the complete human proteome is available in UniProtKB/Swiss-Prot and one of the current priorities of the Chordata protein annotation program is to improve the quality of human sequences provided. To this aim, they are updating sequences which show discrepancies with those predicted from the genome sequence. Dubious isoforms, sequences based on experimental artifacts and protein products derived from erroneous gene model predictions are also revisited. This work is in part done in collaboration with the Hinxton Sequence Forum (HSF), which allows active exchange between UniProt, HAVANA, Ensembl and HGNC groups, as well as with RefSeq database. UniProt is a member of the Consensus CDS project and thye are in the process of reviewing their records to support convergence towards a standard set of protein annotation. They also continuously update human entries with functional annotation, including novel structural, post-translational modification, interaction and enzymatic activity data. In order to identify candidates for re-annotation, they use, among others, information extraction tools such as the STRING database. In addition, they regularly add new sequence variants and maintain disease information. Indeed, this annotation program includes the Variation Annotation Program, the goal of which is to annotate all known human genetic diseases and disease-linked protein variants, as well as neutral polymorphisms.

Proper citation: UniProt Chordata protein annotation program (RRID:SCR_007071) Copy   

•   Source: SciCrunch Registry

https://www.usd.edu/medicine/basic-biomedical-sciences/proteomics-core

Core provides proteomics services to researchers from South Dakota and the surrounding region to rapidly analyze and identify protein expression patterns in their experimental systems.Develops experimental design, protocols, data analysis and interpretation.Provides consulting and advice in grant proposal, as well as data preparation to be submitted to proteomics journal according to requirements.Offers training in use of common equipment such as scanner, spot cutter, imaging software, technique and protocol issues, and sample preparation.

Proper citation: South Dakota University SD BRIN Proteomics Core Facility (RRID:SCR_017743) Copy   

•   Source: SciCrunch Registry

https://www.cimr.cam.ac.uk/about/facilities/bioinformatics

Core provides biological data handling and analysis in differential expression analysis, next generation sequencing, networks, protein architecture, and motif searching for in house researchers.

Proper citation: Cambridge Institute for Medical Research Bioinformatics Core Facility (RRID:SCR_017186) Copy   

•   Source: SciCrunch Registry

http://www.uvm.edu/sbb/cxx/cxx.html

Core for high resolution structural biology at the University of Vermont. X-ray crystallography allows biological and biomedical researchers to visualize proteins, RNA, DNA and their complexes at atomic resolution. The molecular details of specimens as small as DNA binding domains and as large as the ribosome have been elucidated via this powerful method. The CXX provides resources for all stages of macromolecular structure determination.

Proper citation: Vermont University Center for X-Ray Crystallography Core Facility (RRID:SCR_017688) Copy   

•   Source: SciCrunch Registry

http://biophysics.fsu.edu/facilities/protein-expression-facility/

Core to facilitate the large scale expression of recombinant proteins in bacterial, insects, and mammalian cells. Serves primarily faculty and students from the laboratories in the Kasha Laboratory Building and laboratories in Biology, Biochemistry, Chemistry and Nutrition at Florida State University, Tallahassee, FL.

Proper citation: Florida State University Protein Expression Core Facility (RRID:SCR_016757) Copy   

•   Source: SciCrunch Registry

https://www.rockefeller.edu/sbrc/

Core for protein expression and purification as well as all equipment needed for determination of three dimensional structures of biological macromolecules via X-ray crystallography. Houses Rigaku/MSC microMax 007HF generator for X-ray diffraction data collection, equipped with Varimax optics, X-stream 2000 cryosystems and two RaxisIV++ detectors.Also available is stereomicroscope, Nikon SMZ18, for crystal tray observations and crystal mounting., THIS RESOURCE IS NO LONGER IN SERVICE. Documented on September 16,2025.

Proper citation: Rockefeller University Structural Biology Resource Center Core Facility (RRID:SCR_017732) Copy   

•   Source: SciCrunch Registry

http://mass-spec.stanford.edu

Core mass spec and proteomic services include open access lab for trained users with GC/MS, LC/MS, high resolution LC/MS, and MALDI-TOF instruments, help with intact protein analysis, targeted quantitation, drug discovery support, pathway analysis, protein interactions, FFPE tissue analysis, both labeled and label-free proteomics, and more. Please contact SUMS to discuss these and other custom projects including new application development.

Proper citation: Stanford University Vincent Coates Foundation Mass Spectrometry Laboratory Core Facility (RRID:SCR_017801) Copy   

•   Source: SciCrunch Registry

https://www.dbi.udel.edu/resources-and-facilities/protein-characterization

Facility consists of a Beckman Coulter ProteomeLab XL-I analytical ultracentrifuge is configured with a scanning UV/Vis detection system and Rayleigh Interference Optics. Used to characterize variety of biophysical properties of macromolecules such as molecular weight, sedimentation coefficient, diffusion coefficient, equilibrium constant and stoichiometry. Can assess sample heterogeneity (aggregation and purity), molecular conformation (folded or unfolded), composition (assembled or unassembled) and thermodynamic properties of interacting systems. Provides spectrum of data for protein characterization in solution.

Proper citation: Delaware Biotechnology Institute Protein Characterization Core Facility (RRID:SCR_017746) Copy   

•   Source: SciCrunch Registry

http://www.columbia.edu/cu/biology/resources/proteomics/

Core provides identification of proteins and metabolites with differential quantitative expression in cells, tissues or in protein affinity purifications. Particular emphasis is on quantitative analysis of posttranslational modifications such as phosphorylation.

Proper citation: Columbia University Quantitative Proteomics and Metabolomics Core Facility (RRID:SCR_017747) Copy   

•   Source: SciCrunch Registry

http://www.med.unc.edu/csb/pep

Core specializes in production of pure, functional proteins for structural, biophysical, and biochemical studies. Facility offers three categories of service:Protein Expression,Protein Purification,Scientific Consultation, Mentoring, and Training; Offers Isotope labeled proteins for NMR;High production scales for immunizations, drug discovery, structural biology;Endotoxin-free protein production;Stable cell line generation;Expert baculovirus expression;Custom packages to efficiently suit your needs.

Proper citation: North Carolina University at Chapel Hill School of Medicine Protein Expression and Purification Core Facility (RRID:SCR_017843) Copy   

•   Source: SciCrunch Registry

http://proteomics.swmed.edu

Core provides seven mass spectrometry platforms, for shotgun and targeted analyses, run by core staff. Services include protein and peptide identification from gels and solutions, identification and localization of post translational modifications, relative and absolute quantitation of peptides and proteins, intact mass analysis of proteins in solution.

Proper citation: UTSW Proteomics Core (RRID:SCR_017813) Copy   

•   Source: SciCrunch Registry

https://redoxbiologycenter.unl.edu/facilities/metabolomics-and-proteomics-core-facility/

Provides tools of modern functional proteomics and metabolomics. Facility is equipped with chromatography and mass spectrometry based technologies for proteomics and metabolomics (Clinical and non clinical), personalized experimental design consultation and comprehensive, individualized bioinformatics support.Services include:Small molecule exact mass determination or quantitation using positive or negative ion mode;Protein identification using LC/MS/MS analysis and MASCOT and SEQUEST database search;Shot gun proteome analysis of biological samples;Biomarker discovery from biological fluid;Drug protein or drug nucleic acid protein interaction;Protein complex isolation and identifying interacting partners and its quantitation;Protein differential expression analysis and quantitation by 2D-LC MS/MS (MudPIT);Global PTM analysis and quantitation;Specialization in phosphorylation and oxidation analysis;Coomassie Blue and Silver Stained Gel analysis; de novo peptide sequencing by tandem mass spectrometry;Confirmation of mutations in protein ;Customized sequence search of in-house proteins that are not available in database; Post translational modifications (phosphorylation, sumoylation, ubiquitination, oxidation, etc.); Determination of oxidation state of cysteine (disulfide bonds);Intact proteins and peptides mass determination.

Proper citation: Nebraska-Lincoln University Metabolomics and Proteomics Core Facility (RRID:SCR_017789) Copy   

•   Source: SciCrunch Registry

http://htbc.stanford.edu

Core provides fully automated high throughput screening (HTS) of Compound Libraries (130,000+ compounds) for both enzyme/protein-based assays and cell-based assays, using Caliper Life Sciences Staccato system;Genomic siRNA screening with siARRAY whole human genome siRNA library from Dharmacon targeting 21,000 genes, using Agilent Bravo system;High-Content Screening using ImageXpress Micro automated fluorescent microscope with live cell, bright field, phase contrast and integrated plate handling with Thermo Catalyst CRS, and image analysis using MetaXpress software;High Throughput Molecular Biology reagents and services, including access to cDNA libraries (Human ORFeome collection, 15,000 genes) and 96 and 384-well bead clean-ups and PCR setup (Biomek FX and Agilent Bravo), and other automation steps in collaboration with SFGF;High-throughput assay development assistance with cell culture, experiment design, robotic programming and Standard Operating Procedure drafting;Screening data analysis assistance with protocols, hit determination and structure activity analyses using MDL chemical database ISIS/HOST, Plate Manager, Assay Explorer and Report Manager. Use of microplate reader detection systems, including Tecan Infinite M1000 and Infinite M1000 PRO and Molecular Devices Analyst GT for fluorescence; fluorescence polarization; time-resolved fluorescence; absorbance and luminescence (with injectors and AlphaScreen); and Flexstation II 384, for kinetic fluorescence reads to measure calcium mobilization and ion channels.Use of liquid-handling robots, including Sciclone ALH3000 (96- and 384-well pipetting), Agilent Bravo (96- and 384-well pipetting), Velocity11 VPrep (96-well pipetting), Bio-Tek plate washers/dispensers, Matrix Wellmate and Titertek/Labsystems Multidrop microplate dispensers, and Velocity11 PlateLoc plate heat sealer;Training for most of these services.

Proper citation: Stanford University School of Medicine High Throughput Bioscience Center Core Facility (RRID:SCR_017794) Copy   

•   Source: SciCrunch Registry