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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   

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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   

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http://www.novusbio.com/

Commercial antibody vendor which supplies antibodies and other products to life science researchers.

Proper citation: Novus Biologicals (RRID:SCR_004286) Copy   

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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   

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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   

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http://lab.rockefeller.edu/chait/

Biomedical technology research center that develops cutting-edge mass spectrometric tools for analyzing peptides and proteins. It makes its software tools developed for data analysis freely available.

Proper citation: National Resource for the Mass Spectrometric Analysis of Biological Macromolecules (RRID:SCR_009007) Copy   

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http://cudasw.sourceforge.net/

CUDASW++ is a bioinformatics software for Smith-Waterman protein database searches that takes advantage of the massively parallel CUDA architecture of NVIDIA Tesla GPUs to perform sequence searches 10x-50x faster than NCBI BLAST. In this algorithm, we deeply explore the SIMT (Single Instruction, Multiple Thread) and virtualized SIMD (Single Instruction, Multiple Data) abstractions to achieve fast speed. This algorithm has been fully tested on Tesla C1060, Tesla C2050, GeForce GTX 280 and GTX 295 graphics cards, and has been incorporated to NVIDIA Tesla Bio Workbench. * Operating System: Linux * Programming language: CUDA and C * Other requirements: CUDA SDK and Toolkits 2.0 or higher

Proper citation: CUDASW++ (RRID:SCR_008862) Copy   

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https://www.moffitt.org/research-science/shared-resources/proteomics-and-metabolomics/

Provides instrumentation for proteomics and metabolomics studies, including protein, peptide and metabolite separations, MS instrumentation for protein, peptide and metabolite analysis, and data systems, software, and bioinformatics tools for data archiving and analysis. Proteomics Core performs routine analytical proteomics services, including target discovery, identification and quantitation, and also provides platforms for functional proteomics using variety of strategies for protein separation, sub-proteome enrichment, post-translational modification analysis, and quantitation.

Proper citation: Moffitt Cancer Center Proteomics and Metabolomics Core Facility (RRID:SCR_012168) Copy   

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http://sbcb.bioch.ox.ac.uk/cgdb/

A database of membrane protein/lipid interactions by coarse-grained molecular dynamics simulations.

Proper citation: CGDB (RRID:SCR_011959) Copy   

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https://www.mcgill.ca/cian/

Core facility at Biology Department in McGill Faculty of Science. Expertise in Light Microscopy and Image Analysis. Provides light microscopes, ranging from Point Scanning and Spinning Disc Confocals to Multi-Photon, TIRF, Light Sheet and Super-Resolution microscopes. Provides services in Automation/High throughput screening (liquid handler, pinning robot), Protein expression and antibody production. Users get training.

Proper citation: McGill Cell Imaging and Analysis Network Core Facility (RRID:SCR_012623) Copy   

•   Source: SciCrunch Registry
  

http://blanco.biomol.uci.edu/membrane_proteins_xtal.html

Table providing information about integral membrane proteins whose crystallographic, or sometimes NMR, structures have been determined to a resolution sufficient to identify TM helices of helix-bundle membrane proteins (typically 4 - 4.5 angstroms). It is based upon Preusch et al. (1998) as revised by White & Wimley (1999). Reference is made to all of the protein types whose structures have been determined. They have attempted to make the database as inclusive as possible.

Proper citation: Mpstruct (RRID:SCR_013284) Copy   

•   Source: SciCrunch Registry
  

http://www.jhugicc.org/GIConteCenter/pages/cores/proteomicsCore.html

Core facility that uses mass spectrometry coupled to one (1D) and two (2D) dimensional separations by column chromatography or gel electrophoresis to identify, quantify or characterize proteins and their post-translational modifications, that are expressed in well characterized protein fractions from the small intestine, colon, kidney, liver and pancreas. Techniques such as difference gel electrophoresis (DIGE), isobaric tag for relative and absolute quantitation (iTRAQ), tandem mass tags (TMT) and stable isotope labeling of amino acids in cell culture (SILAC) as well as non-labeling methods (MudPIT, multi-dimensional protein identification technology) are available for quantifying relative differences in protein expression and post-translational modifications, such as acetylation, glycosylation, phosphorylation, nitrosation, ubiquitination and novel cleavage sites.

Proper citation: Hopkins Conte Digestive Diseases Basic and Translational Research Core Center Proteomics Core (RRID:SCR_015597) Copy   

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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
  

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   

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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   

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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   

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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
  

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