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http://www.protein.iastate.edu

Core offers protein/peptide sequencing, large and small scale peptide synthesis (Fmoc), matrix assisted laser desorption/ionization (MALDI) mass spectrometry, SDS-PAGE/electroblotting, 2-D gel electrophoresis, isoelectric focusing (IEF), in-gel and solution digestion, tandem mass spectrometry (LC-MS/MS), ion mobility mass spectrometry (IM-MS), digital image acquisition and analysis using Typhoon imaging system and 2D gel documentation/analysis system, and semi-preparative, analytical and micro-analytical high performance liquid chromatography (HPLC). MALDI, HPLC, SDS-PAGE/blotting, IEF, 2D gel electrophoresis, 2D gel documentation/analysis and Typhoon imaging system are all available for user operation after appropriate training.

Proper citation: Iowa State University Office of Biotechnology Protein Core Facility (RRID:SCR_017780) Copy   

•   Source: SciCrunch Registry

http://proteomics.rockefeller.edu/

Core provides analysis of proteins, peptides, lipids, polar metabolites and small molecules by high resolution/high mass spectrometry. Targeted and hypothesis free analysis are offered combined with relative quantitation based on either label free, tandem mass tags or metabolic labelling. Acquisition tools include Data Dependent (DDA) and Data Independent (DIA).

Proper citation: The Rockefeller University Proteomics Resource Center Core Facility (RRID:SCR_017797) Copy   

•   Source: SciCrunch Registry

https://biophysics.fsu.edu/facilities/x-ray-crystallography-facility

Shared macromolecular x-ray crystallography facility provides instruments and expertise for screening, optimizing, imaging, growing, and storing crystals of biological macromolecules. The X-Ray Facility coordinates single crystal x-ray diffraction data collection at third generation synchrotron x-ray source using FSU's membership at the National Synchrotron Light Source II at Brookhaven National Lab, Upton, NY. XRF also offers custom buffer preparation, optimization, and crystal set-up using multi-well format crystallization blocks and plates.XRF has ARI Crystal Gryphon robot, Formulatrix Rock Imager, Formulator 16, Rock Maker software, RUMED incubator, Cryo storage and shipping dewars, Leica S8 AP0 Zoom microscope and other amenities.

Proper citation: Florida State University X-Ray Crystallography Core Facility (RRID:SCR_017922) Copy   

•   Source: SciCrunch Registry

https://www.unlv.edu/genomics

Provides development and support of genomics-based research, serving investigators in Nevada and beyond. Staff can be contracted for select services including ABI 3130 DNA sequencing, BD FACSCalibur flow cytometry, Affymetrix microarray processing, Agilent 2100 Bioanalyzer analysis and Qubit analysis. Facility also provides equipment and training for real-time PCR, Western blot/gel/microarray scanning, and analysis of DNA, RNA and protein samples.

Proper citation: Nevada University Genomics Core Facility (RRID:SCR_018272) Copy   

•   Source: SciCrunch Registry

http://proteomics.northwestern.edu/collaborate

Core offers multiple types of experiments from simple protein identification to protein quantitation. Performs traditional bottom-up proteomics, where proteins are digested with enzyme prior to analysis and intact, top-down proteomics analyses. Services include proteins identification after in-gel or in-solution digestion, top-down mass spectrometry to preserve post-translationally modified forms of proteins present in vivo by measuring them intact, IP-MS Pulldown,BioID service to identify target of biotin ligase that has been tagged onto their protein via traditional cloning methods,Untargeted Quantitative Peptide Proteomics,Targeted Quantitative Peptide Proteomics,Epiproteomic Histone Modification Panel A,Epiproteomic Histone Modification Panel B,Untargeted Metabolomics,Phosphoproteomics,PTM Scan,ChIP-MS.

Proper citation: Northwestern University Proteomics Core Facility (RRID:SCR_017945) Copy   

•   Source: SciCrunch Registry

https://ua.ilab.agilent.com/service_center/show_external/4535?name=analytical-and-biological-mass-spectrometry

Provides equipment and expertise for analysis of variety of biological and small molecules.Services include protein analysis encompassing protein identification, protein and peptide sequence confirmation, intact protein molecular weight determination, complex protein sample analysis, and protein/antibody drug interactions.Developed metabolomics library to support metabolomic and lipidomics analysis. Can identify range of post-translational modifications, determining their presence or absence, as well as quantitating PTMs.Proteomics and small molecule services include workflows for label free,chemical labeling (iTRAQ/TMT) and metabolic labeling (SILAC).Service for molecular synthesis, with monitoring reaction steps,calculating percentage of product, testing for purity, and molecule characterization with high resolution and high mass accuracy.Provides molecular weight and chemical composition determinations, structure elucidations and compound identification analysis or confirmation and accurate mass measurements of synthetic products, measurement of polymers, nucleic acids (DNA/RNA), peptides, proteins, natural products, and assistance with determination of unknowns.

Proper citation: University of Arizona Analytical and Biological Mass Spectrometry Core Facility (RRID:SCR_023370) Copy   

•   Source: SciCrunch Registry

https://aideepmed.com/COACH/

Web application for protein-ligand binding site prediction. Starting from given structure of target proteins, COACH will generate complementray ligand binding site predictions using two comparative methods, TM-SITE and S-SITE, which recognize ligand-binding templates from the BioLiP protein function database by binding-specific substructure and sequence profile comparisons.

Proper citation: COACH (RRID:SCR_027684) Copy   

•   Source: SciCrunch Registry

http://www.amorfix.com/

Product development company focused on therapeutic products and diagnostic devices targeting misfolded protein diseases. On July, 2015 the company name was changed to ProMIS Neurosciences, Inc.

Proper citation: Amorfix (RRID:SCR_003783) Copy   

•   Source: SciCrunch Registry

http://www.proteomics.com/

Commercial company delivering content for personalized medicine in the areas of Biomarker Services, Biomarker Assays, Isobaric and Isotopic Reagents and Proprietary Biomarkers. A global leader in applied proteomics, they use high sensitivity proprietary technologies to detect biomarkers (differentially expressed proteins in diseases) and to develop rapid assays for testing. The biomarkers discovered in body fluids or tissues are validated, developed and commercialized as diagnostic, prognostic or therapeutic products through strategic alliances and out-licensing.

Proper citation: Proteome Sciences (RRID:SCR_004106) Copy   

•   Source: SciCrunch Registry

http://www.thebindingsite.com/

Company provides specialist diagnostic products to clinicians and laboratory professionals worldwide. Specialist protein company committed to research, development, manufacture and distribution of immunodiagnostic assays for global laboratory market. Specialized in antibody specificity technology, Binding Site gives clinicians and laboratory staff tools to significantly improve diagnosis and management of those patients with specific cancers and immune disorders. Binding Site manufactures wide range of products for plasma protein analysis including Freelite, Hevylite and SPAplus.

Proper citation: Binding Site (RRID:SCR_004051) Copy   

•   Source: SciCrunch Registry

http://portal.ncibi.org/gateway/gin.html

GIN-IE is a high precision system for extracting protein/gene interactions, interaction cue words, and directionality from the literature. Syntax-aware inferences about the roles of the entities are made by using the syntactic and dependency parse tree structures of the sentences. Negation and speculation are frequently occurring language phenomena that modify the factuality of the information contained in text. GIN-IE detects and distinguishes interactions that are extracted from negated or speculative sentences. GIN-IE has been integrated with the NCIBI PubMed daily update and processing pipeline. The extracted interactions are accessible through MimiWeb.

Proper citation: Gene Interaction Extraction from the Literature (RRID:SCR_008660) Copy   

•   Source: SciCrunch Registry

Ratings or validation data are available for this resource

http://www.ingenuity.com/products/pathways_analysis.html

A web-based software application that enables users to analyze, integrate, and understand data derived from gene expression, microRNA, and SNP microarrays, metabolomics, proteomics, and RNA-Seq experiments, and small-scale experiments that generate gene and chemical lists. Users can search for targeted information on genes, proteins, chemicals, and drugs, and build interactive models of experimental systems. IPA allows exploration of molecular, chemical, gene, protein and miRNA interactions, creation of custom molecular pathways, and the ability to view and modify metabolic, signaling, and toxicological canonical pathways. In addition to the networks and pathways that can be created, IPA can provide multiple layering of additional information, such as drugs, disease genes, expression data, cellular functions and processes, or a researchers own genes or chemicals of interest.

Proper citation: Ingenuity Pathway Analysis (RRID:SCR_008653) Copy   

•   Source: SciCrunch Registry

http://rebase.neb.com/rebase/

Database of information about restriction enzymes and related proteins containing published and unpublished references, recognition and cleavage sites, isoschizomers, commercial availability, methylation sensitivity, crystal, genome, and sequence data. DNA methyltransferases, homing endonucleases, nicking enzymes, specificity subunits and control proteins are also included. Several tools are available including REBsites, BLAST against REBASE, NEBcutter and REBpredictor. Putative DNA methyltransferases and restriction enzymes, as predicted from analysis of genomic sequences, are also listed. REBASE is updated daily and is constantly expanding. Users may submit new enzyme and/or sequence information, recommend references, or send them corrections to existing data. The contents of REBASE may be browsed from the web and selected compilations can be downloaded by ftp (ftp.neb.com). Additionally, monthly updates can be requested via email.,

Proper citation: REBASE (RRID:SCR_007886) Copy   

•   Source: SciCrunch Registry

http://medblast.sibsnet.org/

THIS RESOURCE IS NO LONGER IN SERVICE, documented August 29, 2016. An algorithm that finds articles most relevant to a genetic sequence. In the genomic era, researchers often want to know more information about a biological sequence by retrieving its related articles. However, there is no available tool yet to achieve conveniently this goal. Here, a new literature-mining tool MedBlast is developed, which uses natural language processing techniques, to retrieve the related articles of a given sequence. An online server of this program is also provided. The genome sequencing projects generate such a large amount of data every day that many molecular biologists often encounter some sequences that they know nothing about. Literature is usually the principal resource of such information. It is relatively easy to mine the articles cited by the sequence annotation; however, it is a difficult task to retrieve those relevant articles without direct citation relationship. The related articles are those described in the given sequence (gene/protein), or its redundant sequences, or the close homologs in various species. They can be divided into two classes: direct references, which include those either cited by the sequence annotation or citing the sequence in its text; indirect references, those which contain gene symbols of the given sequence. A few additional issues make the task even more complicated: (1) symbols may have aliases; and (2) one sequence may have a couple of relatives that we want to take into account too, which include redundant (e.g. protein and gene sequences) and close homologs. Here the issues are addressed by the development of the software MedBlast, which can retrieve the related articles of the given sequence automatically. MedBlast uses BLAST to extend homology relationships, precompiled species-specific thesauruses, a useful semantics technique in natural language processing (NLP), to extend alias relationship, and EUtilities toolset to search and retrieve corresponding articles of each sequence from PubMed. MedBlast take a sequence in FASTA format as input. The program first uses BLAST to search the GenBank nucleic acid and protein non-redundant (nr) databases, to extend to those homologous and corresponding nucleic acid and protein sequences. Users can input the BLAST results directly, but it is recommended to input the result of both protein and nucleic acid nr databases. The hits with low e-values are chosen as the relatives because the low similarity hits often do not contain specific information. Very long sequences, e.g. 100k, which are usually genomic sequences, are discarded too, for they do not contain specific direct references. User can adjust these parameters to meet their own needs.

Proper citation: MedBlast (RRID:SCR_008202) Copy   

•   Source: SciCrunch Registry

http://www.poissonboltzmann.org/apbs/

APBS is a software package for modeling biomolecular solvation through solution of the Poisson-Boltzmann equation (PBE), one of the most popular continuum models for describing electrostatic interactions between molecular solutes in salty, aqueous media. APBS was designed to efficiently evaluate electrostatic properties for such simulations for a wide range of length scales to enable the investigation of molecules with tens to millions of atoms. It also provides implicit solvent models of nonpolar solvation which accurately account for both repulsive and attractive solute-solvent interactions. APBS uses FEtk (the Finite Element ToolKit) to solve the Poisson-Boltzmann equation numerically. FEtk is a portable collection of finite element modeling class libraries written in an object-oriented version of C. It is designed to solve general coupled systems of nonlinear partial differential equations using adaptive finite element methods, inexact Newton methods, and algebraic multilevel methods.

Proper citation: Adaptive Poisson-Boltzmann Solver (RRID:SCR_008387) Copy   

•   Source: SciCrunch Registry

http://www.jcsg.org/

The JCSG is a multi-institutional consortium that aims to explore the expanding protein universe to find new challenges and opportunities to significantly contribute to new biology, chemistry and medicine through development of HT approaches to structural genomics. The mission of JCSG is to to operate a robust HT protein structure determination pipeline as a large-scale production center for PSI-2. A major goal is to ensure that innovative high-throughput approaches are developed that advance not only structural genomics, but also structural biology in general, via investigation of large numbers of high-value structures that populate protein fold and family space and by increasing the efficiency of structure determination at substantially reduced cost. The JCSG centralizes each core activity into single dedicated sites, each handling distinct, but interconnected objectives. This unique approach allows each specialized group to focus on its own area of expertise and provides well-defined interfaces among the groups. In addition, this approach addresses the requirements for the scalability needed to process large numbers of targets at a greatly reduced cost per target. JCSG production groups are: - Administrative Core - Bioinformatics Core - Crystallomics Core - Structure Determination Core - NMR Core JCSG is deeply committed to the development of new technologies that facilitate high throughput structural genomics. The areas of development include hardware, software, new experimental methods, and adaptation of existing technologies to advance genome research. In the hardware arena, their commitment is to the development of technologies that accelerate structure solution by increasing throughput rates at every stage of the production pipeline. Therefore, one major area of hardware development has been the implementation of robotics. In the software arena, they have developed enterprise resource software that track success, failures, and sample histories from target selection to PDB deposition, annotation and target management tools, and helper applications aimed at facilitating and automating multiple steps in the pipeline. Sponsors: The Joint Center for Structural Genomics is funded by the National Institute of General Medical Sciences (NIGMS), as part of the second phase of the Protein Structure Initiative (PSI) of the National Institutes of Health (U54 GM074898).

Proper citation: Joint Center for Structural Genomics (RRID:SCR_008251) Copy   

•   Source: SciCrunch Registry

http://weizhong-lab.ucsd.edu/cd-hit-otu/

Data analysis service and software program that perform Operantional Taxonomic Units (OTUs) finding. It uses a three-step clustering for identifying OTUs. The first-step clustering is raw read filtering and trimming. The second step is error-free reads picking.. At the last step, OTU clustering is done at different distanct cutoffs (0.01, 0.02, 0.03... 0.12).

Proper citation: CD-HIT-OTU (RRID:SCR_006983) Copy   

•   Source: SciCrunch Registry

http://bioinformatics.albany.edu/~dmaps

THIS RESOURCE IS NO LONGER IN SERVCE, documented September 6, 2016. DMAPS database contains pre-computed multiple structure alignments for protein chains in the Protein Data Bank (PDB). Automated structure alignments have been generated for classified protein families using CE-MC algorithm. Alignments have been built only for those families with at least three members. Currently, multiple structure alignments are available for 3050 SCOP-, 3087 CATH-, 664 ENZYME- and 1707 CE-based families. Users will be able to retrieve multiple alignments for a given PDB chain classified by one of these criteria.

Proper citation: DMAPS - A Database of Multiple Alignments for Protein Structures (RRID:SCR_007140) Copy   

•   Source: SciCrunch Registry

http://tango.crg.es/

A computer algorithm to predict aggregation nucleating regions in proteins as well the effect of mutations and environmental conditions on the aggregation propensity of these regions.

Proper citation: TANGO (RRID:SCR_001770) Copy   

•   Source: SciCrunch Registry

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   

•   Source: SciCrunch Registry