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http://www.cgl.ucsf.edu/

Biomedical technology resource center that develops software and web-based resources for the visualization and analysis of molecular structure, and related data, at scales ranging from the atomic to the supramolecular. They create tools for handling and integrating diverse types of biomolecular data, including atomic-resolution coordinates, density maps, sequences, annotations, and networks. Their primary efforts are in the visualization and analysis of structures of molecules and molecular assemblies, enzyme sequence-structure-function relationships, and network representations of protein similarity, binding interactions, and biological pathways. They provide technologies to enable identifying the molecular bases of disease and phenotypic variation, annotating proteins of unknown function, identifying targets for drug development, designing drugs, and engineering proteins with new functions. RBVI distributes software tools, including the popular UCSF Chimera visualization and analysis package, develops and hosts the Structure-Function Linkage Database, and provides access to state-of-the-art computational resources in support of research projects in these areas.

Proper citation: Resource for Biocomputing Visualization and Informatics (RRID:SCR_001374) Copy   

•   Source: SciCrunch Registry

https://ncxt.org/

Biomedical technology research center that develops novel cellular imaging technologies, specifically soft X-ray tomography, for visualizing and quantifying the internal structure of whole, hydrated cells, and high-numerical aperture fluorescence microscopy for locating the position of specific cellular molecules. Data from these two imaging modalities can be combined to form a single, correlated imaging view of a cell.

Proper citation: National Center for X-ray Tomography (RRID:SCR_001433) Copy   

•   Source: SciCrunch Registry

http://rlbl.chem.upenn.edu

Biomedical technology research center and training resource that develops time-resolved laser technologies and instrumentation, with a focus on 2-D IR spectroscopy. The technologies enable atomic-level measurements of the fastest steps in biological processes to elucidate structure and dynamics in biological macromolecules, assemblies and cells. The Center makes most of its instrumentation available for service research projects to outside users nation-wide.

Proper citation: Ultrafast Optical Processes Laboratory (RRID:SCR_006582) Copy   

•   Source: SciCrunch Registry

http://necat.chem.cornell.edu/

Biomedical technology research center for macromolecular crystallography at Sector 24 of the Advanced Photon Source at Argonne National Laboratory. The macromolecules studied by resource users often involve large unit cells, small crystals, weakly diffracting crystals and crystals with weak anomalous scattering. Technological research includes use of silicon monochromators, focusing optics, methods of phase determination, radiation damage, X-ray detectors, automated sample mounting, microdiffraction and crystallographic software.

Proper citation: Northeastern Collaborative Access Team (RRID:SCR_008999) Copy   

•   Source: SciCrunch Registry

http://www.mc.vanderbilt.edu/root/vumc.php?site=ims

Biomedical technology research center that advances the technology of Imaging Mass Spectrometry, facilitates the application of this novel imaging modality to problems of biological and clinical significance, and promotes the adoption of these technologies by a larger community of scientists and clinicians. Technical innovations include next-generation hardware, software and methods. Technology development is conducted by an interdisciplinary team of scientists and engineers, both within the Resource and through collaborative relationships with other universities, research institutes, and private industry. Development milestones are guided by Driving Biological Projects that require specific advancements in Imaging Mass Spectrometry in order to address biological problems. By working together, they anticipate new insights into these biological systems and a better understanding of health and disease at the molecular level that translates to improved patient care. The training mission of the Resource is accomplished through a variety of educational programs where Resource scientists and collaborators share their knowledge and experience with those interested in learning more about the technology.

Proper citation: VU National Research Resource for Imaging Mass Spectrometry (RRID:SCR_006904) Copy   

•   Source: SciCrunch Registry

http://www.nrcam.uchc.edu/

Biomedical technology research center that develops new technologies for modeling cell biological processes. The technologies are integrated through Virtual Cell, a problem-solving environment built on a central database and disseminated as a Web application for the analysis, modeling and simulation of cell biological processes. NRCAM resides at the Center for Cell Analysis and Modeling, CCAM, and provides a vast array of laboratory equipment that can be used for obtaining experimental data needed to create and enhance Virtual Cell models. Microscopy instrumentation includes three confocal laser scanning microscopes including UV excitation, nonlinear optical microscopy utilizing a titanium sapphire pulsed laser, confocal-based fluorescence correlation spectroscopy, wide-field imaging workstation with cooled CCD and rapid excitation filter wheel, and dual-wavelength spectrofluorometer. Access to the facilities and technical staff is open to all researchers., THIS RESOURCE IS NO LONGER IN SERVICE. Documented on September 16,2025.

Proper citation: NRCAM (RRID:SCR_006134) Copy   

•   Source: SciCrunch Registry

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   

•   Source: SciCrunch Registry

http://mmbios.org/

Biomedical technology research center that develops and makes available to the scientific community high performance computing algorithms, tools and software to leverage modeling efforts at disparate scales of structural biology, cellular microphysiology and large-scale bioimage processing and analysis, with the goal of advancing understanding of the molecular and cellular organization and functional mechanisms that underlie synaptic signaling and regulation.

Proper citation: National Center for Multiscale Modeling of Biological Systems (RRID:SCR_009005) Copy   

•   Source: SciCrunch Registry

http://msf.ucsf.edu/

Provides high-performance tandem mass spectrometry and proteomics, including multiplexed quantitative comparative analysis of protein and post-translational modifications, and a suite of tools for the analysis of mass spectrometry proteomics data. It provides both scientific and technical expertise and state-of-the-art high-performance, tandem mass spectrometric instrumentation. The facility also provides a service for small molecule analysis. Significant instrumentation in the facility includes three QSTAR quadrupole orthogonal time of flight instruments, and both an LTQ-Orbitrap platform with electron transfer dissociation (ETD) and an LTQ-FT linear ion trap FT-ICR instrument equipped with the ability to perform electron capture dissociation (ECD). The Center also has a 4700 Proteomic Analyzer MALDI tandem time of flight instrument; as well as a QTRAP 5500 hybrid triple quadrupole linear ion trap instrument; and a Thermo Fisher LTQ Orbitrap Velos. Major research focuses within the Center are the analysis of post-translational modifications, including phosphorylation and O-GlcNAcylation and development of methods for quantitative comparative analysis of protein and post-translational modification levels. The program also continues to develop one of the leading suites of tools for analysis of mass spectrometry proteomics data, Protein Prospector. The current web-based release allows unrestricted searching of MS and MSMS data, as well as the ability to perform comparative quantitative analysis of samples using isotopic-labeling reagents. It is the only freely-available web-based resource that allows this type of analysis.

Proper citation: National Bio-Organic Biomedical Mass Spectrometry Resource Center (RRID:SCR_009004) Copy   

•   Source: SciCrunch Registry

http://scicrunch.org/resources

Portal providing identifiers for Antibodies, Model Organisms, and Tools (software, databases, services) created in support of the Resource Identification Initiative, which aims to promote research resource identification, discovery, and reuse. The portal offers a central location for obtaining and exploring Research Resource Identifiers (RRIDs) - persistent and unique identifiers for referencing a research resource. A critical goal of the RII is the widespread adoption of RRIDs to cite resources in the biomedical literature and other places that reference their generation or use. RRIDs use established community identifiers where they exist, and are cross-referenced in their system where more than one identifier exists for a single resource.

Proper citation: Resource Identification Portal (RRID:SCR_004098) Copy   

•   Source: SciCrunch Registry

http://publications.nigms.nih.gov/insidelifescience/

The NIGMS Inside Life Science series brings you inside the science of health. Each story shows how basic biomedical researchfrom the history of a field to the people doing cutting-edge work todaylays the foundation for advances in disease diagnosis, treatment and prevention. Through explorations of how the body works and highlights from recent studies, you''ll discover even more on what scientists have found and are finding about fundamental life processes. NIGMS supported all of the featured research.

Proper citation: NIGMS Inside Life Science (RRID:SCR_005852) Copy   

•   Source: SciCrunch Registry

http://compbio.cs.princeton.edu/conservation/

Software for scoring protein sequence conservation using the Jensen-Shannon divergence. It can be used to predict catalytic sites and residues near bound ligands.

Proper citation: Conservation (RRID:SCR_016064) Copy   

•   Source: SciCrunch Registry

https://sourceforge.net/projects/saint-apms/files/

Software tool for upgraded implementation of probabilistic scoring of affinity purification mass spectrometry data. Used for filtering high confidence interaction data from affinity purification mass spectrometry experiments. Used for assigning confidence scores to protein-protein interactions based on quantitative proteomics data in AP-MS experiments.

Proper citation: SAINTexpress (RRID:SCR_018562) Copy   

•   Source: SciCrunch Registry

http://www.pyrosetta.org/

Interactive Python based interface to Rosetta molecular modeling suite. Stand alone Python based implementation of Rosetta molecular modeling package that allows users to write custom structure prediction and design algorithms using major Rosetta sampling and scoring functions.

Proper citation: PyRosetta (RRID:SCR_018541) Copy   

•   Source: SciCrunch Registry

https://psbweb05.psb.ugent.be/conet/microbialnetworks/spieceasi.php

Software R package estimates inverse covariance matrix from sequencing data.Statistical method for inference of microbial ecological networks from amplicon sequencing datasets.

Proper citation: Sparse Inverse Covariance Estimation for Ecological Association Inference (RRID:SCR_022646) Copy   

•   Source: SciCrunch Registry

https://cran.r-project.org/web/packages/BGLR/

Software R package implements large collection of Bayesian regression models, including parametric variable selection and shrinkage methods and semiparametric procedures.

Proper citation: Bayesian Generalized Linear Regression (RRID:SCR_022522) Copy   

•   Source: SciCrunch Registry

http://www.montana.edu/massspec/index.html

Provides access to mass spectrometers and mass spectrometry expertise. The facility currently maintains the following equipment Waters Synapt-XS Q-IMS-TOF with Waters I-Class UHPLC; Agilent 6538 Q-TOF with Agilent 1290 UHPLC;Agilent 7800 Inductively Coupled Plasma with Laser Ablation (193 nm);Bruker micrOTOF with Agilent 1290 UHPLC; Agilent 6490 Triple Quadrupole Mass Spectrometer; Bruker MALDI Autoflex; Agilent GC-MS; Waters Synapt G2S-i Q-TOF with Ion Mobility.

Proper citation: Montana State University Mass Spectrometry Core Facility (RRID:SCR_012482) Copy   

•   Source: SciCrunch Registry

https://flowcore.hsc.wvu.edu/

Facility provides instrumentation and scientific support for single cell analysis and sorting. Routinely performs analysis of both eukaryotic and prokaryotic cells for expression of intracellular and extracellular proteins, cell cycle, cell proliferation, cytokine production, and cell sorting based on expression of cell surface antigen(s) and/or expression of genetically engineered intercellular fluorescent proteins.

Proper citation: West Virginia University Flow Cytometry and Single Cell Core Facility (RRID:SCR_017738) Copy   

•   Source: SciCrunch Registry

https://mbim.uams.edu/research-cores/flow-cytometry-core-facility/

Core provides flow cytometry instrumentation and analysis. Instruments include Fortessa, FacsAria and Image Stream.

Proper citation: Arkansas University College of Medicine Flow Cytometry Core Facility (RRID:SCR_017741) 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