The overall goals of the Collaboration and Service Core (C&S) are to provide non-specialists with access to MS technologies, software, methods, technical expertise and support developed in the Washington University (WU) Biomedical Mass Spectrometry (MS) Resource, and to provide experienced investigators with shared access to MS instrumentation and software so they can independently conduct sample analyses. Requests for C&S projects are evaluated by the Operational Team and selected based on established criteria. Completed, ongoing, and new C&S projects are evaluated for impact based on publications/productivity; tracked to document efficient MS instrument utilization; and monitored to insure that MS Resources are shared equitably with WU and outside users who acknowledge the contributions of the WU Biomedical MS Resource and comply with NIH public access policies.

Public Health Relevance

-Public Health Relevance. The Washington University Biomedical Mass Spectrometry Resource has a longstanding history as an active and productive citizen in the NIH Biotechnology Research Resources community. We propose to extend our mission by advancing mass spectrometry technology, development, and research, applying these discoveries to answer critical biomedical research questions, and training the next generation of researchers, towards the ultimate goal of improving public health.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Biotechnology Resource Grants (P41)
Project #
5P41GM103422-40
Application #
9199439
Study Section
Special Emphasis Panel (ZRG1-IMST-B)
Project Start
Project End
Budget Start
2017-01-01
Budget End
2017-12-31
Support Year
40
Fiscal Year
2017
Total Cost
$86,365
Indirect Cost
$29,732
Name
Washington University
Department
Type
Domestic Higher Education
DUNS #
068552207
City
Saint Louis
State
MO
Country
United States
Zip Code
63130
Keul, Nicholas D; Oruganty, Krishnadev; Schaper Bergman, Elizabeth T et al. (2018) The entropic force generated by intrinsically disordered segments tunes protein function. Nature 563:584-588
Goldner, Nicholas K; Bulow, Christopher; Cho, Kevin et al. (2018) Mechanism of High-Level Daptomycin Resistance in Corynebacterium striatum. mSphere 3:
Zhang, Bojie; Cheng, Ming; Rempel, Don et al. (2018) Implementing fast photochemical oxidation of proteins (FPOP) as a footprinting approach to solve diverse problems in structural biology. Methods 144:94-103
Su, Zhaoming; Wu, Chao; Shi, Liuqing et al. (2018) Electron Cryo-microscopy Structure of Ebola Virus Nucleoprotein Reveals a Mechanism for Nucleocapsid-like Assembly. Cell 172:966-978.e12
Zhang, Mengru Mira; Rempel, Don L; Gross, Michael L (2018) A Fast Photochemical Oxidation of Proteins (FPOP) platform for free-radical reactions: the carbonate radical anion with peptides and proteins. Free Radic Biol Med 131:126-132
Shen, G; Li, S; Cui, W et al. (2018) Stabilization of warfarin-binding pocket of VKORC1 and VKORL1 by a peripheral region determines their different sensitivity to warfarin inhibition. J Thromb Haemost 16:1164-1175
Lu, Yue; Goodson, Carrie; Blankenship, Robert E et al. (2018) Primary and Higher Order Structure of the Reaction Center from the Purple Phototrophic Bacterium Blastochloris viridis: A Test for Native Mass Spectrometry. J Proteome Res 17:1615-1623
Fernandez, Estefania; Kose, Nurgun; Edeling, Melissa A et al. (2018) Mouse and Human Monoclonal Antibodies Protect against Infection by Multiple Genotypes of Japanese Encephalitis Virus. MBio 9:
Johnson, Britney; VanBlargan, Laura A; Xu, Wei et al. (2018) Human IFIT3 Modulates IFIT1 RNA Binding Specificity and Protein Stability. Immunity 48:487-499.e5
Girard, T J; Grunz, K; Lasky, N M et al. (2018) Re-evaluation of mouse tissue factor pathway inhibitor and comparison of mouse and human tissue factor pathway inhibitor physiology. J Thromb Haemost 16:2246-2257

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