Our plan is to establish a P41 Research Resource focused on serving the NIH-supported biomedical research community by developing and integrating new proteomic technologies for collaborative and service studies, disseminating the new technologies, and training scientists in their use. Technological developments within the Resource will contribute significant advances to the efforts of prominent collaborative researchers in the areas of microbial pathogenicity and trauma research, chronic virulent infections, and mammary and melanoma oncology. The ability to precisely measure levels of nearly all expressed proteins and their modified forms can provide new insights into the molecular nature of cells, cell signaling pathways and networks, the cell cycle, cellular differentiation, and other processes relevant to human health and to the progression of various disease states. The ability to characterize protein complexes complements this capability and allows hypotheses to be tested and the biological system operation to be defined. Primary objectives of the Resource are to develop and apply an integrated set of biological methods, new analytical technologies, and associated computational and informatics tools for much more rapid, quantitative, sensitive, and comprehensive proteomic measurements than presently possible; and to facilitate the dissemination of these new technologies to the biomedical research community. Our planned technological developments also aim at providing new capabilities for the characterization of protein modifications and the quantitation of protein abundances spanning more than six orders of magnitude. These fundamental developments will be augmented by 1) capabilities for high throughput isolation of protein complexes needed to obtain better information on protein interactions and to test proteomic hypotheses, and 2) computational and bio-informatics tools needed to effectively extract and visualize data with statistically sound measures of quality to aid in development of new biological understandings. Resource technology developments are directed at challenging proteomic investigations, in collaborations selected on the basis of their scientific and biomedical relevance, as well as their capacity to benefit from the Resource's capabilities and challenge the core technology. The Resource will leverage and extend the substantial capabilities already established in the Environmental Molecular Sciences Laboratory that presently include a collaboratory infrastructure, an integrated and multi-disciplinary scientific team, unique mass spectrometric instrumentation, and a powerful suite of proteome data management and analysis tools.

National Institute of Health (NIH)
National Center for Research Resources (NCRR)
Biotechnology Resource Grants (P41)
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Special Emphasis Panel (ZRG1-BECM (40))
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Sheeley, Douglas
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Battelle Pacific Northwest Laboratories
United States
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Smallwood, Heather S; Duan, Susu; Morfouace, Marie et al. (2017) Targeting Metabolic Reprogramming by Influenza Infection for Therapeutic Intervention. Cell Rep 19:1640-1653
Wang, Hui; Barbieri, Christopher E; He, Jintang et al. (2017) Quantification of mutant SPOP proteins in prostate cancer using mass spectrometry-based targeted proteomics. J Transl Med 15:175
Sigdel, Tara K; Gao, Yuqian; He, Jintang et al. (2016) Mining the human urine proteome for monitoring renal transplant injury. Kidney Int 89:1244-52
Webb-Robertson, Bobbie-Jo M; Wiberg, Holli K; Matzke, Melissa M et al. (2015) Review, evaluation, and discussion of the challenges of missing value imputation for mass spectrometry-based label-free global proteomics. J Proteome Res 14:1993-2001
Ibrahim, Yehia M; Baker, Erin S; Danielson 3rd, William F et al. (2015) Development of a New Ion Mobility (Quadrupole) Time-of-Flight Mass Spectrometer. Int J Mass Spectrom 377:655-662
Ream, Thomas S; Haag, Jeremy R; Pontvianne, Frederic et al. (2015) Subunit compositions of Arabidopsis RNA polymerases I and III reveal Pol I- and Pol III-specific forms of the AC40 subunit and alternative forms of the C53 subunit. Nucleic Acids Res 43:4163-78
Malouli, Daniel; Hansen, Scott G; Nakayasu, Ernesto S et al. (2014) Cytomegalovirus pp65 limits dissemination but is dispensable for persistence. J Clin Invest 124:1928-44
Cox, Jonathan T; Marginean, Ioan; Kelly, Ryan T et al. (2014) Improving the sensitivity of mass spectrometry by using a new sheath flow electrospray emitter array at subambient pressures. J Am Soc Mass Spectrom 25:2028-37
Cao, Li; Toli?, Nikola; Qu, Yi et al. (2014) Characterization of intact N- and O-linked glycopeptides using higher energy collisional dissociation. Anal Biochem 452:96-102
Martin, Jessica L; Yates, Phillip A; Soysa, Radika et al. (2014) Metabolic reprogramming during purine stress in the protozoan pathogen Leishmania donovani. PLoS Pathog 10:e1003938

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