This proposal is a competing renewal for the NIGMS P41 National Center for Biomedical Glycomics. Glycomics can be defined in several ways, but in terms of our Center, we define Glycomics as the study of glycans, glycoconjugates, the proteins that regulate their expression, and the proteins that recognize them;in particular, we are interested in developing tools to facilitate learning how these molecules change during early embryonic development and during the onset of disease as a result of mutations that affect glycan expression. To develop technologies that will impact the understanding and regulation of the diversity of glycosylation, therefore, we felt it necessary to focus on Glycomics from more of a Systems Biology approach: investigation of glycosylation in a particular biological context, analysis of the fine details of glycan expression on glycoconjugates produced in specific cell types, identification of the glyco-genes that participate in glycan biosynthesis and the biosynthetic pathways that the enzymes and transporters expressed from the glyco-genes constitute. The structure of the Resource is focused on four Technological Research &Development programs plus Analytical Service and Training: TR&D1: Stem Cell and Induced Pluripotent Stem Cell (IPSC) Resources;TR&D2: Glycomics and Glycoproteomics;TR&D3: Transcriptome and Glycome Regulation;TR&D4: Glycobioinformatics. Our Center lists 31 DBPs, 73 Collaborative Projects, 192 Service projects, and four Courses/Workshops that have had 245 participants over the last four years. We also report 83 publications resulting from research associated with the Center. We have developed technologies in each of our TR&D that have significantly impacted the biomedical research community, and our over-arching goal is to amplify that impact over the next funding period.
The study of Glycomics is in its early stages and is very dependent on the development of tools and technologies. Glycomics involves types of molecules called glycans that are on the surfaces of cells which regulate many physiological processes such as inflammation and innate immunity. We have developed tools to assist biomedical researchers in understanding the structure and functions of these fascinating biomolecules.
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|Teo, Chin Fen; Wells, Lance (2014) Monitoring protein O-linked ?-N-acetylglucosamine status via metabolic labeling and copper-free click chemistry. Anal Biochem 464:70-2|
|Cummings, Richard D; Pierce, J Michael (2014) The challenge and promise of glycomics. Chem Biol 21:1-15|
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|Praissman, Jeremy L; Live, David H; Wang, Shuo et al. (2014) B4GAT1 is the priming enzyme for the LARGE-dependent functional glycosylation of ?-dystroglycan. Elife 3:|
|Zhang, Liping; Syed, Zulfeqhar Ali; van Dijk Härd, Iris et al. (2014) O-glycosylation regulates polarized secretion by modulating Tango1 stability. Proc Natl Acad Sci U S A 111:7296-301|
|Dolezal, Samuel; Hester, Shanterian; Kirby, Pamela S et al. (2014) Elevated levels of glycosylphosphatidylinositol (GPI) anchored proteins in plasma from human cancers detected by C. septicum alpha toxin. Cancer Biomark 14:55-62|
|Katayama, Toshiaki; Wilkinson, Mark D; Aoki-Kinoshita, Kiyoko F et al. (2014) BioHackathon series in 2011 and 2012: penetration of ontology and linked data in life science domains. J Biomed Semantics 5:5|
|Praissman, Jeremy L; Wells, Lance (2014) Mammalian O-mannosylation pathway: glycan structures, enzymes, and protein substrates. Biochemistry 53:3066-78|
|Wang, SuiKang; Xu, YanXia; Li, ZhiLan et al. (2014) OsMOGS is required for N-glycan formation and auxin-mediated root development in rice (Oryza sativa L.). Plant J 78:632-45|
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