This is an application requesting funds to purchase a Q Exactive mass spectrometer and liquid chromatography system that will be used for quantitative proteomics research. The instrument will be integrated into the Robert Wood Johnson Medical School/Rutgers University Biological Mass Spectrometry Facility. Current instrumentation in the Facility is used at maximal capacity and we require additional capabilities to conduct quantitative proteomics experiments for thirteen NIH-funded investigators. Our user group will apply quantitative mass spectrometry to most efficiently address a wide range of important biomedical research areas including neurological disease, bacterial and viral infection, cancer, anaphylaxis, diabetes, digestive disease, and sleep disorders. Specific experiments include quantification of changes in levels and post-translational modifications of clock proteins throughout the circadian cycle, a systems biology approach to understand the lysosome and its role in human neurodegenerative disease, persistence of epitopes on protein food allergens under conditions that simulate gastric digestion, dynamics of post- translational modification of tumor suppressors during oncogenesis and analysis of pathogen-host interactions at different stages in their life cycle for hepatitis C virus, retroviruses, and chlamydia.. The requested instrument will therefore represent a significant asset to our research community and will accelerate the pace of basic and applied NIH-funded health-research at Rutgers University and the Robert Wood Johnson Medical School of UMDNJ.
This is a proposal requesting funds to acquire a specialized mass spectrometer that will be used for projects being conducted by thirteen NIH-supported investigators. The availability of this instrument will accelerate the pace of basic and applied biomedical research into important areas including neurological disease, bacterial and viral infection, sleep disorders, diabetes, food allergies and cancer.
|Cai, Na; Bai, Zhiyong; Nanda, Vikas et al. (2017) Mass Spectrometric Analysis of TRPM6 and TRPM7 Phosphorylation Reveals Regulatory Mechanisms of the Channel-Kinases. Sci Rep 7:42739|
|Wang, Mengjun; Comunale, Mary Ann; Herrera, Harmin et al. (2016) Identification of IgM as a contaminant in lectin-FLISA assays for HCC detection. Biochem Biophys Res Commun 476:140-5|
|Yue, Xuetian; Zhao, Yuhan; Huang, Grace et al. (2016) A novel mutant p53 binding partner BAG5 stabilizes mutant p53 and promotes mutant p53 GOFs in tumorigenesis. Cell Discov 2:16039|
|Tu, Shengjiang; Narendra, Varun; Yamaji, Masashi et al. (2016) Co-repressor CBFA2T2 regulates pluripotency and germline development. Nature 534:387-90|
|Li, Minxing; Cole, Francesca; Patel, Dharm S et al. (2016) 53BP1 ablation rescues genomic instability in mice expressing 'RING-less' BRCA1. EMBO Rep 17:1532-1541|
|Ma, Xiqing; Xu, Qian; Meyer, William A et al. (2016) Hormone regulation of rhizome development in tall fescue (Festuca arundinacea) associated with proteomic changes controlling respiratory and amino acid metabolism. Ann Bot 118:481-94|
|Zhang, Cen; Liu, Juan; Huang, Grace et al. (2016) Cullin3-KLHL25 ubiquitin ligase targets ACLY for degradation to inhibit lipid synthesis and tumor progression. Genes Dev 30:1956-70|
|Zhang, Cen; Liu, Juan; Zhao, Yuhan et al. (2016) Glutaminase 2 is a novel negative regulator of small GTPase Rac1 and mediates p53 function in suppressing metastasis. Elife 5:e10727|
|Mehta, Anand; Comunale, Mary Ann; Rawat, Siddhartha et al. (2016) Intrinsic hepatocyte dedifferentiation is accompanied by upregulation of mesenchymal markers, protein sialylation and core alpha 1,6 linked fucosylation. Sci Rep 6:27965|
|Campos, Eric I; Smits, Arne H; Kang, Young-Hoon et al. (2015) Analysis of the Histone H3.1 Interactome: A Suitable Chaperone for the Right Event. Mol Cell 60:697-709|
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