1. Lcms.nymc.edu - Mutawakkil
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Lcms.nymc.edu - No Description
2. Biomarker selection and a prospective metabolite-based machine ... - NCBI
27 jan 2022 · ... (LCMS) serum samples to generate a prospective diagnostic test for Lyme disease. ... NYMC and healthy control samples obtained from NYMC and Tufts.
We provide a pipeline for data preprocessing, biomarker selection, and classification of liquid chromatography–mass spectrometry (LCMS) serum samples to generate a prospective diagnostic test for Lyme disease. We utilize tools of machine learning ...
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8 nov 2020 · ℹ️ . Check Lcms.nymc traffic estimations, technology used, hosting and owner info. Full analysis about lcms.nymc.edu.
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4. [PDF] NYMC Synapse Volume 1 Issue 1 - Touro Scholar
A brand new newsletter for medical students to keep up to date on the happenings in and around NYMC! Including news from the. Student Senate, Medical. Education ...
5. Summary of Study ST001223 - Metabolomics Workbench
Project Summary: LC-MS metabolomics analyses of early Lyme disease patient sera to identify host metabolic pathways altered from healthy ...
About the Metabolomics Workbench: The National Institutes of Health (NIH) Common Fund Metabolomics Program was developed with the goal of increasing national capacity in metabolomics by supporting the development of next generation technologies, providing training and mentoring opportunities, increasing the inventory and availability of high quality reference standards, and promoting data sharing and collaboration. In support of this effort, the Metabolomics Program's Data Repository and Coordinating Center (DRCC), housed at the San Diego Supercomputer Center (SDSC), University of California, San Diego, has developed the Metabolomics Workbench. The Metabolomics Workbench will serve as a national and international repository for metabolomics data and metadata and will provide analysis tools and access to metabolite standards, protocols, tutorials, training, and more.
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7. Research | Touro University California
The Mass Spectrometry Core is equipped with three GC-MS instruments and one triple quadrupole LC-MS/MS instrument. ... New York Medical College Chartered 1860.
Our faculty and students work together across programs, centers and colleges to conduct research in medicine, education, public health, and pharmacy.
8. Analyses of Lipid Autacoids in Human Corneas by LC/MS/MS-Based ...
Pharmacology and Ophthalmology, New York Medical College, Valhalla, New York ... Extracted samples were analyzed by a triple quadruple linear ion trap LC/MS/MS ...
9. Topological N-glycosylation and site-specific N-glycan sulfation of ...
31 aug 2017 · Bucher's laboratory at the New York Medical College (NYMC) or a ... LC-MS or offline solid phase extraction with PGC cartridges ...
The outbreak of a pandemic influenza H1N1 in 2009 required the rapid generation of high-yielding vaccines against the A/California/7/2009 virus, which were achieved by either addition or deletion of a glycosylation site in the influenza proteins hemagglutinin and neuraminidase. In this report, we have systematically evaluated the glycan composition, structural distribution and topology of glycosylation for two high-yield candidate reassortant vaccines (NIBRG-121xp and NYMC-X181A) by combining various enzymatic digestions with high performance liquid chromatography and multiple-stage mass spectrometry. Proteomic data analyses of the full-length protein sequences determined 9 N-glycosylation sites of hemagglutinin, and defined 6 N-glycosylation sites and the glycan structures of low abundance neuraminidase, which were occupied by high-mannose, hybrid and complex-type N-glycans. A total of ~300 glycopeptides were analyzed and manually validated by tandem mass spectrometry. The specific N-glycan structure and topological location of these N-glycans are highly correlated to the spatial protein structure and the residential ligand binding. Interestingly, sulfation, fucosylation and bisecting N-acetylglucosamine of N-glycans were also reliably identified at the specific glycosylation sites of the two influenza proteins that may serve a crucial role in regulating the protein structure and increasing the protein abundance of the influenza virus reassortants.
