M
Michael A. Demetriou
Researcher at Worcester Polytechnic Institute
Publications - 353
Citations - 9163
Michael A. Demetriou is an academic researcher from Worcester Polytechnic Institute. The author has contributed to research in topics: Distributed parameter system & Actuator. The author has an hindex of 41, co-authored 335 publications receiving 8170 citations. Previous affiliations of Michael A. Demetriou include Mount Sinai Hospital & California Institute of Technology.
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Journal ArticleDOI
Negative regulation of T-cell activation and autoimmunity by Mgat5 N -glycosylation
TL;DR: It is demonstrated that a deficiency in β1,6 N-acetylglucosaminyltransferase V (Mgat5), an enzyme in the N-glycosylation pathway, lowers T-cell activation thresholds by directly enhancing TCR clustering.
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Complex N-Glycan Number and Degree of Branching Cooperate to Regulate Cell Proliferation and Differentiation
Ken S. Lau,Ken S. Lau,Emily A. Partridge,Emily A. Partridge,Ani Grigorian,Cristina I. Silvescu,Vernon N. Reinhold,Michael A. Demetriou,James W. Dennis,James W. Dennis +9 more
TL;DR: Computational and experimental data reveal that features allow nutrient flux stimulated by growth-promoting high-n receptors to drive arrest/differentiation programs by increasing surface levels of low-n glycoproteins.
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Metabolism, Cell Surface Organization, and Disease
TL;DR: Congenital disorders of glycosylation provide insight as extreme hypomorphisms, whereas milder deficiencies may encompass many common chronic conditions, including autoimmunity, metabolic syndrome, and aging.
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Fetuin/α2-HS Glycoprotein Is a Transforming Growth Factor-β Type II Receptor Mimic and Cytokine Antagonist
Michael A. Demetriou,Christoph Binkert,Balram Sukhu,Howard C. Tenenbaum,Howard C. Tenenbaum,James W. Dennis +5 more
TL;DR: These experiments define the TRH1 peptide loop as a cytokine-binding domain in both TβRII and fetuin and suggest that fetuin is a natural antagonist of TGF-β and BMP activities.
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Reduced contact-inhibition and substratum adhesion in epithelial cells expressing GlcNAc-transferase V.
TL;DR: The results suggest that beta 1-6GlcNAc branching of N-linked oligosaccharides contributes directly to relaxed growth controls and reduce substratum adhesion in premalignant epithelial cells.