N-Glycoprotein SRMAtlas

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منابع مشابه

Uridine 5'-Diphosphate-N-Acetylglucosamine: Glycoprotein N-Acetylglucosaminylphosphotransferase

Received for publication 29 January 1981 and in revised form 13 February 1981.

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Encoding Asymmetry of the N-Glycosylation Motif Facilitates Glycoprotein Evolution

Protein N-glycosylation is found in all domains of life and has a conserved role in glycoprotein folding and stability. In animals, glycoproteins transit through the Golgi where the N-glycans are trimmed and rebuilt with sequences that bind lectins, an innovation that greatly increases structural diversity and redundancy of glycoprotein-lectin interaction at the cell surface. Here we ask whethe...

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Circulating N-Linked Glycoprotein Acetyls and Longitudinal Mortality Risk.

RATIONALE Circulating glycoprotein N-acetyl glucosamine residues have recently been associated with incident cardiovascular disease and diabetes mellitus. OBJECTIVE Using a plasma glycan biosignature (GlycA) to identify circulating N-acetyl glycan groups, we examined the longitudinal association between GlycA and mortality among initially healthy individuals. METHODS AND RESULTS We quantifi...

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Quantitative investigation of human cell surface N-glycoprotein dynamics.

Surface glycoproteins regulate nearly every extracellular event and they are dynamic for cells to adapt to the ever-changing extracellular environment. These glycoproteins contain a wealth of information on cellular development and disease states, and have significant biomedical implications. Systematic investigation of surface glycoproteins will result in a better understanding of surface prot...

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Global site-specific N-glycosylation analysis of HIV envelope glycoprotein

HIV-1 envelope glycoprotein (Env) is the sole target for broadly neutralizing antibodies (bnAbs) and the focus for design of an antibody-based HIV vaccine. The Env trimer is covered by ∼90N-linked glycans, which shield the underlying protein from immune surveillance. bNAbs to HIV develop during infection, with many showing dependence on glycans for binding to Env. The ability to routinely asses...

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ژورنال

عنوان ژورنال: Molecular & Cellular Proteomics

سال: 2013

ISSN: 1535-9476

DOI: 10.1074/mcp.o112.026617