Isotope-targeted glycoproteomics (IsoTaG): a mass-independent platform for intact N- and O-glycopeptide discovery and analysis-Reference-Cited by-同舟云学术

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Isotope-targeted glycoproteomics (IsoTaG): a mass-independent platform for intact N- and O-glycopeptide discovery and analysis

Published:2015-04-20 Issue:6 Volume:12 Page:561-567
ISSN:1548-7091
Container-title:Nature Methods
language:en
Short-container-title:Nat Methods

Author:

Woo Christina M,Iavarone Anthony T,Spiciarich David R,Palaniappan Krishnan K,Bertozzi Carolyn R

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Molecular Biology,Biochemistry,Biotechnology

Link

http://www.nature.com/articles/nmeth.3366.pdf

Reference51 articles.

1. Gouyer, V. et al. Inhibition of the glycosylation and alteration in the intracellular trafficking of mucins and other glycoproteins by GalNAcα-O-bn in mucosal cell lines: an effect mediated through the intracellular synthesis of complex GalNAcα-O-bn oligosaccharides. Front. Biosci. 6, D1235–D1244 (2001).

2. Zachara, N.E. & Hart, G.W. Cell signaling, the essential role of O-GlcNAc!. Biochim. Biophys. Acta. 1761, 599–617 (2006).

3. Hudak, J.E., Canham, S.M. & Bertozzi, C.R. Glycocalyx engineering reveals a Siglec-based mechanism for NK cell immunoevasion. Nat. Chem. Biol. 10, 69–75 (2014).

4. Yuzwa, S.A. et al. Increasing O-Glcnac slows neurodegeneration and stabilizes tau against aggregation. Nat. Chem. Biol. 8, 393–399 (2012).

5. Fuster, M.M. & Esko, J.D. The sweet and sour of cancer: glycans as novel therapeutic targets. Nat. Rev. Cancer 5, 526–542 (2005).

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