Literature DB >> 23296534

Approaches for site mapping and quantification of O-linked glycopeptides.

Peng Zhao1, Stephanie H Stalnaker, Lance Wells.   

Abstract

As a complex post-translational event, the biosynthesis, structures, and functions of O-linked glycans have attracted research interests in various aspects. The recent development of novel technologies for the analysis of glycans and glycoproteins sheds new insights with regard to determining site occupancy, structure-function relationships, and the contributions of O-linked glycosylation to physiological and pathological processes. In this chapter, we refer to several approaches for the structural characterization and quantification of O-linked glycopeptides, with a focus on O-GlcNAc and O-Mannose modified glycoproteins.

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Year:  2013        PMID: 23296534     DOI: 10.1007/978-1-62703-146-2_15

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  2 in total

Review 1.  Recent advancements in understanding mammalian O-mannosylation.

Authors:  M Osman Sheikh; Stephanie M Halmo; Lance Wells
Journal:  Glycobiology       Date:  2017-09-01       Impact factor: 4.313

2.  Comparative glycoproteomics of stem cells identifies new players in ricin toxicity.

Authors:  Johannes Stadlmann; Jasmin Taubenschmid; Daniel Wenzel; Anna Gattinger; Gerhard Dürnberger; Frederico Dusberger; Ulrich Elling; Lukas Mach; Karl Mechtler; Josef M Penninger
Journal:  Nature       Date:  2017-09-20       Impact factor: 49.962

  2 in total

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