Chemical Glycobiology

Whitman, Chad M.; Bond, Michelle; Kohler, Jennifer J.

doi:10.1016/b978-008045382-8.00681-x

Cited by 1 publication

(4 citation statements)

References 318 publications

(88 reference statements)

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“…One strategy to access these complexes relies on the formation of covalent interactions between the glycan and the binding protein using photo-cross-linking reagents . Early work in this field focused on the synthesis of glycans, glycopeptides, and glycolipids containing both a photo-cross-linking group and an enrichment moiety (see recent reviews by Kohler and co-workers for more information). , These reagents were used to enrich and identify a variety of GBPs from cell culture media, including the asialoglycoprotein receptor, the adhesion factor BabA on H. pylori , and the B-subunit of cholera toxin. − …”

Section: Functional Glycoproteomicsmentioning

confidence: 99%

“…20–22 Indeed, the field of glycobiology has long been driven by innovations from chemistry, such as glycan and lectin microarrays, small-molecule inhibitors, and chemically synthesized glycans. 21,23,24 …”

Section: Introductionmentioning

confidence: 99%

“…Identifying and characterizing these PTMs remains a major goal in proteomics . Chemical approaches have emerged as powerful tools for probing PTMs at the proteome scale. − Of the more than 300 known protein modifications, glycosylation is one of the most abundant and complex PTMs, and it was one of the first to be probed with chemical tools. − Indeed, the field of glycobiology has long been driven by innovations from chemistry, such as glycan and lectin microarrays, small-molecule inhibitors, and chemically synthesized glycans. ,, …”

Section: Introductionmentioning

confidence: 99%

“…20−22 Indeed, the field of glycobiology has long been driven by innovations from chemistry, such as glycan and lectin microarrays, small-molecule inhibitors, and chemically synthesized glycans. 21,23,24 More recently, chemists have focused on developing tools to help profile protein glycosylation at the level of the proteome. In this review, we discuss key contributions from chemical biology for interrogating the "glycoproteome" by MS. We begin with a discussion of the importance of and challenges in studying protein glycosylation.…”

Section: Introductionmentioning

confidence: 99%

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Chemical Glycoproteomics

Palaniappan

Bertozzi²

2016

Chem. Rev.

233

205

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Chemical tools have accelerated progress in glycoscience, reducing experimental barriers to studying protein glycosylation, the most widespread and complex form of posttranslational modification. For example, chemical glycoproteomics technologies have enabled the identification of specific glycosylation sites and glycan structures that modulate protein function in a number of biological processes. This field is now entering a stage of logarithmic growth, during which chemical innovations combined with mass spectrometry advances could make it possible to fully characterize the human glycoproteome. In this review, we describe the important role that chemical glycoproteomics methods are playing in such efforts. We summarize developments in four key areas: enrichment of glycoproteins and glycopeptides from complex mixtures, emphasizing methods that exploit unique chemical properties of glycans or introduce unnatural functional groups through metabolic labeling and chemoenzymatic tagging; identification of sites of protein glycosylation; targeted glycoproteomics; and functional glycoproteomics, with a focus on probing interactions between glycoproteins and glycan-binding proteins. Our goal with this survey is to provide a foundation on which continued technological advancements can be made to promote further explorations of protein glycosylation.

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