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Cited by 163

The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.

Homogeneous Glycopeptides and Glycoproteins for Biological Investigation

Grogan, Michael J., Pratt, Matthew R., Marcaurelle, Lisa A., Bertozzi, Carolyn R.·2002·Annual Review of Biochemistry

Abstract

▪ Abstract Protein glycosylation is widely recognized as a modulator of protein structure, localization, and cell-cell recognition in multicellular systems. Glycoproteins are typically expressed as mixtures of glycoforms, their oligosaccharides being generated by a template-independent biosynthetic process. Investigation of their function has been greatly assisted by sources of homogeneous material. This review summarizes current efforts to obtain homogeneous glycopeptide and glycoprotein materials by a variety of methods that draw from the techniques of recombinant expression, chemical synthesis, enzymatic transformation, and chemoselective ligation. Some of these techniques remove obstacles to glycoprotein synthesis by installing nonnative linkages and other modifications for facilitated assembly. The end purpose of the described approaches is the production of glycosylated materials for experiments relevant to the biological investigation of glycoproteins, although the strategies presented apply to other posttranslational modifications as well.

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Crossref · 10.1146/annurev.biochem.71.110601.135334

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Metadata

Authors
Grogan, M. J., Pratt, M. R., Marcaurelle, L. A., & Bertozzi, C. R.
Venue
Annual Review of Biochemistry
Published
2002-06
Volume
71
Issue
1
Pages
593-634
ISSN
  • 0066-4154 (ISSN-L)
  • 1545-4509
OpenAlex
W2140433352
Cited by
163
References
4
FWCI
0.64
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Homogeneous Glycopeptides and Glycoproteins for Biological Investigation. https://app.cochat.ai/papers/10.1146/annurev.biochem.71.110601.135334
The paper
Grogan, M. J., Pratt, M. R., Marcaurelle, L. A., & Bertozzi, C. R. (2002). Homogeneous Glycopeptides and Glycoproteins for Biological Investigation. Annual Review of Biochemistry. https://doi.org/10.1146/annurev.biochem.71.110601.135334

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.