The DOI matches its Crossref record; 117 of the 117 references it cites were found in a registry or an index.
The Impact of Glycosylation on the Biological Function and Structure of Human Immunoglobulins
Abstract
Immunoglobulins are the major secretory products of the adaptive immune system. Each is characterized by a distinctive set of glycoforms that reflects the wide variation in the number, type, and location of their oligosaccharides. In a given physiological state, glycoform populations are reproducible; therefore, disease-associated alterations provide diagnostic biomarkers (e.g., for rheumatoid arthritis) and contribute to disease pathogenesis. The oligosaccharides provide important recognition epitopes that engage with lectins, endowing the immunoglobulins with an expanded functional repertoire. The sugars play specific structural roles, maintaining and modulating effector functions that are physiologically relevant and can be manipulated to optimize the properties of therapeutic antibodies. New molecular models of all the immunoglobulins are included to provide a basis for informed and critical discussion. The models were constructed by combining glycan sequencing data with oligosaccharide linkage and dynamics information from the Glycobiology Institute experimental database and protein structural data from “The Protein Data Bank.”
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Cites
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Cited by
Fcγ receptors as regulators of immune responses
Nimmerjahn, F., & Ravetch, J. V. (2008) · Nature Reviews Immunology · doi:10.1038/nri2206 · Cited by 2,947
Structure and function of immunoglobulins
Schroeder, H. W., & Cavacini, L. (2010) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2009.09.046 · Cited by 1,905
Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc
Anthony, R. M., Nimmerjahn, F., Ashline, D. J., Reinhold, V. N., Paulson, J. C., & Ravetch, J. V. (2008) · Science · doi:10.1126/science.1154315 · Cited by 849
Glycosylation as a strategy to improve antibody-based therapeutics
Jefferis, R. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2804 · Cited by 829
“It is generally reported that IgG Fc oligosaccharides of normal human IgG are predominantly devoid of terminal sialic acid residue”
BackgroundFerrara, C., Grau, S., Jäger, C., Sondermann, P., Brünker, P., Waldhauer, I., Hennig, M., Ruf, A., Rufer, A. C., Stihle, M., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1108455108 · Cited by 770
Metadata
- Authors
- Arnold, J. N., Wormald, M. R., Sim, R. B., Rudd, P. M., & Dwek, R. A.
- Venue
- Annual Review of Immunology
- Publisher
- Annual Reviews
- Published
- 2007-04-01
- Volume
- 25
- Issue
- 1
- Pages
- 21-50
- ISSN
- 0732-0582 (ISSN-L)
- 1545-3278
- OpenAlex
- W2100518445
- Cited by
- 1,307
- References
- 117
- FWCI
- 1.92
- Type
- journal article
- Language
- en
- Open access
- closed
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- Arnold, J. N., Wormald, M. R., Sim, R. B., Rudd, P. M., & Dwek, R. A. (2007). The Impact of Glycosylation on the Biological Function and Structure of Human Immunoglobulins. Annual Review of Immunology. https://doi.org/10.1146/annurev.immunol.25.022106.141702
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
