The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Glycosylation of Recombinant Antibody Therapeutics
Abstract
The adaptive immune system has the capacity to produce antibodies with a virtually infinite repertoire of specificities. Recombinant antibodies specific for human targets are established in the clinic as therapeutics and represent a major new class of drug. Therapeutic efficacy depends on the formation of complexes with target molecules and subsequent activation of downstream biologic effector mechanisms that result in elimination of the target. The activation of effector mechanisms is dependent on structural characteristics of the antibody molecule that result from posttranslational modifications, in particular, glycosylation. The production of therapeutic antibody with a consistent human glycoform profile has been and remains a considerable challenge to the biopharmaceutical industry. Recent research has shown that individual glycoforms of antibody may provide optimal efficacy for selected outcomes. Thus a further challenge will be the production of a second generation of antibody therapeutics customized for their clinical indication.
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Role of Oligosaccharide Residues of IgG1-Fc in FcγRIIb Binding
Mimura, Y., Sondermann, P., Ghirlando, R., Lund, J., Young, S. P., Goodall, M., & Jefferis, R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m107478200 · Cited by 236
Self-citationThe α-gal epitope (Galα1-3Galβ1-4GlcNAc-R) in xenotransplantation
Galili, U. (2001) · Biochimie · doi:10.1016/s0300-9084(01)01294-9 · Cited by 212
Cited by
Glycosylation as a strategy to improve antibody-based therapeutics
Jefferis, R. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2804 · Cited by 829
“These effector ligands include three structurally homologous cellular Fc receptor types (FcγRI, FcγRII and FcγRIII), the C1q component of complement and the neonatal Fc receptor (FcRn”
BackgroundSelf-citationHeterogeneity of Monoclonal Antibodies
Liu, H., Gaza-Bulseco, G., Faldu, D., Chumsae, C., & Sun, J. (2008) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.21180 · Cited by 481
Goetze, A. M., Liu, Y. D., Zhang, Z., Shah, B., Lee, E., Bondarenko, P. V., & Flynn, G. C. (2011) · Glycobiology · doi:10.1093/glycob/cwr027 · Cited by 467
Immunogenicity of anti-TNF biologic therapies for rheumatoid arthritis
van Schouwenburg, P. A., Rispens, T., & Wolbink, G. J. (2013) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2013.4 · Cited by 438
Liu, L. (2015) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.24444 · Cited by 428
Metadata
- Authors
- Jefferis, R.
- Venue
- Biotechnology Progress
- Publisher
- Wiley
- Published
- 2008-09-05
- Volume
- 21
- Issue
- 1
- Pages
- 11-16
- ISSN
- 1520-6033 (ISSN-L)
- 8756-7938
- OpenAlex
- W2030932286
- Cited by
- 526
- References
- 7
- FWCI
- 10.26
- Type
- journal article
- Language
- en
- Open access
- closed
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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.
