The DOI matches its Crossref record; 293 of the 293 references it cites were found in a registry or an index.
Exploitation of glycosylation in enveloped virus pathobiology
Open accessAbstract
Glycosylation is a ubiquitous post-translational modification responsible for a multitude of crucial biological roles. As obligate parasites, viruses exploit host-cell machinery to glycosylate their own proteins during replication. Viral envelope proteins from a variety of human pathogens including HIV-1, influenza virus, Lassa virus, SARS, Zika virus, dengue virus, and Ebola virus have evolved to be extensively glycosylated. These host-cell derived glycans facilitate diverse structural and functional roles during the viral life-cycle, ranging from immune evasion by glycan shielding to enhancement of immune cell infection. In this review, we highlight the imperative and auxiliary roles glycans play, and how specific oligosaccharide structures facilitate these functions during viral pathogenesis. We discuss the growing efforts to exploit viral glycobiology in the development of anti-viral vaccines and therapies.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Global trends in emerging infectious diseases
Jones, K. E., Patel, N. G., Levy, M. A., Storeygard, A., Balk, D., Gittleman, J. L., & Daszak, P. (2008) · Nature · doi:10.1038/nature06536 · Cited by 8,338
ASSEMBLY OF ASPARAGINE-LINKED OLIGOSACCHARIDES
Kornfeld, R., & Kornfeld, S. (1985) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.54.070185.003215 · Cited by 4,906
Wiederschain, G. Y. (2009) · Biochemistry (Moscow) · doi:10.1134/s0006297909090156 · Cited by 4,083
Receptor Binding and Membrane Fusion in Virus Entry: The Influenza Hemagglutinin
Skehel, J. J., & Wiley, D. C. (2000) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.69.1.531 · Cited by 2,706
Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
Wilson, I. A., Skehel, J. J., & Wiley, D. C. (1981) · Nature · doi:10.1038/289366a0 · Cited by 2,525
Self-citationDC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells
Geijtenbeek, T. B. H., Kwon, D. S., Torensma, R., van Vliet, S. J., van Duijnhoven, G. C. F., Middel, J., Cornelissen, I. L. M. H. A., Nottet, H. S. L. M., KewalRamani, V. N., Littman, D. R., et al. (2000) · Cell · doi:10.1016/s0092-8674(00)80694-7 · Cited by 2,447
Antibody neutralization and escape by HIV-1
Wei, X., Decker, J. M., Wang, S., Hui, H., Kappes, J. C., Wu, X., Salazar-Gonzalez, J. F., Salazar, M. G., Kilby, J. M., Saag, M. S., et al. (2003) · Nature · doi:10.1038/nature01470 · Cited by 2,421
Varki, A. P., Cummings, R. D., Esko, J. D., Freeze, H. H., Stanley, P., Bertozzi, C. R., Hart, G. W., & Etzler, M. E. (1999) · Cited by 2,384
Rational design of potent sialidase-based inhibitors of influenza virus replication
von Itzstein, M., Wu, W.-Y., Kok, G. B., Pegg, M. S., Dyason, J. C., Jin, B., Van Phan, T., Smythe, M. L., White, H. F., Oliver, S. W., et al. (1993) · Nature · doi:10.1038/363418a0 · Cited by 1,862
Broad neutralization coverage of HIV by multiple highly potent antibodies
Walker, L. M., Huber, M., Doores, K. J., Falkowska, E., Pejchal, R., Julien, J.-P., Wang, S.-K., Ramos, A., Chan-Hui, P.-Y., Moyle, M., et al. (2011) · Nature · doi:10.1038/nature10373 · Cited by 1,480
Self-citation
Cited by
COVID-19: Drug Targets and Potential Treatments
Gil, C., Ginex, T., Maestro, I., Nozal, V., Barrado-Gil, L., Cuesta-Geijo, M. Á., Urquiza, J., Ramírez, D., Alonso, C., Campillo, N. E., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00606 · Cited by 445
Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442
Chumakov, K., Avidan, M. S., Benn, C. S., Bertozzi, S. M., Blatt, L., Chang, A. Y., Jamison, D. T., Khader, S. A., Kottilil, S., Netea, M. G., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2101718118 · Cited by 96
Structure of infective Getah virus at 2.8 A resolution determined by cryo-electron microscopy
Wang, A., Zhou, F., Liu, C., Gao, D., Qi, R., Yin, Y., Liu, S., Gao, Y., Fu, L., Xia, Y., et al. (2022) · Cell Discovery · doi:10.1038/s41421-022-00374-6 · Cited by 41
The GATE glycoprotein complex enhances human cytomegalovirus entry in endothelial cells
Norris, M. J., Henderson, L. A., Siddiquey, M. N. A., Yin, J., Yoo, K., Brunel, S., Mor, M., Saphire, E. O., Benedict, C. A., & Kamil, J. P. (2025) · Nature Microbiology · doi:10.1038/s41564-025-02025-4 · Cited by 14
Metadata
- Authors
- Watanabe, Y., Bowden, T. A., Wilson, I. A., & Crispin, M.
- Venue
- Biochimica et Biophysica Acta (BBA) - General Subjects
- Publisher
- Elsevier BV
- Published
- 2019-10
- Volume
- 1863
- Issue
- 10
- Pages
- 1480-1497
- ISSN
- 0304-4165 (ISSN-L)
- OpenAlex
- W2946482289
- Cited by
- 482
- References
- 293
- FWCI
- 20.98
- Type
- journal article
- Language
- en
- Open access
- hybrid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Exploitation of glycosylation in enveloped virus pathobiology. https://app.cochat.ai/papers/10.1016/j.bbagen.2019.05.012
- The paper
- Watanabe, Y., Bowden, T. A., Wilson, I. A., & Crispin, M. (2019). Exploitation of glycosylation in enveloped virus pathobiology. Biochimica et Biophysica Acta (BBA) - General Subjects. https://doi.org/10.1016/j.bbagen.2019.05.012
Data sources
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.
