The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Structural analysis of full-length SARS-CoV-2 spike protein from an advanced vaccine candidate
Open accessAbstract
Structure of a vaccine candidate: Much effort is being targeted at developing vaccines that will provide protection against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). A trimeric spike protein that decorates the virus is a primary target of the host immune system and the focus of vaccine development. Bangaru et al. present the structure of a leading vaccine candidate: a full-length spike protein with some modifications aimed at enhancing stability that is formulated in polysorbate 80 detergent. The study confirms that the full-length immunogen is in a stable prefusion conformation and provides a basis for understanding immune responses to the vaccine. Science , this issue p. 1089
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Cites
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Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation
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Self-citationImmunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen
Pallesen, J., Wang, N., Corbett, K. S., Wrapp, D., Kirchdoerfer, R. N., Turner, H. L., Cottrell, C. A., Becker, M. M., Wang, L., Shi, W., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707304114 · Cited by 1,073
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Shinde, V., Bhikha, S., Hoosain, Z., Archary, M., Bhorat, Q., Fairlie, L., Lalloo, U., Masilela, M. S. L., Moodley, D., Hanley, S., et al. (2021) · New England Journal of Medicine · doi:10.1056/nejmoa2103055 · Cited by 625
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Shinde, V., Bhikha, S., Hoosain, Z., Archary, M., Bhorat, Q., Fairlie, L., Lalloo, U., Masilela, M. S. L., Moodley, D., Hanley, S., et al. (2021) · doi:10.1101/2021.02.25.21252477 · Cited by 625
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Self-citationSARS-CoV-2 escape in vitro from a highly neutralizing COVID-19 convalescent plasma
Andreano, E., Piccini, G., Licastro, D., Casalino, L., Johnson, N. V., Paciello, I., Monego, S. D., Pantano, E., Manganaro, N., Manenti, A., et al. (2020) · doi:10.1101/2020.12.28.424451
“The SARS-CoV-2 S-protein is composed of two subunits: S1, which contains the receptor-binding domain (RBD) responsible for the interaction with receptors on the host cells, and S2, which mediates membrane fusion and viral entry (7, 8).”
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A self-amplifying RNA vaccine against COVID-19 with long-term room-temperature stability
Voigt, E. A., Gerhardt, A., Hanson, D., Jennewein, M. F., Battisti, P., Reed, S., Singh, J., Mohamath, R., Bakken, J., Beaver, S., et al. (2022) · npj Vaccines · doi:10.1038/s41541-022-00549-y · Cited by 89
Patel, N., Rehman, A., Trost, J. F., Flores, R., Longacre, Z., Guebre-Xabier, M., Zhou, H., Zhou, B., Jacobson, K., Jiang, D., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-61964-y · Cited by 6
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Metadata
- Authors
- Bangaru, S., Ozorowski, G., Turner, H. L., Antanasijevic, A., Huang, D., Wang, X., Torres, J. L., Diedrich, J. K., Tian, J.-H., Portnoff, A. D., Patel, N., Massare, M. J., Yates, J. R., Nemazee, D., Paulson, J. C., Glenn, G., Smith, G., & Ward, A. B.
- Venue
- Science
- Published
- 2020-11-27
- Volume
- 370
- Issue
- 6520
- Pages
- 1089-1094
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W3093842248
- Cited by
- 346
- References
- 13
- FWCI
- 7.79
- Type
- journal article
- Language
- en
- Open access
- hybrid
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