The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Viral membrane fusion
Open accessAbstract
Membrane fusion is an essential step when enveloped viruses enter cells. Lipid bilayer fusion requires catalysis to overcome a high kinetic barrier; viral fusion proteins are the agents that fulfill this catalytic function. Despite a variety of molecular architectures, these proteins facilitate fusion by essentially the same generic mechanism. Stimulated by a signal associated with arrival at the cell to be infected (e.g., receptor or co-receptor binding, proton binding in an endosome), they undergo a series of conformational changes. A hydrophobic segment (a "fusion loop" or "fusion peptide") engages the target-cell membrane and collapse of the bridging intermediate thus formed draws the two membranes (virus and cell) together. We know of three structural classes for viral fusion proteins. Structures for both pre- and postfusion conformations of illustrate the beginning and end points of a process that can be probed by single-virion measurements of fusion kinetics.
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Cites
Membrane Fusion: Grappling with SNARE and SM Proteins
Südhof, T. C., & Rothman, J. E. (2009) · Science · doi:10.1126/science.1161748 · Cited by 2,027
Structure of influenza haemagglutinin at the pH of membrane fusion
Bullough, P. A., Hughson, F. M., Skehel, J. J., & Wiley, D. C. (1994) · Nature · doi:10.1038/371037a0 · Cited by 1,564
Observation of a Membrane Fusion Intermediate Structure
Yang, L., & Huang, H. W. (2002) · Science · doi:10.1126/science.1074354 · Cited by 307
Chanturiya, A., Chernomordik, L. V., & Zimmerberg, J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.26.14423 · Cited by 201
Cited by
Mechanisms of SARS-CoV-2 entry into cells
Jackson, C. B., Farzan, M., Chen, B., & Choe, H. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00418-x · Cited by 3,022
Distinct conformational states of SARS-CoV-2 spike protein
Cai, Y., Zhang, J., Xiao, T., Peng, H., Sterling, S. M., Walsh, R. M., Rawson, S., Rits-Volloch, S., & Chen, B. (2020) · Science · doi:10.1126/science.abd4251 · Cited by 1,221
Yuan, Y., Cao, D., Zhang, Y., Ma, J., Qi, J., Wang, Q., Lu, G., Wu, Y., Yan, J., Shi, Y., et al. (2017) · Nature Communications · doi:10.1038/ncomms15092 · Cited by 760
Wrobel, A. G., Benton, D. J., Xu, P., Roustan, C., Martin, S. R., Rosenthal, P. B., Skehel, J. J., & Gamblin, S. J. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0468-7 · Cited by 544
Marcandalli, J., Fiala, B., Ols, S., Perotti, M., de van der Schueren, W., Snijder, J., Hodge, E., Benhaim, M., Ravichandran, R., Carter, L., et al. (2019) · Cell · doi:10.1016/j.cell.2019.01.046 · Cited by 448
Metadata
- Authors
- Harrison, S. C.
- Venue
- Virology
- Publisher
- Elsevier BV
- Published
- 2015-05
- Volume
- 479-480
- Pages
- 498-507
- ISSN
- 0042-6822 (ISSN-L)
- OpenAlex
- W2048172399
- Cited by
- 697
- References
- 4
- FWCI
- 21.10
- Type
- journal article
- Language
- en
- Open access
- hybrid
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