The DOI matches its Crossref record; 64 of the 64 references it cites were found in a registry or an index.
Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion
Open accessAbstract
Significance: The pandemic potential of coronaviruses was recently demonstrated twice by global outbreaks of deadly pneumonia. The spike (S) glycoprotein initiates infection through conformational changes that remain largely uncharacterized. Here we report the cryoEM structure of an S glycoprotein in the postfusion state, showing large-scale rearrangements compared with the prefusion trimer. We further characterized the refolding of the metastable prefusion conformation using limited proteolysis, mass spectrometry, and single-particle EM. The observed similarity to paramyxovirus F structures demonstrates a conserved refolding trajectory and supports the evolutionary relatedness of their fusion subunits. Finally, our data provide a structural framework for understanding antibody neutralization and for engineering vaccines against this medically important virus family.
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Cites
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 29,915
MolProbity : all-atom structure validation for macromolecular crystallography
Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., & Richardson, D. C. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909042073 · Cited by 14,115
MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
Zheng, S. Q., Palovcak, E., Armache, J.-P., Verba, K. A., Cheng, Y., & Agard, D. A. (2017) · Nature Methods · doi:10.1038/nmeth.4193 · Cited by 7,777
Gctf: Real-time CTF determination and correction
Zhang, K. (2016) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.11.003 · Cited by 3,537
Li, X., Mooney, P., Zheng, S., Booth, C. R., Braunfeld, M. B., Gubbens, S., Agard, D. A., & Cheng, Y. (2013) · Nature Methods · doi:10.1038/nmeth.2472 · Cited by 1,818
Isolation and characterization of a bat SARS-like coronavirus that uses the ACE2 receptor
Ge, X.-Y., Li, J.-L., Yang, X.-L., Chmura, A. A., Zhu, G., Epstein, J. H., Mazet, J. K., Hu, B., Zhang, W., Peng, C., et al. (2013) · Nature · doi:10.1038/nature12711 · Cited by 1,778
Automated molecular microscopy: The new Leginon system
Suloway, C., Pulokas, J., Fellmann, D., Cheng, A., Guerra, F., Quispe, J., Stagg, S., Potter, C. S., & Carragher, B. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.03.010 · Cited by 1,764
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
Bosch, B. J., van der Zee, R., de Haan, C. A. M., & Rottier, P. J. M. (2003) · Journal of Virology · doi:10.1128/jvi.77.16.8801-8811.2003 · Cited by 1,489
Self-citationStructure-Based Design of a Fusion Glycoprotein Vaccine for Respiratory Syncytial Virus
McLellan, J. S., Chen, M., Joyce, M. G., Sastry, M., Stewart-Jones, G. B. E., Yang, Y., Zhang, B., Chen, L., Srivatsan, S., Zheng, A., et al. (2013) · Science · doi:10.1126/science.1243283 · Cited by 1,126
Cited by
Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation
Wrapp, D., Wang, N., Corbett, K. S., Goldsmith, J. A., Hsieh, C.-L., Abiona, O., Graham, B. S., & McLellan, J. S. (2020) · Science · doi:10.1126/science.abb2507 · Cited by 8,897
Structure, function and antigenicity of the SARS-CoV-2 spike glycoprotein
Walls, A. C., Park, Y.-J., Tortorici, M. A., Wall, A., McGuire, A. T., & Veesler, D. (2020) · doi:10.1101/2020.02.19.956581 · Cited by 8,586
Self-citationMechanisms 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
Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody
Pinto, D., Park, Y.-J., Beltramello, M., Walls, A. C., Tortorici, M. A., Bianchi, S., Jaconi, S., Culap, K., Zatta, F., De Marco, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2349-y · Cited by 1,885
Self-citationStructural and functional analysis of a potent sarbecovirus neutralizing antibody
Pinto, D., Park, Y.-J., Beltramello, M., Walls, A. C., Tortorici, M. A., Bianchi, S., Jaconi, S., Culap, K., Zatta, F., De Marco, A., et al. (2020) · doi:10.1101/2020.04.07.023903 · Cited by 1,752
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Metadata
- Authors
- Walls, A. C., Tortorici, M. A., Snijder, J., Xiong, X., Bosch, B.-J., Rey, F. A., & Veesler, D.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2017-10-03
- Volume
- 114
- Issue
- 42
- Pages
- 11157-11162
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2762161295
- Cited by
- 537
- References
- 64
- FWCI
- 36.28
- Type
- journal article
- Language
- en
- Open access
- bronze
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