SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects

Features and development of Coot

Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. D. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 27,510 · see citing works

<i>PHENIX</i> : a comprehensive Python-based system for macromolecular structure solution

Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716 · see citing works

A pneumonia outbreak associated with a new coronavirus of probable bat origin

Zhou, P., Yang, X.-L., Wang, X.-G., Hu, B., Zhang, L., Zhang, W., Si, H.-R., Zhu, Y., Li, B., Huang, C.-L., et al. (2020) · Nature · doi:10.1038/s41586-020-2012-7 · Cited by 21,969 · see citing works

SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor

Hoffmann, M., Kleine-Weber, H., Schroeder, S., Krüger, N., Herrler, T., Erichsen, S., Schiergens, T. S., Herrler, G., Wu, N.-H., Nitsche, A., et al. (2020) · Cell · doi:10.1016/j.cell.2020.02.052 · Cited by 20,286 · see citing works

A new coronavirus associated with human respiratory disease in China

Wu, F., Zhao, S., Yu, B., Chen, Y.-M., Wang, W., Song, Z.-G., Hu, Y., Tao, Z.-W., Tian, J.-H., Pei, Y.-Y., et al. (2020) · Nature · doi:10.1038/s41586-020-2008-3 · Cited by 11,688 · see citing works

cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination

Punjani, A., Rubinstein, J. L., Fleet, D. J., & Brubaker, M. A. (2017) · Nature Methods · doi:10.1038/nmeth.4169 · Cited by 9,168 · see citing works

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 · see citing works

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 · see citing works

MotionCor2 - anisotropic correction of beam-induced motion for improved cryo-electron microscopy

Zheng, S., Palovcak, E. J., Armache, J., Verba, K., Cheng, Y.-F., & Agard, D. (2017) · Nature Methods · doi:10.1038/nmeth.4193 · Cited by 7,678 · see citing works

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Adams, P. D., Afonine, P. V., Bunkòczi, G., Chen, V. B., Davis, I., Echols, N., Headd, J. J., Hung, L., Kapral, G. J., Grosse‐Kunstleve, R. W., et al. (2012) · International Tables for Crystallography · doi:10.1107/97809553602060000865 · Cited by 7,334 · see citing works

Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor

Lan, J., Ge, J., Yu, J., Shan, S., Zhou, H., Fan, S., Zhang, Q., Shi, X., Wang, Q., Zhang, L., et al. (2020) · Nature · doi:10.1038/s41586-020-2180-5 · Cited by 5,983 · see citing works

Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus

Li, W., Moore, M. J., Vasilieva, N., Sui, J., Wong, S. K., Berne, M. A., Somasundaran, M., Sullivan, J. L., Luzuriaga, K., Greenough, T. C., et al. (2003) · Nature · doi:10.1038/nature02145 · Cited by 5,923 · see citing works

RELION: Implementation of a Bayesian approach to cryo-EM structure determination

Scheres, S. H. W. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2012.09.006 · Cited by 5,446 · see citing works

The proximal origin of SARS-CoV-2

Andersen, K. G., Rambaut, A., Lipkin, W. I., Holmes, E. C., & Garry, R. F. (2020) · Nature Medicine · doi:10.1038/s41591-020-0820-9 · Cited by 5,081 · see citing works

Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2

Yan, R., Zhang, Y., Li, Y., Xia, L., Guo, Y., & Zhou, Q. (2020) · Science · doi:10.1126/science.abb2762 · Cited by 4,950 · see citing works

CTFFIND4: Fast and accurate defocus estimation from electron micrographs

Rohou, A. L., & Grigorieff, N. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.08.008 · Cited by 4,926 · see citing works

Structural basis of receptor recognition by SARS-CoV-2

Shang, J., Ye, G., Shi, K., Wan, Y., Luo, C., Aihara, H., Geng, Q., Auerbach, A., & Li, F. (2020) · Nature · doi:10.1038/s41586-020-2179-y · Cited by 3,661 · see citing works

Functional assessment of cell entry and receptor usage for SARS-CoV-2 and other lineage B betacoronaviruses

Letko, M., Marzi, A., & Munster, V. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0688-y · Cited by 3,109 · see citing works

Bats Are Natural Reservoirs of SARS-Like Coronaviruses

Li, W., Shi, Z., Yu, M., Ren, W., Smith, C. S., Epstein, J. H., Wang, H., Crameri, G. S., Hú, Z., Zhang, H., et al. (2005) · Science · doi:10.1126/science.1118391 · Cited by 2,571 · see citing works

Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy

Rosenthal, P. B., & Henderson, R. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.07.013 · Cited by 2,416 · see citing works

Structure of SARS Coronavirus Spike Receptor-Binding Domain Complexed with Receptor

Li, F., Li, W., Farzan, M., & Harrison, S. C. (2005) · Science · doi:10.1126/science.1116480 · Cited by 2,031 · see citing works

Identifying SARS-CoV-2-related coronaviruses in Malayan pangolins

Lam, T. T., Jia, N., Zhang, Y.-W., Shum, M. H.-H., Jiang, J.-F., Zhu, H., Tong, Y., Shi, Y., Ni, X.-B., Liao, Y., et al. (2020) · Nature · doi:10.1038/s41586-020-2169-0 · Cited by 1,877 · see citing works

SPHIRE-crYOLO is a fast and accurate fully automated particle picker for cryo-EM

Wagner, T., Merino, F., Stabrin, M., Moriya, T., Antoni, C., Apelbaum, A., Hagel, P., Sitsel, O., Raisch, T., Prumbaum, D., et al. (2019) · Communications Biology · doi:10.1038/s42003-019-0437-z · Cited by 1,217 · see citing works

Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites

Belouzard, S., Chu, V. C., & Whittaker, G. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809524106 · Cited by 1,073 · see citing works

Immunogenicity 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 · see citing works

Host cell proteases: Critical determinants of coronavirus tropism and pathogenesis

Millet, J. K., & Whittaker, G. R. (2014) · Virus Research · doi:10.1016/j.virusres.2014.11.021 · Cited by 887 · see citing works

Viral membrane fusion

Harrison, S. C. (2015) · Virology · doi:10.1016/j.virol.2015.03.043 · Cited by 705 · see citing works

Host cell entry of Middle East respiratory syndrome coronavirus after two-step, furin-mediated activation of the spike protein

Millet, J. K., & Whittaker, G. R. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1407087111 · Cited by 673 · see citing works

Role of hemagglutinin cleavage for the pathogenicity of influenza virus.

Steinhauer, D. A. (1999) · Virology · doi:10.1006/viro.1999.9716 · Cited by 663 · see citing works

GraFix: sample preparation for single-particle electron cryomicroscopy

Kastner, B., Fischer, N., Golas, M. M., Sander, B. O., Dube, P., Boehringer, D., Hartmuth, K., Deckert, J., Hauer, F., Wolf, E., et al. (2007) · Nature Methods · doi:10.1038/nmeth1139 · Cited by 578 · see citing works

Emergence of SARS-CoV-2 through recombination and strong purifying selection

Li, X., Giorgi, E. E., Marichannegowda, M. H., Foley, B. T., Xiao, C., Kong, X., Chen, Y., Gnanakaran, S., Korber, B., & Gao, F. (2020) · Science Advances · doi:10.1126/sciadv.abb9153 · Cited by 392 · see citing works

Namdinator – automatic molecular dynamics flexible fitting of structural models into cryo-EM and crystallography experimental maps

Kidmose, R. T., Juhl, J., Nissen, P., Boesen, T. P., Karlsen, J. L., & Pedersen, B. P. (2019) · IUCrJ · doi:10.1107/s2052252519007619 · Cited by 387 · see citing works

One number does not fit all: Mapping local variations in resolution in cryo-EM reconstructions

Giovanni Cardone, A., Heymann, J. B., & Steven, A. C. (2013) · Journal of Structural Biology · doi:10.1016/j.jsb.2013.08.002 · Cited by 384 · see citing works

Rare driver mutations in head and neck squamous cell carcinomas converge on NOTCH signaling

Loganathan, S. K., Schleicher, K., Malik, A., Quevedo, R., Langille, E. R., Teng, K., Oh, R. H., Rathod, B., Tsai, R., Samavarchi‐Tehrani, P., et al. (2020) · Science · doi:10.1126/science.aax0902 · Cited by 286 · see citing works

Coexistence of multiple coronaviruses in several bat colonies in an abandoned mineshaft

Ge, X.-Y., Wang, N., Zhang, W., Hu, B., Li, B., Zhang, Y.-Z., Zhou, J.-H., Luo, C.-M., Yang, X., Wu, L.-J., et al. (2016) · Virologica Sinica · doi:10.1007/s12250-016-3713-9 · Cited by 153 · see citing works

Novel SARS-like Betacoronaviruses in Bats, China, 2011

Yang, L., Wú, Z., Ren, X., Yang, F., He, G., Zhang, J., Dong, J., Sun, L., Zhu, Y., Du, J., et al. (2013) · Emerging infectious diseases · doi:10.3201/eid1906.121648 · Cited by 109 · see citing works

Characteristics of SARS-CoV-2 and COVID-19

Hu, B., Guo, H., Zhou, P., & Shi, Z.-L. (2021) · Nature Reviews Microbiology · doi:10.1038/s41579-020-00459-7 · Cited by 5,291 · see citing works

Post-acute COVID-19 syndrome

Nalbandian, A., Sehgal, K., Gupta, A., Madhavan, M. V., McGroder, C., Stevens, J. S., Cook, J. R., Nordvig, A. S., Shalev, D., Sehrawat, T. S., et al. (2021) · Nature Medicine · doi:10.1038/s41591-021-01283-z · Cited by 4,862 · see citing works

SARS-CoV-2 variants, spike mutations and immune escape

Harvey, W. T., Carabelli, A. M., Jackson, B., Gupta, R. K., Thomson, E. C., Harrison, E. M., Ludden, C., Reeve, R., Rambaut, A., COVID-19 Genomics UK (COG-UK) Consortium, et al. (2021) · Nature Reviews Microbiology · doi:10.1038/s41579-021-00573-0 · Cited by 3,528 · see citing works

Deep Mutational Scanning of SARS-CoV-2 Receptor Binding Domain Reveals Constraints on Folding and ACE2 Binding

Starr, T. N., Greaney, A. J., Hilton, S. K., Ellis, D., Crawford, K. H. D., Dingens, A. S., Navarro, M. J., Bowen, J. E., Tortorici, M. A., Walls, A. C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.08.012 · Cited by 1,956 · see citing works

Genomics and epidemiology of the P.1 SARS-CoV-2 lineage in Manaus, Brazil

Faria, N. R., Mellan, T. A., Whittaker, C., Claro, I. M., Candido, D. D. S., Mishra, S., Crispim, M. A. E., Sales, F. C. S., Hawryluk, I., McCrone, J. T., et al. (2021) · Science · doi:10.1126/science.abh2644 · Cited by 1,461 · see citing works

SARS-CoV-2 B.1.617.2 Delta variant replication and immune evasion

Mlcochova, P., Kemp, S. A., Dhar, M. S., Papa, G., Meng, B., Ferreira, I. A. T. M., Datir, R., Collier, D. A., Albecka, A., Singh, S., et al. (2021) · Nature · doi:10.1038/s41586-021-03944-y · Cited by 1,337 · see citing works

The T cell immune response against SARS-CoV-2

Moss, P. A. H. (2022) · Nature Immunology · doi:10.1038/s41590-021-01122-w · Cited by 1,205 · see citing works

SARS-CoV-2 evolution during treatment of chronic infection

Kemp, S. A., Collier, D. A., Datir, R. P., Ferreira, I. A. T. M., Gayed, S., Jahun, A., Hosmillo, M., Rees-Spear, C., Mlcochova, P., Lumb, I. U., et al. (2021) · Nature · doi:10.1038/s41586-021-03291-y · Cited by 1,097 · see citing works

N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2

McCallum, M., De Marco, A., Lempp, F. A., Tortorici, M. A., Pinto, D., Walls, A. C., Beltramello, M., Chen, A., Liu, Z., Zatta, F., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.028 · Cited by 901 · see citing works

Preexisting and de novo humoral immunity to SARS-CoV-2 in humans

Ng, K. W., Faulkner, N., Cornish, G. H., Rosa, A., Harvey, R., Hussain, S., Ulferts, R., Earl, C., Wrobel, A. G., Benton, D. J., et al. (2020) · Science · doi:10.1126/science.abe1107 · Cited by 886 · see citing works

Receptor binding and priming of the spike protein of SARS-CoV-2 for membrane fusion

Benton, D. J., Wrobel, A. G., Xu, P., Roustan, C., Martin, S. R., Rosenthal, P. B., Skehel, J. J., & Gamblin, S. J. (2020) · Nature · doi:10.1038/s41586-020-2772-0 · Cited by 763 · see citing works

Loss of furin cleavage site attenuates SARS-CoV-2 pathogenesis

Johnson, B. A., Xie, X., Bailey, A. L., Kalveram, B., Lokugamage, K. G., Muruato, A., Zou, J., Zhang, X., Juelich, T., Smith, J. K., et al. (2021) · Nature · doi:10.1038/s41586-021-03237-4 · Cited by 694 · see citing works

Case Study: Prolonged Infectious SARS-CoV-2 Shedding from an Asymptomatic Immunocompromised Individual with Cancer

Avanzato, V. A., Matson, M. J., Seifert, S. N., Pryce, R., Williamson, B. N., Anzick, S. L., Barbian, K., Judson, S. D., Fischer, E. R., Martens, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.049 · Cited by 703 · see citing works

Potent SARS-CoV-2 neutralizing antibodies directed against spike N-terminal domain target a single supersite

Cerutti, G., Guo, Y., Zhou, T., Gorman, J., Lee, M., Rapp, M., Reddem, E. R., Yu, J., Bahna, F., Bimela, J., et al. (2021) · Cell Host &amp; Microbe · doi:10.1016/j.chom.2021.03.005 · Cited by 519 · see citing works

SARS-CoV-2 N protein promotes NLRP3 inflammasome activation to induce hyperinflammation

Pan, P., Shen, M., Yu, Z., Ge, W., Chen, K., Tian, M., Xiao, F., Wang, Z., Wang, J., Jia, Y., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25015-6 · Cited by 496 · see citing works

Virus-Receptor Interactions of Glycosylated SARS-CoV-2 Spike and Human ACE2 Receptor

Zhao, P., Praissman, J. L., Grant, O. C., Cai, Y., Xiao, T., Rosenbalm, K. E., Aoki, K., Kellman, B. P., Bridger, R., Barouch, D. H., et al. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.08.004 · Cited by 444 · see citing works

Free fatty acid binding pocket in the locked structure of SARS-CoV-2 spike protein

Toelzer, C., Gupta, K., Yadav, S. K. N., Borucu, U., Davidson, A. D., Williamson, M. K., Shoemark, D. K., Garzoni, F., Staufer, O., Milligan, R., et al. (2020) · Science · doi:10.1126/science.abd3255 · Cited by 419 · see citing works

The emergence, genomic diversity and global spread of SARS-CoV-2

Li, J., Lai, S., Gao, G. F., & Shi, W. (2021) · Nature · doi:10.1038/s41586-021-04188-6 · Cited by 408 · see citing works

Recurrent emergence of SARS-CoV-2 spike deletion H69/V70 and its role in the Alpha variant B.1.1.7

Meng, B., Kemp, S. A., Papa, G., Datir, R. P., Ferreira, I. A. T. M., Marelli, S., Harvey, W. T., Lytras, S., Mohamed, A., Gallo, G., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109292 · Cited by 397 · see citing works

Conformational dynamics of SARS-CoV-2 trimeric spike glycoprotein in complex with receptor ACE2 revealed by cryo-EM

Xu, C., Wang, Y., Liu, C., Zhang, C., Han, W., Hong, X., Wang, Y., Qin, H., Wang, S., Zhao, Q., et al. (2020) · Science Advances · doi:10.1126/sciadv.abe5575 · Cited by 377 · see citing works

Cryo-EM Structures of SARS-CoV-2 Spike without and with ACE2 Reveal a pH-Dependent Switch to Mediate Endosomal Positioning of Receptor-Binding Domains

Zhou, T., Tsybovsky, Y., Gorman, J., Rapp, M., Cerutti, G., Chuang, G., Katsamba, P. S., Sampson, J. M., Schön, A., Bimela, J. S., et al. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.11.004 · Cited by 340 · see citing works

TMPRSS2 expression dictates the entry route used by SARS‐CoV‐2 to infect host cells

Koch, J., Uckeley, Z. M., Doldan, P., Stanifer, M. L., Boulant, S., & Lozach, P. (2021) · The EMBO Journal · doi:10.15252/embj.2021107821 · Cited by 345 · see citing works

SARS-CoV-2 variant evasion of monoclonal antibodies based on in vitro studies

Cox, M., Peacock, T. P., Harvey, W. T., Hughes, J., Wright, D. W., Willett, B. J., Thomson, E. C., Gupta, R. K., Peacock, S. J., Robertson, D. L., et al. (2022) · Nature Reviews Microbiology · doi:10.1038/s41579-022-00809-7 · Cited by 336 · see citing works

Molecular mechanism of interaction between SARS-CoV-2 and host cells and interventional therapy

Zhang, Q., Xiang, R., Huo, S., Zhou, Y., Jiang, S., Wang, Q., & Yu, F. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00653-w · Cited by 341 · see citing works

COVID-19 mRNA vaccines: Platforms and current developments

Szabó, G. T., Mahiny, A. J., & Vlatkovic, I. (2022) · Molecular Therapy · doi:10.1016/j.ymthe.2022.02.016 · Cited by 308 · see citing works

Structural biology of SARS-CoV-2: open the door for novel therapies

Yan, W., Zheng, Y., Zeng, X., He, B., & Cheng, W. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00884-5 · Cited by 293 · see citing works

Genetic and structural basis for SARS-CoV-2 variant neutralization by a two-antibody cocktail

Dong, J., Zost, S. J., Greaney, A. J., Starr, T. N., Dingens, A. S., Chen, E. C., Chen, R. E., Case, J. B., Sutton, R. E., Gilchuk, P., et al. (2021) · Nature Microbiology · doi:10.1038/s41564-021-00972-2 · Cited by 285 · see citing works

Recurrent emergence and transmission of a SARS-CoV-2 spike deletion H69/V70

Kemp, S. A., Meng, B., Ferriera, I. A., Datir, R., Harvey, W. T., Papa, G., Lytras, S., Collier, D. A., Mohamed, A., Gallo, G., et al. (2020) · doi:10.1101/2020.12.14.422555 · Cited by 252 · see citing works

The SARS-CoV-2 Lambda variant exhibits enhanced infectivity and immune resistance

Kimura, I., Kosugi, Y., Wu, J., Zahradník, J., Yamasoba, D., Butlertanaka, E. P., Tanaka, Y., Uriu, K., Liu, Y., Morizako, N., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.110218 · Cited by 210 · see citing works

Mutations and Evolution of the SARS-CoV-2 Spike Protein

Magazine, N., Zhang, T., Wu, Y., McGee, M. C., Veggiani, G., & Huang, W. (2022) · Viruses · doi:10.3390/v14030640 · Cited by 218 · see citing works

Hydroxychloroquine-mediated inhibition of SARS-CoV-2 entry is attenuated by TMPRSS2

Ou, T., Mou, H., Zhang, L., Ojha, A., Choe, H., & Farzan, M. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009212 · Cited by 208 · see citing works

The SARS-CoV-2 Spike protein has a broad tropism for mammalian ACE2 proteins

Conceicao, C., Thakur, N., Human, S., Kelly, J. T., Logan, L., Bialy, D., Bhat, S., Stevenson-Leggett, P., Zagrajek, A. K., Hollinghurst, P., et al. (2020) · PLoS Biology · doi:10.1371/journal.pbio.3001016 · Cited by 211 · see citing works

Waves and variants of SARS-CoV-2: understanding the causes and effect of the COVID-19 catastrophe

Thakur, V., Bhola, S., Thakur, P., Patel, S. K. S., Kulshrestha, S., Ratho, R. K., & Kumar, P. (2022) · Infection · doi:10.1007/s15010-021-01734-2 · Cited by 210 · see citing works

Real-Time Conformational Dynamics of SARS-CoV-2 Spikes on Virus Particles

Lu, M., Uchil, P. D., Li, W., Zheng, D., Terry, D. S., Gorman, J., Shi, W., Zhang, B., Zhou, T., Ding, S., et al. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.11.001 · Cited by 194 · see citing works

Immune Evasion of SARS-CoV-2 Emerging Variants: What Have We Learnt So Far?

Lazarević, I., Pravica, V., Miljanovic, D., & Cupic, M. D. (2021) · Viruses · doi:10.3390/v13071192 · Cited by 188 · see citing works

Proteolytic activation of SARS‐CoV‐2 spike protein

Takeda, M. (2021) · Microbiology and Immunology · doi:10.1111/1348-0421.12945 · Cited by 182 · see citing works

Reduced neutralisation of the Delta (B.1.617.2) SARS-CoV-2 variant of concern following vaccination

Davis, C., Logan, N. A., Tyson, G. B., Orton, R. J., Harvey, W. T., Perkins, J. S., Mollett, G., Blacow, R., Peacock, T. P., Barclay, W., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1010022 · Cited by 188 · see citing works

Peptide and peptide-based inhibitors of SARS-CoV-2 entry

Schütz, D., Ruiz‐Blanco, Y. B., Münch, J., Kirchhoff, F., Sánchez‐García, E., & Müller, J. A. (2020) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2020.11.007 · Cited by 179 · see citing works

Structural basis for SARS-CoV-2 Delta variant recognition of ACE2 receptor and broadly neutralizing antibodies

Wang, Y., Liu, C., Zhang, C., Wang, Y., Qin, H., Xu, S., Li, Z., Yang, Y. P., Huang, Z. W., & Cong, Y. (2022) · Nature Communications · doi:10.1038/s41467-022-28528-w · Cited by 169 · see citing works

Diversity and evolution of the animal virome

Harvey, E., & Holmes, E. C. (2022) · Nature Reviews Microbiology · doi:10.1038/s41579-021-00665-x · Cited by 165 · see citing works

The structural basis of accelerated host cell entry by SARS‐CoV‐2†

Seyran, M., Takayama, K., Uversky, V. N., Lundstrom, K. H., Palù, G., Sherchan, S. P., Attrish, D., Rezaei, N., Aljabali, A. A. A., Ghosh, S., et al. (2020) · FEBS Journal · doi:10.1111/febs.15651 · Cited by 159 · see citing works

The effect of the D614G substitution on the structure of the spike glycoprotein of SARS-CoV-2

Benton, D. J., Wrobel, A. G., Roustan, C., Borg, A., Xu, P., Martin, S. R., Rosenthal, P. B., Skehel, J. J., & Gamblin, S. J. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2022586118 · Cited by 153 · see citing works

Omicron SARS-CoV-2 mutations stabilize spike up-RBD conformation and lead to a non-RBM-binding monoclonal antibody escape

Zhao, Z., Zhou, J., Tian, M., Huang, M., Liu, S., Xie, Y., Han, P., Bai, C., Han, P., Zheng, A., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-32665-7 · Cited by 146 · see citing works

TMEM106B is a receptor mediating ACE2-independent SARS-CoV-2 cell entry

Baggen, J., Jacquemyn, M., Persoons, L., Vanstreels, E., Pye, V. E., Wrobel, A. G., Calvaresi, V., Martin, S. R., Roustan, C., Cronin, N., et al. (2023) · Cell · doi:10.1016/j.cell.2023.06.005 · Cited by 153 · see citing works

SARS-CoV-2 can recruit a heme metabolite to evade antibody immunity

Rosa, A., Pye, V. E., Graham, C., Muir, L., Seow, J., Ng, K., Cook, N., Rees-Spear, C., Parker, E., dos Santos, M. S., et al. (2021) · SciAdv · doi:10.1126/sciadv.abg7607 · Cited by 120 · see citing works

A potent SARS-CoV-2 neutralising nanobody shows therapeutic efficacy in the Syrian golden hamster model of COVID-19

Huo, J., Mikolajek, H., Bas, A. L., Clark, J., Sharma, P., Kipar, A., Dormon, J., Norman, C. S., Weckener, M., Clare, D., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25480-z · Cited by 146 · see citing works

SARS-CoV-2 entry into human airway organoids is serine protease-mediated and facilitated by the multibasic cleavage site

Mykytyn, A. Z., Breugem, T. I., Riesebosch, S., Schipper, D., van den Doel, P. B., Rottier, R. J., Lamers, M. M., & Haagmans, B. L. (2021) · eLife · doi:10.7554/elife.64508 · Cited by 150 · see citing works

Effect of SARS-CoV-2 B.1.1.7 mutations on spike protein structure and function

Yang, T., Yu, P., Chang, Y., Liang, K.-H., Tso, H.-C., Ho, M., Wy, C., Lin, H.-T., Wu, H., & Hsu, S. D. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-021-00652-z · Cited by 159 · see citing works

SARS-CoV-2 and Three Related Coronaviruses Utilize Multiple ACE2 Orthologs and Are Potently Blocked by an Improved ACE2-Ig

Li, Y., Wang, H., Tang, X., Fang, S., Ma, D., Du, C., Wang, Y., Pan, H., Yao, W., Zhang, R., et al. (2020) · Journal of Virology · doi:10.1128/jvi.01283-20 · Cited by 142 · see citing works

The Polybasic Cleavage Site in SARS-CoV-2 Spike Modulates Viral Sensitivity to Type I Interferon and IFITM2

Winstone, H., Lista, M. J., Reid, A. C., Bouton, C. R., Pickering, S., Galão, R. P., Kerridge, C., Doores, K. J., Swanson, C. M., & Neil, S. J. D. (2021) · Journal of Virology · doi:10.1128/jvi.02422-20 · Cited by 135 · see citing works

The SARS-CoV-2 Spike protein disrupts human cardiac pericytes function through CD147 receptor-mediated signalling: a potential non-infective mechanism of COVID-19 microvascular disease

Avolio, E., Carrabba, M., Milligan, R., Williamson, M. K., Beltrami, A. P., Gupta, K., Elvers, K. T., Gamez, M., Foster, R. R., Gillespie, K. M., et al. (2021) · Clinical Science · doi:10.1042/cs20210735 · Cited by 144 · see citing works

D614G mutation of SARS-CoV-2 spike protein enhances viral infectivityPreprint

Hu, J., He, C., Gao, Q., Zhang, G., Cao, X., Long, Q., Deng, H., Huang, L., Chen, J., Wang, K., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.20.161323 · Cited by 138 · see citing works

Binding and molecular basis of the bat coronavirus RaTG13 virus to ACE2 in humans and other species

Liu, K., Pan, X., Li, L., Yu, F., Zheng, A., Du, P., Han, P., Meng, Y., Zhang, Y., Wu, L., et al. (2021) · Cell · doi:10.1016/j.cell.2021.05.031 · Cited by 139 · see citing works

N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2

McCallum, M., Marco, A. D., Lempp, F., Tortorici, M. A., Pinto, D., Walls, A. C., Beltramello, M., Chen, A., Liu, Z., Zatta, F., et al. (2021) · doi:10.1101/2021.01.14.426475 · Cited by 901 · see citing works

Proteolytic Activation of SARS-CoV-2 Spike at the S1/S2 Boundary: Potential Role of Proteases beyond Furin

Tang, T., Jaimes, J. A., Bidon, M. K., Straus, M. R., Daniel, S., & Whittaker, G. R. (2021) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.0c00701 · Cited by 130 · see citing works

Antibody and B cell responses to SARS-CoV-2 infection and vaccination

Röltgen, K., & Boyd, S. D. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.06.009 · Cited by 136 · see citing works

Molecular diversity of coronavirus host cell entry receptors

Millet, J. K., Jaimes, J. A., & Whittaker, G. R. (2020) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuaa057 · Cited by 129 · see citing works

The SARS-CoV-2 and other human coronavirus spike proteins are fine-tuned towards temperature and proteases of the human airways

Laporte, M., Raeymaekers, V., Berwaer, R. V., Vandeput, J., Marchand-Casas, I., Thibaut, H. J., Looveren, D. V., Martens, K., Hoffmann, M., Maes, P., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009500 · Cited by 123 · see citing works

Zoonotic disease and virome diversity in bats

Brussel, K. V., & Holmes, E. C. (2021) · Current Opinion in Virology · doi:10.1016/j.coviro.2021.12.008 · Cited by 128 · see citing works

Structure genomics of SARS-CoV-2 and its Omicron variant: drug design templates for COVID-19

Wu, C., Yin, W., Jiang, Y., & Xu, H. E. (2022) · Acta Pharmacologica Sinica · doi:10.1038/s41401-021-00851-w · Cited by 127 · see citing works

The role of cell surface sialic acids for SARS-CoV-2 infection

Sun, X. (2021) · Glycobiology · doi:10.1093/glycob/cwab032 · Cited by 120 · see citing works

Characterising proteolysis during SARS-CoV-2 infection identifies viral cleavage sites and cellular targets with therapeutic potential

Meyer, B., Chiaravalli, J., Gellenoncourt, S., Brownridge, P., Bryne, D. P., Daly, L. A., Grauslys, A., Walter, M., Agou, F., Chakrabarti, L. A., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25796-w · Cited by 116 · see citing works

Bat and pangolin coronavirus spike glycoprotein structures provide insights into SARS-CoV-2 evolution

Zhang, S., Qiao, S., Yu, J., Zeng, J., Shan, S., Tian, L., Lan, J., Zhang, L., & Wang, X. (2021) · Nature Communications · doi:10.1038/s41467-021-21767-3 · Cited by 113 · see citing works

Selection Analysis Identifies Clusters of Unusual Mutational Changes in Omicron Lineage BA.1 That Likely Impact Spike Function

Martin, D. P., Lytras, S., Lucaci, A. G., Maier, W., Grüning, B. A., Shank, S. D., Weaver, S., MacLean, O. A., Orton, R. J., Lemey, P., et al. (2022) · Molecular Biology and Evolution · doi:10.1093/molbev/msac061 · Cited by 124 · see citing works

Structural basis for the different states of the spike protein of SARS-CoV-2 in complex with ACE2

Yan, R., Zhang, Y., Li, Y., Ye, F., Guo, Y., Xia, L., Zhong, X., Chi, X., & Zhou, Q. (2021) · Cell Research · doi:10.1038/s41422-021-00490-0 · Cited by 113 · see citing works

Emergence in late 2020 of multiple lineages of SARS-CoV-2 Spike protein variants affecting amino acid position 677Preprint

Hodcroft, E. B., Domman, D., Snyder, D. J., Oguntuyo, K. Y., Diest, M. V., Densmore, K. H., Schwalm, K. C., Femling, J., Carroll, J. L., Scott, R. S., et al. (2021) · medRxiv · doi:10.1101/2021.02.12.21251658 · Cited by 109 · see citing works

Essential role of TMPRSS2 in SARS-CoV-2 infection in murine airways

Iwata‐Yoshikawa, N., Kakizaki, M., Shiwa-Sudo, N., Okura, T., Tahara, M., Fukushi, S., Maeda, K., Kawase, M., Asanuma, H., Tomita, Y., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-33911-8 · Cited by 108 · see citing works

The Antiviral, Anti-Inflammatory Effects of Natural Medicinal Herbs and Mushrooms and SARS-CoV-2 Infection

Shahzad, F., Anderson, D. C., & Najafzadeh, M. (2020) · Nutrients · doi:10.3390/nu12092573 · Cited by 110 · see citing works

HIV-1 and SARS-CoV-2: Patterns in the evolution of two pandemic pathogens

Fischer, W., Giorgi, E. E., Chakraborty, S., Nguyen, K., Tanmoy Bhattacharya, A., Theiler, J. P., Goloboff, P. A., Yoon, H., Abfalterer, W., Foley, B. T., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.05.012 · Cited by 106 · see citing works

A selective sweep in the Spike gene has driven SARS-CoV-2 human adaptation

Kang, L., He, G., Sharp, A. K., Wang, X., Brown, A. M., Michalak, P., & Weger‐Lucarelli, J. (2021) · Cell · doi:10.1016/j.cell.2021.07.007 · Cited by 97 · see citing works

Novel cleavage sites identified in SARS-CoV-2 spike protein reveal mechanism for cathepsin L-facilitated viral infection and treatment strategies

Zhao, M., Zhu, Y., Zhang, L., Zhong, G., Tai, L., Liu, S., Yin, G., Lü, J., He, Q., Li, M.-J., et al. (2022) · Cell Discovery · doi:10.1038/s41421-022-00419-w · Cited by 98 · see citing works

Tissue-specific and interferon-inducible expression of nonfunctional ACE2 through endogenous retroelement co-option

Ng, K. W., Attig, J., Bolland, W., Young, G. R., Major, J., Wrobel, A. G., Gamblin, S. J., Wack, A., & Kassiotis, G. (2020) · Nature Genetics · doi:10.1038/s41588-020-00732-8 · Cited by 103 · see citing works

In silico comparison of SARS-CoV-2 spike protein-ACE2 binding affinities across species and implications for virus origin

Piplani, S., Singh, P. K., Winkler, D. A., & Petrovsky, N. (2021) · Scientific Reports · doi:10.1038/s41598-021-92388-5 · Cited by 105 · see citing works

CD147-spike protein interaction in COVID-19: Get the ball rolling with a novel receptor and therapeutic target

Behl, T., Kaur, I., Aleya, L., Sehgal, A., Singh, S., Sharma, N., Bhatia, S., Al‐Harrasi, A., & BUNGAU, S. G. (2021) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2021.152072 · Cited by 102 · see citing works

Development and structural basis of a two-MAb cocktail for treating SARS-CoV-2 infections

Zhang, C., Wang, Y., Zhu, Y., Liu, C., Gu, C., Xu, S., Wang, Y., Zhou, Y., Wang, Y., Han, W., et al. (2021) · Nature Communications · doi:10.1038/s41467-020-20465-w · Cited by 101 · see citing works

Angiotensin-converting enzyme 2 (ACE2) expression increases with age in patients requiring mechanical ventilation

Baker, S. A., Kwok, S., Berry, G. J., & Montine, T. J. (2021) · PLoS ONE · doi:10.1371/journal.pone.0247060 · Cited by 97 · see citing works

The SARS-CoV-2 spike protein: balancing stability and infectivity

Berger, I., & Schaffitzel, C. (2020) · Cell Research · doi:10.1038/s41422-020-00430-4 · Cited by 96 · see citing works

Nucleic Acid-Based Diagnostic Tests for the Detection SARS-CoV-2: An Update

Yu, C. Y., Chan, K., Yean, C. Y., & Ang, G. Y. (2021) · Diagnostics · doi:10.3390/diagnostics11010053 · Cited by 93 · see citing works

Role of host factors in SARS-CoV-2 entry

Evans, J. P., & Liu, S. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100847 · Cited by 93 · see citing works

Fine-tuning the spike: role of the nature and topology of the glycan shield in the structure and dynamics of the SARS-CoV-2 S

Harbison, A. M., Fogarty, C. A., Phung, T. K., Satheesan, A., Schulz, B. L., & Fadda, E. (2021) · Chemical Science · doi:10.1039/d1sc04832e · Cited by 87 · see citing works

Computational Insights into the Conformational Accessibility and Binding Strength of SARS-CoV-2 Spike Protein to Human Angiotensin-Converting Enzyme 2

Peng, C., Zhu, Z., Shi, Y., Wang, X., Mu, K., Yang, Y., Zhang, X., Xu, Z., & Zhu, W. (2020) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.0c02958 · Cited by 89 · see citing works

The origins of COVID‐19 pandemic: A brief overview

Hao, Y., Wang, Y., Wang, M.-Y., Zhou, L., Shi, J., Cao, J., & Wang, D. (2022) · Transboundary and Emerging Diseases · doi:10.1111/tbed.14732 · Cited by 103 · see citing works

Challenges and opportunities for antiviral monoclonal antibodies as COVID-19 therapy

Cruz-Teran, C. A., Tiruthani, K., McSweeney, M. D., Ma, A. D., Pickles, R., & Lai, S. (2020) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2020.12.004 · Cited by 77 · see citing works

Population immunity predicts evolutionary trajectories of SARS-CoV-2

Meijers, M., Ruchnewitz, D., Eberhardt, J., Łuksza, M., & Lässig, M. (2023) · Cell · doi:10.1016/j.cell.2023.09.022 · Cited by 97 · see citing works

Identification of immunodominant linear epitopes from SARS-CoV-2 patient plasma

Soler, L. F., Daguer, J., Barluenga, S., Vadas, O., Cohen, P., Pagano, S., Yerly, S., Kaiser, L., Vuilleumier, N., & Winssinger, N. (2020) · PLoS ONE · doi:10.1371/journal.pone.0238089 · Cited by 89 · see citing works

Structure and binding properties of Pangolin-CoV spike glycoprotein inform the evolution of SARS-CoV-2

Wrobel, A. G., Benton, D. J., Xu, P., Calder, L. J., Borg, A., Roustan, C., Martin, S. R., Rosenthal, P. B., Skehel, J. J., & Gamblin, S. J. (2021) · Nature Communications · doi:10.1038/s41467-021-21006-9 · Cited by 86 · see citing works

Immunogenicity and efficacy of mRNA COVID-19 vaccine MRT5500 in preclinical animal models

Kalnin, K. V., Plitnik, T., Kishko, M., Zhang, J., Zhang, D., Beauvais, A., Anosova, N. G., Tibbitts, T., DiNapoli, J., Ulinski, G., et al. (2021) · npj Vaccines · doi:10.1038/s41541-021-00324-5 · Cited by 82 · see citing works

Structural dynamics in the evolution of SARS-CoV-2 spike glycoprotein

Calvaresi, V., Wrobel, A. G., Toporowska, J., Hammerschmid, D., Doores, K. J., Bradshaw, R. T., Parsons, R. B., Benton, D. J., Roustan, C., Reading, E., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36745-0 · Cited by 82 · see citing works

Recent Advances of Conducting Polymers and Their Composites for Electrochemical Biosensing Applications

Luong, J. H. T., Narayan, T., Solanki, S., & Malhotra, B. D. (2020) · Journal of Functional Biomaterials · doi:10.3390/jfb11040071 · Cited by 79 · see citing works

SARS-CoV-2 Infection: New Molecular, Phylogenetic, and Pathogenetic Insights. Efficacy of Current Vaccines and the Potential Risk of Variants

Rotondo, J. C., Martini, F., Maritati, M., Mazziotta, C., Mauro, G. D., Lanzillotti, C., Barp, N., Gallerani, A., Tognon, M. G., & Contini, C. (2021) · Viruses · doi:10.3390/v13091687 · Cited by 78 · see citing works

SARS-CoV-2 B.1.617.2 Delta variant replication, sensitivity to neutralising antibodies and vaccine breakthrough

Mlcochova, P., Kemp, S., Dhar, M. S., Papa, G., Meng, B., Mishra, S., Whittaker, C., Mellan, T., Ferreira, I., Datir, R., et al. (2021) · doi:10.1101/2021.05.08.443253 · Cited by 90 · see citing works

Site-Specific O-Glycosylation Analysis of SARS-CoV-2 Spike Protein Produced in Insect and Human Cells

Bagdonaite, I., Thompson, A. J., Wang, X., Søgaard, M., Fougeroux, C. E., Frank, M., Diedrich, J. K., Yates, J. R., Salanti, A., Vakhrushev, S. Y., et al. (2021) · Viruses · doi:10.3390/v13040551 · Cited by 77 · see citing works

Assassination and the Law of Armed Conflict

Zengel, P. (1991) · eYLS (Yale Law School) · Cited by 75 · see citing works

Chemosensory Dysfunction in COVID-19: Integration of Genetic and Epidemiological Data Points to D614G Spike Protein Variant as a Contributing Factor

Butowt, R., Bilińska, K., & von Bartheld, C. S. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00596 · Cited by 76 · see citing works

Evolution of the SARS-CoV-2 Omicron spike

Parsons, R., & Acharya, P. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113444 · Cited by 74 · see citing works

The Emergence of the Spike Furin Cleavage Site in SARS-CoV-2

Chan, Y. A., & Zhan, S. H. (2021) · Molecular Biology and Evolution · doi:10.1093/molbev/msab327 · Cited by 73 · see citing works

Evolution of the SARS-CoV-2 spike protein in the human host

Wrobel, A. G., Benton, D. J., Roustan, C., Borg, A., Hussain, S., Martin, S. R., Rosenthal, P. B., Skehel, J. J., & Gamblin, S. J. (2022) · Nature Communications · doi:10.1038/s41467-022-28768-w · Cited by 68 · see citing works

Multivalent 9-O-Acetylated-sialic acid glycoclusters as potent inhibitors for SARS-CoV-2 infection

Petitjean, S. J. L., Chen, W., Koehler, M., Jimmidi, R., Yang, J., Mohammed, D., Juniku, B., Stanifer, M. L., Boulant, S., Vincent, S. P., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30313-8 · Cited by 70 · see citing works

The inherent flexibility of receptor binding domains in SARS-CoV-2 spike protein

Dokainish, H. M., Re, S., Mori, T., Kobayashi, C., Jung, J., & Sugita, Y. (2022) · eLife · doi:10.7554/elife.75720 · Cited by 68 · see citing works

Insights on the mutational landscape of the SARS-CoV-2 Omicron variant receptor-binding domain

Miller, N. L., Clark, T., Raman, R., & Sasisekharan, R. (2022) · Cell Reports Medicine · doi:10.1016/j.xcrm.2022.100527 · Cited by 78 · see citing works

Bat and pangolin coronavirus spike glycoprotein structures provide insights into SARS-CoV-2 evolution

Zhang, S., Qiao, S., Yu, J., Zeng, J., Shan, S., Tian, L., Lan, J., Zhang, L., & Wang, X. (2021) · Zenodo (CERN European Organization for Nuclear Research) · doi:10.5281/zenodo.17262000

Receptor binding and priming of the spike protein of SARS-CoV-2 for membrane fusion

Benton, D. J., Wrobel, A. G., Xu, P., Roustan, C., Martin, S. R., Rosenthal, P. B., Skehel, J. J., & Gamblin, S. J. (2020) · Nature · doi:10.1038/s41586-020-2772-0 · Cited by 763 · see citing works

Structural basis of receptor recognition by SARS-CoV-2

Shang, J., Ye, G., Shi, K., Wan, Y., Luo, C., Aihara, H., Geng, Q., Auerbach, A., & Li, F. (2020) · Nature · doi:10.1038/s41586-020-2179-y · Cited by 3,661 · see citing works

Structural Analysis Of The Receptor Binding Motif Of Spike Glycoprotein Explains The High Stability Of SARS-CoV-2 RBD/hACE2-complexPreprint

Pandya, A. N. (2020) · doi:10.31219/osf.io/e42tb

Structure and binding properties of Pangolin-CoV spike glycoprotein inform the evolution of SARS-CoV-2

Wrobel, A. G., Benton, D. J., Xu, P., Calder, L. J., Borg, A., Roustan, C., Martin, S. R., Rosenthal, P. B., Skehel, J. J., & Gamblin, S. J. (2021) · Nature Communications · doi:10.1038/s41467-021-21006-9 · Cited by 86 · see citing works