The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2
Open accessAbstract
How SARS-CoV-2 binds to human cells: Scientists are racing to learn the secrets of severe acute respiratory syndrome–coronavirus 2 (SARS-CoV-2), which is the cause of the pandemic disease COVID-19. The first step in viral entry is the binding of the viral trimeric spike protein to the human receptor angiotensin-converting enzyme 2 (ACE2). Yan et al. present the structure of human ACE2 in complex with a membrane protein that it chaperones, B 0 AT1. In the context of this complex, ACE2 is a dimer. A further structure shows how the receptor binding domain of SARS-CoV-2 interacts with ACE2 and suggests that it is possible that two trimeric spike proteins bind to an ACE2 dimer. The structures provide a basis for the development of therapeutics targeting this crucial interaction. Science , this issue p. 1444
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
A novel coronavirus from patients with pneumonia in China, 2019
Zhu, N., Zhang, D., Wang, W., Li, X., Yang, B., Song, J., Zhao, X., Huang, B., Shi, W., Lu, R., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2001017 · Cited by 28,244
PHENIX : 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
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
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
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
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
Identification of a novel coronavirus in patients with severe acute respiratory syndrome
Drosten, C., Günther, S., Preiser, W., van der Werf, S., Brodt, H.-R., Becker, S., Rabenau, H., Panning, M., Kolesnikova, L., Fouchier, R. A. M., et al. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa030747 · Cited by 4,574
A crucial role of angiotensin converting enzyme 2 (ACE2) in SARS coronavirus–induced lung injury
Kuba, K., Imai, Y., Rao, S., Gao, H., Guo, F., Guan, B., Huan, Y., Yang, P., Zhang, Y., Deng, W., et al. (2005) · Nature Medicine · doi:10.1038/nm1267 · Cited by 3,445
Self-citationRosenthal, P. B., & Henderson, R. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.07.013 · Cited by 2,416
Angiotensin-converting enzyme 2 is an essential regulator of heart function
Crackower, M. A., Sarao, R., Oudit, G. Y., Yagil, C., Kozieradzki, I., Scanga, S. E., Oliveira-dos-Santos, A. J., da Costa, J., Zhang, L., Pei, Y., et al. (2002) · Nature · doi:10.1038/nature00786 · Cited by 1,733
Cited by
Pulmonary Vascular Endothelialitis, Thrombosis, and Angiogenesis in Covid-19
Ackermann, M., Verleden, S. E., Kuehnel, M., Haverich, A., Welte, T., Laenger, F., Vanstapel, A., Werlein, C., Stark, H., Tzankov, A., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2015432 · Cited by 5,613
Korber, B., Fischer, W. M., Gnanakaran, S., Yoon, H., Theiler, J., Abfalterer, W., Hengartner, N., Giorgi, E. E., Bhattacharya, T., Foley, B., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.043 · Cited by 4,281
Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2
Wang, Q., Zhang, Y., Wu, L., Niu, S., Song, C., Zhang, Z., Lu, G., Qiao, C., Hu, Y., Yuen, K.-Y., et al. (2020) · Cell · doi:10.1016/j.cell.2020.03.045 · Cited by 2,892
“During the revision of our manuscript, the full-length hACE2 structure was reported to form a dimer in the presence of B0AT1 (an amino acid transporter), as revealed by cryoelectron microscopy (cryo-EM) analysis (Yan et al., 2020).”
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
Evidence for gastrointestinal infection of SARS-CoV-2
Xiao, F., Tang, M., Zheng, X., Liu, Y., Li, X., & Shan, H. (2020) · Gastroenterology · doi:10.1053/j.gastro.2020.02.055 · Cited by 2,836
Rogers, J. P., Chesney, E., Oliver, D., Pollak, T. A., McGuire, P., Fusar-Poli, P., Zandi, M. S., Lewis, G., & David, A. S. (2020) · The Lancet Psychiatry · doi:10.1016/s2215-0366(20)30203-0 · Cited by 2,407
Longitudinal analyses reveal immunological misfiring in severe COVID-19
Lucas, C., Wong, P., Klein, J., Castro, T. B. R., Silva, J., Sundaram, M., Ellingson, M. K., Mao, T., Oh, J. E., Israelow, B., et al. (2020) · Nature · doi:10.1038/s41586-020-2588-y · Cited by 2,074
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
Human organoids: model systems for human biology and medicine
Kim, J., Koo, B.-K., & Knoblich, J. A. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0259-3 · Cited by 2,187
Neurological associations of COVID-19
Ellul, M. A., Benjamin, L., Singh, B., Lant, S., Michael, B. D., Easton, A., Kneen, R., Defres, S., Sejvar, J., & Solomon, T. (2020) · The Lancet Neurology · doi:10.1016/s1474-4422(20)30221-0 · Cited by 2,156
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
Gheblawi, M., Wang, K., Viveiros, A., Nguyen, Q., Zhong, J.-C., Turner, A. J., Raizada, M. K., Grant, M. B., & Oudit, G. Y. (2020) · Circulation Research · doi:10.1161/circresaha.120.317015 · Cited by 1,882
Airborne transmission of SARS-CoV-2: The world should face the reality
Morawska, L., & Cao, J. (2020) · Environment International · doi:10.1016/j.envint.2020.105730 · Cited by 1,728
Structural 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
SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies
Barnes, C. O., Jette, C. A., Abernathy, M. E., Dam, K.-M. A., Esswein, S. R., Gristick, H. B., Malyutin, A. G., Sharaf, N. G., Huey-Tubman, K. E., Lee, Y. E., et al. (2020) · Nature · doi:10.1038/s41586-020-2852-1 · Cited by 1,599
A neutralizing human antibody binds to the N-terminal domain of the Spike protein of SARS-CoV-2
Chi, X., Yan, R., Zhang, J., Zhang, G., Zhang, Y., Hao, M., Zhang, Z., Fan, P., Dong, Y., Yang, Y., et al. (2020) · Science · doi:10.1126/science.abc6952 · Cited by 1,385
Self-citationBurley, S. K., Bhikadiya, C., Bi, C., Bittrich, S., Chen, L., Crichlow, G. V., Christie, C. H., Dalenberg, K., Di Costanzo, L., Duarte, J. M., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkaa1038 · Cited by 1,581
“spike protein with angiotensin converting enzyme 2, 6M17 (25)] help explain the biological and biochemical mechanisms central to the pathogenicity of the virus.”
BackgroundSARS-CoV-2 Reverse Genetics Reveals a Variable Infection Gradient in the Respiratory Tract
Hou, Y. J., Okuda, K., Edwards, C. E., Martinez, D. R., Asakura, T., Dinnon, K. H., Kato, T., Lee, R. E., Yount, B. L., Mascenik, T. M., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.042 · Cited by 1,488
Probable Pangolin Origin of SARS-CoV-2 Associated with the COVID-19 Outbreak
Zhang, T., Wu, Q., & Zhang, Z. (2020) · Current Biology · doi:10.1016/j.cub.2020.03.022 · Cited by 1,397
Escape from neutralizing antibodies by SARS-CoV-2 spike protein variants
Weisblum, Y., Schmidt, F., Zhang, F., DaSilva, J., Poston, D., Lorenzi, J. C., Muecksch, F., Rutkowska, M., Hoffmann, H.-H., Michailidis, E., et al. (2020) · eLife · doi:10.7554/elife.61312 · Cited by 1,308
A human neutralizing antibody targets the receptor-binding site of SARS-CoV-2
Shi, R., Shan, C., Duan, X., Chen, Z., Liu, P., Song, J., Song, T., Bi, X., Han, C., Wu, L., et al. (2020) · Nature · doi:10.1038/s41586-020-2381-y · Cited by 1,286
Self-citationBaum, A., Fulton, B. O., Wloga, E., Copin, R., Pascal, K. E., Russo, V., Giordano, S., Lanza, K., Negron, N., Ni, M., et al. (2020) · Science · doi:10.1126/science.abd0831 · Cited by 1,253
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
Structural basis for inhibition of the RNA-dependent RNA polymerase from SARS-CoV-2 by remdesivir
Yin, W., Mao, C., Luan, X., Shen, D.-D., Shen, Q., Su, H., Wang, X., Zhou, F., Zhao, W., Gao, M., et al. (2020) · Science · doi:10.1126/science.abc1560 · Cited by 1,219
Self-citationStudies in humanized mice and convalescent humans yield a SARS-CoV-2 antibody cocktail
Hansen, J., Baum, A., Pascal, K. E., Russo, V., Giordano, S., Wloga, E., Fulton, B. O., Yan, Y., Koon, K., Patel, K., et al. (2020) · Science · doi:10.1126/science.abd0827 · Cited by 1,210
Pedersen, S. F., & Ho, Y.-C. (2020) · Journal of Clinical Investigation · doi:10.1172/jci137647 · Cited by 1,137
Chua, R. L., Lukassen, S., Trump, S., Hennig, B. P., Wendisch, D., Pott, F., Debnath, O., Thürmann, L., Kurth, F., Völker, M. T., et al. (2020) · Nature Biotechnology · doi:10.1038/s41587-020-0602-4 · Cited by 1,035
Why does COVID-19 disproportionately affect older people?
Mueller, A. L., McNamara, M. S., & Sinclair, D. A. (2020) · Aging · doi:10.18632/aging.103344 · Cited by 1,128
Molecular Architecture of the SARS-CoV-2 Virus
Yao, H., Song, Y., Chen, Y., Wu, N., Xu, J., Sun, C., Zhang, J., Weng, T., Zhang, Z., Wu, Z., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.018 · Cited by 1,060
“angiotensin-converting enzyme-2 (ACE2) through the receptor binding domain (RBD), an essential step for membrane fusion (Hoffmann et al., 2020; Lan et al., 2020; Shang et al., 2020; Wang et al., 2020; Yan et al., 2020; Zhou et al., 2020).”
BackgroundStructural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein Variant
Yurkovetskiy, L., Wang, X., Pascal, K. E., Tomkins-Tinch, C., Nyalile, T. P., Wang, Y., Baum, A., Diehl, W. E., Dauphin, A., Carbone, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.032 · Cited by 1,025
Barnes, C. O., West, A. P., Huey-Tubman, K. E., Hoffmann, M. A. G., Sharaf, N. G., Hoffman, P. R., Koranda, N., Gristick, H. B., Gaebler, C., Muecksch, F., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.025 · Cited by 795
BNT162b vaccines protect rhesus macaques from SARS-CoV-2
Vogel, A. B., Kanevsky, I., Che, Y., Swanson, K. A., Muik, A., Vormehr, M., Kranz, L. M., Walzer, K. C., Hein, S., Güler, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03275-y · Cited by 694
De novo design of picomolar SARS-CoV-2 miniprotein inhibitors
Cao, L., Goreshnik, I., Coventry, B., Case, J. B., Miller, L., Kozodoy, L., Chen, R. E., Carter, L., Walls, A. C., Park, Y.-J., et al. (2020) · Science · doi:10.1126/science.abd9909 · Cited by 742
Immune response, inflammation, and the clinical spectrum of COVID-19
García, L. F. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01441 · Cited by 739
Structural basis of a shared antibody response to SARS-CoV-2
Yuan, M., Liu, H., Wu, N. C., Lee, C.-C. D., Zhu, X., Zhao, F., Huang, D., Yu, W., Hua, Y., Tien, H., et al. (2020) · Science · doi:10.1126/science.abd2321 · Cited by 589
Antibody-dependent enhancement and SARS-CoV-2 vaccines and therapies
Lee, W. S., Wheatley, A. K., Kent, S. J., & DeKosky, B. J. (2020) · Nature Microbiology · doi:10.1038/s41564-020-00789-5 · Cited by 676
Circular RNA Vaccines against SARS-CoV-2 and Emerging Variants
Qu, L., Yi, Z., Shen, Y., Lin, L., Chen, F., Xu, Y., Wu, Z., Tang, H., Zhang, X., Tian, F., et al. (2021) · doi:10.1101/2021.03.16.435594 · Cited by 636
Damas, J., Hughes, G. M., Keough, K. C., Painter, C. A., Persky, N. S., Corbo, M., Hiller, M., Koepfli, K.-P., Pfenning, A. R., Zhao, H., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2010146117 · Cited by 633
Ultrapotent human antibodies protect against SARS-CoV-2 challenge via multiple mechanisms
Tortorici, M. A., Beltramello, M., Lempp, F. A., Pinto, D., Dang, H. V., Rosen, L. E., McCallum, M., Bowen, J., Minola, A., Jaconi, S., et al. (2020) · Science · doi:10.1126/science.abe3354 · Cited by 510
Molecular interaction and inhibition of SARS-CoV-2 binding to the ACE2 receptor
Yang, J., Petitjean, S. J. L., Koehler, M., Zhang, Q., Dumitru, A. C., Chen, W., Derclaye, S., Vincent, S. P., Soumillion, P., & Alsteens, D. (2020) · Nature Communications · doi:10.1038/s41467-020-18319-6 · Cited by 615
Structural Basis for Potent Neutralization of Betacoronaviruses by Single-Domain Camelid Antibodies
Wrapp, D., De Vlieger, D., Corbett, K. S., Torres, G. M., Wang, N., Van Breedam, W., Roose, K., van Schie, L., Hoffmann, M., Pöhlmann, S., et al. (2020) · Cell · doi:10.1016/j.cell.2020.04.031 · Cited by 610
Nikolich-Zugich, J., Knox, K. S., Rios, C. T., Natt, B., Bhattacharya, D., & Fain, M. J. (2020) · GeroScience · doi:10.1007/s11357-020-00186-0 · Cited by 577
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 & Microbe · doi:10.1016/j.chom.2021.03.005 · Cited by 519
Self-citationSARS-CoV-2 spike L452R variant evades cellular immunity and increases infectivity
Motozono, C., Toyoda, M., Zahradnik, J., Saito, A., Nasser, H., Tan, T. S., Ngare, I., Kimura, I., Uriu, K., Kosugi, Y., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.06.006 · Cited by 586
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
Walls, A. C., Fiala, B., Schäfer, A., Wrenn, S., Pham, M. N., Murphy, M., Tse, L. V., Shehata, L., O’Connor, M. A., Chen, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.043 · Cited by 532
Ortiz-Prado, E., Simbaña-Rivera, K., Gómez- Barreno, L., Rubio-Neira, M., Guaman, L. P., Kyriakidis, N. C., Muslin, C., Jaramillo, A. M. G., Barba-Ostria, C., Cevallos-Robalino, D., et al. (2020) · Diagnostic Microbiology and Infectious Disease · doi:10.1016/j.diagmicrobio.2020.115094 · Cited by 458
Humoral and circulating follicular helper T cell responses in recovered patients with COVID-19
Juno, J. A., Tan, H.-X., Lee, W. S., Reynaldi, A., Kelly, H. G., Wragg, K., Esterbauer, R., Kent, H. E., Batten, C. J., Mordant, F. L., et al. (2020) · Nature Medicine · doi:10.1038/s41591-020-0995-0 · Cited by 437
Immunological characteristics govern the transition of COVID-19 to endemicity
Lavine, J. S., Bjornstad, O. N., & Antia, R. (2021) · Science · doi:10.1126/science.abe6522 · Cited by 416
CoV-AbDab: the coronavirus antibody database
Raybould, M. I. J., Kovaltsuk, A., Marks, C., & Deane, C. M. (2021) · Bioinformatics · doi:10.1093/bioinformatics/btaa739 · Cited by 383
SARS-CoV-2 proteome microarray for global profiling of COVID-19 specific IgG and IgM responses
Jiang, H.-W., Li, Y., Zhang, H.-N., Wang, W., Yang, X., Qi, H., Li, H., Men, D., Zhou, J., & Tao, S.-C. (2020) · Nature Communications · doi:10.1038/s41467-020-17488-8 · Cited by 329
Self-citationGrzelak, L., Temmam, S., Planchais, C., Demeret, C., Tondeur, L., Huon, C., Guivel-Benhassine, F., Staropoli, I., Chazal, M., Dufloo, J., et al. (2020) · Science Translational Medicine · doi:10.1126/scitranslmed.abc3103 · Cited by 310
SARS-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 S1 subunit presents two highly immunogenic domains, the N-terminal domain (NTD) and the RBD, which are the major targets of polyclonal and monoclonal neutralizing antibodies (4, 9, 10).”
Engineered ACE2 receptor traps potently neutralize SARS-CoV-2
Glasgow, A., Glasgow, J., Limonta, D., Solomon, P., Lui, I., Zhang, Y., Nix, M. A., Rettko, N. J., Zha, S., Yamin, R., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2016093117 · Cited by 251
Self-citationExopolysaccharides as Antimicrobial Agents: Mechanism and Spectrum of Activity
Abdalla, A. K., Ayyash, M. M., Olaimat, A. N., Osaili, T. M., Al-Nabulsi, A. A., Shah, N. P., & Holley, R. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.664395 · Cited by 268
Spectrum of neuropsychiatric manifestations in COVID-19.
Nalleballe, K., Reddy Onteddu, S., Sharma, R., Dandu, V., Brown, A., Jasti, M., Yadala, S., Veerapaneni, K., Siddamreddy, S., Avula, A., et al. (2020) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2020.06.020 · Cited by 235
De novo design of potent and resilient hACE2 decoys to neutralize SARS-CoV-2
Linsky, T. W., Vergara, R., Codina, N., Nelson, J. W., Walker, M. J., Su, W., Barnes, C. O., Hsiang, T.-Y., Esser-Nobis, K., Yu, K., et al. (2020) · Science · doi:10.1126/science.abe0075 · Cited by 216
Walls, A. C., Miranda, M. C., Schäfer, A., Pham, M. N., Greaney, A., Arunachalam, P. S., Navarro, M.-J., Tortorici, M. A., Rogers, K., O’Connor, M. A., et al. (2021) · Cell · doi:10.1016/j.cell.2021.09.015 · Cited by 185
“SARS-CoV-2 infects host cells through the attachment of the viral transmembrane spike (S) glycoprotein to angiotensin-converting enzyme 2 (ACE2), followed by fusion of the viral and host membranes (Hoffmann et al., 2020; Lan et al., 2020; Letko et al., 2020; Shang et al., 2020; Walls et al., 2020a; Wang et al., 2020;…”
Crosstalk between the renin–angiotensin, complement and kallikrein–kinin systems in inflammation
Bekassy, Z., Lopatko Fagerström, I., Bader, M., & Karpman, D. (2022) · Nature reviews. Immunology · doi:10.1038/s41577-021-00634-8 · Cited by 167
Shan, S., Luo, S., Yang, Z., Hong, J., Su, Y., Ding, F., Fu, L., Li, C., Chen, P., Ma, J., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2122954119 · Cited by 157
Dugan, H. L., Stamper, C. T., Li, L., Changrob, S., Asby, N. W., Halfmann, P. J., Zheng, N.-Y., Huang, M., Shaw, D. G., Cobb, M. S., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.05.001 · Cited by 134
Vogel, A. B., Kanevsky, I., Che, Y., Swanson, K. A., Muik, A., Vormehr, M., Kranz, L. M., Walzer, K. C., Hein, S., Güler, A., et al. (2020) · doi:10.1101/2020.09.08.280818 · Cited by 126
COVID-19 and Diabetes: A Collision and Collusion of Two Diseases
Feldman, E. L., Savelieff, M. G., Hayek, S. S., Pennathur, S., Kretzler, M., & Pop-Busui, R. (2020) · Diabetes · doi:10.2337/dbi20-0032 · Cited by 136
Furin cleavage sites naturally occur in coronaviruses
Wu, Y., & Zhao, S. (2021) · Stem Cell Research · doi:10.1016/j.scr.2020.102115 · Cited by 117
Potential neutralizing antibodies discovered for novel corona virus using machine learning
Magar, R., Yadav, P., & Barati Farimani, A. (2021) · Scientific Reports · doi:10.1038/s41598-021-84637-4 · Cited by 114
Martínez-Mármol, R., Giordano-Santini, R., Kaulich, E., Cho, A.-N., Przybyla, M., Riyadh, M. A., Robinson, E., Chew, K. Y., Amor, R., Meunier, F. A., et al. (2023) · Science Advances · doi:10.1126/sciadv.adg2248 · Cited by 94
Sarzani, R., Giulietti, F., Di Pentima, C., Giordano, P., & Spannella, F. (2020) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00189.2020 · Cited by 86
Emergence of bat-related betacoronaviruses: hazard and risks
Frutos, R., Serra-Cobo, J., Pinault, L., Lopez Roig, M., & Devaux, C. A. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.591535 · Cited by 66
Cryo-EM: the resolution revolution and drug discovery
de Oliveira, T. M., van Beek, L., Shilliday, F., Debreczeni, J. É., & Phillips, C. (2021) · SLAS DISCOVERY · doi:10.1177/2472555220960401 · Cited by 73
Zang, J., Gu, C., Zhou, B., Zhang, C., Yang, Y., Xu, S., Bai, L., Zhang, R., Deng, Q., Yuan, Z., et al. (2020) · Cell Discovery · doi:10.1038/s41421-020-00199-1 · Cited by 67
APOE interacts with ACE2 inhibiting SARS-CoV-2 cellular entry and inflammation in COVID-19 patients
Zhang, H., Shao, L., Lin, Z., Long, Q.-X., Yuan, H., Cai, L., Jiang, G., Guo, X., Yang, R., Zhang, Z., et al. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01118-4 · Cited by 67
Self-citationMutations that adapt SARS-CoV-2 to mink or ferret do not increase fitness in the human airway
Zhou, J., Peacock, T. P., Brown, J. C., Goldhill, D. H., Elrefaey, A. M. E., Penrice-Randal, R., Cowton, V. M., De Lorenzo, G., Furnon, W., Harvey, W. T., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110344 · Cited by 64
“A series of molecular interactions between amino acids in the spike RBD and the interacting surface of ACE2 result in SARS-CoV-2 binding to human ACE2 with high affinity (Conceicao et al., 2020; Yan et al., 2020).”
Molecular mechanisms and epidemiology of COVID-19 from an allergist’s perspective
Hosoki, K., Chakraborty, A., & Sur, S. (2020) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2020.05.033 · Cited by 63
Zhao, H., Wang, T.-C., Li, X.-F., Zhang, N.-N., Li, L., Zhou, C., Deng, Y.-Q., Cao, T.-S., Yang, G., Li, R.-T., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00861-4 · Cited by 60
Self-citationImpact of COVID-19 on Alzheimer’s Disease Risk: Viewpoint for Research Action
Abate, G., Memo, M., & Uberti, D. (2020) · Healthcare · doi:10.3390/healthcare8030286 · Cited by 56
Deng, P., Ke, Z., Ying, B., Qiao, B., & Yuan, L. (2020) · Clinica Chimica Acta · doi:10.1016/j.cca.2020.07.018 · Cited by 47
Robinson, S. A., Raybould, M. I. J., Schneider, C., Wong, W. K., Marks, C., & Deane, C. M. (2021) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1009675 · Cited by 46
DNA damage response at telomeres boosts the transcription of SARS‐CoV‐2 receptor ACE2 during aging
Sepe, S., Rossiello, F., Cancila, V., Iannelli, F., Matti, V., Cicio, G., Cabrini, M., Marinelli, E., Alabi, B. R., di Lillo, A., et al. (2022) · The EMBO Reports · doi:10.15252/embr.202153658 · Cited by 42
Karki, N., Verma, N., Trozzi, F., Tao, P., Kraka, E., & Zoltowski, B. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041573 · Cited by 43
Cong, Y., Feng, Y., Ni, H., Zhi, F., Miao, Y., Fang, B., Zhang, L., & Zhang, J. Z. H. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.1c00241 · Cited by 40
Simonetti, B., Daly, J. L., & Cullen, P. J. (2023) · Traffic · doi:10.1111/tra.12885 · Cited by 39
Ahmed-Hassan, H., Sisson, B., Shukla, R. K., Wijewantha, Y., Funderburg, N. T., Li, Z., Hayes, D., Demberg, T., & Liyanage, N. P. M. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01979 · Cited by 47
Yamamoto, M., Tomita, K., Hirayama, Y., Inoue, J.-I., Kawaguchi, Y., & Gohda, J. (2022) · doi:10.1101/2022.03.21.485084 · Cited by 36
Can N95 respirators be reused after disinfection? And for how many times?
Liao, L., Xiao, W., Zhao, M., Yu, X., Wang, H., Wang, Q., Chu, S., & Cui, Y. (2020) · doi:10.1101/2020.04.01.20050443 · Cited by 433
Hennrich, A. A., Sawatsky, B., Santos-Mandujano, R., Banda, D. H., Oberhuber, M., Schopf, A., Pfaffinger, V., Wittwer, K., Riedel, C., Pfaller, C. K., et al. (2021) · PLOS Pathogens · doi:10.1371/journal.ppat.1009064 · Cited by 30
Kim, J., Mukherjee, A., Nelson, D., Jozic, A., & Sahay, G. (2020) · doi:10.1101/2020.07.24.205583 · Cited by 28
Robinson, E. L., Alkass, K., Bergmann, O., Maguire, J. J., Roderick, H. L., & Davenport, A. P. (2020) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2020.08.009 · Cited by 25
Control of SARS-CoV-2 infection by MT1-MMP-mediated shedding of ACE2
Guo, X., Cao, J., Cai, J.-P., Wu, J., Huang, J., Asthana, P., Wong, S. K. K., Ye, Z.-W., Gurung, S., Zhang, Y., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-35590-x · Cited by 25
Self-citationDevaux, C. A., & Camoin-Jau, L. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.1042200 · Cited by 20
Yim, W., Cheng, D., Patel, S., Kui, R., Meng, Y. S., & Jokerst, J. V. (2020) · medRxiv · doi:10.1101/2020.07.07.20148551 · Cited by 104
Insights in Chloroquine Action: Perspectives and Implications in Malaria and COVID‐19
Pillat, M. M., Krüger, A., Guimarães, L. M. F., Lameu, C., de Souza, E. E., Wrenger, C., & Ulrich, H. (2020) · Cytometry Part A · doi:10.1002/cyto.a.24190 · Cited by 17
Kuiper, M. J., Wilson, L. O. W., Mangalaganesh, S., Lee, C., Reti, D., & Vasan, S. S. (2021) · ILAR Journal · doi:10.1093/ilar/ilab031 · Cited by 14
Bignon, E., Marazzi, M., Grandemange, S., & Monari, A. (2022) · Chemical Science · doi:10.1039/d2sc00108j · Cited by 13
AI-driven prediction of SARS-CoV-2 variant binding trends from atomistic simulations
Capponi, S., Wang, S., Navarro, E. J., & Bianco, S. (2021) · The European Physical Journal E · doi:10.1140/epje/s10189-021-00119-5 · Cited by 12
Lok, S., Lau, T. N. H., Trost, B., Tong, A. H. Y., Wintle, R. F., Engstrom, M. D., Stacy, E., Waits, L. P., Scrafford, M., & Scherer, S. W. (2022) · G3 Genes|Genomes|Genetics · doi:10.1093/g3journal/jkac138 · Cited by 6
Piccoli, L., Park, Y.-J., Tortorici, M. A., Czudnochowski, N., Walls, A. C., Beltramello, M., Silacci-Fregni, C., Pinto, D., Rosen, L. E., Bowen, J. E., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.037 · Cited by 1,395
A Privacy-Preserving Crowd Flow Prediction Framework Based on Federated Learning during Epidemics
Wang, W., Yang, G., Bao, L., Ma, K., & Zhou, H. (2022) · Security and Communication Networks · doi:10.1155/2022/8712597 · Cited by 5
Dynamic expedition of leading mutations in SARS-CoV-2 spike glycoproteins
Hasan, M., He, Z., Jia, M., Leung, A. C. F., Natarajan, K., Xu, W., Yap, S., Zhou, F., Chen, S., Su, H., et al. (2024) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2024.05.037 · Cited by 3
Yang, Y., Qiao, L., Jiang, Y., Wang, Z., Zhang, D., Buratto, D., Huang, L., & Zhou, R. (2026) · eLife · doi:10.7554/elife.107785 · Cited by 2
Ye, M., Liang, Z., Zhou, D., Pike, A. C. W., Wang, S., Wang, D., Bakshi, S., Brooke, L., Williams, E. P., Elkins, J. M., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-69421-0 · Cited by 1
Metadata
- Authors
- Yan, R., Zhang, Y., Li, Y., Xia, L., Guo, Y., & Zhou, Q.
- Venue
- Science
- Published
- 2020-03-27
- Volume
- 367
- Issue
- 6485
- Pages
- 1444-1448
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W3010441732
- Cited by
- 5,040
- References
- 14
- FWCI
- 134.05
- 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
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.
