Cited by 5,983SARS-CoV-2 and COVID-19 ResearchEnzyme Structure and FunctionAnimal Virus Infections Studies

The DOI matches its Crossref record; 37 of the 38 references it cites were found in a registry or an index.

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

Open access

Lan, Jun, Ge, Jiwan, Yu, Jinfang, Shan, Sisi, Zhou, Huan, Fan, Shilong, Zhang, Qi, Shi, Xuanling, Wang, Qisheng, Zhang, Linqi, Wang, Xinquan·2020·Nature

DOI 10.1038/s41586-020-2180-5

Published version of a preprint

Open this paper in CoChat — free account Open PDF

Abstract

A new and highly pathogenic coronavirus (severe acute respiratory syndrome coronavirus-2, SARS-CoV-2) caused an outbreak in Wuhan city, Hubei province, China, starting from December 2019 that quickly spread nationwide and to other countries around the world 1-3. Here, to better understand the initial step of infection at an atomic level, we determined the crystal structure of the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 bound to the cell receptor ACE2. The overall ACE2-binding mode of the SARS-CoV-2 RBD is nearly identical to that of the SARS-CoV RBD, which also uses ACE2 as the cell receptor 4. Structural analysis identified residues in the SARS-CoV-2 RBD that are essential for ACE2 binding, the majority of which either are highly conserved or share similar side chain properties with those in the SARS-CoV RBD. Such similarity in structure and sequence strongly indicate convergent evolution between the SARS-CoV-2 and SARS-CoV RBDs for improved binding to ACE2, although SARS-CoV-2 does not cluster within SARS and SARS-related coronaviruses 1-3,5. The epitopes of two SARS-CoV antibodies that target the RBD are also analysed for binding to the SARS-CoV-2 RBD, providing insights into the future identification of cross-reactive antibodies.

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

Crossref · 10.1038/s41586-020-2180-5

Cites

37 of 37 references verified0 citation errors · 0 not checkable

Statistics

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.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Clinical features of patients infected with 2019 novel coronavirus in Wuhan, China
Huang, C., Wang, Y., Li, X., Ren, L., Zhao, J., Hu, Y., Zhang, L., Fan, G., Xu, J., Gu, X., et al. (2020) · The Lancet · doi:10.1016/s0140-6736(20)30183-5 · Cited by 48,884
Self-citation
[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
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
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
Self-citation
Phaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612
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
Clinical characteristics of 138 hospitalized patients with 2019 Novel Coronavirus-Infected pneumonia in Wuhan, China
Wang, D., Hu, B., Hu, C., Zhu, F., Liu, X., Zhang, J., Wang, B., Xiang, H., Cheng, Z., Xiong, Y., et al. (2020) · JAMA · doi:10.1001/jama.2020.1585 · Cited by 20,148
Self-citation
La certeza de lo impredecible
Martínez–González, M. B. (2020) · DSPACE System - Metalibrary (University of the Coast) · Cited by 18,292
NMRPipe: A multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197809 · Cited by 15,961

Show all 38 references

Sorted by citations

Items 301–400 of 1,026

Broad host range of SARS-CoV-2 and the molecular basis for SARS-CoV-2 binding to cat ACE2
Wu, L., Chen, Q., Liu, K., Wang, J., Han, P., Zhang, Y., Hu, Y., Meng, Y., Pan, X., Qiao, C., et al. (2020) · Cell Discovery · doi:10.1038/s41421-020-00210-9 · Cited by 183
Self-citation
Cryo-electron microscopy structures of the N501Y SARS-CoV-2 spike protein in complex with ACE2 and 2 potent neutralizing antibodies
Zhu, X. Q., Mannar, D., Srivastava, S. S., Berezuk, A., Demers, J., Saville, J. W., Leopold, K., Li, W., Dimitrov, D. S., Tuttle, K. S., et al. (2021) · PLoS Biology · doi:10.1371/journal.pbio.3001237 · Cited by 183
SARS-CoV-2 Cell Entry Factors ACE2 and TMPRSS2 Are Expressed in the Microvasculature and Ducts of Human Pancreas but Are Not Enriched in β Cells
Coate, K. C., Cha, J., Shrestha, S., Wang, W., Gonçalves, L. M., Almaça, J., Kapp, M., Fasolino, M., Morgan, A. R., Dai, C., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.11.006 · Cited by 182
Plasma-activated water: An alternative disinfectant for S protein inactivation to prevent SARS-CoV-2 infection
Guo, L., Yao, Z., Yang, L., Zhang, H., Qi, Y., Gou, L., Wang, X., Liu, D., Zhang, L., Cheng, Y., et al. (2020) · Chemical Engineering Journal · doi:10.1016/j.cej.2020.127742 · Cited by 182
Self-citation
Potential benefits and risks of omega-3 fatty acids supplementation to patients with COVID-19
Rogero, M. M., Leão, M. D. C., Santana, T. M., Pimentel, M. V. D. M. B., Carlini, G. C. G., da Silveira, T. F. F., Gonçalves, R. C., & de Castro, I. A. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.07.005 · Cited by 181
COVID-19 vaccination for people with severe mental illness: why, what, and how?
Mazereel, V., Assche, K. V., Detraux, J., & Binder, M. D. (2021) · The Lancet Psychiatry · doi:10.1016/s2215-0366(20)30564-2 · Cited by 181
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 180
The impact of ABO blood group on COVID-19 infection risk and mortality: A systematic review and meta-analysis
Liu, N., Zhang, T., Ma, L., Zhang, H., Wang, H., Wei, W., Pei, H., & Li, H. (2020) · Blood Reviews · doi:10.1016/j.blre.2020.100785 · Cited by 180
Potential anti-COVID-19 agents, cepharanthine and nelfinavir, and their usage for combination treatment
Ohashi, H., Watashi, K., Saso, W., Shionoya, K., Iwanami, S., Hirokawa, T., Shirai, T., Kanaya, S., Ito, Y., Kim, K. S., et al. (2021) · iScience · doi:10.1016/j.isci.2021.102367 · Cited by 180
Neutralization, effector function and immune imprinting of Omicron variants
Addetia, A., Piccoli, L., Case, J. B., Park, Y., Beltramello, M., Guarino, B., Dang, H. V., de Melo, G. D., Pinto, D., Sprouse, K. R., et al. (2023) · Nature · doi:10.1038/s41586-023-06487-6 · Cited by 179
Analysis of the susceptibility to COVID-19 in pregnancy and recommendations on potential drug screening
Zhao, X., Jiang, Y., Zhao, Y., Xi, H., Liu, C., Qu, F., & Feng, X. (2020) · European Journal of Clinical Microbiology & Infectious Diseases · doi:10.1007/s10096-020-03897-6 · Cited by 178
Comparison of Severe Acute Respiratory Syndrome Coronavirus 2 Spike Protein Binding to ACE2 Receptors from Human, Pets, Farm Animals, and Putative Intermediate Hosts
Zhai, X., Sun, J., Yan, Z., Zhang, J., Zhao, J., Zhao, Z., Gao, Q., He, W.-T., Veit, M., & Su, S. (2020) · Journal of Virology · doi:10.1128/jvi.00831-20 · Cited by 177
Impact of Thiol–Disulfide Balance on the Binding of Covid-19 Spike Protein with Angiotensin-Converting Enzyme 2 Receptor
Hati, S., & Bhattacharyya, S. (2020) · ACS Omega · doi:10.1021/acsomega.0c02125 · Cited by 177
Multisystem Inflammatory Syndrome in Children (MIS-C), a Post-viral Myocarditis and Systemic Vasculitis—A Critical Review of Its Pathogenesis and Treatment
McMurray, J. C., May, J. W., Cunningham, M. W., & Jones, O. Y. (2020) · Frontiers in Pediatrics · doi:10.3389/fped.2020.626182 · Cited by 177
Cell-mimicking nanodecoys neutralize SARS-CoV-2 and mitigate lung injury in a non-human primate model of COVID-19
Li, Z., Wang, Z., Dinh, P., Zhu, D., Popowski, K. D., Lutz, H., Hu, S., Lewis, M. G., Cook, A., Andersen, H., et al. (2021) · Nature Nanotechnology · doi:10.1038/s41565-021-00923-2 · Cited by 175
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 175
A Single Immunization with Spike-Functionalized Ferritin Vaccines Elicits Neutralizing Antibody Responses against SARS-CoV‑2 in Mice
Powell, A. E., Zhang, K., Sanyal, M., Tang, S., Weidenbacher, P. A. B., Li, S., Pham, T. D., Pak, J. E., Chiu, W., & Kim, P. S. (2021) · ACS Central Science · doi:10.1021/acscentsci.0c01405 · Cited by 174
Design and Numerical Analysis of a Graphene-Coated SPR Biosensor for Rapid Detection of the Novel Coronavirus
Akib, T. B. A., Mou, S. F., Rahman, M. M., Rana, M. M., Islam, M. R., Mehedi, I. M., Mahmud, M. A. P., & Kouzani, A. Z. (2021) · Sensors · doi:10.3390/s21103491 · Cited by 174
Plants Metabolites: Possibility of Natural Therapeutics Against the COVID-19 Pandemic
Bhuiyan, F. R., Howlader, S., Raihan, T., & Hasan, M. (2020) · Frontiers in Medicine · doi:10.3389/fmed.2020.00444 · Cited by 173
Mutations in SARS-CoV-2 variants of concern link to increased spike cleavage and virus transmission
Escalera, A., Gonzalez-Reiche, A. S., Aslam, S., Mena, I., Laporte, M., Pearl, R. L., Fossati, A., Rathnasinghe, R., Alshammary, H., van de Guchte, A., et al. (2022) · Cell Host & Microbe · doi:10.1016/j.chom.2022.01.006 · Cited by 173
Flavonols as potential antiviral drugs targeting SARS-CoV-2 proteases (3CLpro and PLpro), spike protein, RNA-dependent RNA polymerase (RdRp) and angiotensin-converting enzyme II receptor (ACE2)
Mouffouk, C., Mouffouk, S., Mouffouk, S., Hambaba, L., & Haba, H. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.173759 · Cited by 172
A multiscale coarse-grained model of the SARS-CoV-2 virion
Yu, A., Pak, A. J., He, P., Monje‐Galvan, V., Casalino, L., Gaieb, Z., Dommer, A. C., Amaro, R. E., & Voth, G. A. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2020.10.048 · Cited by 169
Mink, SARS-CoV-2, and the Human-Animal Interface
Fenollar, F., Mediannikov, O., Maurin, M., Devaux, C. A., Colson, P., Levasseur, A., Fournier, P., & Raoult, D. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.663815 · Cited by 169
V367F Mutation in SARS-CoV-2 Spike RBD Emerging during the Early Transmission Phase Enhances Viral Infectivity through Increased Human ACE2 Receptor Binding Affinity
Ou, J., Zhou, Z., Dai, R., Zhang, J., Zhao, S., Wu, X., Lan, W., Ren, Y., Cui, L., Lan, Q., et al. (2021) · Journal of Virology · doi:10.1128/jvi.00617-21 · Cited by 169
Self-citation
Predicting hosts based on early SARS-CoV-2 samples and analyzing the 2020 pandemic
Guo, Q., Li, M., Wang, C., Guo, J., Jiang, X., Tan, J., Wu, S. V., Wang, P., Xiao, T., Zhou, M., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-96903-6 · Cited by 169
Cell entry by SARS-CoV-2
Peng, R., Wu, L.-A., Wang, Q., Qi, J., & Gao, G. F. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2021.06.001 · Cited by 168
Self-citation
Association of Circulating Sex Hormones With Inflammation and Disease Severity in Patients With COVID-19
Dhindsa, S., Zhang, N., McPhaul, M. J., Wu, Z. R., Ghoshal, A. K., Erlich, E. C., Mani, K. M., Randolph, G. J., Edwards, J. R., Mudd, P. A., et al. (2021) · JAMA Network Open · doi:10.1001/jamanetworkopen.2021.11398 · Cited by 167
Potent cross-reactive antibodies following Omicron breakthrough in vaccinees
Nutalai, R., Zhou, D., Tuekprakhon, A., Ginn, H. M., Supasa, P., Liu, C., Huo, J., Mentzer, A. J., Duyvesteyn, H. M. E., Dijokaite-Guraliuc, A., et al. (2022) · Cell · doi:10.1016/j.cell.2022.05.014 · Cited by 167
Microstructure, pathophysiology, and potential therapeutics of COVID‐19: A comprehensive review
Singh, S. P., Pritam, M., Pandey, B., & Yadav, T. P. (2021) · Journal of Medical Virology · doi:10.1002/jmv.26254 · Cited by 166
Structure-guided covalent stabilization of coronavirus spike glycoprotein trimers in the closed conformation
McCallum, M., Walls, A. C., Bowen, J. E., Corti, D., & Veesler, D. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0483-8 · Cited by 166
Molecular insights into receptor binding of recent emerging SARS-CoV-2 variants
Han, P., Su, C., Zhang, Y., Bai, C., Zheng, A., Qiao, C., Wang, Q., Niu, S., Chen, Q., Zhang, Y., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-26401-w · Cited by 166
Self-citation
Potential of Flavonoid-Inspired Phytomedicines against COVID-19
Ngwa, W. F., Kumar, R., Thompson, D., Lyerly, W., Moore, R., Reid, T., Lowe, H. I. C., & Toyang, N. J. (2020) · Molecules · doi:10.3390/molecules25112707 · Cited by 165
Broad and Differential Animal Angiotensin-Converting Enzyme 2 Receptor Usage by SARS-CoV-2
Zhao, X., Chen, D., Szabla, R., Zheng, M., Li, G., Du, P., Zheng, S., Li, X., Song, C., Li, R., et al. (2020) · Journal of Virology · doi:10.1128/jvi.00940-20 · Cited by 165
Current advances in the development of SARS-CoV-2 vaccines
Awadasseid, A., Wu, Y., Tanaka, Y., & Zhang, W. (2021) · International Journal of Biological Sciences · doi:10.7150/ijbs.52569 · Cited by 164
COVID-19-associated cardiovascular morbidity in older adults: a position paper from the Italian Society of Cardiovascular Researches
Moccia, F. D., Gerbino, A., Lionetti, V., Miragoli, M., Munaron, L., Pagliaro, P., Pasqua, T., Penna, C. R. R., Rocca, C., Samaja, M., et al. (2020) · GeroScience · doi:10.1007/s11357-020-00198-w · Cited by 165
Airborne Transmission of COVID-19: Aerosol Dispersion, Lung Deposition, and Virus-Receptor Interactions
Zuo, Y. Y., Uspal, W. E., & Wei, T. (2020) · ACS Nano · doi:10.1021/acsnano.0c08484 · Cited by 164
Pathogenesis of Respiratory Viral and Fungal Coinfections
Salazar, F., Bignell, E., Brown, G. D., Cook, P. C., & Warris, A. (2021) · Clinical Microbiology Reviews · doi:10.1128/cmr.00094-21 · Cited by 164
Acute and chronic neurological disorders in COVID-19: potential mechanisms of disease
Balcom, E. F., Nath, A., & Power, C. (2021) · Brain · doi:10.1093/brain/awab302 · Cited by 163
Structural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529
Zhou, T., Wang, L., Misasi, J., Pegu, A., Zhang, Y., Harris, D. R., Olia, A. S., Talana, C. A., Yang, E. S., Chen, M., et al. (2022) · Science · doi:10.1126/science.abn8897 · Cited by 163
RNA-dependent RNA polymerase: Structure, mechanism, and drug discovery for COVID-19
Jiang, Y., Yin, W., & Xu, H. E. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.08.116 · Cited by 161
Ivermectin Docks to the SARS-CoV-2 Spike Receptor-binding Domain Attached to ACE2
Lehrer, S. P., & Rheinstein, P. H. (2020) · In Vivo · doi:10.21873/invivo.12134 · Cited by 161
COVID-19-Associated Neurological Disorders: The Potential Route of CNS Invasion and Blood-Brain Barrier Relevance
Achar, A., & Ghosh, C. (2020) · Cells · doi:10.3390/cells9112360 · Cited by 160
COVID-19: Progress in diagnostics, therapy and vaccination
Liu, X., Liu, C., Liu, G., Luo, W., & Xia, N. (2020) · Theranostics · doi:10.7150/thno.47987 · Cited by 159
ABO blood group and COVID‐19: a review on behalf of the ISBT COVID‐19 Working Group
Goel, R., Bloch, E. M., Pirenne, F., Al‐Riyami, A. Z., Crowe, E. P., Dau, L., Land, K. J., Townsend, M. J., Thachil, J. V., Rahimi‐Levene, N., et al. (2021) · Vox Sanguinis · doi:10.1111/vox.13076 · Cited by 159
An Alternative Binding Mode of IGHV3-53 Antibodies to the SARS-CoV-2 Receptor Binding Domain
Wu, N. C., Yuan, M., Liu, H., Lee, C.-C. D., Zhu, X., Bangaru, S., Torres, J. L., Caniels, T. G., Brouwer, P. J. M., van Gils, M. J., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108274 · Cited by 158
Endothelial cell damage is the central part of COVID-19 and a mouse model induced by injection of the S1 subunit of the spike protein
Nuovo, G. J., MAGRO, C. M. J., Shaffer, T., Awad, H., Suster, D. I., Mikhail, S., He, B., Michaille, J., Liechty, B., & Tili, E. (2020) · Annals of Diagnostic Pathology · doi:10.1016/j.anndiagpath.2020.151682 · Cited by 158
Deep learning guided optimization of human antibody against SARS-CoV-2 variants with broad neutralization
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
Self-citation
Gene of the month: the 2019-nCoV/SARS-CoV-2 novel coronavirus spike protein
Pillay, T. S. (2020) · Journal of Clinical Pathology · doi:10.1136/jclinpath-2020-206658 · Cited by 157
The basis of a more contagious 501Y.V1 variant of SARS-CoV-2
Liu, H., Zhang, Q., Wei, P., Chen, Z., Aviszus, K., Yang, J. J., Downing, W., Peterson, S., Liang, B., Liang, B., et al. (2021) · Cell Research · doi:10.1038/s41422-021-00496-8 · Cited by 156
Self-citation
SARS-CoV-2 exacerbates proinflammatory responses in myeloid cells through C-type lectin receptors and Tweety family member 2
Qiao, L., Liu, J., Zhao, S., Castro, M. F. G., Laurent-Rolle, M., Dong, J., Ran, X., Damani‐Yokota, P., Tang, H., Karakousi, T. R., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.05.006 · Cited by 156
The SARS-CoV-2 Exerts a Distinctive Strategy for Interacting with the ACE2 Human Receptor
Brielle, E. S., Schneidman‐Duhovny, D., & Linial, M. (2020) · Viruses · doi:10.3390/v12050497 · Cited by 155
Two Years into the COVID-19 Pandemic: Lessons Learned
da Silva, S. J. R., do Nascimento, J. C. F., Mendes, R. P. G., Guarines, K. M., da Silva, C. T. A., da Silva, P. G., de Magalhães, J. J. F., Vigar, J. R. J., Silva‐Júnior, A., Kohl, A., et al. (2022) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.2c00204 · Cited by 155
Selection, biophysical and structural analysis of synthetic nanobodies that effectively neutralize SARS-CoV-2
Custódio, T. F., Das, H., Sheward, D. J., Hanke, L., Pažický, S., Pieprzyk, J., Sorgenfrei, M., Schroer, M. A., Gruzinov, A. Y., Jeffries, C. M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19204-y · Cited by 154
Key Interacting Residues between RBD of SARS-CoV-2 and ACE2 Receptor: Combination of Molecular Dynamics Simulation and Density Functional Calculation
Jawad, B., Adhikari, P., Podgornik, R., & Ching, W. Y. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.1c00560 · Cited by 154
Transmission of SARS-CoV-2 from humans to animals and potential host adaptation
Tan, C. C. S., Lam, S. D., Richard, D., Owen, C. J., Berchtold, D., Orengo, C. A., Nair, M. S., Kuchipudi, S. V., Kapur, V., van Dorp, L., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30698-6 · Cited by 154
Porcine epidemic diarrhea virus: Molecular mechanisms of attenuation and vaccines
Li, Z., Ma, Z., Li, Y., Gao, S., & Xiao, S. (2020) · Microbial Pathogenesis · doi:10.1016/j.micpath.2020.104553 · Cited by 153
Hypertension and COVID-19: Current Evidence and Perspectives
Gallo, G., Calvez, V., & Savoia, C. (2022) · High Blood Pressure & Cardiovascular Prevention · doi:10.1007/s40292-022-00506-9 · Cited by 153
Drug design and repurposing with DockThor-VS web server focusing on SARS-CoV-2 therapeutic targets and their non-synonym variants
Guedes, I. A., Costa, L. S. C., Santos, K. B., Karl, A. L. M., Rocha, G. K., Teixeira, I. M., Galheigo, M. M., Medeiros, V., Krempser, E., Custódio, F. L., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-84700-0 · Cited by 152
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 151
Is the Rigidity of SARS-CoV-2 Spike Receptor-Binding Motif the Hallmark for Its Enhanced Infectivity? Insights from All-Atom Simulations
Spinello, A., Saltalamacchia, A., & Magistrato, A. (2020) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.0c01148 · Cited by 150
Antibody-mediated neutralization of SARS-CoV-2
Gruell, H., Vanshylla, K., Weber, T., Barnes, C. O., Kreer, C., & Klein, F. (2022) · Immunity · doi:10.1016/j.immuni.2022.05.005 · Cited by 150
Antiviral Polymers: Past Approaches and Future Possibilities
Bianculli, R. H., Mase, J. D., & Schulz, M. D. (2020) · Macromolecules · doi:10.1021/acs.macromol.0c01273 · Cited by 149
Antibody neutralization of SARS-CoV-2 through ACE2 receptor mimicry
Ge, J., Wang, R., Ju, B., Zhang, Q., Sun, J., Chen, P., Zhang, S., Tian, Y., Shan, S., Cheng, L., et al. (2021) · Nature Communications · doi:10.1038/s41467-020-20501-9 · Cited by 149
Self-citation
Molecular characteristics, immune evasion, and impact of SARS-CoV-2 variants
Sun, C., Xie, C., Bu, G., Zhong, L., & Zeng, M. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01039-2 · Cited by 149
Human Intestinal Defensin 5 Inhibits SARS-CoV-2 Invasion by Cloaking ACE2
Wang, C., Wang, S., Li, D., Wei, D., Zhao, J., & Wang, J. (2020) · Gastroenterology · doi:10.1053/j.gastro.2020.05.015 · Cited by 148
Prospect of SARS-CoV-2 spike protein: Potential role in vaccine and therapeutic development
Samrat, S. K., Tharappel, A. M., Li, Z., & Li, H. (2020) · Virus Research · doi:10.1016/j.virusres.2020.198141 · Cited by 148
Lower Circulating Interferon-Gamma Is a Risk Factor for Lung Fibrosis in COVID-19 Patients
Hu, Z., Xu, J. M., Yin, J., Li, L., Hou, W., Zhang, L., Zhou, Z., Yu, Y., Li, H., Feng, Y., et al. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.585647 · Cited by 148
Self-citation
The Potential Intermediate Hosts for SARS-CoV-2
Zhao, J., Cui, W., & Tian, B. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.580137 · Cited by 148
Angiotensin-converting enzyme 2 (ACE2): SARS-CoV-2 receptor and RAS modulator
Bian, J., & Li, Z. (2020) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2020.10.006 · Cited by 148
Spike and nsp6 are key determinants of SARS-CoV-2 Omicron BA.1 attenuation
Chen, D. W., Chin, C. V., Kenney, D., Tavares, A. H., Khan, N., Conway, H. L., Liu, G., Choudhary, M. C., Gertje, H. P., O’Connell, A. K., et al. (2023) · Nature · doi:10.1038/s41586-023-05697-2 · Cited by 148
Mesenchymal stem cell therapy for acute respiratory distress syndrome: from basic to clinics
Qin, H., & Zhao, A. (2020) · Protein & Cell · doi:10.1007/s13238-020-00738-2 · Cited by 147
Can SARS-CoV-2 Virus Use Multiple Receptors to Enter Host Cells?
Gadanec, L. K., McSweeney, K. R., Qaradakhi, T., Ali, B. A., Zulli, A., & Apostolopoulos, V. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22030992 · Cited by 147
Mutations derived from horseshoe bat ACE2 orthologs enhance ACE2-Fc neutralization of SARS-CoV-2
Mou, H., Quinlan, B. D., Peng, H., Liu, G., Guo, Y., Peng, S., Zhang, L., Davis-Gardner, M. E., Gardner, M. R., Crynen, G. C., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009501 · Cited by 147
Self-citation
Small-Molecule Inhibitors of the Coronavirus Spike: ACE2 Protein–Protein Interaction as Blockers of Viral Attachment and Entry for SARS-CoV-2
Bojadzic, D., Alcazar, O., Chen, J., Chuang, S.-T., Capcha, J. M. C., Shehadeh, L. A., & Buchwald, P. (2021) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.1c00070 · Cited by 147
An Effective MM/GBSA Protocol for Absolute Binding Free Energy Calculations: A Case Study on SARS-CoV-2 Spike Protein and the Human ACE2 Receptor
Forouzesh, N., & Mishra, N. (2021) · Molecules · doi:10.3390/molecules26082383 · Cited by 146
Resilience of S309 and AZD7442 monoclonal antibody treatments against infection by SARS-CoV-2 Omicron lineage strains
Case, J. B., Mackin, S., Errico, J. M., Chong, Z., Madden, E. A., Whitener, B. M., Guarino, B., Schmid, M., Rosenthal, K., Ren, K., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31615-7 · Cited by 146
Nanotechnology-based strategies against SARS-CoV-2 variants
Huang, X., Kon, E., Han, X., Zhang, X., Kong, N., Mitchell, M. J., Peer, D., & Tao, W. (2022) · Nature Nanotechnology · doi:10.1038/s41565-022-01174-5 · Cited by 146
Molecularly Imprinted Polymers as Synthetic Antibodies for Protein Recognition: The Next Generation
Bui, B. T. S., Mier, A., & Haupt, K. (2023) · Small · doi:10.1002/smll.202206453 · Cited by 146
SARS-CoV-2 and COVID-19: A genetic, epidemiological, and evolutionary perspective
Sironi, M., Hasnain, S. E., Rosenthal, B. M., Phan, T. G., Luciani, F., Shaw, M., Sallum, M. A. M., Mirhashemi, M. E., Morand, S., & Gónzález‐Candelas, F. (2020) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2020.104384 · Cited by 145
COVID-19 and the Kidneys: An Update
Benedetti, C., Waldman, M. A., Zaza, G., Riella, L. V., & Cravedi, P. (2020) · Frontiers in Medicine · doi:10.3389/fmed.2020.00423 · Cited by 145
Interaction of the spike protein RBD from SARS-CoV-2 with ACE2: Similarity with SARS-CoV, hot-spot analysis and effect of the receptor polymorphism
Othman, H., Bouslama, Z., Brandenburg, J., da Rocha, J., Hamdi, Y., Ghedira, K., Srairi‐Abid, N., & Hazelhurst, S. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.05.028 · Cited by 144
Quinolines-Based SARS-CoV-2 3CLpro and RdRp Inhibitors and Spike-RBD-ACE2 Inhibitor for Drug-Repurposing Against COVID-19: An in silico Analysis
Alexpandi, R., Mesquita, J. F. D., Pandian, S. K., & Ravi, A. V. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.01796 · Cited by 144
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 144
Deep learning for predicting COVID-19 malignant progression
Fang, C., Bai, S., Chen, Q., Zhou, Y., Xia, L., Qin, L., Gong, S., Xie, X., Zhou, C., Tu, D., et al. (2021) · Medical Image Analysis · doi:10.1016/j.media.2021.102096 · Cited by 144
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 143
A trimeric human angiotensin-converting enzyme 2 as an anti-SARS-CoV-2 agent
Xiao, T., Lü, J., Zhang, J., Johnson, R. I., McKay, L. G. A., Storm, N., Lavine, C. L., Peng, H., Cai, Y., Rits‐Volloch, S., et al. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-00549-3 · Cited by 142
In silico Screening of Natural Compounds as Potential Inhibitors of SARS-CoV-2 Main Protease and Spike RBD: Targets for COVID-19
Teli, D., Shah, M. B., & Chhabria, M. T. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.599079 · Cited by 142
Toward Rapid and Sensitive Detection of SARS-CoV-2 with Functionalized Magnetic Nanoparticles
Zhong, J., Rösch, E. L., Viereck, T., Schilling, M., & Ludwig, F. (2021) · ACS Sensors · doi:10.1021/acssensors.0c02160 · Cited by 142
Ultrasensitive and Simultaneous Detection of Two Specific SARS-CoV-2 Antigens in Human Specimens Using Direct/Enrichment Dual-Mode Fluorescence Lateral Flow Immunoassay
Wang, C., Cheng, X., Liu, L., Zhang, X., Yang, X., Zheng, S., Rong, Z., & Wang, S. (2021) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.1c11461 · Cited by 141
Scientific rationale for developing potent RBD-based vaccines targeting COVID-19
Kleanthous, H., Silverman, J. M., Makar, K. W., Yoon, I.-K., Jackson, N. M., & Vaughn, D. W. (2021) · npj Vaccines · doi:10.1038/s41541-021-00393-6 · Cited by 139
Impact of COVID-19 on Cardiovascular Disease
Vosko, I., Zirlik, A., & Bugger, H. (2023) · Viruses · doi:10.3390/v15020508 · Cited by 139
Detection and Characterization of Bat Sarbecovirus Phylogenetically Related to SARS-CoV-2, Japan
Murakami, S., Kitamura, T., Suzuki, J., Sato, R., Aoi, T., Fujii, M., Matsugo, H., Kamiki, H., Ishida, H., Takenaka‐Uema, A., et al. (2020) · Emerging infectious diseases · doi:10.3201/eid2612.203386 · Cited by 138
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 138
SARS-CoV-2–Specific Antibody Detection for Seroepidemiology: A Multiplex Analysis Approach Accounting for Accurate Seroprevalence
den Hartog, G., Schepp, R. M., Kuijer, M., GeurtsvanKessel, C., van Beek, J., Rots, N., Koopmans, M. P. G., van der Klis, F. R. M., & van Binnendijk, R. S. (2020) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiaa479 · Cited by 137
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 137
Impact of Tobacco Smoking on the Risk of COVID-19: A Large Scale Retrospective Cohort Study
Paleiron, N., Mayet, A., Marbac, V., Périsse, A., Barazzutti, H., Brocq, F.-X., Janvier, F., Dautzenberg, B., & Bylicki, O. (2020) · Nicotine & Tobacco Research · doi:10.1093/ntr/ntab004 · Cited by 137
Unique and complementary suppression of cGAS-STING and RNA sensing- triggered innate immune responses by SARS-CoV-2 proteins
Rui, Y., Su, J., Shen, S., Hu, Y., Huang, D., Zheng, W., Lou, M., Shi, Y., Wang, M., Chen, S., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00515-5 · Cited by 137
Nanobody cocktails potently neutralize SARS-CoV-2 D614G N501Y variant and protect mice
Pymm, P., Adair, A., Chan, L., Cooney, J. P., Mordant, F. L., Allison, C. C., López, E., Haycroft, E. R., O’Neill, M. T., Tan, L. L., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2101918118 · Cited by 137
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 136
Self-citation
Rationale for targeting complement in COVID‐19
Polycarpou, A., Howard, M. C., Farrar, C. A., Greenlaw, R., Fanelli, G., Wallis, R., Klavinskis, L. S., & Sacks, S. H. (2020) · EMBO Molecular Medicine · doi:10.15252/emmm.202012642 · Cited by 135

Authors: Lan, J., Ge, J., Yu, J., Shan, S., Zhou, H., Fan, S., Zhang, Q., Shi, X., Wang, Q., Zhang, L., & Wang, X.
Affiliations: Tsinghua University (CN)
Chinese Academy of Sciences (CN)
Corresponding author: Zhang, Qi
Zhang, Linqi
Wang, Xinquan
ORCID: Lan, Jun
Ge, Jiwan
Yu, Jinfang
Shan, Sisi
Zhou, Huan
Fan, Shilong
Zhang, Qi
Shi, Xuanling
Wang, Qisheng
Zhang, Linqi
Wang, Xinquan
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2020-03-30
Volume: 581
Issue: 7807
Pages: 215-220
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/s41586-020-2180-5
OpenAlex: W3014067025
Cited by: 5,983
References: 38
Citations by year: 2026: 207 · 2025: 404 · 2024: 573 · 2023: 797 · 2022: 1237 · 2021: 1678 · 2020: 1076
FWCI: 152.41
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Nature (publishedVersion)
bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
PubMed (publishedVersion)
RePEc: Research Papers in Economics (submittedVersion)
Funders: Salt Science Research Foundation
Tencent
Tsinghua University (20201080053)
Beijing Municipal Science and Technology Commission (171100000517-001 and -003)
Beijing Advanced Innovation Center for Structural Biology, Tsinghua University
Topics: Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
Keywords: SARS-CoV-2, spike protein, receptor binding domain, ACE2, crystal structure, SARS-CoV, convergent evolution, antibody epitopes, cross-reactive antibodies, viral entry, binding site residues
MeSH terms: Protein Domains, Betacoronavirus, Angiotensin-Converting Enzyme 2, SARS-CoV-2, Amino Acid Sequence, Epitopes, Binding Sites, Humans, Hydrogen Bonding, Peptidyl-Dipeptidase A, Models, Molecular, Protein Binding, Receptors, Virus, Salts, Water, Sequence Alignment, Conserved Sequence, Crystallography, X-Ray, Evolution, Molecular, Severe acute respiratory syndrome-related coronavirus, Antibodies, Neutralizing, Spike Glycoprotein, Coronavirus

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

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

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks