The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
Receptor Recognition by the Novel Coronavirus from Wuhan: an Analysis Based on Decade-Long Structural Studies of SARS Coronavirus
Open accessAbstract
The recent emergence of Wuhan coronavirus (2019-nCoV) puts the world on alert. 2019-nCoV is reminiscent of the SARS-CoV outbreak in 2002 to 2003. Our decade-long structural studies on the receptor recognition by SARS-CoV have identified key interactions between SARS-CoV spike protein and its host receptor angiotensin-converting enzyme 2 (ACE2), which regulate both the cross-species and human-to-human transmissions of SARS-CoV. One of the goals of SARS-CoV research was to build an atomic-level iterative framework of virus-receptor interactions to facilitate epidemic surveillance, predict species-specific receptor usage, and identify potential animal hosts and animal models of viruses. Based on the sequence of 2019-nCoV spike protein, we apply this predictive framework to provide novel insights into the receptor usage and likely host range of 2019-nCoV. This study provides a robust test of this reiterative framework, providing the basic, translational, and public health research communities with predictive insights that may help study and battle this novel 2019-nCoV.
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.
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“RBD contains a core structure and a variable receptor-binding motif (RBM; 437–508 a.a.) which interacts and attaches with the host cell ACE-2 receptor (Fig. 2) [7].”
From Waves and variants of SARS-CoV-2: understanding the causes and effect of the COVID-19 catastrophe (2022) · cites this paper as [7]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“RBD contains a core structure and a variable receptor-binding motif (RBM; 437–508 a.a.) which interacts and attaches with the host cell ACE-2 receptor (Fig. 2) [7].”
From Waves and variants of SARS-CoV-2: understanding the causes and effect of the COVID-19 catastrophe (2022) · cites this paper as [7]
Experimental — accuracy not yet measured
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
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 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 · cited 1×
“Our structural analyses confidently predict that 2019-nCoV uses ACE2 as its host receptor, consistent with two other new publications (30, 31).”
ResultFast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega
Sievers, F., Wilm, A., Dineen, D., Gibson, T., Karplus, K., Li, W.-Z., Lopez, R., McWilliam, H., Remmert, M., Söding, J., et al. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.75 · Cited by 15,576 · cited 1×
“Protein sequence alignments were done using Clustal Omega (33).”
MethodAngiotensin-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 · cited 2×
“2) but is ancestral to both human SARS-CoV (epidemic strain isolated in year 2002) and bat SARS-CoV strains that use ACE2 receptor to enter and infect primary host lung cells (11, 17).”
BackgroundOrigin and evolution of pathogenic coronaviruses
Cui, J., Li, F., & Shi, Z. (2018) · Nature Reviews Microbiology · doi:10.1038/s41579-018-0118-9 · Cited by 5,729 · cited 2×
“It is believed that bats and palm civets were the natural and intermediate reservoirs for SARS-CoV, respectively, and that SARS-CoV transmitted from palm civets to humans in an animal market in Southern China (12–14).”
BackgroundSelf-citationLetko, M., Marzi, A., & Munster, V. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0688-y · Cited by 3,109
Coronavirus as a possible cause of severe acute respiratory syndrome
Peiris, M. J. S., Lai, S., Poon, L. L. M., Guan, Y., Yam, L., Lim, W., Nicholls, J. M., Yee, W., Yan, W., Cheung, M., et al. (2003) · The Lancet · doi:10.1016/s0140-6736(03)13077-2 · Cited by 2,916
Structure, Function, and Evolution of Coronavirus Spike Proteins
Li, F. (2016) · Annual Review of Virology · doi:10.1146/annurev-virology-110615-042301 · Cited by 2,740 · cited 1×
“An envelope-anchored spike protein mediates coronavirus entry into host cells by first binding to a host receptor and then fusing viral and host membranes (16).”
BackgroundSelf-citationA Major Outbreak of Severe Acute Respiratory Syndrome in Hong Kong
Lee, N. L. S., Hui, D. S. C., Wu, A. K. L., Chan, P. K. S., Cameron, P. A., Joynt, G. M., Ahuja, A. T., Yung, M. Y., Leung, C. B., To, K. F., et al. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa030685 · Cited by 2,638
Guan, Y., Zheng, B., He, Y., Liu, X. L., Zhuang, Z. X., Cheung, C. L., Luo, S., Li, P. H., Zhang, L., Guan, Y., et al. (2003) · Science · doi:10.1126/science.1087139 · Cited by 2,404
Cited by
Sorted by citations
Items 601–700 of 1,004
Facing the COVID‐19 outbreak: What should we know and what could we do?
Yang, Y., Shang, W., & Rao, X. (2020) · Journal of Medical Virology · doi:10.1002/jmv.25720 · Cited by 85
Post COVID‐19 : a solution scan of options for preventing future zoonotic epidemics
Petrovan, S. O., Aldridge, D. C., Bartlett, H., Bladon, A. J., Booth, H. L., Broad, S., Broom, D. M., Burgess, N. D., Cleaveland, S., Cunningham, A. A., et al. (2021) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12774 · Cited by 89
“…SARS-CoV-2 has been found in several species of horseshoe bat Rhinolophus spp., which likely represent the ancestral or evolutionary (natural) host of the virus (Zhou et al ., 2020 a ), although the ability of this closest known relative of SARS-CoV-2 to infect humans is poor (Wan et al ., 2020).”
A Comprehensive Review of Tocilizumab in COVID‐19 Acute Respiratory Distress Syndrome
Khiali, S., Khani, E., & Entezari‐Maleki, T. (2020) · The Journal of Clinical Pharmacology · doi:10.1002/jcph.1693 · Cited by 87
Lubbe, L., Cozier, G. E., Oosthuizen, D., Acharya, K. R., & Sturrock, E. D. (2020) · Clinical Science · doi:10.1042/cs20200899 · Cited by 93
Sanches, P. R. D. S., Charlie‐Silva, I., Braz, H. L. B., Bittar, C., Calmon, M. F., Rahal, P., & Cilli, E. M. (2021) · Journal of Virus Eradication · doi:10.1016/j.jve.2021.100054 · Cited by 88
Osei, S. A., Biney, R. P., Anning, A. S., Nortey, L. N., & Ghartey‐Kwansah, G. (2022) · BMC Infectious Diseases · doi:10.1186/s12879-022-07064-4 · Cited by 85
The Pathophysiology of Long COVID throughout the Renin-Angiotensin System
Khazaal, S., Harb, J., Rima, M., Annweiler, C., Wu, Y., Cao, Z., Khattar, Z. A., Legros, C., Kovacic, H., Fajloun, Z., et al. (2022) · Molecules · doi:10.3390/molecules27092903 · Cited by 87
“In fact, SARS-CoV-2 activates the RAS by attaching, via its spike protein, to the ACE2 receptor, which is involved in the degradation of Ang II [16].”
BackgroundZheng, Z., Monteil, V., Maurer‐Stroh, S., Yew, C. W., Leong, C., Mohd-Ismail, N. K., Arularasu, S. C., Chow, V. T. K., Lin, R. T. P., Mirazimi, A., et al. (2020) · Eurosurveillance · doi:10.2807/1560-7917.es.2020.25.28.2000291 · Cited by 82
Prajapat, M., Shekhar, N., Sarma, P., Avti, P., Singh, S. K., Kaur, H., Bhattacharyya, A., Kumar, S., Sharma, S., Prakash, A., et al. (2020) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2020.107716 · Cited by 88
Rezakhani, L., Kelishadrokhi, A. F., Soleimanizadeh, A., & Rahmati, S. (2020) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2020.105009 · Cited by 84
Rosa, R. B., Dantas, W. M., do Nascimento, J. C. F., da Silva, M. V., de Oliveira, R. N., & Pena, L. (2021) · Viruses · doi:10.3390/v13030379 · Cited by 89
“SARS-CoV-2 presents a high affinity for human ACE2, but low affinity for ACE2 from other organisms [59].”
BackgroundSavla, S. R., Prabhavalkar, K. S., & Bhatt, L. K. (2021) · Expert Review of Anti-infective Therapy · doi:10.1080/14787210.2021.1915129 · Cited by 88
Antiviral performance of graphene-based materials with emphasis on COVID-19: A review
Seifi, T., & Kamali, A. R. (2021) · Medicine in Drug Discovery · doi:10.1016/j.medidd.2021.100099 · Cited by 87
“transmembrane protein on the cell surface [24,25].”
Phenolic compounds disrupt spike-mediated receptor-binding and entry of SARS-CoV-2 pseudo-virions
Goc, A., Sumera, W., Rath, M., & Niedzwiecki, A. (2021) · PLoS ONE · doi:10.1371/journal.pone.0253489 · Cited by 84
Research Progress on the Antiviral Activity of Glycyrrhizin and its Derivatives in Liquorice
Huan, C., Xu, Y. Q., Zhang, W., Guo, T., Pan, H., & Gao, S. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.680674 · Cited by 88
RdRp inhibitors and COVID-19: Is molnupiravir a good option?
Hashemian, S. M. R., Pourhanifeh, M. H., Hamblin, M. R., Shahrzad, M. K., & Mirzaei, H. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.112517 · Cited by 84
“The host cell-SARS-CoV-2 binding occurs via ACE2 receptor expressed on epithelial cells in the lungs, brain, kidney, intestines, and blood vessel endothelial cells [29].”
ACE2 protein expression in lung tissues of severe COVID-19 infection
Gheware, A., Ray, A., Rana, D., Bajpai, P., Nambirajan, A., Subramanian, A., Mathur, P., Trikha, A., Arava, S., Das, P., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-07918-6 · Cited by 89
Abassi, Z. A., Skorecki, K. L., Heyman, S. N., Kinaneh, S., & Armaly, Z. (2020) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00097.2020 · Cited by 83
“Remarkably, AT2 express many genes that are profoundly involved in the reproduction and transmission of the virus (16).”
BackgroundPandemia COVID-19, la nueva emergencia sanitaria de preocupación internacional: una revisión
Crespo, R. M., & Morales-Crespo, M. M. (2020) · Medicina de Familia SEMERGEN · doi:10.1016/j.semerg.2020.05.010 · Cited by 115
Shi, D., Wu, W., Wáng, Q., Xu, K., Xie, J., Wu, J., Lv, L., Sheng, J., Guo, J., Wang, K., et al. (2020) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiaa388 · Cited by 83
Synonymous mutations and the molecular evolution of SARS-CoV-2 origins
Wang, H., Pipes, L., & Nielsen, R. (2020) · Virus Evolution · doi:10.1093/ve/veaa098 · Cited by 83
Targets and strategies for vaccine development against SARS-CoV-2
Malik, J. A., Mulla, A. H., Farooqi, T., Pottoo, F. H., Anwar, S., & Rengasamy, K. R. R. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111254 · Cited by 81
“BNT162b1 encodes an optimized S2RBD antigen, while BNT162b2 encodes an optimized SARS-CoV-2 full-length S protein.”
InfluentialImmunological Aspects of SARS-CoV-2 Infection and the Putative Beneficial Role of Vitamin-D
Peng, M.-Y., Liu, W.-C., Zheng, J.-Q., Lu, C., Hou, Y., Zheng, C., Song, J.-Y., Lu, K., & Chao, Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22105251 · Cited by 86
“Angiotensin-converting enzyme (ACE) 2 (ACE2), which is expressed in most human cells, acts as a receptor for SARS-CoV-2 [15].”
BackgroundGastrointestinal Manifestations of COVID-19: A Review of What We Know
Groff, A., Kavanaugh, M., Ramgobin, D., McClafferty, B., Aggarwal, C. S., Golamari, R. R., & Jain, R. (2021) · Ochsner Journal · doi:10.31486/toj.20.0086 · Cited by 82
The mechanisms and clinical application of Traditional Chinese Medicine Lianhua-Qingwen capsule
Shen, X.-H., & Yin, F. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111998 · Cited by 83
“COVID19 is caused by novel coronavirus SARS-COV-2 which belong to β coronavirus [9].”
Zuo, J., Meng, T., Wang, Y., & Tang, W. (2023) · Pharmaceuticals · doi:10.3390/ph16050641 · Cited by 83
“Recent research showed that the receptor-binding domain of SARS-CoV-2 was specific for the human ACE-2 receptor, so the human ACE2 receptor acted as an important mediator of the SARS-CoV-2 infection [22,23].”
BackgroundCOVID-19 Spiraling of Frailty in Older Italian Patients
Abbatecola, A. M., & Incalzi, R. A. (2020) · The journal of nutrition health & aging · doi:10.1007/s12603-020-1357-9 · Cited by 83
“Angiotensin converting enzymes 2 (ACE-2) are expressed on myocytes, renal endothelial and epithelial lung cells (13) and have shown to act as receptors for SARS-CoV-2 (14) .”
BackgroundSequence signatures of two public antibody clonotypes that bind SARS-CoV-2 receptor binding domain
Tan, T. J. C., Yuan, M., Kuzelka, K., Padron, G. C., Beal, J. R., Chen, X., Wang, Y., Rivera-Cardona, J., Zhu, X., Stadtmueller, B. M., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24123-7 · Cited by 75
COVID ‐19 treatment by repurposing drugs until the vaccine is in sight
Phadke, M., & Saunik, S. (2020) · Drug Development Research · doi:10.1002/ddr.21666 · Cited by 82
“The former is more for SARS and the latter is for MERS.”
BackgroundYu, X., Sun, X., Cui, P., Pān, H., Lin, S., Han, R., Jiang, C., Fang, Q., Kong, D., Zhu, Y., et al. (2020) · Transboundary and Emerging Diseases · doi:10.1111/tbed.13604 · Cited by 81
Telmisartan as tentative angiotensin receptor blocker therapeutic for COVID ‐19
Rothlin, R. P., Vetulli, H. M., Duarte, M., & Pelorosso, F. G. (2020) · Drug Development Research · doi:10.1002/ddr.21679 · Cited by 85
Drug repurposing against COVID-19: focus on anticancer agents
Ciliberto, G., Mancini, R., & Paggi, M. G. (2020) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-020-01590-2 · Cited by 81
“To this end, it is mandatory to work prospectively to produce or identify better antiviral drugs and prophylactic/therapeutic MoAb therapies, as well as possibly targeting vital pathogenic factors, such as, in the case of SARS-CoV-2, Spike protein RBD [36, 98] or the main protease Mpro [99].”
BackgroundCOVID-19: fighting the invisible enemy with microRNAs
Chauhan, N., Jaggi, M., Chauhan, S. C., & Yallapu, M. M. (2020) · Expert Review of Anti-infective Therapy · doi:10.1080/14787210.2020.1812385 · Cited by 80
“Growing evidences argue that receptor binding domain of SARS-CoV-2 spike protein gets activated after its cleavage by Transmembrane Serine Protease 2 (TMPRSS2) and binds to the Angiotensin Converting Enzyme 2 (ACE2) receptor of the host cells (Figure 2A) [20-22].”
BackgroundLi, Y., Chu, F., Li, P., Johnson, N. L., Li, T., Wang, Y., An, R., Dan-tong, W., Chen, J., Su, Z., et al. (2021) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2021.113854 · Cited by 81
Evaluation of the prognostic role of NLR, LMR, PLR, and LCR ratio in COVID‐19 patients
Erdoğan, A., Can, F. E., & Gönüllü, H. (2021) · Journal of Medical Virology · doi:10.1002/jmv.27097 · Cited by 82
“Recent studies have shown that the virus enters alveolar cells by binding to the receptor and activates macrophages, allowing inflammatory factors to be released.(11) As a result, factors and chemokines that use other mononuclear cells are released.”
BackgroundStructural definition of a pan-sarbecovirus neutralizing epitope on the spike S2 subunit
Hurlburt, N. K., Homad, L. J., Sinha, I. R., Jennewein, M. F., MacCamy, A. J., Wan, Y.-H., Boonyaratanakornkit, J. B., Sholukh, A. M., Jackson, A. M., Zhou, P.-P., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-03262-7 · Cited by 80
Self-citationWan, S., Li, M., Ye, Z., Yang, C., Cai, Q., Duan, S., & Song, B. (2020) · Academic Radiology · doi:10.1016/j.acra.2020.04.033 · Cited by 82
“The presentation of diarrhea may be related to the pathogenesis of SARS-CoV-2, because this virus binds to human receptor angiotensin-converting enzyme 2 (45), which shows high expression in the gastrointestinal tract (22,46).”
Does Early Childhood Vaccination Protect Against COVID-19?
Sidiq, K. R., Sabir, D. K., Ali, S. M., & Kodzius, R. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.00120 · Cited by 81
Payus, A. O., Lin, C. L. S., Noh, M. M., Jeffree, M. S., & Raymond, A. A. (2020) · Biomolecules and Biomedicine · doi:10.17305/bjbms.2020.4860 · Cited by 82
“The level of IL-6 is positively correlated with the severity of COVID-19 symptoms [31].”
BackgroundAngiotensin-converting enzyme 2 (ACE2) receptor and SARS-CoV-2: Potential therapeutic targeting
Sharifkashani, S., Bafrani, M. A., Khaboushan, A. S., Pirzadeh, M., Kheirandish, A., Yavarpour‐Bali, H., Hessami, A., Saghazadeh, A., & Rezaei, N. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.173455 · Cited by 81
“Second, the SARS-CoV-2 may also be transmitted between humans and animals (Wan et al., 2020).”
BackgroundChanges of serum IL‐10, IL‐1β, IL‐6, MCP‐1, TNF‐α, IP‐10 and IL‐4 in COVID‐19 patients
Lu, Q., Zhu, Z., Tan, C., Zhou, H., Hu, Y., Shen, G., Zhu, P., Yang, G., & Xie, X. (2021) · International Journal of Clinical Practice · doi:10.1111/ijcp.14462 · Cited by 89
“In COVID-19 patients, the serum levels of all cytokines were significant positively correlated with age, the poor prognosis of the elderly may be related to this; some of they have relationships with the gender or antibody, the former may be related to the high level of ACE2 in male reproductive system [17-19]; the le…”
BackgroundA Review of SARS-CoV2: Compared With SARS-CoV and MERS-CoV
Zhou, H., Yang, J., Zhou, C. S., Chen, B., Fang, H., Chen, S., Zhang, X., Wang, L., & Zhang, L. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.628370 · Cited by 87
SARS-CoV-2 Spike triggers barrier dysfunction and vascular leak via integrins and TGF-β signaling
Biering, S. B., de Sousa, F. T. G., Tjang, L. V., Pahmeier, F., Zhu, C., Ruan, R., Blanc, S. F., Patel, T. S., Worthington, C. M., Glasner, D. R., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34910-5 · Cited by 92
“Given ourobservationsthat SARS-CoV-2SmediatesbarrierdysfunctioninanACE2-independentmanner, we utilized WT C57BL/6J mice that do not express human ACE2 and arenotpermissive toinfection bymost SARS-CoV-2 variants,including the Wuhan and Washington isolates 9,37 .”
Self-citationShah, H., Khan, M. S. H., Dhurandhar, N. V., & Hegde, V. (2021) · Acta Diabetologica · doi:10.1007/s00592-020-01636-z · Cited by 80
Sayad, B., Sobhani, M., & Khodarahmi, R. (2020) · Archives of Medical Research · doi:10.1016/j.arcmed.2020.04.018 · Cited by 79
Yang, Z.-D., Gao-Jun, Z., Jin, R., Zhi-sheng, L., Zong-Qi, D., Xie, X., & Guo-wei, S. (2020) · Journal of Infection · doi:10.1016/j.jinf.2020.04.030 · Cited by 80
Kar, P., Sharma, N. R., Singh, B., Sen, A., & Roy, A. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1780947 · Cited by 84
“was performed at the active pocket of the RBD of the SARS-CoV-2 spike protein (PDB ID: 6LZG), in light of prior knowledge about the active site residues that bind with human receptor ACE2 (Andersen et al., 2020; Hasan et al., 2020; Tai et al., 2020; Wan et al., 2020).”
BackgroundInfluentialThe Impact of SARS-Cov-2 Virus Infection on the Endocrine System
Somasundaram, N. P., Ranathunga, I., Ratnasamy, V., Wijewickrama, P. S. A., Dissanayake, H. A., Yogendranathan, N., Gamage, K. K. K., de Silva, N. L., Sumanatilleke, M., Katulanda, P., et al. (2020) · Journal of the Endocrine Society · doi:10.1210/jendso/bvaa082 · Cited by 84
Hozhabri, H., Piceci‐Sparascio, F., Sohrabi, H., Mousavifar, L., Roy, R., Scribano, D., Luca, A. D., Ambrosi, C., & Sarshar, M. (2020) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph17165648 · Cited by 86
“SARS-CoV, MERS-CoV and SARS-CoV-2 bind to different host receptors to gain entry into host cells [4,51,52].”
BackgroundJanssen, R., Visser, M. P. J., Dofferhoff, A. S. M., Vermeer, C., Janssens, W., & Walk, J. (2020) · British Journal Of Nutrition · doi:10.1017/s0007114520003979 · Cited by 84
“These proteins are also the most immunogenic part of the virus(45).”
The development of Nanosota-1 as anti-SARS-CoV-2 nanobody drug candidates
Ye, G., Gallant, J. P., Massey, C., Shi, K., Tai, W., Zheng, J., Odle, A. E., Vickers, M. A., Shang, J., Wan, Y., et al. (2021) · eLife · doi:10.7554/elife.64815 · Cited by 78
“The RBDs of SARS-CoV-2 and a closely related SARS-CoV-1 both recognize human angiotensin-converting enzyme 2 (ACE2) as their receptor (Li, 2015; Wan et al., 2020; Li et al., 2003; Zhou et al., 2020).”
BackgroundSelf-citationChen, C., Boorla, V. S., Banerjee, D., Chowdhury, R., Cavener, V. S., Nissly, R. H., Gontu, A., Boyle, N. R., Vandegrift, K. J., Nair, M. S., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2106480118 · Cited by 81
Dai, Y., Hu, F., Li, H., Huang, H.-Y., Wang, D., & Liang, Y. (2020) · Annals of Translational Medicine · doi:10.21037/atm.2020.03.61 · Cited by 79
Is there an impact of the COVID-19 pandemic on male fertility? The ACE2 connection
Younis, J. S., Abassi, Z. A., & Skorecki, K. L. (2020) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00183.2020 · Cited by 79
Dehury, B., Raina, V., Misra, N., & Suar, M. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1802348 · Cited by 80
“…is primarily determined by the affinity between the viral RBD domain of spike protein and the host receptor ACE2, and there are some specific amino acid residues that are potentially involved in the interaction and viral binding (Huentelman et al., 2004; Wan et al., 2020; Zhang et al., 2005).”
BackgroundResultInfluentialBalmeh, N., Mahmoudi, S., Mohammadi, N., & Karabedianhajiabadi, A. (2020) · Informatics in Medicine Unlocked · doi:10.1016/j.imu.2020.100407 · Cited by 79
“The most important receptors for SARS-Cov-2 are ACE2 [31] TMPRSS2 [32], and GRP78 [6], which by blocking these receptors can protect the body against the virus.”
Manipulation of ACE2 expression in COVID-19
Chaudhry, F., Lavandero, S., Xie, X., Sabharwal, B., Zheng, Y., Correa, A. A., Narula, J., & Levy, P. D. (2020) · Open Heart · doi:10.1136/openhrt-2020-001424 · Cited by 83
Kuriakose, J., Montezano, A. C. I., & Touyz, R. M. (2021) · Clinical Science · doi:10.1042/cs20200480 · Cited by 79
Omrani, M., Keshavarz, M., Ebrahimi, S. N., Mehrabi, M., McGaw, L. J., Abdalla, M. A., & Mehrbod, P. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.586993 · Cited by 79
“Some analysis suggested that SARS-CoV-2 recognizes human ACE2 more efficiently than SARS-CoV, increasing the capacity of SARS-CoV-2 to transmit from human to human (Wan et al., 2020).”
BackgroundDoes Ibuprofen Worsen COVID-19?
Moore, N., Carleton, B., Blin, P., Bosco-Levy, P., & Droz, C. (2020) · Drug Safety · doi:10.1007/s40264-020-00953-0 · Cited by 78
“A suggestion that ibuprofen might upregulate ACE-2, thereby increasing the entrance of COVID-19 into the cells [4, 14].”
BackgroundTargeting SARS-CoV2 Spike Protein Receptor Binding Domain by Therapeutic Antibodies
Hussain, A., Hasan, A., Babadaei, M. M. N., Bloukh, S. H., Chowdhury, M. E. H., Sharifi, M., Haghighat, S., & Falahati, M. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110559 · Cited by 78
“While this data revealed that SARS-CoV2 may interact with human ACE2 with a high binding affinity, theoretical investigations demonstrated that the formation of this complex is not favorable and the RBD sequence is not similar with that in SARS-CoV to be potential for interaction with receptor [30, 33].”
Laurini, E., Marson, D., Aulić, S., Fermeglia, M., & Pricl, S. (2020) · ACS Nano · doi:10.1021/acsnano.0c04674 · Cited by 77
A fractional-order differential equation model of COVID-19 infection of epithelial cells
Chatterjee, A. N., & Ahmad, B. (2021) · Chaos Solitons & Fractals · doi:10.1016/j.chaos.2021.110952 · Cited by 78
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 81
Do children need a longer time to shed SARS-CoV-2 in stool than adults?
Ma, X., Su, L., Zhang, Y., Zhang, X., Gai, Z., & Zhang, Z. (2020) · Journal of Microbiology Immunology and Infection · doi:10.1016/j.jmii.2020.03.010 · Cited by 76
Blockade of SARS-CoV-2 infection by recombinant soluble ACE2
Alhenc‐Gelas, F., & Drüeke, T. B. (2020) · Kidney International · doi:10.1016/j.kint.2020.04.009 · Cited by 77
“SARS-CoV-2, the coronavirus responsible for the current COVID-19 pandemic, is believed to bind mainly or exclusively to angiotensin-converting enzyme 2 (ACE2), a cell-surface protein otherwise known for its enzymatic, carboxypeptidase-type activity and its physiological role in the reninangiotensin system.(1,2) ACE2 a…”
BackgroundPotential new treatment strategies for COVID-19: is there a role for bromhexine as add-on therapy?
Depfenhart, M., de Villiers, D., Lemperle, G. H., Meyer, M., & Somma, S. D. (2020) · Internal and Emergency Medicine · doi:10.1007/s11739-020-02383-3 · Cited by 83
Role of the early secretory pathway in SARS-CoV-2 infection
Sicari, D., Chatziioannou, A. A., Koutsandreas, T., Sitia, R., & Chevet, É. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.202006005 · Cited by 76
Hrenak, J., & Šimko, F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218038 · Cited by 79
“A mutation in the receptor-binding domain of the SARS-CoV-2 spike protein S compared to SARS-CoV is responsible for a higher affinity of SARS-CoV-2 to ACE2 [67].”
BackgroundRenin-Angiotensin-Aldosterone System Inhibitors in Patients with Covid-19
Feldman, A., Arruda, G., & de Souza, O. F. (2020) · Journal of Cardiac Arrhythmias · doi:10.24207/jca.v33i3.3405 · Cited by 82
Implications of SARS‐CoV‐2 infection for neurogastroenterology
Marasco, G., Lenti, M. V., Cremon, C., Barbaro, M. R., Stanghellini, V., Sabatino, A. D., & Barbara, G. (2021) · Neurogastroenterology & Motility · doi:10.1111/nmo.14104 · Cited by 78
Gowda, P., Patrick, S., Joshi, S. D., Kumawat, R. K., & Sen, E. (2021) · Cytokine · doi:10.1016/j.cyto.2021.155496 · Cited by 79
“This was followed by infection of the cells with SARS-CoV-2 [42] at an MOI (multiplicity of infection) of 0.”
Lin, W., Fan, J., Hu, L., Zhang, Y., Ooi, J. D., Meng, T., Jin, P., Ding, X., Peng, L., Song, L., et al. (2021) · Chinese Medical Journal · doi:10.1097/cm9.0000000000001439 · Cited by 77
“2019-nCoV had a receptor-binding domain similar to that of SARS-CoV, directly binding to angiotensin-converting enzyme II (ACE2), strongly suggesting that 2019-nCoV uses ACE2 as its receptor.([5-8])”
BackgroundNovel virus-like nanoparticle vaccine effectively protects animal model from SARS-CoV-2 infection
Geng, Q., Tai, W., Baxter, V. K., Shi, J., Wan, Y., Zhang, X., Montgomery, S. A., Taft-Benz, S., Anderson, E. J., Knight, A. C., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009897 · Cited by 78
Self-citationManzoor, T., Saleem, A., Farooq, N., Dar, L. A., Nazir, J., Saleem, S., Ismail, S., Gugjoo, M. B., Shiekh, P. A., & Ahmad, S. M. (2023) · Inflammation and Regeneration · doi:10.1186/s41232-023-00266-6 · Cited by 81
“ACE2 SARS-CoV-2 receptors generated on MSCderived EVs decrease the viral infection by competitively inhibiting SARS-CoV-2 binding to alveolar cells, mainly AT2 cells [112] (Fig.”
BackgroundSun, C., Chen, L., Yang, J., Luo, C., Zhang, Y., Li, J., Yang, J., Zhang, J., & Xie, L. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.02.16.951723 · Cited by 77
Azim, K. F., Ahmed, S. R., Banik, A., Khan, M. M. R., Deb, A., & Somana, S. R. (2020) · Informatics in Medicine Unlocked · doi:10.1016/j.imu.2020.100367 · Cited by 75
Predicting novel drugs for SARS-CoV-2 using machine learning from a >10 million chemical space
Kowalewski, J., & Ray, A. (2020) · Heliyon · doi:10.1016/j.heliyon.2020.e04639 · Cited by 76
Vivarelli, S., Falzone, L., Grillo, C. M., Scandurra, G., Torino, F., & Libra, M. (2020) · Cancers · doi:10.3390/cancers12082237 · Cited by 75
“The host’s infection is initiated by the SARS-CoV-2 spike (S) protein binding to the extracellular enzymatic domain of the transmembrane angiotensin-converting enzyme 2 (ACE2) cellular receptor, expressed by the epithelial and endothelial cells within the alveoli [8].”
BackgroundMa, N., Li, P., Wang, X., Yu, Y., Tan, X., Chen, P., Li, S., & Jiang, F. (2020) · JAMA Ophthalmology · doi:10.1001/jamaophthalmol.2020.3690 · Cited by 76
Cardiovascular Complications Associated with COVID-19 and Potential Therapeutic Strategies
Samidurai, A., & Das, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186790 · Cited by 82
“In addition, a single mutation at N501T in the spike protein strengthened the binding efficiency of SARS-CoV-2 to Angiotensin-Converting Enzyme 2 (ACE2), the primary mode of entry into host cell [17].”
BackgroundBhowmik, D., Nandi, R., Prakash, A., & Kumar, D. (2021) · Heliyon · doi:10.1016/j.heliyon.2021.e06515 · Cited by 79
“Previous studies on protein-protein docking, molecular dynamics, and virtual screening studies on SARS-CoV-2 spike glycoprotein (nCoVSP) as well human ACE-2 receptor already evaluated the binding pockets and essential residues in the RBD and their interaction with the hotspots in ACE-2 receptor (Wu et al., 2011; Shang…”
COVID‐19‐induced endotheliitis: emerging evidence and possible therapeutic strategies
Calabretta, E., Moraleda, J. M., Iacobelli, M., Jara, R., Vlodavsky, I., O’Gorman, P., Pagliuca, A., Mo, C. C., Baron, R. M., Aghemo, A., et al. (2021) · British Journal of Haematology · doi:10.1111/bjh.17240 · Cited by 75
Recent advances in developing small-molecule inhibitors against SARS-CoV-2
Xiang, R., Yu, Z., Wang, Y., Wang, L., Huo, S., Li, Y., Liang, R., Hao, Q., Ying, T., Gao, Y., et al. (2021) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.06.016 · Cited by 77
“Like SARS-CoV, SARS-CoV-2 uses a glycosylated, homotrimeric class I fusion S protein to gain entry into host cells 31 e 33 .”
Gęca, T., Wojtowicz, K., Guzik, P. W., & Góra, T. (2022) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph19116555 · Cited by 80
“intestines (enterocytes) [39], kidneys (proximal tubule cells) [34,35,40], as well as the heart muscle (myocardium cells) [36,37,41].”
BackgroundElevations of serum cancer biomarkers correlate with severity of COVID‐19
Wei, X., Su, J., Yang, K., Wei, J., Wan, H., Cao, X., Tan, W., & Wang, H. (2020) · Journal of Medical Virology · doi:10.1002/jmv.25957 · Cited by 75
Targeting Cytokine Storm to Manage Patients with COVID-19: A Mini-Review
Roshanravan, N., Seif, F., Ostadrahimi, A., Pouraghaei, M., & Ghaffari, S. (2020) · Archives of Medical Research · doi:10.1016/j.arcmed.2020.06.012 · Cited by 77
Wang, K., Zhang, X., Sun, J., Ye, J., Wang, F., Hua, J., Zhang, H., Shi, T., Li, Q., & Wu, X. (2020) · CHEST Journal · doi:10.1016/j.chest.2020.06.015 · Cited by 75
“Sputum has been reported to be more sensitive than NPS in SARS-CoV-2 RNA detection because SARSCoV-2 mainly bind with angiotensin-converting enzyme 2 receptor of the lower respiratory tract.(13-15) However, the use of sputum specimen in clinical practice is quite limited because only a proportion of patients with COVI…”
Gupta, S. K., Singh, V. K., Varadwaj, P. K., Chakravartty, N., Katta, A. V. S. K. M., Lekkala, S. P., Thomas, G., Narasimhan, S., Reddy, A. R., & Lachagari, V. B. R. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1837679 · Cited by 75
“The receptor binding domain (RBD) region of S glycoprotein is recognized by the critical lysine 31 residue of the hACE2 receptor protein (Wan et al., 2020).”
BackgroundChoudhury, A., Das, N. C., Patra, R., Bhattacharya, M., Ghosh, P., Patra, B. C., & Mukherjee, S. (2021) · Future Virology · doi:10.2217/fvl-2020-0342 · Cited by 75
“After its entry into the respiratory system, the spike glycoprotein ectodomain present on the viral capsid binds to the angiotensin-converting enzyme-2 (ACE2) transmembrane receptor protein, consequently, the RNA genome enters the alveolar cells by receptor-mediated endocytosis [8].”
BackgroundCOVID-19 and Hypertension: The What, the Why, and the How
Muhamad, S.-A., Ugusman, A., Kumar, J., Skiba, D. S., Hamid, A. A., & Aminuddin, A. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.665064 · Cited by 76
FocusCovid: automated COVID-19 detection using deep learning with chest X-ray images
Agrawal, T., & Choudhary, P. (2021) · Evolving Systems · doi:10.1007/s12530-021-09385-2 · Cited by 79
“There is a similarity between the spike proteins of SARS-CoV and SARS coronavirus 2 (SARS-CoV-2), for this reason, it is assumed that SARS-CoV-2 also uses ACE2 as its receptor (Wan et al. 2020).”
BackgroundDiscovery of potential small molecular SARS-CoV-2 entry blockers targeting the spike protein
Wang, L., Wu, Y. L., Yao, S., Ge, H., Zhu, Y., Chen, K., Chen, W., Zhang, Y., Zhu, W. J., Wang, H., et al. (2021) · Acta Pharmacologica Sinica · doi:10.1038/s41401-021-00735-z · Cited by 77
“SARS-CoV-2 and SARS-CoV are beta coronaviruses, which are enveloped, single, and positive-stranded RNA viruses [3].”
BackgroundPotential immuno-nanomedicine strategies to fight COVID-19 like pulmonary infections
Bonam, S. R., Kotla, N. G., Bohara, R. A., Rochev, Y. A., Webster, T. J., & Bayry, J. (2020) · Nano Today · doi:10.1016/j.nantod.2020.101051 · Cited by 76
“Like other SARS-CoV, SARS-CoV-2 also uses the angiotensin 1converting enzyme 2 (ACE2; a close homolog of ACE) for entry into the cells [10,11], in addition to ACE2, it also uses other cellular proteases including transmembrane protease serine 2 (TMPRSS2) [12,13], which is useful in priming of the process of SARS-CoV-2.”
BackgroundThe Promise of AI in Detection, Diagnosis, and Epidemiology for Combating COVID-19: Beyond the Hype
Abdulkareem, M., & Petersen, S. E. (2021) · Frontiers in Artificial Intelligence · doi:10.3389/frai.2021.652669 · Cited by 83
The Renin-Angiotensin System: A Key Role in SARS-CoV-2-Induced COVID-19
El-Arif, G., Farhat, A., Khazaal, S., Annweiler, C., Kovacic, H., Wu, Y., Cao, Z., Fajloun, Z., Khattar, Z. A., & Sabatier, J. (2021) · Molecules · doi:10.3390/molecules26226945 · Cited by 76
“During viral infection, SARS-CoV-2 over-activates the RAS by binding to the ACE2 receptor, which normally has the function of degrading Ang II [21].”
BackgroundShen, Y., Yu, J., Zhou, J., & Hu, G. (2024) · Journal of Medical Internet Research · doi:10.2196/59024 · Cited by 107
“Furthermore, the early identification of the genome sequence of SARS-CoV-2 virus by researchers facilitated the rapid development of diagnostic tests and the initiation of vaccine development efforts [109-111].”
Abdelmageed, M. I., Abdelmoneim, A. H., Mustafa, M. I., Elfadol, N. M., Murshed, N. S., Shantier, S. W., & Makhawi, A. M. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.02.04.934232 · Cited by 74
Vaccine development and therapeutic design for 2019‐nCoV/SARS‐CoV‐2: Challenges and chances
Ghaebi, M., Osali, A., Valizadeh, H., Roshangar, L., & Ahmadi, M. (2020) · Journal of Cellular Physiology · doi:10.1002/jcp.29771 · Cited by 73
“There is also some evidence that coronaviruses make use of certain antibodies for entry to the cell as an alternative mechanism of target cell binding (Wan et al., 2020).”
BackgroundXu, C. L. H., Raval, M., Schnall, J., Kwong, J. C., & Holmes, N. E. (2020) · The Pediatric Infectious Disease Journal · doi:10.1097/inf.0000000000002814 · Cited by 73
“Furthermore, ACE2 protein, a proven cell receptor for SARS-CoV-2, is abundantly expressed in the gastrointestinal tract.(8,9) Endoscopic sampling of patients with SARS-CoV-2 has recently demonstrated an intracellular staining of viral nucleocapsid protein in the gastric, duodenal and rectal epithelia.”
Background
Metadata
- Authors
- Wan, Y., Shang, J., Graham, R., Baric, R. S., & Li, F.
- Affiliations
- University of Minnesota (US)
- University of North Carolina at Chapel Hill (US)
- Corresponding author
- Li, Fang
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 2020-03-17
- Volume
- 94
- Issue
- 7
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- PMC
- PMC7081895
- OpenAlex
- W3004348779
- Cited by
- 4,341
- References
- 38
- Citations by year
- 2026: 27 · 2025: 75 · 2024: 170 · 2023: 299 · 2022: 619 · 2021: 1273 · 2020: 1865
- FWCI
- 133.25
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Virology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- HHS | NIH | National Institute of Allergy and Infectious Diseases (R01AI089728, R01AI110700)
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
- Health Sciences › Medicine › Infectious Diseases › Viral Infections and Outbreaks Research
- Keywords
- SARS-CoV-2, SARS-CoV, spike protein, angiotensin-converting enzyme 2, receptor recognition, host range prediction, interspecies transmission, human-to-human transmission, animal models, disease surveillance
- MeSH terms
- Protein Domains, Betacoronavirus, Angiotensin-Converting Enzyme 2, COVID-19, SARS-CoV-2, Amino Acid Sequence, Animals, China, Chiroptera, Humans, Peptidyl-Dipeptidase A, Models, Molecular, Phylogeny, Pneumonia, Viral, Receptors, Virus, Sequence Alignment, Coronavirus Infections, Severe acute respiratory syndrome-related coronavirus, Host Specificity, 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
