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Molecular Architecture of the SARS-CoV-2 Virus
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Abstract
SARS-CoV-2 is an enveloped virus responsible for the COVID-19 pandemic. Despite recent advances in the structural elucidation of SARS-CoV-2 proteins, the detailed architecture of the intact virus remains to be unveiled. Here we report the molecular assembly of the authentic SARS-CoV-2 virus using cryoelectron tomography (cryo-ET) and subtomogram averaging (STA). Native structures of the S proteins in pre- and postfusion conformations were determined to average resolutions of 8.7-11 Å. Compositions of the N-linked glycans from the native spikes were analyzed by mass spectrometry, which revealed overall processing states of the native glycans highly similar to that of the recombinant glycoprotein glycans. The native conformation of the ribonucleoproteins (RNPs) and their higher-order assemblies were revealed. Overall, these characterizations revealed the architecture of the SARS-CoV-2 virus in exceptional detail and shed light on how the virus packs its ∼30-kb-long single-segmented RNA in the ∼80-nm-diameter lumen.
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“Therefore, the S protein is considered the main antigen for vaccine design.228–230”
From Advances in COVID-19 mRNA vaccine development (2022) · cites this paper as [228]
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“The trimeric S protein on the surface of SARS-CoV-2 plays a key role in mediating host cell invasion.”
From Advances in COVID-19 mRNA vaccine development (2022) · cites this paper as [228]
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AlphaFold2 and CryoEM: Revisiting CryoEM modeling in near-atomic resolution density maps
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Structural review of SARS-CoV-2 antiviral targets
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“org 6 abundant than the spike protein but also because the spike protein has structural changes between prefusion and postfusion (58).”
BackgroundSelf-citationMolecular dynamics studies reveal structural and functional features of the SARS‐CoV‐2 spike protein
Pipitò, L., Rujan, R., Reynolds, C. A., & Deganutti, G. (2022) · BioEssays · doi:10.1002/bies.202200060 · Cited by 19
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“Tilting and twisting of spikes on the surface of virions were previously reported for cor-onaviruses SARS-CoV-2 18,19,24 and PEDV 31 , as well as Env on HIV-1 virions and the puri fi ed ectodomain of In fl uenza hemagglutinin (HA) 18,65,66 .”
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Chakravarty, S. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00637 · Cited by 23
SARS-CoV-2 Unrevealed: Ultrastructural and Nanomechanical Analysis
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Three-Dimensional Reconstruction-Characterization of Polymeric Membranes: A Review
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Rigid monoclonal antibodies improve detection of SARS-CoV-2 nucleocapsid protein
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“In the presence of RNA, NP and CTD form a single bipartite RNA interaction site, which constitutes the basic building block of the nucleocapsid of SARS-CoV-2.(14,15) Abundance, stability,(12) and location at the surface of higher-order ribonucleoprotein assembly on RNA(15,16) make NP a viable antigen for the selection…”
BackgroundInfluentialModelling the adsorption of proteins to nanoparticles at the solid-liquid interface
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Preparation for the challenge of heavily mutated Omicron variant
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“The betacoronavirus SARS-CoV-2 virions (60–140 nm in diameter) are composed of a single-stranded positive-sense RNA molecule packed in a coating protein and enveloped into lipids (Figure 1A) [3].”
BackgroundIntramuscular mRNA BNT162b2 vaccine against SARS-CoV-2 induces neutralizing salivary IgA
Stolovich-Rain, M., Kumari, S., Friedman, A., Kirillov, S., Socol, Y., Billan, M., Pal, R. R., Das, K., Golding, P., Oiknine‐Djian, E., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2022.933347 · Cited by 23
“, majority of trimeric spike vertices are 20–25 nm apart) (63, 64), circulatory IgGs and IgAs, being mostly monomeric, might bind to only a single glycoprotein spike, restricted by their Fab arm spread of (10–14 nm).”
BackgroundRecent advances towards natural plants as potential inhibitors of SARS-Cov-2 targets
He, Z., Yuan, J., Zhang, Y., Li, R., Mo, M., Wang, Y., & Ti, H. (2023) · Pharmaceutical Biology · doi:10.1080/13880209.2023.2241518 · Cited by 23
“SARS-CoV-2 is a positive-strand single-stranded RNA coronavirus with a 30 kb-long sequence (Yao et al. 2020).”
BackgroundOptical Tracking of the Interfacial Dynamics of Single SARS-CoV‑2 Pseudoviruses
Liu, Y., Lv, Z.-T., Yang, S., & Liu, X. (2021) · Environmental Science & Technology · doi:10.1021/acs.est.0c06962 · Cited by 22
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Glycosylation and Serological Reactivity of an Expression-enhanced SARS-CoV-2 Viral Spike Mimetic
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“51,52,58 Also, we confirm earlier observations 18 that both forms of the recombinant protein have indistinguishable binding properties to the receptor, ACE2, indicating the functional form of protein is intact.”
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Recycling of aged RO membranes as NF/UF membranes: Biosafety evaluation and aging process
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Nanomaterial-Based Biosensors for SARS-CoV-2 and Future Epidemics
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SARS-CoV-2 spike conformation determines plasma neutralizing activityPreprint
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“The absence of prefusion-stabilizing S mutations in the latter vaccine might explain this outcome due to the metastable nature of the S trimer which is prone to shedding the S1 subunit and refolding to form postfusion trimers (10, 35, 43, 45, 51).”
Proteomics in the COVID‐19 Battlefield: First Semester Check‐Up
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Fighting viruses with computers, right now
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Self-citationVirus‐Mimic mRNA Vaccine for Cancer Treatment
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“S is a 180 kDa glycoprotein anchored in the viral membrane and protruding as homotrimers from the viral surface (the ‘‘corona”) [3].”
Wu, J., Yang, Y. X., Zhang, D., Liu, B., Zheng, Q., Xie, X., Liu, S.-Q., Ge, S., Hou, Z., & Xia, N. (2021) · IEEE Transactions on Neural Networks and Learning Systems · doi:10.1109/tnnls.2021.3131325 · Cited by 21
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“SARS-CoV-2, a new type of β-coronavirus [2], is a sphere-like particle with an envelope [3], which contains four major structural proteins: nucleocapsid (N)-, spike (S)-, envelope-, and membrane-protein [4].”
BackgroundEvolution of Virology: Science History through Milestones and Technological Advancements
Zuo, K., Gao, W., Wu, Z., Zhang, L., Wang, J., Yuan, X., Li, C., Xiang, Q., Lu, L., & Liu, H. (2024) · Viruses · doi:10.3390/v16030374 · Cited by 20
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“Stable interactions between RNPs and M-proteins are involved in strengthening the coronavirus assemblage and may protect the virus against environmental and physical challenges [11, 12].”
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Gender and genetic factors impacting COVID-19 severity
Ranjan, J., Ravindra, A., & Mishra, B. (2021) · Journal of Family Medicine and Primary Care · doi:10.4103/jfmpc.jfmpc_769_21 · Cited by 20
“Spike proteins are projected from the envelope and are mainly responsible for the entry of virus into the host cells.[12] The entry of virus to host cell is mediated by the binding of the receptor‐binding domain (RBD) of the spike protein of virus to the peptidase domain of the angiotensin‐converting enzyme‐2 (ACE‐2)…”
BackgroundPraissman, J. L., & Wells, L. (2021) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2021.100103 · Cited by 19
Cyclosporin A: A Repurposable Drug in the Treatment of COVID-19?
Devaux, C. A., Melenotte, C., Piercecchi‐Marti, M., Delteil, C., & Raoult, D. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.663708 · Cited by 19
“The genomic length of SARS-CoV2 is about 30 kb and encodes as many as 14 open reading frames (ORFs) leading to the synthesis of 29 proteins (7, 8).”
BackgroundContributions of vibrational spectroscopy to virology: A review
Chaudhary, I. I., Jackson, N., Denning, D., O'Neill, L. A. J., & Byrne, H. J. (2022) · Clinical Spectroscopy · doi:10.1016/j.clispe.2022.100022 · Cited by 21
de Lacam, E. G. C., Blazhynska, M., Chen, H., Gumbart, J. C., & Chipot, C. J. (2022) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.2c00604 · Cited by 19
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Near-Native Visualization of SARS-CoV-2 Induced Membrane Remodeling and Virion Morphogenesis
Bergner, T., Zech, F., Hirschenberger, M., Stenger, S., Sparrer, K. M. J., Kirchhoff, F., & Read, C. (2022) · Viruses · doi:10.3390/v14122786 · Cited by 19
“The spherical or ellipsoidal SARS-CoV-2 virions are composed of a lipid membrane envelope and have a mean diameter between ~85 to 110 nm at their long axis [2,3].”
BackgroundPhase Separation: The Robust Modulator of Innate Antiviral Signaling and SARS-CoV-2 Infection
Zheng, Y., & Gao, C. (2023) · Pathogens · doi:10.3390/pathogens12020243 · Cited by 19
“It has been indicated that unmodified N protein, when combined in vitro with short fragments of the viral genome, forms partially ordered gel-like condensates and discrete 15 nm particles similar to the vRNP structures observed within virions [70,84,89].”
BackgroundMethodWu, J., Wang, L., Hua, Y., Li, M., Zhou, L., Bates, D. W., & Yang, J. (2023) · Journal of Medical Internet Research · doi:10.2196/45419 · Cited by 20
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“This protein is anchored on the virus surface membrane as a homotrimer prefusion structure and each of the protomers consists of two subunits, S1 and S2 [5, 6].”
BackgroundPulsed-beam transmission electron microscopy and radiation damage
Flannigan, D. J., & VandenBussche, E. (2023) · Micron · doi:10.1016/j.micron.2023.103501 · Cited by 19
Huang, J., Wang, C., Wang, P., Mo, W., Zhou, M., Le, W., Qi, D., Wei, L. C., Fan, Q., Yue, Y., et al. (2023) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.3c08819 · Cited by 19
Barth, R. F., Buja, L. M., Barth, A. L., Carpenter, D. E., & Parwani, A. V. (2021) · Archives of Pathology & Laboratory Medicine · doi:10.5858/arpa.2020-0820-sa · Cited by 23
“SARS-CoV-2 is the seventh member of the family of coronaviruses that can infect humans.(6,52,53) Coronaviruses are RNA viruses with a single-stranded, 5capped, positive strand RNA molecule ranging from 26 to 32 kb, including at least 6 open reading frames (ORF).”
BackgroundProbing the formation, structure and free energy relationships of M protein dimers of SARS-CoV-2
Cao, Y.-P., Yang, R.-R., Wang, W., Jiang, S., Yang, C., Liu, N.-B., Dai, H.-J., Lee, I., Meng, X.-F., & Yuan, Z. (2022) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.01.007 · Cited by 16
“The structure of the M protein is still unknown, mostly because the virus TMD complicates the identification of the M protein by cryo-EM [6].”
In Vivo Engineered CAR-T Cell Therapy: Lessons Built from COVID-19 mRNA Vaccines
Meng, S., Hara, T., Miura, Y., Arao, Y., Saito, Y., Inoue, K., Hirotsu, T., Vecchione, A. M., Satoh, T., & Ishii, H. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26073119 · Cited by 23
“In the RBD-up conformation, the RBD is exposed and capable of binding to the ACE2 receptor on host cells, playing a critical role in viral entry [34].”
Zhao, M., Su, P.-Y., Castro, D. A., Tripler, T. N., Hu, Y., Cook, M., Ko, A. I., Farhadian, S., Israelow, B., Cruz, C. S. D., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009683 · Cited by 17
Wu, J., Nie, J., Zhang, L., Song, H., An, Y., Liang, Z., Yang, J., Ding, R., Liu, S., Li, Q., et al. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00874-7 · Cited by 18
“The S protein, located on the surface of viral particles, is the main antigenic target of protective immune responses.(3,4) Almost all SARS-CoV-2 vaccines in the various stages of development have been based on the S protein, particularly on that of the original strain.”
BackgroundHow promising are HIV-1-based virus-like particles for medical applications
Martins, S. A., Santos, J. F., Silva, R. D. M., Rosa, C., Verde, S. C., Correia, J. D. G., & Melo, R. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.997875 · Cited by 18
“HIV-1 Gag VLPs display a similar size to WT SARS-CoV-2 viral particles and can therefore be used as platforms for the display of its epitopes (Yao et al., 2020; Lavado-Garcıá et al., 2021).”
MethodChen, W., Shao, Y., Peng, X., Liang, B., Xu, J., & Xing, D. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.1035969 · Cited by 18
“Accessory proteins are not necessary for virus replication but can help the virus fight host viral defense mechanisms (Kim et al., 2020; Yao et al., 2020).”
BackgroundSelf-citationMo, W., Wen, J., Huang, J., Yue, Y., Zhou, M., Ni, S., Le, W., Wei, L. C., Qi, D., Wang, S., et al. (2023) · Journal of Applied Spectroscopy · doi:10.1007/s10812-023-01487-w · Cited by 17
Ye, C., Park, J., Chiem, K., Dravid, P., Allué‐Guardia, A., Garcia‐Vilanova, A., Tamayo, P. P., Shivanna, V., Kapoor, A., Walter, M. R., et al. (2023) · Microbiology Spectrum · doi:10.1128/spectrum.00653-23 · Cited by 18
“frame (ORF) frameshifted polyprotein (ORF1a/ORF1ab) and four structural proteins, namely, the spike (S), envelope (E), membrane (M), and nucleocapsid (N) proteins (3).”
BackgroundCryo-electron tomography of viral infection — from applications to biosafety
Zimmermann, L., & Chlanda, P. (2023) · Current Opinion in Virology · doi:10.1016/j.coviro.2023.101338 · Cited by 23
Alpuche‐Lazcano, S. P., Stuible, M., Akache, B., Tran, A., Kelly, J. F., Hrapovic, S., Robotham, A. C., Haqqani, A. S., Star, A. T., Renner, T. M., et al. (2023) · Communications Medicine · doi:10.1038/s43856-023-00340-7 · Cited by 18
“2e) than SARS-CoV-2 virions produced in Vero E6 cells 36,37 .”
DiIorio, M. C., & Kulczyk, A. (2023) · Micromachines · doi:10.3390/mi14091674 · Cited by 17
Wang, Y., Zhang, Z., Yang, M., Xiong, X., Yan, Q., Cao, L., Wei, P., Zhang, Y., Zhang, L., Lv, K., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2023.113653 · Cited by 16
Self-citationVirion morphology and on-virus spike protein structures of diverse SARS-CoV-2 variants
Ke, Z., Peacock, T. P., Brown, J. C., Sheppard, C., Croll, T. I., Kotecha, A., Goldhill, D. H., Barclay, W., & Briggs, J. A. G. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00303-1 · Cited by 16
“These earlier findings indicate that the virions are approximately spherical with a diameter of 80-90 nm and 25-48 S per virion on the B.1 strain 8,40–42 .”
InfluentialDickey, T. H., Ma, R., Orr-Gonzalez, S., Ouahes, T., Patel, P. Y., McAleese, H., Butler, B., Eudy, E., Eaton, B., Murphy, M. J., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112266 · Cited by 19
SARS-CoV-2 Assembly and Egress Pathway Revealed by Correlative Multi-Modal Multi-Scale Cryo-ImagingPreprint
Mendonça, L., Howe, A., Gilchrist, J. B., Sun, D., Knight, M. L., Zanetti-Domingues, L. C., Bateman, B. C., Krebs, A.-S., Chen, L., Radecke, J., et al. (2020) · SSRN Electronic Journal · doi:10.2139/ssrn.3733984 · Cited by 18
Lin, H., Chen, C.-C., Chiao, D.-J., Chang, T.-Y., Chen, X.-A., Young, J., & Kuo, S.-C. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.11.020 · Cited by 17
“The S2 domain is responsible for viral membrane fusion [4,5].”
COVID-19–Related Chronic Bilateral Dacryoadenitis
Kase, S., & Ishida, S. (2022) · JAMA Ophthalmology · doi:10.1001/jamaophthalmol.2021.6364 · Cited by 17
Moreno, C. R. D. C., Conway, S. G., Assis, M., Genta, P. R., Pachito, D. V., Júnior, A. R. T., Sguillar, D. A., Moreira, G. A., Drager, L. F., & Bacelar, A. (2022) · Sleep Science · doi:10.5935/1984-0063.20220027 · Cited by 18
“2022;15(1):1-7 4 Help-seeking for sleep and mental disturbances on COVID-19”
BackgroundInfluentialA New Neutralization Epitope in the Spike Protein of Porcine Epidemic Diarrhea Virus
Liu, J., Shi, H., Chen, J., Zhang, X., Shi, D., Ji, Z., Jing, Z., & Li, F. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23179674 · Cited by 17
“These results suggest that the neutralization ability of mAb 5F7 is weaker than that of mAb 1B9, and the manner of neutralization of mAb 5F7 may be via the agglutination PEDV or via limiting the rotational freedom of the spikes, which may facilitate the exploring ability of the virus and improve its ability to engage…”
BackgroundSelf-citationYang, Z., Liu, J., Zhu, X., Yang, F., Zhang, Q., & Shah, H. A. (2022) · Frontiers of Computer Science · doi:10.1007/s11704-022-2163-9 · Cited by 17
Kordyukova, L. V., Moiseenko, A. V., Serebryakova, M. V., Shuklina, M. A., Sergeeva, M. V., Lioznov, D. A., & Shanko, A. V. (2023) · Viruses · doi:10.3390/v15020480 · Cited by 17
“Negative staining allowed us to unambiguously distinguish single spikes of different morphologies on the surface of virions that were earlier characterized by cryo-EM/ET and classified as flail-like spikes (wider ones, supposedly representing the pre-fusion conformation of the S-trimer) or needle-like spikes (narrower…”
BackgroundMethodInfluentialSARS-CoV-2 Spike-Mediated Entry and Its Regulation by Host Innate Immunity
Yu, S., Hu, H., Ai, Q., Bai, R., Ma, K., Zhou, M., & Wang, S. (2023) · Viruses · doi:10.3390/v15030639 · Cited by 20
Disulfide stabilization reveals conserved dynamic features between SARS-CoV-1 and SARS-CoV-2 spikes
Zhang, X., Li, Z., Zhang, Y., Liu, Y., Wang, J., Liu, B., Chen, Q., Wang, Q., Fu, L., Wang, P., et al. (2023) · Life Science Alliance · doi:10.26508/lsa.202201796 · Cited by 16
Advances in the Search for SARS-CoV-2 Mpro and PLpro Inhibitors
Diogo, M. A., Cabral, A. G. T., & de Oliveira, R. B. (2024) · Pathogens · doi:10.3390/pathogens13100825 · Cited by 19
“Notably, the virus features a large homotrimeric glycoprotein (~600 kDa) protruding from its surface, which plays a crucial role in mediating interactions with host cells during the infection process, similar to other viruses within the same genus (Figure 1) [6,7].”
BackgroundInterfering with Host Proteases in SARS-CoV-2 Entry as a Promising Therapeutic Strategy
Müller, P., Maus, H., Hammerschmidt, S. J., Knaff, P. M., Mailänder, V., Schirmeister, T., & Kersten, C. (2021) · Current Medicinal Chemistry · doi:10.2174/0929867328666210526111318 · Cited by 17
Implications of Glycosaminoglycans on Viral Zoonotic Diseases
Bauer, S., Zhang, F., & Linhardt, R. J. (2021) · Diseases · doi:10.3390/diseases9040085 · Cited by 16
“Coronavirus structure under microscope adapted from [52].”
Yao, Z., Zhao, T., Su, W., You, S., & Wang, C. (2022) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2022.129669 · Cited by 16
“The spike(s) protein, one of the structural proteins on SARS-CoV-2, binds to the host cell surface receptor angiotensin-converting enzyme 2 (ACE2) via the receptor binding domain (RBD) (Yao et al., 2020).”
Kayabölen, A., Akcan, U., Özturan, D., Polat, H. Ü., Şahin, G. N., Degirmenci, N. P., Bayraktar, C., Söyler, G., Sarayloo, E., Nurtop, E., et al. (2022) · Advanced Science · doi:10.1002/advs.202201294 · Cited by 14
“Given that an average of 20-40 Spike trimers are found on a SARS-CoV-2 virion (62, 63), most of these trimers should be blocked to neutralize the virion (64).”
BackgroundLuo, Z., Ni, K., Zhou, Y., Chang, G., Yu, J., Zhang, C., Yin, W., Chen, D., Li, S., Kuang, S., et al. (2022) · Food Control · doi:10.1016/j.foodcont.2022.109340 · Cited by 16
Self-citationMore or less deadly? A mathematical model that predicts SARS-CoV-2 evolutionary direction
Xu, Z., Wei, D., Zeng, Q.-C., Zhang, H.-M., Sun, Y.-H., & Demongeot, J. (2023) · Comput. Biol. Medicine · doi:10.1016/j.compbiomed.2022.106510 · Cited by 16
Buffington, J., Duan, Z.-J., Kwon, H., Hong, J., Li, D., Feng, M.-Q., Xie, H., & Ho, M. (2023) · The FASEB Journal · doi:10.1096/fj.202202099rr · Cited by 12
Cryo-electron microscopy in the fight against COVID-19—mechanism of virus entry
Bodakuntla, S., Kuhn, C. C., Biertümpfel, C., & Mizuno, N. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1252529 · Cited by 17
Yang, J., Lin, S., Chen, Z., Yang, F., Guo, L., Wang, L., Duan, Y., Zhang, X., Dai, Y., Yin, K., et al. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1011804 · Cited by 16
Role of short chain fatty acids on astrocytes and microglia in Alzheimer's disease brain
Wtpsk, S., Burton, M., Fernando, W. M. K. T., Jayasena, V., Brennan, C. S., & Fernando, W. M. A. D. B. (2024) · International Journal of Food Science & Technology · doi:10.1111/ijfs.17380 · Cited by 18
Executable network of SARS-CoV-2-host interaction predicts drug combination treatments
Howell, R. S. M., Clarke, M. A., Reuschl, A., Chen, T., Abbott-Imboden, S., Singer, M., Lowe, D. M., Bennett, C. L., Chain, B., Jolly, C. L., et al. (2022) · npj Digital Medicine · doi:10.1038/s41746-022-00561-5 · Cited by 17
Fedorov, V. A., Kholina, E. G., Khruschev, S., Kovalenko, I. B., Rubin, A., & Strakhovskaya, M. G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23137304 · Cited by 16
“The N protein binds to viral RNA to form an RNP assembly [5] and determines its packaging in the ~80 nm-diameter lumen [6].”
BackgroundAshur, I., Alter, J., Werbner, M., Ogungbile, A., Dessau, M. A., Gal-Tanamy, M., & Vernick, S. (2021) · Talanta · doi:10.1016/j.talanta.2021.123147 · Cited by 16
“While binding of 3⸱10 10 M S1-RBD was shown to increase the average Rct by 33%(±7), an increase of Rct = 11%(±5) resulted from the binding of ~104 virus particles/mL that reportedly express much lower antigen concentrations [50,51].”
BackgroundThe atomic portrait of SARS‐CoV‐2 as captured by cryo‐electron microscopy
Fertig, T. E., Chiţoiu, L., Terinte‐Balcan, G., Peteu, V. E., Marta, D. S., & Gherghiceanu, M. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.17103 · Cited by 14
Ozawa, T., Tani, H., Anraku, Y., Kita, S., Igarashi, E., Saga, Y., Inasaki, N., Kawasuji, H., Yamada, H., Sasaki, S., et al. (2022) · mAbs · doi:10.1080/19420862.2022.2072455 · Cited by 18
“SARS-CoV-2 expresses homotrimeric spike proteins on their surface.(4,5) The spike monomer comprises two domains (S1 and S2 domains), of which the S1 domain comprises two sub-domains (a receptor-binding domain [RBD] and N-terminal domain [NTD]).”
BackgroundEvaluation of inactivation of bovine coronavirus by low-level radiofrequency irradiation
Cantu, J. C., Butterworth, J. W., Mylacraine, K. S., Ibey, B. L., Gamboa, B. M., Johnson, L. R., Thomas, R. J., Payne, J. A., Roach, W. P., & Echchgadda, I. (2023) · Scientific Reports · doi:10.1038/s41598-023-36887-7 · Cited by 15
Swain, J., Mérida, P., Rubio, K., Bracquemond, D., Neyret, A., Aguilar-Ordóñez, I., Günther, S., Barreto, G., & Muriaux, D. M. (2023) · iScience · doi:10.1016/j.isci.2023.107384 · Cited by 20
Cryo-electron tomography to study viral infection
Graham, M., & Zhang, P. (2023) · Biochemical Society Transactions · doi:10.1042/bst20230103 · Cited by 16
Metadata
- Authors
- Yao, H., Song, Y., Chen, Y., Wu, N., Xu, J., Sun, C., Zhang, J., Weng, T., Zhang, Z., Wu, Z., Cheng, L., Shi, D., Lu, X., Lei, J., Crispin, M., Shi, Y., Li, L., & Li, S.
- Affiliations
- First Affiliated Hospital Zhejiang University (CN)
- Tsinghua University (CN)
- Center for Life Sciences (CN)
- University of Southampton (GB)
- Westlake University (CN)
- Corresponding author
- Li, Lanjuan
- Li, Sai
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2020-10
- Volume
- 183
- Issue
- 3
- Pages
- 730-738.e13
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC7474903
- OpenAlex
- W3083130172
- Cited by
- 1,060
- References
- 82
- Citations by year
- 2026: 78 · 2025: 98 · 2024: 157 · 2023: 201 · 2022: 236 · 2021: 252 · 2020: 38
- FWCI
- 23.88
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- SSRN Electronic Journal (acceptedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- ePrints Soton (University of Southampton) (acceptedVersion)
- Funders
- Zhejiang University
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- SARS-CoV-2, spike protein, N-glycans, ribonucleoprotein, viral RNA packaging, viral assembly
- MeSH terms
- Betacoronavirus, SARS-CoV-2, Animals, Chlorocebus aethiops, Humans, Models, Molecular, Protein Conformation, Mass Spectrometry, Vero Cells, Viral Proteins, Virus Cultivation, Virus Assembly, Cryoelectron Microscopy
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