The N501Y spike substitution enhances SARS-CoV-2 transmission

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

Receptor Recognition by the Novel Coronavirus from Wuhan: an Analysis Based on Decade-Long Structural Studies of SARS Coronavirus

Wan, Y., Shang, J., Graham, R., Baric, R. S., & Li, F. (2020) · Journal of Virology · doi:10.1128/jvi.00127-20 · Cited by 4,341

The New Statistics: Why and How

Cumming, G. (2014) · Psychological Science · doi:10.1177/0956797613504966 · Cited by 3,200 · cited 1×

Structural and functional properties of SARS-CoV-2 spike protein: potential antivirus drug development for COVID-19

Huang, Y., Yang, C., Xu, X.-F., Xü, W., & Liu, S. (2020) · Acta Pharmacologica Sinica · doi:10.1038/s41401-020-0485-4 · Cited by 2,288

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

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

Assessing transmissibility of SARS-CoV-2 lineage B.1.1.7 in England

The COVID-19 Genomics UK (COG-UK) consortium, Volz, E., Mishra, S., Chand, M., Barrett, J. C., Johnson, R., Geidelberg, L., Hinsley, W. R., Laydon, D. J., Dabrera, G., et al. (2021) · Nature · doi:10.1038/s41586-021-03470-x · Cited by 1,611

Spike mutation D614G alters SARS-CoV-2 fitness

Plante, J. A., Liu, Y., Liu, J., Xia, H., Johnson, B. A., Lokugamage, K. G., Zhang, X., Muruato, A. E., Zou, J., Fontes-Garfias, C. R., et al. (2021) · Nature · doi:10.1038/s41586-020-2895-3 · Cited by 1,558

Simulation of the Clinical and Pathological Manifestations of Coronavirus Disease 2019 (COVID-19) in a Golden Syrian Hamster Model: Implications for Disease Pathogenesis and Transmissibility

Chan, J. F., Zhang, J., Yuan, S., Poon, V. K., Chan, C. C., Lee, A. C.-Y., Chan, W.-M., Fan, Z., Tsoi, H.-W., Wen, L., et al. (2020) · Clinical Infectious Diseases · doi:10.1093/cid/ciaa325 · Cited by 1,048

SARS-CoV-2 D614G variant exhibits efficient replication ex vivo and transmission in vivo

Hou, Y. J., Chiba, S., Halfmann, P., Ehre, C., Kuroda, M., Dinnon, K. H., Leist, S. R., Schäfer, A., Nakajima, N., Takahashi, K., et al. (2020) · Science · doi:10.1126/science.abe8499 · Cited by 900

Resistance of SARS-CoV-2 variants to neutralization by monoclonal and serum-derived polyclonal antibodies

Chen, R. E., Zhang, X., Case, J. B., Winkler, E. S., Liu, Y., VanBlargan, L. A., Liu, J., Errico, J. M., Xie, X., Suryadevara, N., et al. (2021) · Nature Medicine · doi:10.1038/s41591-021-01294-w · Cited by 881

Nanomaterial‐Based Optical Biosensors for SARS‐CoV‐2 Detection: A Retrospective of the Pandemic

Martin, F., Harroun, S. G., & Meunier, M. (2025) · Advanced Sensor Research · doi:10.1002/adsr.202400188 · Cited by 3

A Comparative Study between Spanish and British SARS-CoV-2 Variants

Ruiz, J. A. J., Ramírez, C. L., & López-Campos, J. L. (2021) · Current Issues in Molecular Biology · doi:10.3390/cimb43030140 · Cited by 3

Introducción a la topología

Roig, J. M., & Domínguez, E. O. (1993) · Dialnet (Universidad de la Rioja) · Cited by 3

Variations in spike gene of SARS-CoV-2 isolated in Vietnam

Thai, Q. K., Huynh, P., & Le, D. D. (2022) · International Journal of Biosciences (IJB) · doi:10.12692/ijb/21.5.83-92 · Cited by 3

SARS-CoV-2 Variants of Concern Have Acquired Mutations Associated With an Increased Spike CleavagePreprint

Escalera, A., Gonzalez-Reiche, A. S., Aslam, S., Mena, I., Pearl, R. L., Laporte, M., Fossati, A., Rathnasinghe, R., Alshammary, H., van de Guchte, A., et al. (2021) · SSRN Electronic Journal · doi:10.2139/ssrn.3915655 · Cited by 3

Improved binding affinity of the Omicron’s spike protein with hACE2 receptor is the key factor behind its increased virulencePreprint

Kumar, R., Murugan, N. A., & Srivastava, V. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.28.474338 · Cited by 3

Reduced infectivity but increased immune escape of the new SARS-CoV-2 variant of concern OmicronPreprint

Hu, J., Peng, P., Wu, K., Long, Q., Chen, J., Wang, K., Tang, N., & Huang, A. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.24.474110 · Cited by 3

Characterization of various remdesivir-resistant mutations of SARS-CoV-2 by mathematical modeling and molecular dynamics simulationPreprint

Torii, S., Kim, K. S., Koseki, J., Suzuki, R., Iwanami, S., Fujita, Y., Jeong, Y. D., Matsuura, Y., Shimamura, T., Iwami, S., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.02.22.481436 · Cited by 3

Building Blocks of Understanding: Constructing a Reverse Genetics Platform for studying determinants of SARS-CoV-2 replicationPreprint

Olguin-Nava, M., Bohn, P. S., Hennig, T., Börtlein, C., Gribling-Burrer, A.-S., Schmidt, N., Caliskan, N., Dölken, L., Munschauer, M., & Smyth, R. P. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.02.05.578560 · Cited by 3

Rapid worldwide spread of 17MPLF spike insertion mutants (JN.1-JN.1.25, KP.1, KP.2, KQ.1, KR.1, XDD, XDP, XDK, XDQ subvariants) of omicron coronaviruses and spike gene 5’-end sequencing problemPreprint

Chakraborty, A. K. (2024) · Research Square · doi:10.21203/rs.3.rs-4741070/v1 · Cited by 3

Replication of SARS-CoV-2 Omicron lineages is defined by TMPRSS2 use in environments where ACE2 is complexed with solute carriers SLC6A19 and SLC6A20Preprint

Aggarwal, A., Ognenovska, S., Ison, T., Fichter, C., Milogiannakis, V., Afzal, M., Stella, A. O., Waters, S. A., Esneau, C., Bartlett, N. W., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.07.663433 · Cited by 3

Meeting report: 38th international conference on antiviral research in Las Vegas, United States of America, March 17–21, 2025

Jordan, R., Archin, N. M., Cagno, V., Feng, J. Y., Guo, H., Herrero, L. J., Janeba, Z., Meanwell, N. A., Moffat, J. F., Neyts, J. H., et al. (2025) · Antiviral Research · doi:10.1016/j.antiviral.2025.106222 · Cited by 2

Evolutionary Insight into Fatal Human Coronaviruses (hCoVs) with a Focus on Circulating SARS-CoV-2 Variants Under Monitoring (VUMs)

Izhari, M. A., Alghamdi, F., Alodeani, E. A., Salem, A., Almontasheri, A. H. A., Dardari, D. M. M., Hadadi, M. A. A., Gosady, A. R. A., Alghamdi, W. A., Alzahrani, B. A., et al. (2025) · Biomedicines · doi:10.3390/biomedicines13102450 · Cited by 2

Single molecule force spectroscopy for evaluating inhibitors of SARS-CoV-2 variants of concern

Zhu, R., Oh, Y. J., & Hinterdorfer, P. (2026) · European Biophysics Journal · doi:10.1007/s00249-026-01818-7 · Cited by 2

Implemented occupational health surveillance limits the spread of SARS-CoV-2 Omicron at the workplace

Gesto, J. S. M., Cabanelas, A., Farjun, B., dos Santos, M. C., Fidalgo-Neto, A. A., Kuriyama, S. N., & Souza, T. M. L. (2022) · Frontiers in Medicine · doi:10.3389/fmed.2022.910176 · Cited by 2

SARS-CoV-2 Variants: Impact of Spike Mutations on Vaccine and Therapeutic Strategies

Raman, R., Patel, K. J., & Ranjan, K. (2022) · Springer eBooks · doi:10.1007/978-3-031-08045-6_7 · Cited by 4

The SARS-CoV-2 Delta (B.1.617.2) variant with spike N501Y mutation in the shadow of Omicron emergence

Salimović-Bešić, I., Dedeić-Ljubović, A., Zahirović, E., Hasanović, M., Šehić, M., Vukovikj, M., Boshevska, G., Vegar-Zubović, S., Mehmedika-Suljić, E., & Izetbegović, S. (2022) · Heliyon · doi:10.1016/j.heliyon.2022.e12650 · Cited by 2

Revealing the genotypic variants and proteomic mutations in Turkish SARS-CoV-2 driving evolution and virulence

Prathiviraj, R., Prinsha, K., Hassan, S., Kumar, S., Kiran, G. S., & Selvin, J. (2023) · Medicine in Omics · doi:10.1016/j.meomic.2023.100024 · Cited by 2

The Intra-Host Evolution of SARS-CoV-2 After Neutralizing Antibody Therapy, Revealed by Nanopore Sequencing

Zeng, H., Zu, W., Wang, H., Yuan, J., Cheng, L., Xu, G., Huang, Y.-G., Liu, Y., Zhang, S., & Zhang, Z. (2024) · Zoonoses · doi:10.15212/zoonoses-2023-0032 · Cited by 2

Computational analysis of mutations in SARS-CoV-2 variants spike protein and protein interactions

Moreira, E. U. M., Mariano, D., & de Melo-Minardi, R. C. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-95646-8.00043-3 · Cited by 2

Development and evaluation of vaccination strategies for addressing the continuous evolution SARS-CoV-2 based on recombinant trimeric protein technology: Potential for cross-neutralizing activity and broad coronavirus response

Du, P. F., Li, N., Tang, S., Zhou, Z., Liu, Z., Wang, T., Li, J., Zeng, S., & Chen, J. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e34492 · Cited by 2

Genetic Diversity and Spatiotemporal Distribution of SARS-CoV-2 Variants in Guinea: A Meta-Analysis of Sequence Data (2020–2023)

Gnimadi, T. A. C., Kadio, K. J. J. O., Mathew, M. J., Diallo, H., Soumah, A. K., Kéita, A. K., Hounmenou, C. G., Fernandez, N., Vidal, N., Guichet, E., et al. (2025) · Viruses · doi:10.3390/v17020204 · Cited by 2

Bridging epidemiological and malthusian fitness: Insights into SARS-CoV-2 dynamics

Fort, H. (2025) · Next research. · doi:10.1016/j.nexres.2025.100223 · Cited by 2

From Entry to Outbreak in a High School Setting: Clinical and Wastewater Surveillance of a Rare SARS-CoV-2 Variant

Sachse, S., Kraiselburd, I., Anastasiou, O. E., Elsner, C., Goretzki, S. C., Goer, S., Koldehoff, M., Thomas, A. S., Schoth, J., Voigt, S., et al. (2025) · Viruses · doi:10.3390/v17040477 · Cited by 2

The Possible Mechanistic Basis of Individual Susceptibility to Spike Protein Injury

Halma, M. T. J., Vottero, P., Thorp, J. A., Peers, T., Tuszyński, J. A., & Marik, P. E. (2025) · Advances in Virology · doi:10.1155/av/7990876 · Cited by 2

Direct measurement of SARS-CoV-2 spike RBD binding to integrin α v β 6 by single-molecule force spectroscopy

Feng, T., Tian, F., Li, J., Dong, X., Tong, B., & Zheng, P. (2025) · Chemical Communications · doi:10.1039/d5cc03034j · Cited by 2

Broad-spectrum Respiratory Virus Entry Inhibitors

Zhao, H., & Yuen, K. (2022) · Advances in experimental medicine and biology · doi:10.1007/978-981-16-8702-0_9 · Cited by 2

Omicron (B.1.1.529) BA.1 or BA.2-related effects on immune responses in previously naïve versus imprinted individuals: immune imprinting as an advantage in the humoral immune response against novel variants

Sonnleitner, S. T., Walder, S., Knabl, L., Poernbacher, R., Tschurtschenthaler, T., Hinterbichler, E., Sonnleitner, S., Muehlmann, V., Posch, W., & Walder, G. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1165769 · Cited by 2

Sensitivity to Neutralizing Antibodies and Resistance to Type I Interferons in SARS-CoV-2 R.1 Lineage Variants, Canada

Jacob, R. A., Zhang, A., Ajoge, H. O., D’Agostino, M. R., Nirmalarajah, K., Shigayeva, A., Demian, W. L., Baker, S. J. C., Derakhshani, H., Rossi, L., et al. (2023) · Emerging infectious diseases · doi:10.3201/eid2907.230198 · Cited by 2

Molecular detection of SARS-CoV-2 in domestic cats in close contact with positively-infected owners in Tehran, Iran in 2021

Saneei, D., Jamshidi, S., Langeroudi, A. G., Akbarein, H., Nadji, S. A., Shoarzargari, L., Salehi-Vaziri, ‪., Ghavihelm, A. M., Rajeoni, A. H., & Shahbazi, V. (2023) · Journal of Feline Medicine and Surgery Open Reports · doi:10.1177/20551169231172620 · Cited by 2

Overview of immunological & virological factors driving the evolution & global spread of SARS-CoV-2 variants

Ramasamy, R. (2023) · International Journal of Microbiology Research · doi:10.4103/ijmr.ijmr_2591_22 · Cited by 2

Mechanistic study of the transmission pattern of the SARS‐CoV ‐2 omicron variant

An, K., Yang, X., Luo, M., Yan, J., Xu, P., Zhang, H., Li, Y., Wu, S., Warshel, A., & Bai, C. (2024) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26663 · Cited by 2

A long-term cohort study: the immune evasion and decreasing neutralization dominated the SARS-CoV-2 breakthrough infection

Liu, Q., Jin, M., Mei, F., Fan, H., Gu, M., Zhang, Y., Qian, S., Tan, X., Ji, L., Zhang, Z., et al. (2024) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2024.1381877 · Cited by 2

Emergence of the SARS-CoV-2 Omicron Variant: Current Treatments and Vaccines for COVID-19

Vidian, V., Dikson, Litanto, V., Christy, S. N. A., & Jo, J. (2022) · Exploratory Research and Hypothesis in Medicine · doi:10.14218/erhm.2022.00084 · Cited by 2

Rapid cloning-free mutagenesis of new SARS-CoV-2 variants using a novel reverse genetics platformPreprint

Kipfer, E. T., Hauser, D., Lett, M. J., Otte, F., Urda, L., Zhang, Y., Lang, C. M. R., Chami, M., Mittelholzer, C., & Klimkait, T. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.11.540343 · Cited by 2

Making sense of chaos: uncovering the mechanisms of conformational entropyPreprint

Wankowicz, S. A. M., & Fraser, J. S. (2023) · ChemRxiv · doi:10.26434/chemrxiv-2023-9b5k7 · Cited by 3

Assessment of the Humoral Immune Response to the SARS-CoV-2 Spike Protein Receptor Binding MotifPreprint

Monteiro, M. E. D. S., Lechuga, G. C., Gomes, L. R., Carvalho, J. P. R. S., Napoleão-Pêgo, P., Morel, C. M., Provance, D. W., & De-Simone, S. G. (2023) · Preprints.org · doi:10.20944/preprints202311.0296.v1 · Cited by 2

Accelerated Adaptation of SARS-CoV-2 Variants in Mice Lacking IFITM3 Preserves Distinct Tropism and PathogenesisPreprint

Denz, P. J., Papa, J. L., McFadden, M. I., Rao, P. R., Roettger, J. E., Forero, A., & Yount, J. S. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.27.635150 · Cited by 2

Structural and Functional Impacts of SARS-CoV-2 Spike Protein Mutations: Insights from Predictive Modeling and Analytics (Preprint)Preprint

Netsey, E. K., Naandam, S. M., Asante, J., Kuukua, A. E., Yadem, A. C., Owusu, G., Shaffer, J. G., Srivastav, S. K., Doumbia, S., Owusu‐Dabo, E., et al. (2025) · doi:10.2196/preprints.73637 · Cited by 2

SARS-CoV-2 Vaccinated Breakthrough Infections With Fatal and Critical Outcomes in the Department of Antioquia, ColombiaPreprint

Cardona, A., Villegas, S., Lopez, M. S., Maya, M. A., Ortiz-Restrepo, C., Hernandez-Ortiz, O., Ciuoderis, K., Pérez, L., Betancour, I., Muñoz, C., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-963938/v1 · Cited by 2

Structural Analysis of the Spike Protein of SARS‐CoV‐2 Variants and Other Betacoronaviruses Using Molecular Dynamics

Bolivar‐Muñoz, J., Vits, S., Bermúdez-Santana, C. I., & Galindo, J. F. (2022) · ChemPhysChem · doi:10.1002/cphc.202200382 · Cited by 1

Positive‐strand RNA viruses—a Keystone Symposia report

Cable, J., Denison, M. R., Kielian, M. C., Jackson, W. T., Bartenschlager, R. F. W., Ahola, T., Mukhopadhyay, S., Fremont, D. H., Kuhn, R. J., Shannon, A., et al. (2023) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.14957 · Cited by 1

Upper Respiratory Infection Drives Clinical Signs and Inflammatory Responses Following Heterologous Challenge of SARS-CoV-2 Variants of Concern in K18 Mice

Nichols, J. H., Williams, E. P., Parvathareddy, J., Cao, X., Kong, Y., Fitzpatrick, E. A., Webby, R. J., & Jonsson, C. B. (2023) · Viruses · doi:10.3390/v15040946 · Cited by 1

Timeline of the pandemic: epidemiology, global spread, variants and waves

Liu, Y.-X., Luo, J.-Y., Liu, R., Li, Y., & Guan, W. (2024) · European Respiratory Society eBooks · doi:10.1183/2312508x.10018823 · Cited by 1

Insights into the Replication Kinetics Profiles of Malaysian SARS-CoV-2 Variant Alpha, Beta, Delta, and Omicron in Vero E6 Cell Line

Zawawi, Z. M., Kalyanasundram, J., Zain, R. M., Ripen, A. M., Basri, D., & Yap, W. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251910541 · Cited by 1

SARS-CoV-2 variant survey: Comparison of RT-PCR screening with TGS and variant distribution across two divisions of Bangladesh

Kawser, Z., Rahman, S., Westeel, E., Habib, M. T., Hossain, M., Bulbul, M. R. H., Mukta, S. A., Islam, M. Z., Hossain, M. Z., Afrad, M. H., et al. (2024) · PLoS ONE · doi:10.1371/journal.pone.0311993

AnnCovDB: a manually curated annotation database for mutations in SARS-CoV-2 spike protein

Zhang, X., Lei, Z., Zhang, J., Yang, T., Liu, X., Xue, J., & Ni, M. (2025) · Database · doi:10.1093/database/baaf002 · Cited by 1

Molecular Basis of High-Blood-Pressure-Enhanced and High-Fever-Temperature-Weakened Receptor-Binding Domain/Peptidase Domain Binding: A Molecular Dynamics Simulation Study

Xie, X., Zhang, Y., Fang, Y. G., Wu, J., & Li, Q. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26073250 · Cited by 1

Comparison of the pathogenicity of multiple SARS ‐ CoV ‐2 variants in mouse models

Lv, Q., Liu, M., Qi, F., Liu, M., Li, F., Deng, R., Liang, X., Xu, Y., Song, Z., Yan, Y., et al. (2025) · Animal Models and Experimental Medicine · doi:10.1002/ame2.70029 · Cited by 1

A programmable CRISPR-Cas12a assay for ultrasensitive detection of SARS-CoV-2 mutations

Yu, L., Tang, Z., Yi, H., Xie, H., Liao, H., Qi, L., Wang, H., Xiao, X., He, S., Li, W., et al. (2025) · Microchemical Journal · doi:10.1016/j.microc.2025.115721 · Cited by 1

SARS-CoV-2 Evolution in Humans Enables Its Transmission to Nonhuman Primates

Chiu, Y.-T., Huang, Y.-S., Pan, M. Y.-C., Chang, C.-Y., Chiu, C.-C., Nguyễn, H. V., Lee, T.-H., Sun, Y., Li, W., & Wang, L. H.-C. (2025) · Molecular Biology and Evolution · doi:10.1093/molbev/msaf281 · Cited by 1

Split prism-assisted optical aptasensor for ultrasensitive and reliable detection of SARS-CoV-2

Cho, H. M., Chegal, W., Jeoung, S. C., Choi, J. H., Bu, J., & Kim, D. H. (2025) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2025.139185 · Cited by 1

Evolutionary aspect of spike glycoprotein's conformational dynamics

Xu, W., Guo, T., & Su, H. (2026) · Physical Chemistry Chemical Physics · doi:10.1039/d5cp04391c · Cited by 1

Designing a novel vaccine against COVID-19 based on spike SARS-Cov-2 notable mutations using immunoinformatics approaches

Rahimnahal, S., Yousefizadeh, S., & Mohammadi, Y. S. (2026) · PLoS ONE · doi:10.1371/journal.pone.0334662 · Cited by 1

Structural Constraints Acting on the SARS-CoV-2 Spike Protein Reveal Limited Space for Viral Adaptation

Herzig, J. C., Magwira, M. L., & Lovell, S. C. (2026) · Genome Biology and Evolution · doi:10.1093/gbe/evag049 · Cited by 1

Коронавірусний S-антиген як маркер ефективної вакцинації

Спиридонов, В. Г., & Мельничук, М. Д. (2021) · Reports of the National Academy of Sciences of Ukraine · doi:10.15407/dopovidi2021.03.096 · Cited by 1

Advances in Modelling COVID-19 in Animals

Nickl, P., Raishbrook, M. J., Syding, L. A., & Sedláček, R. (2022) · Frontiers in Drug Discovery · doi:10.3389/fddsv.2022.899587 · Cited by 1

Longitudinal Analyses after COVID-19 Recovery or Prolonged Infection Reveal Unique Immunological Signatures after Repeated Vaccinations

Hisamatsu, D., Ikeda, A., Ito, L., Matsushita, Y., Hiki, M., Mori, H., Tabe, Y., Naito, T., & Akazawa, C. (2022) · Vaccines · doi:10.3390/vaccines10111815 · Cited by 1

Structural basis for the broad and potent cross-reactivity of an N501Y-centric antibody against sarbecoviruses

Jeong, B.-S., Jeon, J. Y., Lai, C., Yun, H.-Y., Jung, J. U., & Oh, B. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1049867 · Cited by 1

Mutation Sites and Evolutionary Analysis of SARS-CoV-2 Omicron Spike Protein

吴, 秀. (2022) · Hans Journal of Computational Biology · doi:10.12677/hjcb.2022.124008 · Cited by 1

Antigen-Heterologous Vaccination Regimen Triggers Alternate Antibody Targeting in SARS-CoV-2-DNA-Vaccinated Mice

Frische, A., Krogfelt, K. A., Fomsgaard, A., & Lassaunière, R. (2024) · Vaccines · doi:10.3390/vaccines12030218 · Cited by 1

A positive selection at binding site 501 in the B.1 lineage might have triggered the highly infectious sub-lineages of SARS-CoV-2

Tiwary, B. K. (2024) · Gene · doi:10.1016/j.gene.2024.148427 · Cited by 1

Exploring the interplay of biodiversity and mutation in cyclic competition systems

Choi, J., Park, J., & Jang, B. (2024) · Chaos Solitons & Fractals · doi:10.1016/j.chaos.2024.115627 · Cited by 1

Variation and evolution analysis of SARS-CoV-2 using self-game sequence optimization

Liu, Z., Shen, Y., Jiang, Y., Zhu, H., Hu, H., Kang, Y., Chen, M., & Li, Z. (2024) · Frontiers in Microbiology · doi:10.3389/fmicb.2024.1485748 · Cited by 1

Production of a monoclonal antibody targeting the SARS-CoV-2 Omicron spike protein and analysis of SARS-CoV-2 Omicron mutations related to monoclonal antibody resistance

Kim, J., Kim, S., Park, S., Kim, D., Kim, M., Baek, K., Kang, B. M., Shin, H.-E., Lee, M.-H., Lee, Y., et al. (2024) · Microbes and Infection · doi:10.1016/j.micinf.2024.105461 · Cited by 1

Structural and functional constraints on spike activation and host protease utilization limit cell entry of SARS-CoV-2-related bat coronaviruses

Li, Q., Cai, X., Li, X., Zhang, Y.-B., Li, R., Kang, Z., Wan, D., Wang, J., Li, L., Yang, J., et al. (2025) · Journal of Virology · doi:10.1128/jvi.01007-25 · Cited by 1

Influence of SARS-CoV-2 variants on stillbirth rate - data from the CRONOS registry

Schaumann, N., Mand, N., Groten, T., Hiller, G. G. R., Andresen, K., Büchel, J., Pastuschek, J., Pecks, U., Schäffler, H., Iannaccone, A., et al. (2025) · Placenta · doi:10.1016/j.placenta.2025.10.008 · Cited by 1

Chronic infections can generate SARS-CoV-2-like bursts of viral evolution without epistasis

Rodríguez-Horta, E., Strahan, J., Dinner, A. R., & Barton, J. P. (2026) · Virus Evolution · doi:10.1093/ve/veag008 · Cited by 1

SARS-CoV-2 Genome Analysis of Pediatric Patients in Konya Region, Turkey

Taşbent, F. E., Özdemir, M., Akcan, Ö. M., & Kurt, E. K. (2021) · Journal of Pediatric Infectious Diseases · doi:10.1055/s-0041-1736561 · Cited by 1

The genomic and clinical features of the COVID-19 Omicron variant: a narrative review

Hertanto, D. M., Sutanto, H., Lusida, M. I., Kuntaman, K., & Santoso, D. (2022) · F1000Research · doi:10.12688/f1000research.110647.1 · Cited by 2

Cell Entry and Unusual Replication of SARS-CoV-2

McCann, N. R., & Castellino, F. (2022) · Current Drug Targets · doi:10.2174/1389450124666221014102927 · Cited by 1

Employing an in-silico approach in the evaluation of Aloe vera metabolites as inhibitors of Omicron RBD and the ROS-dependent cellular signaling processes

Kepel, B. J., Kalalo, M. J., & Tallei, T. E. (2022) · Journal of Applied Pharmaceutical Science · doi:10.7324/japs.2023.130304 · Cited by 1

Deciphering the evolutionary mechanisms of SARS‐CoV‐2: Absence of ORF8 protein and its potential advantage in the emergence of viral lineages

Velázquez-Salinas, L. (2023) · Journal of Medical Virology · doi:10.1002/jmv.29002 · Cited by 1

BNT162b2-Elicited Neutralization of Delta Plus, Lambda, and Other VariantsPreprint

Liu, J., Liu, Y., Xia, H., Zou, J., Weaver, S. C., Swanson, K. A., Cai, H., Cutler, M. W., Cooper, D., Muik, A., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.09.13.460163 · Cited by 1

Identification of Genotypic Variants and its Proteomic mutations of Brazilian SARS-CoV-2 IsolatesPreprint

Prathiviraj, R., Chellapandi, P., Kiran, G. S., & Selvin, J. (2021) · doi:10.22541/au.162578181.18050136/v1

The SARS-CoV-2 infection in Thailand: analysis of spike variants complemented by protein structure insightsPreprint

Ittisoponpisan, S., Yahangkiakan, S., Sternberg, M. J. E., & David, A. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.01.474713 · Cited by 1

Broadly neutralizing and protective nanobodies against diverse sarbecovirusesPreprint

Li, M., Ren, Y., Aw, Z. Q., Chen, B., Yang, Z., Lei, Y., Cheng, L., Liang, Q., Hong, J., Yang, Y., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.04.12.488087 · Cited by 1

Investigating the mutations in the SARS-CoV-2 proteins among European countriesPreprint

Abavisani, M., Rahimian, K., Khayami, R., Kodori, M., Sisakht, M. M., Mahmanzar, M., & Meshkat, Z. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.06.23.497239 · Cited by 1

Hybrid CRSIPR/Cas Protein for One-Pot Detection of DNA and RNAPreprint

Guk, K., Yi, S., Kim, H., Bae, Y., Yong, D., Kim, S., Lee, K., Lim, E., Kang, T., & Jung, J. (2022) · SSRN Electronic Journal · doi:10.2139/ssrn.4139900 · Cited by 1

Rapid threat detection in SARS-CoV-2Preprint

Barrett, C. L., Huang, F. W. D., Li, T. J. X., Warren, A. S., & Reidys, C. M. (2022) · medRxiv · doi:10.1101/2022.08.05.22278480 · Cited by 1

SARS-CoV-2 variant transition dynamics are associated with vaccination rates, number of co-circulating variants, and natural immunityPreprint

Beesley, L. J., Moran, K. R., Wagh, K., Castro, L. A., Theiler, J. P., Yoon, H., Fischer, W., Hengartner, N., Korber, B., & Valle, S. Y. D. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.18.517139 · Cited by 1

T492I mutation alters SARS-CoV-2 properties via modulating viral non-structural proteinsPreprint

Lin, X., Sha, Z., Trimpert, J., Kunec, D., Jiang, C., Xiong, Y., Xu, B., Zhu, Z., Xue, W., & Wu, H. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.01.15.524090 · Cited by 1

Riding the Wave: Unveiling the Conformational Waves from RBD to ACE2Preprint

Maroli, N. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.12.540230 · Cited by 1

Evolution of transient RNA structure-RNA polymerase interactions in respiratory RNA virus genomesPreprint

Rigby, C., Sabsay, K. R., Bisht, K., Eggink, D., Jalal, H., & Velthuis, A. J. W. T. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.25.542331 · Cited by 1

Within-host evolution of SARS-CoV-2: how often are de novo mutations transmitted?Preprint

Korosec, C. S., Wahl, L. M., & Heffernan, J. M. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.08.552503 · Cited by 1

Human microbiota is a reservoir of SARS-CoV-2 advantageous mutationsPreprint

Cao, B., Wang, X., Yin, W., Gao, Z., & Xia, B. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.11.16.567485 · Cited by 1

The G36S, M147I, G265S, T568I, N852S new mutations in the Spike of Omicron JN.1 subvariants: New subvariants JN.1.1 to JN.1.5 nomenclature and oligonucleotides design for JN.1 subvariants detectionPreprint

Chakraborty, A. K. (2024) · Research Square · doi:10.21203/rs.3.rs-3879032/v1 · Cited by 1

Increased Pathogenicity and Transmission of SARS-CoV-2 Omicron Xbb.1.9 Sublineage, Including Hk.3 and Eg.5.1Preprint

Jin, Q., Liu, R., Wang, W., Xie, J., Wang, T., Xiang, H., Xia, X., Li, J., Wang, X., & Gao, Y. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.10.598324 · Cited by 1

Evolution of Omicron lineage towards increased fitness in the upper respiratory tract in the absence of severe lung pathologyPreprint

Wickenhagen, A., Flagg, M., Port, J. R., Yinda, C. K., Goldin, K., Gallogly, S., Schulz, J. E., Lutterman, T. R., Williamson, B. N., Kaiser, F. K., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.13.598902 · Cited by 1

INP-Guided Network Pharmacology Discloses Multi-Target Therapeutic Strategy Against Cytokine and IgE Storms in the SARS-CoV-2 NB.1.8.1 VariantPreprint

Manikyam, H. K., & Joshi, S. K. (2025) · Research Square · doi:10.21203/rs.3.rs-6819274/v1 · Cited by 1

Mechanism-based classification of SARS-CoV-2 Variants by Molecular Dynamics Resembles Phylogenetic TreePreprint

Arns, T., d’Hérouël, A. F., May, P., Tkatchenko, A., & Skupin, A. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.11.28.568639 · Cited by 1

Emerging SARS-CoV-2 variant BA.3.2 is more poorly neutralized by responses focused on other contemporary strainsPreprint

Stuart, D. I., Dijokaite-Guraliuc, A., Duyvesteyn, H. M. E., Liu, C., Lu, Z.-P., Supasa, P., Kronsteiner, B., Jeffery, K. J., Stafford, L., Klenerman, P., et al. (2026) · Research Square · doi:10.21203/rs.3.rs-9585124/v1 · Cited by 1

Alpha variant versus D614G strain in the Syrian hamster modelPreprint

Cochin, M., Lucıanı, L., Touret, F., Driouich, J., Petit, P.-R., Moureau, G., Baronti, C., Laprie, C., Thirion, L., Maes, P., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.19.440435

Drug Repurposing for COVID-19 Using Molecular Docking Tools

Öztaş, D. Y. (2021) · Chapman University Digital Commons (Chapman University) · doi:10.36837/chapman.000286

Emerging Coronavirus Mutant - The Delta Plus: A Review

Patil, R., & Choughule, P. M. (2021) · ENVIRO Dental Journal · doi:10.12944/edj.03.02.04

Most Concern Strains of Coronavirus-2 and Diagnostic Protocol in Iraqi’s Hospitals: A review

Musafer, H. K., Abdulrazaq, R. A., AL-Bayati, M. A., Kaabi, S. A. G., & Abdulateef, B. (2022) · Mağallaẗ ʻulūm al-rāfidayn · doi:10.33899/rjs.2022.172934

Model evolution in SARS-CoV-2 spike protein sequences using a generative neural networkPreprint

Kumar, A. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.04.12.487999

mRNA-1273 and Ad26.COV2.S Vaccines Protect Against the B.1.621 Variant of SARS-CoV-2Preprint

Darling, T. L., Ying, B., Whitener, B. M., VanBlargan, L. A., Bricker, T. L., Liang, C.-Y., Joshi, A., Bamunuarachchi, G., Seehra, K., Schmitz, A. J., et al. (2022) · SSRN Electronic Journal · doi:10.2139/ssrn.4001952

RT-RPA-Cas12a-Based Discrimination of SARS-CoV-2 Variants of ConcernPreprint

Tang, G., Zhang, Z., Tan, W., Long, F., Sun, J., Li, Y., Zou, S., Yang, Y., Cai, K., Li, S., et al. (2022) · medRxiv · doi:10.1101/2022.05.11.22274884

A study protocol for a double-blind randomised placebo-controlled trial evaluating the efficacy of carrageenan nasal and throat spray for COVID-19 prophylaxis – ICE COVIDPreprint

Jessop, Z. M., Gibson, J. A. G., Lim, J. P., Jovic, T. H., Combellack, E. J., Dobbs, T., Carter, K., Hiles, S., Islam, S., Healy, B., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-1180029/v1

Quantifying the transmission advantage associated with N501Y substitution of SARS-CoV-2 in the UK: an early data-driven analysis

Zhao, S., Lou, J., Cao, L., Zheng, H., Chong, K. C., Chen, Z., Chan, R. W. Y., Zee, B. C.-Y., Chan, P. K. S., & Wang, M. H. (2021) · Journal of Travel Medicine · doi:10.1093/jtm/taab011 · Cited by 77

Exploring the Interaction between E484K and N501Y Substitutions of SARS-CoV-2 in Shaping the Transmission Advantage of COVID-19 in Brazil: A Modeling Study

Zhao, S., Ran, J., & Han, L. (2021) · American Journal of Tropical Medicine and Hygiene · doi:10.4269/ajtmh.21-0412 · Cited by 7

In Silico Investigation of the New UK (B.1.1.7) and South African (501Y.V2) SARS-CoV-2 Variants with a Focus at the ACE2–Spike RBD Interface

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N501Y mutation of spike protein in SARS-CoV-2 strengthens its binding to receptor ACE2

Tian, F., Tong, B., Sun, L., Shi, S., Zheng, B., Wang, Z., Dong, X., & Zheng, P. (2021) · eLife · doi:10.7554/elife.69091 · Cited by 394

SARS-COV-2 Lineage B.1.1.7: Origin, Spread, Symptoms and Countermeasures

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