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

Severe COVID-19 is a T cell immune dysregulatory disorder triggered by SARS-CoV-2

Ameratunga, R., Woon, S.-T., Steele, R., Lehnert, K., Leung, E. Y., & Brooks, A. E. S. (2022) · Expert Review of Clinical Immunology · doi:10.1080/1744666x.2022.2074403 · Cited by 16

Rapid SARS-CoV-2 Variants Enzymatic Detection (SAVED) by CRISPR-Cas12a

Yang, J., Barua, N., Rahman, M. N., Li, C., Lo, N. W. S., Yeong, K.-Y., Tsang, T. F., Yang, X., Cheung, Y., Tsang, A. K. L., et al. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.03260-22 · Cited by 15

Exploring the pharmacological aspects of natural phytochemicals against SARS-CoV-2 Nsp14 through an in silico approach

De, A., Bhattacharya, S., Debroy, B., Bhattacharya, A., & Pal, K. (2023) · In Silico Pharmacology · doi:10.1007/s40203-023-00143-7 · Cited by 15

Exigency of Plant-Based Vaccine against COVID-19 Emergence as Pandemic Preparedness

Chattopadhyay, A., Jailani, A. A. K., & Mandal, B. (2023) · Vaccines · doi:10.3390/vaccines11081347 · Cited by 16

Evolution of transient RNA structure–RNA polymerase interactions in respiratory RNA virus genomes

Rigby, C. V., Sabsay, K. R., Bisht, K., Eggink, D., Jalal, H., & Velthuis, A. J. W. T. (2023) · Virus Evolution · doi:10.1093/ve/vead056 · Cited by 15

Antibody evasion associated with the RBD significant mutations in several emerging SARS-CoV-2 variants and its subvariants

Bhattacharya, M., Chatterjee, S., Lee, S., Dhama, K., & Chakraborty, C. (2023) · Drug Resistance Updates · doi:10.1016/j.drup.2023.101008 · Cited by 16

COVID-19-Related Age Profiles for SARS-CoV-2 Variants in England and Wales and States of the USA (2020 to 2022): Impact on All-Cause Mortality

Jones, R., & Ponomarenko, A. (2023) · Infectious Disease Reports · doi:10.3390/idr15050058 · Cited by 15

SARS-CoV-2 Omicron Subvariants Do Not Differ Much in Binding Affinity to Human ACE2: A Molecular Dynamics Study

Nguyen, H. L., Nguyen, T. Q., & Li, M. S. (2024) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.3c06270 · Cited by 17

Neutral evolution test of the spike protein of SARS-CoV-2 and its implications in the binding to ACE2

López-Cortés, G. I., Palacios-Pérez, M., Zamudio, G. S., Veledíaz, H. F., Ortega, E., & José, M. V. (2021) · Scientific Reports · doi:10.1038/s41598-021-96950-z · Cited by 15

Human models for COVID‐19 research

Woodall, M. N. J., Masonou, T., Case, K., & Smith, C. M. (2021) · The Journal of Physiology · doi:10.1113/jp281499 · Cited by 13

SARS‐CoV‐2 spike evolutionary behaviors; simulation of N501Y mutation outcomes in terms of immunogenicity and structural characteristic

Rostami, N., Choupani, E., Hernandez, Y., Arab, S. S., Jazayeri, S. M., & Gomari, M. M. (2021) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30181 · Cited by 14

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) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.08.05.455290 · Cited by 15

Structural proteins of human coronaviruses: what makes them different?

Minigulov, N., Boranbayev, K., Bekbossynova, A., Gadilgereyeva, B., & Filchakova, O. (2024) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2024.1458383 · Cited by 18

Differences in New Variant of Concern Replication at Physiological Temperatures In Vitro

Stauft, C. B., Sangare, K., & Wang, T. T. (2022) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiac264 · Cited by 14

Evolution of Sequence and Structure of SARS-CoV-2 Spike Protein: A Dynamic Perspective

Sinha, A., Sangeet, S., & Roy, S. (2023) · ACS Omega · doi:10.1021/acsomega.3c00944 · Cited by 14

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

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) · eLife · doi:10.7554/elife.89035 · Cited by 14

Natural products as a source of Coronavirus entry inhibitors

Szabó, D., Crowe, A. P., Mamotte, C. D. S., & Strappe, P. (2024) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2024.1353971 · Cited by 14

SARS-CoV-2 ORF3a drives dynamic dense body formation for optimal viral infectivity

Hartmann, S., Radochonski, L., Ye, C., Martínez‐Sobrido, L., & Chen, J. (2025) · Nature Communications · doi:10.1038/s41467-025-59475-x · Cited by 18

SARITA: a large language model for generating the S1 subunit of the SARS-CoV-2 spike protein

Rancati, S., Nicora, G., Bergomi, L., Buonocore, T. M., Czyż, D. M., Parimbelli, E., Bellazzi, R., Salemi, M., Prosperi, M., & Marini, S. (2025) · Briefings in Bioinformatics · doi:10.1093/bib/bbaf384 · Cited by 17

Screening and Whole Genome Sequencing of SARS-CoV-2 Circulating During the First Three Waves of the COVID-19 Pandemic in Libreville and the Haut-Ogooué Province in Gabon

Lekana-Douki, S. E., N’dilimabaka, N., Levasseur, A., Colson, P., Andeko, J. C., Minko, O. Z., Mve-Ella, O. B., Fournier, P., Devaux, C. A., Mvé-Ondo, B., et al. (2022) · Frontiers in Medicine · doi:10.3389/fmed.2022.877391 · Cited by 14

The spike glycoprotein of highly pathogenic human coronaviruses: structural insights for understanding infection, evolution and inhibition

Qiao, S., Zhang, S., Ge, J., & Wang, X. (2022) · FEBS Open Bio · doi:10.1002/2211-5463.13454 · Cited by 16

Temporal changes in the accessory protein mutations of SARS‐CoV‐2 variants and their predicted structural and functional effects

Cruz, C. A. K., & Medina, P. M. B. (2022) · Journal of Medical Virology · doi:10.1002/jmv.27964 · Cited by 13

Prediction of Recurrent Mutations in SARS-CoV-2 Using Artificial Neural Networks

Saldivar‐Espinoza, B., Macip, G., Garcia‐Segura, P., Mestres‐Truyol, J., Puigbò, P., Cereto‐Massagué, A., Pujadas, G., & García-Vallvé, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232314683 · Cited by 15

The End or a New Era of Development of SARS-CoV-2 Virus: Genetic Variants Responsible for Severe COVID-19 and Clinical Efficacy of the Most Commonly Used Vaccines in Clinical Practice

Miteva, D., Kitanova, M., Batselova, H., Lazova, S., Chervenkov, L., Peshevska-Sekulovska, M., Sekulovski, M., Gulinac, M., Vasilev, G., Tomov, L., et al. (2023) · Vaccines · doi:10.3390/vaccines11071181 · Cited by 16

Prediction of SARS-CoV-2 Omicron Variant Immunogenicity, Immune Escape and Pathogenicity, through the Analysis of Spike Protein-Specific Core Unique Peptides

Pierros, V., Kontopodis, E., Stravopodis, D. J., & Tsangaris, G. T. (2022) · Vaccines · doi:10.3390/vaccines10030357 · Cited by 13

Cancer vaccines: advances, hurdles, and future directions

Vlachostergios, P. J. (2025) · Exploration of Targeted Anti-tumor Therapy · doi:10.37349/etat.2025.1002350 · Cited by 13

“Mutation blacklist” and “mutation whitelist” of SARS-CoV-2

Sun, Y., Wang, M., Lin, W., Dong, W., & Xu, J. (2022) · Journal of Biosafety and Biosecurity · doi:10.1016/j.jobb.2022.06.006 · Cited by 13

Evolutionary progression of collective mutations in Omicron sub-lineages towards efficient RBD-hACE2: Allosteric communications between and within viral and human proteins

Barozi, V., Edkins, A. L., & Bishop, Ö. T. (2022) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.08.015 · Cited by 13

Blood transcriptomics analysis offers insights into variant-specific immune response to SARS-CoV-2

Hoffmann, M., Willruth, L.-L., Dietrich, A., Lee, H., Knabl, L., Trummer, N., Baumbach, J., Furth, P. A., Hennighausen, L. G., & List, M. (2024) · Scientific Reports · doi:10.1038/s41598-024-53117-w · Cited by 13

SARS-CoV-2 rapidly evolves lineage-specific phenotypic differences when passaged repeatedly in immune-naïve mice

Willett, J., Gravel, A., Dubuc, I., Gudimard, L., Andrade, A. C. D. S. P., Lacasse, É., Fortin, P. R., Liu, J., Cervantes, J. A., Gálvez, J. H., et al. (2024) · Communications Biology · doi:10.1038/s42003-024-05878-3 · Cited by 12

Evolutionary Traits and Genomic Surveillance of SARS-CoV-2 in South America

Ortíz-Pineda, P. A., & Sierra-Torres, C. H. (2022) · Global Health · doi:10.1155/2022/8551576 · Cited by 13

Factor Xa cleaves SARS-CoV-2 spike protein to block viral entry and infection

Dong, W., Wang, J., Tian, L., Zhang, J., Settles, E. W., Qin, C., Kollath, D. R., Itogawa, A. N., Celona, K. R., Yi, J., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-37336-9 · Cited by 13

The Impact of Mutation Sets in Receptor-Binding Domain of SARS-CoV-2 Variants on Stability of the RBD–ACE2 Complex

Peka, M., & Balatsky, V. (2023) · Future Virology · doi:10.2217/fvl-2022-0152 · Cited by 13

The furin cleavage site is required for pathogenesis, but not transmission, of SARS-CoV-2

Morgan, A. L., Vu, M. N., Zhou, Y., Lokugamage, K. G., Meyers, W. M., Alvarado, R. E., Ahearn, Y. P., Estes, L. K., Plante, J. A., Johnson, B. A., et al. (2025) · Journal of Virology · doi:10.1128/jvi.00467-25 · Cited by 13

Global Prevalence of Adaptive and Prolonged Infections’ Mutations in the Receptor-Binding Domain of the SARS-CoV-2 Spike Protein

Lennerstrand, J., & Palanisamy, N. (2021) · Viruses · doi:10.3390/v13101974 · Cited by 12

The Key Site Variation and Immune Challenges in SARS-CoV-2 Evolution

Liu, Y., & Ye, Q. (2023) · Vaccines · doi:10.3390/vaccines11091472 · Cited by 12

Evolutionary trajectory of diverse SARS-CoV-2 variants at the beginning of COVID-19 outbreak

Lv, J.-X., Liu, X., Pei, Y.-Y., Song, Z.-G., Chen, X., Hu, S.-J., She, J., Liu, Y., Chen, Y.-M., & Zhang, Y.-Z. (2024) · Virus Evolution · doi:10.1093/ve/veae020 · Cited by 16

Cell type-specific adaptation of the SARS-CoV-2 spike

Carrascosa-Sàez, M., Marqués, M.-C., IBV-Covid19-Pipeline, T., Geller, R., Elena, S. F., Rahmeh, A., Dufloo, J., & Sanjuán, R. (2024) · Virus Evolution · doi:10.1093/ve/veae032 · Cited by 13

Strengths and limitations of SARS-CoV-2 virus-like particle systems

Sultana, R., & Stahelin, R. V. (2024) · Virology · doi:10.1016/j.virol.2024.110285 · Cited by 14

Immunological drivers of zoonotic virus emergence, evolution, and endemicity

Purushotham, J. N., Lutz, H. L., Parker, E., & Andersen, K. G. (2025) · Immunity · doi:10.1016/j.immuni.2025.03.014 · Cited by 15

SARS-CoV-2 and vascular dysfunction: a growing role for pericytes

McQuaid, C., & Montagne, A. (2022) · Cardiovascular Research · doi:10.1093/cvr/cvac143 · Cited by 12

Genomic epidemiology and evolutionary analysis during XBB.1.16-predominant periods of SARS-CoV-2 omicron variant in Bangkok, Thailand: December 2022–August 2023

Puenpa, J., Chansaenroj, J., Suwannakarn, K., & Poovorawan, Y. (2024) · Scientific Reports · doi:10.1038/s41598-023-50856-0 · Cited by 12

Rapid SARS-CoV-2 Intra-Host and Within-Household Emergence of Novel Haplotypes

Manuto, L., Grazioli, M., Spitaleri, A., Fontana, P., Bianco, L., Bertolotti, L., Bado, M., Mazzotti, G., Bianca, F., Onelia, F., et al. (2022) · Viruses · doi:10.3390/v14020399 · Cited by 10

Early cross-coronavirus reactive signatures of protective humoral immunity against COVID-19Preprint

Kapłonek, P., Wang, C., Bartsch, Y. C., Fischinger, S., Gorman, M. J., Bowman, K. A., Kang, J., Dayal, D., Martin, P., Nowak, R. P., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.11.443609 · Cited by 12

Nucleocapsid Mutations R203K/G204R Increase the Infectivity, Fitness and Virulence of SARS-CoV-2Preprint

Wu, H., Xing, N., Meng, K., Fu, B., Xue, W., Dong, P., Tang, W., Xiao, Y., Liu, G., Luo, H., et al. (2021) · SSRN Electronic Journal · doi:10.2139/ssrn.3896432 · Cited by 12

Arylcoumarin perturbs SARS-CoV-2 pathogenesis by targeting the S-protein/ACE2 interaction

Singh, R., Kumar, A., Rane, J. S., Khan, R., Tripathi, G., Ajay, A. K., Prakash, A., & Ray, S. (2022) · Scientific Reports · doi:10.1038/s41598-022-20759-7 · Cited by 11

Photoacoustic detection of SARS-CoV-2 spike N501Y single-nucleotide polymorphism based on branched rolling circle amplification

Xiao, J., Yuan, C., Ding, M., Hu, W., Hu, Z., & Tian, B. (2022) · Talanta · doi:10.1016/j.talanta.2022.124047 · Cited by 11

Mutations of SARS-CoV-2 Structural Proteins in the Alpha, Beta, Gamma, and Delta Variants: Bioinformatics Analysis

Khetran, S. R., & Mustafa, R. (2023) · JMIR Bioinformatics and Biotechnology · doi:10.2196/43906 · Cited by 13

VP2 residue N142 of coxsackievirus A10 is critical for the interaction with KREMEN1 receptor and neutralizing antibodies and the pathogenicity in mice

Li, X., Liu, Z., Yan, X., Tian, Y., Liu, K., Zhao, Y., Shao, J., Hao, P., & Zhang, C. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1011662 · Cited by 11

CRISPR‐Cas system: A promising tool for rapid detection of SARS‐CoV‐2 variants

Li, J., Zhang, K., Lin, G., & Li, J. (2024) · Journal of Medical Virology · doi:10.1002/jmv.29356 · Cited by 11

Fighting Mutations with Mutations: Evolutionarily Adapting a DNA Aptamer for High‐Affinity Recognition of Mutated Spike Proteins of SARS‐CoV‐2

Wang, Q., Li, J., Zhang, Z., Amini, R., Derdall, A., Gu, J., Xia, J., Salena, B. J., Yamamura, D. L. R., Soleymani, L., et al. (2024) · Angewandte Chemie International Edition · doi:10.1002/anie.202415226 · Cited by 11

Comparative analysis of replication and immune evasion among SARS-CoV-2 subvariants BA.2.86, JN.1, KP.2, and KP.3

Hu, Y., Zou, J., Nguyen, M., Chang, H. C., Yeung, J., Hao, H., Shi, P., Ren, P., & Xie, X. (2025) · mBio · doi:10.1128/mbio.03503-24 · Cited by 11

Virus-specific host responses and gene signatures following infection with major SARS-CoV-2 variants of concern: role of ZBP1 in viral clearance and lung inflammation

Elsharkawy, A., Jahantigh, H. R., Guglani, A., Stone, S., Arora, K., & Kumar, M. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1557535 · Cited by 12

Binding and entering: COVID finds a new home

Vu, M. N., & Menachery, V. D. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009857 · Cited by 10

Circulation of SARS-CoV-2 Variants among Children from November 2020 to January 2022 in Trieste (Italy)

Dolci, M., Signorini, L., Cason, C., Campisciano, G., Kunderfranco, P., Pariani, E., Galli, C., Petix, V., Ferrante, P., Delbue, S., et al. (2022) · Microorganisms · doi:10.3390/microorganisms10030612 · Cited by 11

Ganoderma microsporum immunomodulatory protein acts as a multifunctional broad-spectrum antiviral against SARS-CoV-2 by interfering virus binding to the host cells and spike-mediated cell fusion

Ho, H. P. T., Vo, D. N. K., Lin, T., Hung, J.-N., Chiu, Y.-H., & Tsai, M. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113766 · Cited by 11

ACE2 receptor polymorphism in humans and animals increases the risk of the emergence of SARS-CoV-2 variants during repeated intra- and inter-species host-switching of the virus

Devaux, C. A., & Fantini, J. (2023) · Frontiers in Microbiology · doi:10.3389/fmicb.2023.1199561 · Cited by 10

Immunogenicity and safety in pigs of PHH-1V, a SARS-CoV-2 RBD fusion heterodimer vaccine candidate

Moros, A., Prenafeta, A., Barreiro, A., Perozo, E., Fernández, A., Cañete, M., González‐González, L., Garriga, C., Pradenas, E., Marfil, S., et al. (2023) · Vaccine · doi:10.1016/j.vaccine.2023.07.008 · Cited by 9

SARS-CoV-2 infection in immunosuppression evolves sub-lineages which independently accumulate neutralization escape mutations

Lustig, G., Ganga, Y., Rodel, H. E., Tegally, H., Khairallah, A., Jackson, L., Cele, S., Khan, K., Jule, Z., Reedoy, K., et al. (2023) · Virus Evolution · doi:10.1093/ve/vead075 · Cited by 12

Assessment of the binding interactions of SARS-CoV-2 spike glycoprotein variants

Raghu, D., Hamill, P., Banaji, A., McLaren, A., & Hsu, Y.-T. (2021) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2021.09.006 · Cited by 11

A low-cost TaqMan minor groove binder probe-based one-step RT-qPCR assay for rapid identification of N501Y variants of SARS-CoV-2

Chan, C. T.-M., Leung, J. S.-L., Lee, L.-K., Lo, H. W.-H., Wong, E. Y.-K., Wong, D. S.-H., Ng, T. T.-L., Lao, H.-Y., Lu, K. K., Jim, S. H.-C., et al. (2021) · Journal of Virological Methods · doi:10.1016/j.jviromet.2021.114333 · Cited by 11

An encodable multiplex microsphere-phase amplification sensing platform detects SARS-CoV-2 mutations

Zhong, Z., Wang, J., He, S., Su, X., Huang, W., Chen, M., Zhuo, Z., Zhu, X., Fang, M., Li, T., et al. (2022) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2022.114032 · Cited by 11

Human organoid systems reveal in vitro correlates of fitness for SARS-CoV-2 B.1.1.7Preprint

Lamers, M. M., Breugem, T. I., Mykytyn, A. Z., Wang, Y., Gröen, N., Knoops, K., Schipper, D., van der Vaart, J., Koopman, C. D., Zhang, J., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.03.441080 · Cited by 11

Evolving spike-protein N -glycosylation in SARS-CoV-2 variantsPreprint

Baboo, S., Diedrich, J. K., Torres, J. L., Copps, J., Singh, B., Garrett, P. T., Ward, A. B., Paulson, J. C., & Yates, J. R. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.08.539897 · Cited by 10

Variant mutation in SARS-CoV-2 nucleocapsid enhances viral infection via altered genomic encapsidationPreprint

Kubinski, H. C., Despres, H. W., Johnson, B. A., Schmidt, M. M., Jaffrani, S. A., Mills, M. G., Lokugamage, K. G., Dumas, C. M., Shirley, D. J., Estes, L. K., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.03.08.584120 · Cited by 11

Distinct pathways for evolution of enhanced receptor binding and cell entry in SARS-like bat coronaviruses

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On the Evolutionary Trajectory of SARS-CoV-2: Host Immunity as a Driver of Adaptation in RNA Viruses

Warger, J., & Gaudieri, S. (2022) · Viruses · doi:10.3390/v15010070 · Cited by 11

Platelet αIIbβ3 integrin binds to SARS-CoV-2 spike protein of alpha strain but not wild type and omicron strains

Ito, K., Goto, K., Shirakawa, R., Horiuchi, H., & Ogasawara, K. (2023) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2023.03.057 · Cited by 10

Potent Omicron-neutralizing antibodies isolated from a patient vaccinated 6 months before Omicron emergence

Hastie, K. M., Yu, X., Ana‐Sosa‐Batiz, F., Zyla, D. S., Harkins, S., Hariharan, C., Wasserman, H., Zandonatti, M. A., Miller, R., Maule, E., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112421 · Cited by 9

Rapid isolation of pan-neutralizing antibodies against Omicron variants from convalescent individuals infected with SARS-CoV-2

Yu, P., Ran, J., Yang, R., Zhu, H., Song, L., Wu, Y., Zhao, T., & Xiong, T.-C. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1374913 · Cited by 11

A Comparison of Seegene Technologies Novaplex SARS-CoV-2 Variants I, II, and IV Assays with Spike Gene Sequencing for Detection of Known Severe Acute Respiratory Syndrome Coronavirus 2 Variants

Nielsen, M. C., Machado, R. R. G., Mitchell, B. M., McConnell, A. J., Saada, N. I., Weaver, S. C., & Ren, P. (2022) · Journal of Molecular Diagnostics · doi:10.1016/j.jmoldx.2022.02.001 · Cited by 10

Analysis of the mutation dynamics of SARS-CoV-2 genome in the samples from Georgia State of the United States

Ahmad, W., Ahmad, S., & Basha, R. M. (2022) · Gene · doi:10.1016/j.gene.2022.146774 · Cited by 9

Higher Omicron JN.1 Coronavirus Transmission due to Unique 17MPLF Spike Insertion compensating 24LPP, 69HV, 145Y, 211N and 483V deletions in the spikePreprint

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Characterization of SARS-CoV-2 Variants in Military and Civilian Personnel of an Air Force Airport during Three Pandemic Waves in Italy

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