An Infectious cDNA Clone of SARS-CoV-2

Clinical features of patients infected with 2019 novel coronavirus in Wuhan, China

Huang, C., Wang, Y., Li, X., Ren, L., Zhao, J., Hu, Y., Zhang, L., Fan, G., Xu, J., Gu, X., et al. (2020) · The Lancet · doi:10.1016/s0140-6736(20)30183-5 · Cited by 48,884

A novel coronavirus from patients with pneumonia in China, 2019

Zhu, N., Zhang, D., Wang, W., Li, X., Yang, B., Song, J., Zhao, X., Huang, B., Shi, W., Lu, R., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2001017 · Cited by 28,244

A pneumonia outbreak associated with a new coronavirus of probable bat origin

Zhou, P., Yang, X.-L., Wang, X.-G., Hu, B., Zhang, L., Zhang, W., Si, H.-R., Zhu, Y., Li, B., Huang, C.-L., et al. (2020) · Nature · doi:10.1038/s41586-020-2012-7 · Cited by 21,969

Characteristics of and Important Lessons From the Coronavirus Disease 2019 (COVID-19) Outbreak in China: Summary of a Report of 72 314 Cases From the Chinese Center for Disease Control and Prevention

Wu, Z., & McGoogan, J. M. (2020) · JAMA · doi:10.1001/jama.2020.2648 · Cited by 17,016

First case of 2019 novel coronavirus in the United States

Holshue, M. L., DeBolt, C., Lindquist, S., Lofy, K. H., Wiesman, J., Bruce, H., Spitters, C., Ericson, K., Wilkerson, S., Tural, A., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2001191 · Cited by 6,030

SARS and MERS: recent insights into emerging coronaviruses

de Wit, E., van Doremalen, N., Falzarano, D., & Munster, V. J. (2016) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2016.81 · Cited by 3,510

The spike glycoprotein of the new coronavirus 2019-nCoV contains a furin-like cleavage site absent in CoV of the same clade

Coutard, B., Valle, C., de Lamballerie, X. N., Canard, B., Seidah, N. G., & Decroly, É. (2020) · Antiviral Research · doi:10.1016/j.antiviral.2020.104742 · Cited by 1,706

Epidemiological, demographic, and clinical characteristics of 47 cases of Middle East respiratory syndrome coronavirus disease from Saudi Arabia: a descriptive study

Assiri, A., Al-Tawfiq, J. A., Al-Rabeeah, A. A., Al-Rabiah, F. A., Al-Hajjar, S., Al-Barrak, A., Flemban, H., Al-Nassir, W. N., Balkhy, H. H., Al-Hakeem, R. F., et al. (2013) · The Lancet Infectious Diseases · doi:10.1016/s1473-3099(13)70204-4 · Cited by 1,435

A bright monomeric green fluorescent protein derived from Branchiostoma lanceolatum

Shaner, N. C., Lambert, G. G., Chammas, A., Ni, Y., Cranfill, P. J. C., Baird, M. A., Sell, B., Allen, J. R., Day, R. N., Israelsson, M., et al. (2013) · Nature Methods · doi:10.1038/nmeth.2413 · Cited by 1,260

A SARS-like cluster of circulating bat coronaviruses shows potential for human emergence

Menachery, V. D., Yount, B. L., Debbink, K. M., Agnihothram, S., Gralinski, L. E., Plante, J. A., Graham, R. L., Scobey, T., Ge, X., Donaldson, E., et al. (2015) · Nature Medicine · doi:10.1038/nm.3985 · Cited by 901

TRIM7 ubiquitinates SARS-CoV-2 membrane protein to limit apoptosis and viral replication

González-Orozco, M., Hsiang-Chi, T., Hage, A., Xia, H., Behera, P., Afreen, K. S., Peñaflor-Téllez, Y., Giraldo, M. I., Huante, M. B., Puebla-Clark, L., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-54762-5 · Cited by 17

Reinventing positive-strand RNA virus reverse genetics

Lindenbach, B. D. (2022) · Advances in virus research · doi:10.1016/bs.aivir.2022.03.001 · Cited by 20

Acquisition of Furin Cleavage Site and Further SARS-CoV-2 Evolution Change the Mechanisms of Viral Entry, Infection Spread, and Cell Signaling

Frolova, E. I., Palchevska, O., Lukash, T., Domínguez, F. D. B. P., Britt, W. J., & Frolov, I. V. (2022) · Journal of Virology · doi:10.1128/jvi.00753-22 · Cited by 19

Discovery of lead natural products for developing pan-SARS-CoV-2 therapeutics

Pérez‐Vargas, J., Shapira, T., Olmstead, A. D., Villanueva, I., Thompson, C. A. H., Ennis, S., Gao, G., Guzman, J. D., Williams, D. E., Wang, M., et al. (2022) · Antiviral Research · doi:10.1016/j.antiviral.2022.105484 · Cited by 19

Loss-of-function mutation in Omicron variants reduces spike protein expression and attenuates SARS-CoV-2 infection

Vu, M. N., Alvarado, R. E., Morris, D. R., Lokugamage, K. G., Zhou, Y., Morgan, A. L., Ahearn, Y. P., Hazell, N. C., Estes, L. K., McLeland, A. M., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-76680-4 · Cited by 21

The NSP3 protein of SARS-CoV-2 binds fragile X mental retardation proteins to disrupt UBAP2L interactions

Garvanska, D. H., Alvarado, R. E., Mundt, F., Lindqvist, R., Duel, J. K., Coscia, F., Nilsson, E., Lokugamage, K. G., Johnson, B. A., Plante, J. A., et al. (2024) · EMBO Reports · doi:10.1038/s44319-023-00043-z · Cited by 19

SARS-CoV-2 and oncolytic EV-D68-encoded proteases differentially regulate pyroptosis

Shen, S., Guo, H., Li, Y., Zhang, L., Tang, Y., Li, H., Li, X., Wang, P., Yu, X., & Wei, W. (2024) · Journal of Virology · doi:10.1128/jvi.01909-23 · Cited by 18

Reverse genetic systems: Rational design of coronavirus live attenuated vaccines with immune sequelae

Ma, Z., Li, Z., Dong, L., Yang, T., & Xiao, S. (2020) · Advances in virus research · doi:10.1016/bs.aivir.2020.06.003 · Cited by 18

BNT162b vaccines are immunogenic and protect non-human primates against SARS-CoV-2Preprint

Vogel, A. B., Kanevsky, I., Che, Y., Swanson, K. A., Muik, A., Vormehr, M., Kranz, L. M., Walzer, K. C., Hein, S., Güler, A., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.12.11.421008 · Cited by 18

Plasmacytoid dendritic cells produce type I interferon and reduce viral replication in airway epithelial cells after SARS-CoV-2 infectionPreprint

Cervantes‐Barragán, L., Vanderheiden, A., Royer, C. J., Davis-Gardner, M. E., Ralfs, P., Chirkova, T., Anderson, L. J., Grakoui, A., & Suthar, M. S. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.12.443948 · Cited by 20

Atovaquone and Berberine Chloride Reduce SARS-CoV-2 Replication In Vitro

Rodriguez-Rodriguez, B. A., Noval, M. G., Kaczmarek, M. E., Jang, K. K., Thannickal, S. A., Kottkamp, A. C., Brown, R. S., Kielian, M. C., Cadwell, K., & Stapleford, K. A. (2021) · Viruses · doi:10.3390/v13122437 · Cited by 18

Nanobubble Ozone Stored in Hyaluronic Acid Decorated Liposomes: Antibacterial, Anti-SARS-CoV-2 Effect and Biocompatibility Tests

Sabancı, A. Ü., Alkan, P. E., Mujde, C., Polat, H. U., Erguzeloglu, C. O., Bisgin, A., Ozakın, C., & Temel, Ş. G. (2022) · International Journal of Nanomedicine · doi:10.2147/ijn.s328090 · Cited by 17

VE607 stabilizes SARS-CoV-2 Spike in the “RBD-up” conformation and inhibits viral entry

Ding, S., Ullah, I., Gong, S. Y., Grover, J. R., Mohammadi, M., Chen, Y., Vézina, D., Beaudoin-Bussières, G., Verma, V. T., Goyette, G., et al. (2022) · iScience · doi:10.1016/j.isci.2022.104528 · Cited by 18

Cross-neutralization and viral fitness of SARS-CoV-2 Omicron sublineages

Xia, H., Yeung, J., Kalveram, B., Bills, C. J., Chen, J. Y.-C., Kurhade, C., Zou, J., Widen, S. G., Mann, B. R., Kondor, R. J. G., et al. (2023) · Emerging Microbes & Infections · doi:10.1080/22221751.2022.2161422 · Cited by 17

SARS‐CoV‐2 infection of polarized human airway epithelium induces necroptosis that causes airway epithelial barrier dysfunction

Hao, S., Ning, K., Küz, Ç. A., Xiong, M., Zou, W., Park, S. Y., McFarlin, S., Yan, Z., & Qiu, J. (2023) · Journal of Medical Virology · doi:10.1002/jmv.29076 · Cited by 19

Infants and young children generate more durable antibody responses to SARS-CoV-2 infection than adults

Joshi, D., Nyhoff, L. E., Zarnitsyna, V. I., Moreno, A., Manning, K. E., Linderman, S. L., Burrell, A. R., Stephens, K., Norwood, C., Mantus, G. E., et al. (2023) · iScience · doi:10.1016/j.isci.2023.107967 · Cited by 17

A deep convolution neural network for automated COVID-19 disease detection using chest X-ray images

Thangaraj, R., Pandiyan, P., Ramakrishnan, J., Nallakumar, R., & Eswaran, S. (2023) · Healthcare Analytics · doi:10.1016/j.health.2023.100278 · Cited by 19

A Bioluminescent 3CLPro Activity Assay to Monitor SARS-CoV-2 Replication and Identify Inhibitors

Mathieu, C., Touret, F., Jacquemin, C., Janin, Y. L., Nougaırède, A., Brailly, M., Mazelier, M., Décimo, D., Vasseur, V., Hans, A., et al. (2021) · Viruses · doi:10.3390/v13091814 · Cited by 17

Ferulic acid derivatives block coronaviruses HCoV-229E and SARS-CoV-2 replication in vitro

Pasquereau, S., Galais, M., Bellefroid, M., Pachón-Angona, I., Morot-Bizot, S., Ismaïli, L., Lint, C. M. V., & Herbein, G. (2022) · Scientific Reports · doi:10.1038/s41598-022-24682-9 · Cited by 17

S:D614G and S:H655Y are Gateway Mutations that Act Epistatically to Promote SARS-CoV-2 Variant FitnessPreprint

Yurkovetskiy, L., Egri, S. B., Kurhade, C., Díaz-Salinas, M. A., Jaimes, J. A., Nyalile, T., Xie, X., Choudhary, M. C., Dauphin, A., Li, J. Z., et al. (2023) · SSRN Electronic Journal · doi:10.1101/2023.03.30.535005 · Cited by 18

Structure-based discovery of highly bioavailable, covalent, broad-spectrum coronavirus M Pro inhibitors with potent in vivo efficacy

Detomasi, T. C., Degotte, G., Huang, S., Suryawanshi, R. K., Diallo, A., Lizzadro, L., Belinchón, F. J. Z., Taha, T. Y., Li, J., Richards, A., et al. (2025) · Science Advances · doi:10.1126/sciadv.adt7836 · Cited by 21

Construction and characterization of two SARS‐CoV‐2 minigenome replicon systems

Zhang, H., Fischer, D. K., Shuda, M., Moore, P. S., Gao, S., Ambrose, Z., & Guo, H. (2022) · Journal of Medical Virology · doi:10.1002/jmv.27650 · Cited by 16

Persicamidines—Unprecedented Sesquarterpenoids with Potent Antiviral Bioactivity against Coronaviruses

Keller, L., Oueis, E., Kaur, A., Safaei, N., Kirsch, S. H., Gunesch, A. P., Haid, S., Rand, U., Čičin‐Šain, L., Fu, C., et al. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202214595 · Cited by 16

High-resolution photocatalytic mapping of SARS-CoV-2 spike interactions on the cell surface

Datta, S., Chen, D. W., Tavares, A. H., Robles, T. R., Ryu, K. A., Khan, N., Bechtel, T. J., Bertoch, J. M., White, C., Hazuda, D. J., et al. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2023.06.028 · Cited by 18

Establishment of enterically transmitted hepatitis virus animal models using lipid nanoparticle-based full-length viral genome RNA delivery system

Liu, T., Li, J., Yin, X., Lu, F., Zhao, H. J., Wang, L., & Qin, C. (2024) · Gut · doi:10.1136/gutjnl-2024-332784 · Cited by 15

Establishment of a reverse genetics system for SARS-CoV-2 using circular polymerase extension reactionPreprint

Torii, S., Ono, C., Suzuki, R., Morioka, Y., Anzai, I., Fauzyah, Y., Maeda, Y., Kamitani, W., Fukuhara, T., & Matsuura, Y. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.09.23.309849 · Cited by 16

The translational landscape of SARS-CoV-2 and infected cellsPreprint

Puray‐Chavez, M., Lee, N., Tenneti, K., Wang, Y., Vuong, H. R., Liu, Y., Horani, A., Huang, T., Gunsten, S. P., Case, J. B., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.03.367516 · Cited by 16

A Nucleocapsid-based Transcomplementation Cell Culture System of SARS-CoV-2 to Recapitulate the Complete Viral Life Cycle

Yu, Y., Ju, X., & Ding, Q. (2021) · BIO-PROTOCOL · doi:10.21769/bioprotoc.4257 · Cited by 15

Identification of a 1.4-kb-Long Sequence Located in the nsp12 and nsp13 Coding Regions of SARS-CoV-2 Genomic RNA That Mediates Efficient Viral RNA Packaging

Terasaki, K., Narayanan, K., & Makino, S. (2023) · Journal of Virology · doi:10.1128/jvi.00659-23 · Cited by 15

A single-dose of intranasal vaccination with a live-attenuated SARS-CoV-2 vaccine candidate promotes protective mucosal and systemic immunity

Adam, A., Kalveram, B., Chen, J. Y.-C., Yeung, J., Rodriguez, L., Singh, A., Shi, P., Xie, X., & Wang, T. (2023) · npj Vaccines · doi:10.1038/s41541-023-00753-4 · Cited by 16

Compounds derived from Humulus lupulus inhibit SARS-CoV-2 papain-like protease and virus replication

Herzog, A.-M., Göbel, K., Marongiu, L., Ruétalo, N., Alonso, M. C., Leischner, C., Busch, C., Burkard, M., Lauer, U. M., Geurink, P. P., et al. (2023) · Phytomedicine · doi:10.1016/j.phymed.2023.155176 · Cited by 15

Long-term efficacy of the peptide-based COVID-19 T cell activator CoVac-1 in healthy adults

Tandler, C., Heitmann, J. S., Michel, T., Marconato, M., Jaeger, S. U., Tegeler, C. M., Denk, M., Richter, M., Oezbek, M. T., Maringer, Y., et al. (2023) · International Journal of Infectious Diseases · doi:10.1016/j.ijid.2023.11.009 · Cited by 15

One-pot Golden Gate Assembly of an avian infectious bronchitis virus reverse genetics system

Bilotti, K., Keep, S., Sikkema, A. P., Pryor, J. M., Kirk, J., Földes, K., Doyle, N., Wu, G., Freimanis, G., Dowgier, G., et al. (2024) · PLoS ONE · doi:10.1371/journal.pone.0307655 · Cited by 15

The Mac1 ADP-ribosylhydrolase is a therapeutic target for SARS-CoV-2

Suryawanshi, R. K., Jaishankar, P., Correy, G. J., Rachman, M. M., O’Leary, P. C., Taha, T. Y., Matsui, Y., Belinchón, F. J. Z., McCavitt-Malvido, M., Doruk, Y. U., et al. (2025) · eLife · doi:10.7554/elife.103484.3 · Cited by 15

Evaluation of a SARS-CoV-2 lateral flow assay using the plaque reduction neutralization test

Xie, X., Nielsen, M. C., Muruato, A. E., Fontes-Garfias, C. R., & Ren, P. (2020) · Diagnostic Microbiology and Infectious Disease · doi:10.1016/j.diagmicrobio.2020.115248 · Cited by 15

Making sense of spike D614G in SARS-CoV-2 transmission

Shi, A. C., & Xie, X. (2021) · Science China Life Sciences · doi:10.1007/s11427-020-1893-9 · Cited by 15

Adjuvanting a subunit SARS-CoV-2 nanoparticle vaccine to induce protective immunity in non-human primatesPreprint

Arunachalam, P. S., Walls, A. C., Golden, N., Atyeo, C. G., Fischinger, S., Li, C., Aye, P. P., Navarro, M. J., Lai, L., Edara, V. V., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.02.10.430696 · Cited by 15

Gut microbiome dysbiosis during COVID-19 is associated with increased risk for bacteremia and microbial translocationPreprint

Venzon, M., Bernard, L., Klein, J., Axelrad, J. E., Zhang, C., Hussey, G. A., Sullivan, A. P., Casanovas‐Massana, A., Noval, M. G., Valero-Jimenez, A. M., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.07.15.452246 · Cited by 15

Neutralization of Omicron SARS-CoV-2 by 2 or 3 doses of BNT162b2 vaccinePreprint

Xia, H., Zou, J., Kurhade, C., Cai, H., Yang, Q., Cutler, M. W., Cooper, D., Muik, A., Jansen, K. U., Xie, X., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.21.476344 · Cited by 15

Targeting the Fusion Process of SARS-CoV-2 Infection by Small Molecule Inhibitors

Park, S. B., Irvin, P., Hu, Z., Khan, M., Hu, X., Zeng, Q., Chen, C., Xu, M., Leek, M., Zang, R., et al. (2022) · mBio · doi:10.1128/mbio.03238-21 · Cited by 15

Nanobubble Ozone Stored in Hyaluronic Acid Decorated Liposomes: Antibacterial, Anti-SARS-CoV-2 Effect and Biocompatibility Tests

Sabancı, A. Ü., Alkan, P. E., Mujde, C., Polat, H. Ü., Erguzeloglu, C. O., Bişgin, A., Ozakın, C., & Temel, Ş. G. (2022) · Dove Medical Press (Taylor and Francis Group) · Cited by 14

NS1 Protein N-Linked Glycosylation Site Affects the Virulence and Pathogenesis of Dengue Virus

Fang, E., Li, M., Liu, X., Hu, K., Liu, L., Zhang, Z., Li, X., Peng, Q., & Li, Y. (2023) · Vaccines · doi:10.3390/vaccines11050959 · Cited by 14

Acetate-encapsulated Linolenic Acid Liposomes Reduce SARS-CoV-2 and RSV Infection

McGill, A. R., Markoutsa, E., Mayilsamy, K., Green, R. J., Sivakumar, K., Mohapatra, S., & Mohapatra, S. S. (2023) · Viruses · doi:10.3390/v15071429 · 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

Tetherin Restricts SARS-CoV-2 despite the Presence of Multiple Viral Antagonists

Hagelauer, E., Lotke, R., Kmieć, D., Hu, D., Hohner, M., Stopper, S., Nchioua, R., Kirchhoff, F., Sauter, D., & Schindler, M. (2023) · Viruses · doi:10.3390/v15122364 · Cited by 14

A basally active cGAS-STING pathway limits SARS-CoV-2 replication in a subset of ACE2 positive airway cell models

Puray‐Chavez, M., Eschbach, J. E., Xia, M., LaPak, K. M., Zhou, Q., Jasuja, R., Pan, J., Xu, J., Zhou, Z., Mohammed, S., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-52803-7 · Cited by 14

Broad-Spectrum Antiviral Activity of 3D8, a Nucleic Acid-Hydrolyzing Single-Chain Variable Fragment (scFv), Targeting SARS-CoV-2 and Multiple Coronaviruses In Vitro

Lee, G., Budhathoki, S., Lee, G., Oh, K.-J., Ham, Y. K., Kim, Y.-J., Lim, Y., Hoang, P. T., Lee, Y., Lim, S.-W., et al. (2021) · Viruses · doi:10.3390/v13040650 · Cited by 14

Laboratory-Generated DNA Can Cause Anomalous Pathogen Diagnostic Test Results

Robinson‐McCarthy, L. R., Mijalis, A. J., Filsinger, G. T., de Puig, H., Donghia, N. M., Schaus, T. E., Rasmussen, R. A., Ferreira, R., Lunshof, J. E., Chao, G., et al. (2021) · Microbiology Spectrum · doi:10.1128/spectrum.00313-21 · Cited by 14

Potential of Quinine Sulfate for COVID-19 Treatment and Its Safety Profile: Review

Latarissa, I. R., Barliana, M. I., Meiliana, A., & Lestari, K. (2021) · Clinical Pharmacology Advances and Applications · doi:10.2147/cpaa.s331660 · Cited by 17

Dichotomy between the humoral and cellular responses elicited by mRNA and adenoviral vector vaccines against SARS-CoV-2

Ukey, R., Bruiners, N., Mishra, H. K., Mishra, P. K., McCloskey, D., Onyuka, A., Chen, F., Pinter, A., Weiskopf, D., Sette, A., et al. (2022) · BMC Medicine · doi:10.1186/s12916-022-02252-0 · Cited by 16

Cross-neutralization and cross-protection among SARS-CoV-2 viruses bearing different variant spikes

Liu, Y., Liu, J., Zou, J., Kalveram, B., Machado, R. R. G., Ren, P., Türeli, S., Smith, D. J., Weaver, S. C., Xie, X., et al. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01137-1 · Cited by 14

Intravital imaging of three different microvascular beds in SARS-CoV-2–infected mice

Castanheira, F. V. S., Nguyen, R., Willson, M. E., Davoli-Ferreira, M., David, B. A., Kelly, M. M., Lee, W., Kratofil, R. M., Zhang, W. X., Bui-Marinos, M. P., et al. (2023) · Blood Advances · doi:10.1182/bloodadvances.2022009430 · Cited by 14

Neutralization of SARS-CoV-2 Omicron sublineages by 4 doses of mRNA vaccinePreprint

Xie, X., Zou, J., Kurhade, C., Liu, M., Ren, P., & Shi, P. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.07.29.502055 · Cited by 14

A Rapid Method for Generating Infectious SARS-CoV-2 and Variants Using Mutagenesis and Circular Polymerase Extension Cloning

Kim, B. K., Choi, W.-S., Jeong, J. H., Oh, S., Park, J., Yun, Y. S., Min, S. C., Kang, D. H., Kim, E., Ryu, H., et al. (2023) · Microbiology Spectrum · doi:10.1128/spectrum.03385-22 · Cited by 14

SARS-CoV-2-related bat viruses evade human intrinsic immunity but lack efficient transmission capacity

Peña-Hernández, M. A., Alfajaro, M. M., Filler, R. B., Moriyama, M., Keeler, E. L., Ranglin, Z. E., Kong, Y., Mao, T., Menasché, B. L., Mankowski, M. C., et al. (2024) · Nature Microbiology · doi:10.1038/s41564-024-01765-z · Cited by 15

SARS-CoV-2 EndoU-ribonuclease regulates RNA recombination and impacts viral fitness

Zhou, Y., Ahearn, Y. P., Lokugamage, K. G., Morgan, A. L., Alvarado, R. E., Estes, L. K., Meyers, W. M., McLeland, A. M., Murray, J. T., Rouse, J. R., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-67001-2 · Cited by 13

Evaluation of Cellular and Serological Responses to Acute SARS-CoV-2 Infection Demonstrates the Functional Importance of the Receptor-Binding Domain

Mantus, G. E., Nyhoff, L. E., Kauffman, R. C., Edara, V. V., Lai, L., Floyd, K. A., Shi, P., Menachery, V. D., Edupuganti, S., Scherer, E. M., et al. (2021) · The Journal of Immunology · doi:10.4049/jimmunol.2001420 · Cited by 13

IFN-γ-mediated control of SARS-CoV-2 infection through nitric oxide

Silva, B. J. D. A., Krogstad, P. A., Teles, R. M. B., Andrade, P. R., Rajfer, J., Ferrini, M. G., Yang, O. O., Bloom, B. R., & Modlin, R. L. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1284148 · Cited by 15

A single intranasal dose of human parainfluenza virus type 3-vectored vaccine induces effective antibody and memory T cell response in the lungs and protects hamsters against SARS-CoV-2

Ilinykh, P. A., Periasamy, S., Huang, K., Kuzmina, N. A., Ramanathan, P., Meyer, M. N., Mire, C. E., Kuzmin, I. V., Bharaj, P., Endsley, J. R., et al. (2022) · npj Vaccines · doi:10.1038/s41541-022-00471-3 · Cited by 14

A Single-Round Infection Fluorescent SARS-CoV-2 Neutralization Test for COVID-19 Serological Testing at a Biosafety Level-2 Laboratory

Zou, J., Xia, H., Shi, P., Xie, X., & Ren, P. (2022) · Viruses · doi:10.3390/v14061211 · Cited by 12

Brilacidin, a Non-Peptide Defensin-Mimetic Molecule, Inhibits SARS-CoV-2 Infection by Blocking Viral Entry.

Xu, C., Wang, A., Honnen, W. J., Pinter, A., Weston, W., Harness, J. A., Narayanan, A., & Chang, T. L.-Y. (2022) · PubMed · Cited by 13

One Health Investigation of SARS-CoV-2 in People and Animals on Multiple Mink Farms in Utah

Cossaboom, C. M., Wendling, N. M., Lewis, N. M., Rettler, H., Harvey, R. R., Amman, B. R., Towner, J. S., Spengler, J. R., Erickson, R., Burnett, C. L., et al. (2022) · Viruses · doi:10.3390/v15010096 · Cited by 13

Home-made enzymatic premix and Illumina sequencing allow for one-step Gibson assembly and verification of virus infectious clones

Zhao, M., García, B., Gallo, A., Tzanetakis, I. E., Simón‐Mateo, C., Garcı́a, J. A., & Pasin, F. (2020) · Phytopathology Research · doi:10.1186/s42483-020-00077-4 · Cited by 13

Ultrapotent and broad neutralization of SARS-CoV-2 variants by modular, tetravalent, bi-paratopic antibodies

Miersch, S., Sharma, N., Saberianfar, R., Chen, C., Caccuri, F., Zani, A., Caruso, A., Case, J. B., Diamond, M., Amarasinghe, G. K., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110905 · Cited by 14

The oral drug nitazoxanide restricts SARS-CoV-2 infection and attenuates disease pathogenesis in Syrian hamstersPreprint

Miorin, L., Mire, C. E., Ranjbar, S., Hume, A. J., Huang, J., Crossland, N. A., White, K. M., Laporte, M., Kehrer, T., Haridas, V., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.02.08.479634 · Cited by 12

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

Toward Understanding Molecular Bases for Biological Diversification of Human Coronaviruses: Present Status and Future Perspectives

Koma, T., Adachi, S., Doi, N., Adachi, A., & Nomaguchi, M. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.02016 · Cited by 13

Enhanced virulence and waning vaccine-elicited antibodies account for breakthrough infections caused by SARS-CoV-2 delta and beyond

Kwon, H., Košíková, M., Tang, W., Ortega‐Rodriguez, U., Radvák, P., Xiang, R., Mercer, K. E., Muskhelishvili, L., Davis, K., Ward, J. M., et al. (2022) · iScience · doi:10.1016/j.isci.2022.105507 · Cited by 11

Use of a Bacterial Artificial Chromosome to Generate Recombinant SARS-CoV-2 Expressing Robust Levels of Reporter Genes

Ye, C., & Martínez‐Sobrido, L. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.02732-22 · Cited by 12

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

Mucosal vaccination induces protection against SARS-CoV-2 in the absence of detectable neutralizing antibodies

Zhong, C., Xia, H., Adam, A., Wang, B., Hajnik, R. L., Liang, Y., Rafael, G. H., Zou, J., Wang, X., Sun, J., et al. (2021) · npj Vaccines · doi:10.1038/s41541-021-00405-5 · Cited by 13

Construction of a Dengue NanoLuc Reporter Virus for In Vivo Live Imaging in Mice

Fang, E., Liu, X., Li, M., Liu, J., Zhang, Z., Liu, X., Li, X., Li, W., Peng, Q., Yu, Y., et al. (2022) · Viruses · doi:10.3390/v14061253 · Cited by 12

Exploring inactivation of SARS-CoV-2, MERS-CoV, Ebola, Lassa, and Nipah viruses on N95 and KN95 respirator material using photoactivated methylene blue to enable reuse

Scholte, F. E. M., Kabra, K. B., Tritsch, S. R., Montgomery, J. M., Spiropoulou, C. F., Mores, C. N., & Harcourt, B. H. (2022) · American Journal of Infection Control · doi:10.1016/j.ajic.2022.02.016 · Cited by 12

SARS-CoV-2 infection of intestinal epithelia cells sensed by RIG-I and DHX-15 evokes innate immune response and immune cross-talk

Zhang, L., Zhang, Y., Wang, R., Liu, X., Zhao, J., Tsuda, M., & Li, Y. (2023) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.1035711 · Cited by 12

Oligonucleotide abundance biases aid design of a type IIS synthetic genomics framework with plant virome capacity

Pasin, F. (2021) · Biotechnology Journal · doi:10.1002/biot.202000354 · Cited by 12

Profound CD8 T cell responses towards the SARS-CoV-2 ORF1ab in COVID-19 patientsPreprint

Gangaev, A., Ketelaars, S. L. C., Patiwael, S., Dopler, A., Isaeva, O. I., Hoefakker, K., Biasi, S. D., Mussini, C., Guaraldi, G., Girardis, M., et al. (2020) · doi:10.21203/rs.3.rs-33197/v1 · 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

XBB.1.5 monovalent booster improves antibody binding and neutralization against emerging SARS-CoV-2 Omicron variantsPreprint

Jain, S., Kumar, S., Lai, L., Linderman, S. L., Malik, A. A., Ellis, M. L., Godbole, S., Solis, D., Sahoo, M. K., Bechnak, K., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.02.03.578771 · Cited by 12

The KDM6A-KMT2D-p300 axis regulates susceptibility to diverse coronaviruses by mediating viral receptor expression

Wei, J., Alfajaro, M. M., Cai, W. L., Graziano, V. R., Strine, M. S., Filler, R. B., Biering, S. B., Sarnik, S. A., Patel, S., Menasché, B. L., et al. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1011351 · Cited by 10

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

Induction of significant neutralizing antibodies against SARS-CoV-2 by a highly attenuated pangolin coronavirus variant with a 104nt deletion at the 3'-UTR

Lu, S., Luo, S., Liu, C., Li, M., An, X., Li, M., Hou, J. W., Fan, H., Mao, P., Tong, Y., et al. (2022) · Emerging Microbes & Infections · doi:10.1080/22221751.2022.2151383 · Cited by 11

High-Throughput SARS-CoV-2 Antiviral Testing Method Using the Celigo Image Cytometer

Clair, L. A. S., Chan, L. L., Boretsky, A. R., Lin, B., Spedding, M., & Perera, R. M. (2023) · Journal of Fluorescence · doi:10.1007/s10895-023-03289-x · Cited by 11

Cell type dependent stability and virulence of a recombinant SARS-CoV-2, and engineering of a propagation deficient RNA replicon to analyze virus RNA synthesis

Wang, L., Guzman, M., Muñoz‐Santos, D., Honrubia, J. M., Ripoll-Gómez, J., Delgado, R. B., Sola, I., Enjuanes, L., & Zúñiga, S. (2023) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2023.1268227 · Cited by 11

An anti-SARS-CoV-2 non-neutralizing antibody with Fc-effector function defines a new NTD epitope and delays neuroinvasion and death in K18-hACE2 micePreprint

Beaudoin-Bussières, G., Chen, Y.-Z., Ullah, I., Prévost, J., Tolbert, W., Symmes, K., Ding, S.-L., Benlarbi, M., Gong, S., Tauzin, A., et al. (2021) · bioRxiv · doi:10.1101/2021.09.08.459408 · Cited by 15

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

The XBB.1.5 COVID-19 vaccine elicits a durable antibody response to ancestral and XBB.1.5 SARS-CoV-2 spike proteins

Kumar, S., Jain, S., Wali, B., Zarnitsyna, V. I., Joshi, D., Ellis, M. L., Lai, L., Malik, A. A., McPherson, T., Godbole, S., et al. (2025) · Science Translational Medicine · doi:10.1126/scitranslmed.adu8067 · Cited by 12

The efficacy of herbal medicines on the length of stay and negative conversion time/rate outcomes in patients with COVID-19: a systematic review

Latarissa, I. R., Meiliana, A., Sormin, I. P., Sugiono, E., Wathoni, N., Barliana, M. I., & Lestari, K. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1383359 · Cited by 10

A method for the generation of pseudovirus particles bearing SARS coronavirus spike protein in high yields

Fujioka, Y., Kashiwagi, S., Yoshida, A., Satoh, A. O., Fujioka, Y., Amano, M., Yamauchi, Y., & Ohba, Y. (2022) · Cell Structure and Function · doi:10.1247/csf.21047 · Cited by 12

Review on In Silico Methods, High-throughput Screening Techniques, and Cell Culture Based In Vitro Assays for SARS-CoV-2

Çetin, Y., Aydınlık, Ş., Güngör, A., Kan, T., Avşar, T., & Durdağı, S. (2022) · Current Medicinal Chemistry · doi:10.2174/0929867329666220627121416 · Cited by 11

Assembly of plant virus agroinfectious clones using biological material or DNA synthesis

Pasin, F. (2022) · STAR Protocols · doi:10.1016/j.xpro.2022.101716 · Cited by 10

Generation of a SARS-CoV-2 Reverse Genetics System and Novel Human Lung Cell Lines That Exhibit High Virus-Induced Cytopathology

Khan, J. Q., Rohamare, M., Rajamanickam, K., Bhanumathy, K. K., Lew, J. M., Kumar, A., Falzarano, D., Vizeacoumar, F. J., & Wilson, J. A. (2023) · Viruses · doi:10.3390/v15061281 · Cited by 10

Defining Distinct RNA-Protein Interactomes of SARS-CoV-2 Genomic and Subgenomic RNAs

Whitworth, I. T., Knoener, R. A., Puray‐Chavez, M., Halfmann, P., Romero, S., Baddouh, M., Scalf, M., Kawaoka, Y., Kutluay, S. B., Smith, L. M., et al. (2023) · Journal of Proteome Research · doi:10.1021/acs.jproteome.3c00506 · Cited by 10

Advanced microscopy technologies enable rapid response to SARS‐CoV ‐2 pandemic

Cortese, M., & Laketa, V. (2021) · Cellular Microbiology · doi:10.1111/cmi.13319 · Cited by 9

SARS-CoV-2 Antibody Neutralization Assay Platforms Based on Epitopes Sources: Live Virus, Pseudovirus, and Recombinant S Glycoprotein RBD

Septisetyani, E. P., Prasetyaningrum, P. W., Anam, K., & Santoso, A. (2021) · Immune Network · doi:10.4110/in.2021.21.e39 · Cited by 11

The Mac1 ADP-ribosylhydrolase is a therapeutic target for SARS-CoV-2Preprint

Suryawanshi, R. K., Jaishankar, P., Correy, G. J., Rachman, M. M., O’Leary, P. C., Taha, T. Y., Matsui, Y., Belinchón, F. J. Z., McCavitt-Malvido, M., Doruk, Y. U., et al. (2025) · eLife · doi:10.7554/elife.103484 · Cited by 19

Suppression of SARS-CoV-2 nucleocapsid protein dimerization by ISGylation and its counteraction by viral PLpro

Bang, W., Kim, J., Seo, K., Lee, J., Han, J. H., Park, D., Cho, J.-H., Shin, D., Kim, K., Song, M. J., et al. (2024) · Frontiers in Microbiology · doi:10.3389/fmicb.2024.1490944 · Cited by 10

The SARS-CoV-2 nucleocapsid protein interferes with the full enzymatic activation of UPF1 and its interaction with UPF2

Nuccetelli, V., Mghezzi-Habellah, M., Deymier, S., Roisin, A., Gérard, F. C. A., Rocchi, C., Coureux, P., Gouet, P., Cimarelli, A., Mocquet, V., et al. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf010 · Cited by 9

A global collaboration for systematic analysis of broad-ranging antibodies against the SARS-CoV-2 spike protein

Schendel, S., Yu, X.-Y., Halfmann, P., Mahita, J., Ha, B., Hastie, K., Li, H.-Y., Bedinger, D., Troup, C. B., Li, K., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115499 · Cited by 5

Rapid reconstruction of infectious bronchitis virus expressing fluorescent protein from its nsp2 gene based on transformation-associated recombination platform

Li, Y., Duan, L., Tang, L., Huang, M., Zhao, Y., Zhang, G., & Zhao, J. (2025) · Journal of Virology · doi:10.1128/jvi.00535-25 · Cited by 9

Uncovering Novel Viral Innate Immune Evasion Strategies: What Has SARS-CoV-2 Taught Us?

Tay, D. J. W., Lew, Z. Z. R., Chu, J. J. H., & Tan, K. S. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.844447 · Cited by 9

Engineering SARS-CoV-2 using a reverse genetic system

Xie, X., Lokugamage, K. G., Zhang, X., Vu, M. N., Muruato, A. E., Menachery, V. D., & Shi, P. (2021) · Nature Protocols · doi:10.1038/s41596-021-00491-8 · Cited by 171

Efficient and modular reverse genetics system for rapid generation of recombinant severe acute respiratory syndrome coronavirus 2

Bae, S., & Myoung, J. (2025) · The Journal of Microbiology · doi:10.71150/jm.2504015 · Cited by 3

Establishment of a reverse genetics system for SARS-CoV-2 using circular polymerase extension reactionPreprint

Torii, S., Ono, C., Suzuki, R., Morioka, Y., Anzai, I., Fauzyah, Y., Maeda, Y., Kamitani, W., Fukuhara, T., & Matsuura, Y. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.09.23.309849 · Cited by 16

A versatile reverse genetics platform for SARS-CoV-2 and other positive-strand RNA viruses

Amarilla, A. A., Sng, J. D. J., Parry, R. H., Deerain, J. M., Potter, J. R., Setoh, Y. X., Rawle, D. J., Le, T. T., Modhiran, N., Wang, X., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23779-5 · Cited by 159

Bacterial Artificial Chromosome Reverse Genetics Approaches for SARS-CoV-2

Chiem, K., Nogales, A., Almazán, F., Ye, C., & Martínez‐Sobrido, L. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3533-9_9 · Cited by 1