Cited by 590SARS-CoV-2 and COVID-19 ResearchRNA Research and Splicinginterferon and immune responses

The DOI matches its Crossref record; 96 of the 100 references it cites were found in a registry or an index.

SARS-CoV-2 Disrupts Splicing, Translation, and Protein Trafficking to Suppress Host Defenses

Open access

Banerjee, Abhik K., Blanco, Mario R., Bruce, Emily A., Honson, Drew D., Chen, Linlin M., Chow, Amy, Bhat, Prashant, Ollikainen, Noah, Quinodoz, Sofia A., Loney, Colin, Thai, Jasmine, Miller, Zachary D., Lin, Aaron E., Schmidt, Madaline M., Stewart, Douglas G., Goldfarb, Daniel, De Lorenzo, Giuditta, Rihn, Suzannah J., Voorhees, Rebecca M., Botten, Jason W., Majumdar, Devdoot, Guttman, Mitchell·2020·Cell

DOI 10.1016/j.cell.2020.10.004PMC PMC7543886

Open this paper in CoChat — free account Open PDF

Abstract

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a recently identified coronavirus that causes the respiratory disease known as coronavirus disease 2019 (COVID-19). Despite the urgent need, we still do not fully understand the molecular basis of SARS-CoV-2 pathogenesis. Here, we comprehensively define the interactions between SARS-CoV-2 proteins and human RNAs. NSP16 binds to the mRNA recognition domains of the U1 and U2 splicing RNAs and acts to suppress global mRNA splicing upon SARS-CoV-2 infection. NSP1 binds to 18S ribosomal RNA in the mRNA entry channel of the ribosome and leads to global inhibition of mRNA translation upon infection. Finally, NSP8 and NSP9 bind to the 7SL RNA in the signal recognition particle and interfere with protein trafficking to the cell membrane upon infection. Disruption of each of these essential cellular functions acts to suppress the interferon response to viral infection. Our results uncover a multipronged strategy utilized by SARS-CoV-2 to antagonize essential cellular processes to suppress host defenses.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1016/j.cell.2020.10.004

Cites

96 of 96 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Trimmomatic: a flexible trimmer for Illumina sequence data
Bolger, A. M., Lohse, M., & Usadel, B. (2014) · Bioinformatics · doi:10.1093/bioinformatics/btu170 · Cited by 65,548
Fast gapped-read alignment with Bowtie 2
Langmead, B., & Salzberg, S. L. (2012) · Nature Methods · doi:10.1038/nmeth.1923 · Cited by 56,400
STAR: ultrafast universal RNA-seq aligner
Dobin, A., Davis, C. A., Schlesinger, F., Drenkow, J., Zaleski, C., Jha, S., Batut, P., Chaisson, M., & Gingeras, T. R. (2013) · Bioinformatics · doi:10.1093/bioinformatics/bts635 · Cited by 51,709
The Protein Data Bank
Berman, H. M. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.235 · Cited by 40,196
The PyMOL Molecular Graphics System
DeLano, W. L. (2002) · Medical Entomology and Zoology · Cited by 18,147
Integrative genomics viewer
Robinson, J. T., Thorvaldsdóttir, H., Winckler, W., Guttman, M., Lander, E. S., Getz, G., & Mesirov, J. P. (2011) · Nature Biotechnology · doi:10.1038/nbt.1754 · Cited by 15,390
Self-citation
The Molecular Signatures Database Hallmark Gene Set Collection
Liberzon, A., Birger, C., Thorvaldsdóttir, H., Ghandi, M., Mesirov, J. P., & Tamayo, P. (2015) · Cell Systems · doi:10.1016/j.cels.2015.12.004 · Cited by 13,807
Recognition of double-stranded RNA and activation of NF-κB by Toll-like receptor 3
Alexopoulou, L., Holt, A. C., Medzhitov, R., & Flavell, R. A. (2001) · Nature · doi:10.1038/35099560 · Cited by 6,129
The proximal origin of SARS-CoV-2
Andersen, K. G., Rambaut, A., Lipkin, W. I., Holmes, E. C., & Garry, R. F. (2020) · Nature Medicine · doi:10.1038/s41591-020-0820-9 · Cited by 5,081
Comparative Protein Structure Modeling Using Modeller
Eswar, N., Webb, B., Martı́-Renom, M. A., Madhusudhan, M. S., Eramian, D., Shen, M., Pieper, U., & Šali, A. (2006) · Current Protocols in Bioinformatics · doi:10.1002/0471250953.bi0506s15 · Cited by 4,618

Flagged first, then by citations

Show all 100 references

4 of the 100 references couldn’t be matched to a known paper.

Sorted by citations

Items 301–400 of 590

Buffy Coat Transcriptomic Analysis Reveals Alterations in Host Cell Protein Synthesis and Cell Cycle in Severe COVID-19 Patients
Cavalcante, L. T. D. F., da Fonseca, G. C., Leon, L. A. A., Salvio, A. L., Brustolini, O. J. B., Gerber, A. L., Guimarães, A. P. D. C., Marques, C. A. B., Fernandes, R. A., Filho, C. H. F. R., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232113588 · Cited by 8
Yin and yang of interferons: lessons from the coronavirus disease 2019 (COVID-19) pandemic
Akusjärvi, S. S., & Zanoni, I. (2024) · Current Opinion in Immunology · doi:10.1016/j.coi.2024.102423 · Cited by 17
CASA: a comprehensive database resource for the COVID-19 Alternative Splicing Atlas
Chen, Y., Wang, G., Li, J., Xia, L., Zhu, L., Li, W., Luo, Q., Liao, Y., Lin, Y., Bi, L., et al. (2022) · Journal of Translational Medicine · doi:10.1186/s12967-022-03699-8 · Cited by 8
Topoisomerase 1 inhibition therapy protects against SARS-CoV-2-induced inflammation and death in animal modelsPreprint
Ho, J., Mok, B. W.-Y., Campisi, L., Jordan, T. X., Yildiz, S., Parameswaran, S., Wayman, J. A., Gaudreault, N. N., Meekins, D. A., Indran, S. V., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.12.01.404483 · Cited by 8
Ageing impairs the airway epithelium defence response to SARS-CoV-2Preprint
Capraro, A., Wong, S. L., Adhikari, A., Allan, K. M., Patel, H. R., Zhong, L., Raftery, M. J., Jaffé, A., Yeang, M., Aggarwal, A., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.05.437453 · Cited by 9
Alpha- and betacoronavirus cis-acting RNA elements
Madhugiri, R., Nguyen, H. V., Slanina, H., & Ziebuhr, J. (2024) · Current Opinion in Microbiology · doi:10.1016/j.mib.2024.102483 · Cited by 7
SARS-CoV-2 Selectively Induces the Expression of Unproductive Splicing Isoforms of Interferon, Class I MHC, and Splicing Machinery Genes
Dias, T. L., Mamede, I., de Toledo, N. E., Queiroz, L. R., de Castro, Í. M. S., Polidoro, R. B., Del‐Bem, L., Nakaya, H. I., & Franco, G. R. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25115671 · Cited by 7
Nuclear RNA-binding proteins meet cytoplasmic viruses
Castelló, A., & Kamel, W. (2025) · RNA · doi:10.1261/rna.080313.124 · Cited by 7
A comprehensive review of current insights into the virulence factors of SARS-CoV-2
Wang, Y., Xia, B., & Gao, Z. (2025) · Journal of Virology · doi:10.1128/jvi.02049-24 · Cited by 7
Pattern Recognition Receptors (PRRs) Expression and Activation in COVID-19 and Long COVID: From SARS-CoV-2 Escape Mechanisms to Emerging PRR-Targeted Immunotherapies
Maddaloni, L., Bugani, G., Fracella, M., Bitossi, C., D’Auria, A., Aloisi, F., Azri, A., Santinelli, L., M’hadheb-Gharbi, M. B., Pierangeli, A., et al. (2025) · Microorganisms · doi:10.3390/microorganisms13092176 · Cited by 8
Development of a recombinant nucleocapsid protein‐based ELISA for the detection of IgM and IgG antibodies to SARS‐CoV‐2
Ranjbar, M., Asadi, M., Nourigorji, M., Sarkari, B., Mostafavi‐Pour, Z., Zomorodian, K., Shabaninejad, Z., Taheri‐Anganeh, M., Maleksabet, A., Moghadami, M., et al. (2021) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.2308 · Cited by 6
SARS-CoV-2 variant-specific differences in inhibiting the effects of the PKR-activated integrated stress response
Christ, W., Klingström, J., & Tynell, J. (2023) · Virus Research · doi:10.1016/j.virusres.2023.199271 · Cited by 8
SARS‐CoV‐2 NSP12 utilizes various host splicing factors for replication and splicing regulation
Yang, L., Zeng, X., Luo, R., Ren, S., Liang, L., Huang, Q., Tang, Y., Fan, H. X., Ren, H., Zhang, W., et al. (2024) · Journal of Medical Virology · doi:10.1002/jmv.29396 · Cited by 7
Immune response stability to the SARS-CoV-2 mRNA vaccine booster is influenced by differential splicing of HLA genes
Santos-Rebouças, C. B., Ferreira, C. D. S., Nogueira, J. D. S., Brustolini, O. J. B., de Almeida, L. G. P., Gerber, A. L., Guimarães, A. P. D. C., Piergiorge, R. M., Struchiner, C. J., Pôrto, L. C., et al. (2024) · Scientific Reports · doi:10.1038/s41598-024-59259-1 · Cited by 7
Computational Methods to Study Human Transcript Variants in COVID-19 Infected Lung Cancer Cells
Sun, J., Fahmi, N. A., Nassereddeen, H., Cheng, S. L. A., Martinez, I., Fan, D., Yong, J., & Zhang, W. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22189684 · Cited by 7
HYGIEIA: HYpothesizing the Genesis of Infectious Diseases and Epidemics through an Integrated Systems Biology Approach
Ward, B., Yombi, J. C., Balligand, J., Cani, P. D., Collet, J., Greef, J. D., Dewulf, J. P., Gatto, L., Haufroid, V., Jodogne, S., et al. (2022) · Viruses · doi:10.3390/v14071373 · Cited by 7
Comparison of Intracellular Transcriptional Response of NHBE Cells to Infection with SARS-CoV-2 Washington and New York Strains
Scott, T. M., Solis‐Leal, A., Lopez, J. B., Robison, R. A., Berges, B. K., & Pickett, B. E. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.1009328 · Cited by 7
Blood RNA alternative splicing events as diagnostic biomarkers for infectious disease
Zhang, Z., Sauerwald, N., Cappuccio, A., Ramos, I., Nair, V. D., Nudelman, G., Zaslavsky, E., Ge, Y., Gaitas, A., Ren, H., et al. (2023) · Cell Reports Methods · doi:10.1016/j.crmeth.2023.100395 · Cited by 7
Understanding COVID-19 progression with longitudinal peripheral blood mononuclear cell proteomics: Changes in the cellular proteome over time
Leite, G. G. F., Brunialti, M. K. C., Pietrobom, P. M. P., Ferreira, P. R. A., Arakaki, J. S. O., Cunha‐Neto, E., Ferreira, B. L., Ronsein, G. E., Tashima, A. K., & Salomão, R. (2023) · iScience · doi:10.1016/j.isci.2023.107824 · Cited by 7
Modulation of various host cellular machinery during COVID‐19 infection
Malvankar, S., Singh, A., Kumar, Y., Sahu, S., Shah, M., Murghai, Y., Seervi, M., Srivastava, R. K., & Verma, B. (2023) · Reviews in Medical Virology · doi:10.1002/rmv.2481 · Cited by 7
Therapeutic potential of natural alkaloid emetine against emerging COVID-19 and future viral pandemics
Dinda, B., Dinda, S., Dinda, M., Sarma, I. S., Majumdar, S., & Saha, S. (2024) · European Journal of Medicinal Chemistry Reports · doi:10.1016/j.ejmcr.2024.100173 · Cited by 6
Human Coronavirus-229E Hijacks Key Host-Cell RNA-Processing Complexes for Replication
Sarkar, S., Feng, S., Mitchell, H. D., Berger, M. R., Zhang, T., Attah, I. K., Hutchinson-Bunch, C. M., Prozapas, V. N., Engbrecht, K. M., King, S. J., et al. (2025) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5c00400 · Cited by 6
Nucleic Acid Detection through RNA‐Guided Protease Activity in Type III‐E CRISPR‐Cas Systems
He, Q., Lei, X., Liu, Y., Wang, X., Ji, N., Yin, H. H., Wang, H., Zhang, H., & Yu, G. (2023) · ChemBioChem · doi:10.1002/cbic.202300401 · Cited by 6
Epigenetic repression of antiviral genes by SARS-CoV-2 NSP1
Anastasakis, D. G., Benhalevy, D., Çuburu, N., Altan‐Bonnet, N., & Hafner, M. (2024) · PLoS ONE · doi:10.1371/journal.pone.0297262 · Cited by 6
Ribosome stalling during c-myc translation presents actionable cancer cell vulnerability
Khaket, T. P., Rimal, S., Wang, X., Bhurtel, S., Wu, Y.-C., & Lu, B. (2024) · PNAS Nexus · doi:10.1093/pnasnexus/pgae321 · Cited by 6
Interaction of Newcastle disease virus V protein with EFTUD2 modulates MDA5 pathway to suppress viral replication
Yin, H., Zhang, F., Zhou, Z., Huang, Y., & Chen, R. (2025) · Poultry Science · doi:10.1016/j.psj.2025.105470 · Cited by 6
Step‐by‐step design of proteins for small molecule interaction: A review on recent milestones
Pereira, J. M. R., Vieira, M., & Santos, S. M. (2021) · Protein Science · doi:10.1002/pro.4098 · Cited by 7
Co-Regulation of Protein Coding Genes by Transcription Factor and Long Non-Coding RNA in SARS-CoV-2 Infected Cells: An In Silico Analysis
Saha, C., Laha, S., Chatterjee, R., & Bhattacharyya, N. P. (2021) · Non-Coding RNA · doi:10.3390/ncrna7040074 · Cited by 6
How SARS-CoV-2 dodges immune surveillance and facilitates infection: an analytical review
Wang, Q., Wu, X., Mao, Q., Gao, F., Liu, M., Song, Z., Bian, L., & Liang, Z. (2022) · Expert Review of Anti-infective Therapy · doi:10.1080/14787210.2022.2078307 · Cited by 5
Single-cell RNA-sequencing data analysis reveals a highly correlated triphasic transcriptional response to SARS-CoV-2 infection
Sánchez, P. A. G., & Elena, S. F. (2022) · Communications Biology · doi:10.1038/s42003-022-04253-4 · Cited by 8
SARS-CoV-2 infection severity and mortality is modulated by repeat-mediated regulation of alternative splicing
Mehta, P., Chattopadhyay, P., Ravi, V., Tarai, B., Budhiraja, S., & Pandey, R. (2023) · Microbiology Spectrum · doi:10.1128/spectrum.01351-23 · Cited by 6
Non-Structural Proteins (Nsp): A Marker for Detection of Human Coronavirus Families
Tamayo‐Ordoñez, M. C., Rosas-García, N. M., Ayil‐Gutiérrez, B. A., Bello–López, J. M., Tamayo‐Ordóñez, F. A., Franseschi, F. A., Damas‐Damas, S., & Tamayo-Ordóñez, Y. D. J. (2023) · Pathogens · doi:10.3390/pathogens12091185 · Cited by 7
The role of post-transcriptional regulation in SARS-CoV-2 infection and pathogenicity
Wang, X., Chang, Z., Zhao, T., Zhong, W., Shi, J., Wang, G., & Xu, X. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1256574 · Cited by 6
RNA sequence analysis of nasopharyngeal swabs from asymptomatic and mildly symptomatic patients with COVID-19
Faridl, M., Mellyani, K., Khoirunnisa, K., Septiani, P., Giri-Rachman, E. A., Nugrahapraja, H., Rahmawati, E., Alamanda, C. N. C., Ristandi, R. B., Rachman, R. W., et al. (2022) · International Journal of Infectious Diseases · doi:10.1016/j.ijid.2022.06.035 · Cited by 7
Integrative genomics important to understand host–pathogen interactions
Mehta, P., Swaminathan, A., Yadav, A., Chattopadhyay, P., Shamim, U., & Pandey, R. (2022) · Briefings in Functional Genomics · doi:10.1093/bfgp/elac021 · Cited by 6
Translation landscape of SARS-CoV-2 noncanonical subgenomic RNAs
Wu, K., Wang, D., Wang, J., & Zhou, Y. (2022) · Virologica Sinica · doi:10.1016/j.virs.2022.09.003 · Cited by 6
Discovery and functional interrogation of SARS-CoV-2 protein-RNA interactionsPreprint
Yeo, G. W.-M., Xiang, J. S., Mueller, J., Luo, E., Yee, B., Schafer, D., Schmok, J., Tan, F., Rothamel, K., McVicar, R. N., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.02.21.481223 · Cited by 6
Early innate immune response and evolution of a SARS-CoV-2 furin cleavage site inactive variant in bat cells
Baid, K., Shrivastava, S., Luc, J., Richard, D. J., Aguiar, J. A., Machado, Y. J., Aicher, S., Siwak, K. C., LeBlanc, E. V., Khatooni, Z., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115929 · Cited by 7
Self-citation
NamiRNA‐Enhancer Network: The Changing Era Challenge and Chance of miRNA
Chen, L., Liang, Y. J., Wei, H., Liu, M., Wu, J. C., Li, W., Li, W., Jin, Y., Li, Y., Zhao, W., et al. (2025) · Advanced Science · doi:10.1002/advs.202506830 · Cited by 8
Self-citation
Reprogramming innate immunity through viral interference: A double-edged strategy for enhancing and containing gene therapies
Liu, Z., & Song, S. (2026) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2026.102911 · Cited by 5
SARS-CoV-2 disrupts host gene networks: Unveiling key hub genes as potential therapeutic targets for COVID-19 management
Majewska, M., Maździarz, M. A., Krawczyk, K., Paukszto, Ł., Makowczenko, K. G., Lepiarczyk, E., Lipka, A., Wiszpolska, M., Górska, A., Moczulska, B., et al. (2024) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2024.109343 · Cited by 5
Decoding the genome of SARS-CoV-2: a pathway to drug development through translation inhibition
Wu, S., Xiao, T., Chen, H., & Li, X. (2024) · RNA Biology · doi:10.1080/15476286.2024.2433830 · Cited by 5
Transcription Kinetics in the Coronavirus Life Cycle
Grelewska‐Nowotko, K., Elhag, A. E., & Turowski, T. W. (2025) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.70000 · Cited by 5
Structural insights into the assembly and regulation of 2′-O RNA methylation by SARS-CoV-2 nsp16/nsp10
Misra, A., Rahisuddin, R., Parihar, M., Arya, S., Viswanathan, T., Jackson, N. D., Qi, S., Chan, S., Harris, R. S., Martínez‐Sobrido, L., et al. (2025) · Structure · doi:10.1016/j.str.2025.03.009 · Cited by 6
Understanding COVID-19 Pathogenesis: A Drug-Repurposing Effort to Disrupt Nsp-1 Binding to Export Machinery Receptor Complex
Vasudevan, S., & Baraniuk, J. N. (2021) · Pathogens · doi:10.3390/pathogens10121634 · Cited by 5
The landscape of differential splicing and transcript alternations in severe COVID ‐19 infection
Mukherjee, S. B., Mukherjee, S., Detroja, R., & Frenkel‐Morgenstern, M. (2023) · FEBS Journal · doi:10.1111/febs.16723 · Cited by 5
Investigation of the effects of N-Acetylglucosamine on the stability of the spike protein in SARS-CoV-2 by molecular dynamics simulations
Tekin, E. D. (2023) · Computational and Theoretical Chemistry · doi:10.1016/j.comptc.2023.114049 · Cited by 5
Application of weighted gene co-expression network and immune infiltration for explorations of key genes in the brain of elderly COVID-19 patients
Huang, L., Qin, W., Guo, Z., Li, X., Li, F., & Wang, X. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1157179 · Cited by 5
Priority index for critical Covid-19 identifies clinically actionable targets and drugs
Zhang, Z., Wang, S., Jiang, L., Wei, J., Lu, C., Li, S., Diao, Y., Fang, Z., He, S., Tan, T., et al. (2024) · Communications Biology · doi:10.1038/s42003-024-05897-0 · Cited by 5
Self-citation
Inhibition of SARS-CoV-2 growth in the lungs of mice by a peptide-conjugated morpholino oligomer targeting viral RNA
Sakai, A., Singh, G., Khoshbakht, M., Bittner, S., Löhr, C. V., Diaz-Tapia, R., Warang, P., White, K. M., Luo, L. L., Tolbert, B. S., et al. (2024) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2024.102331 · Cited by 5
Self-citation
Identification of Novel COVID-19 Biomarkers by Multiple Feature Selection Strategies
Zhang, S., Qu, R., Wang, P., & Wang, S. (2021) · Computational and Mathematical Methods in Medicine · doi:10.1155/2021/2203636 · Cited by 5
Selenoprotein S Interacts with the Replication and Transcription Complex of SARS-CoV-2 by Binding Nsp7
Ghelichkhani, F., Gonzalez, F. A., Kapitonova, M. A., & Rozovsky, S. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168008 · Cited by 7
NOVEL MUTATIONS IN THE NON-STRUCTURE PROTEIN 2 OF SARS-CoV-2
Nakhaei, M., Ghoreshi, Z., Rukerd, M. R. Z., Askarpour, H., & --, N. (2023) · Mediterranean Journal of Hematology and Infectious Diseases · doi:10.4084/mjhid.2023.059 · Cited by 5
SARS-CoV-2: Insights from the Immunopathogenesis and Current Clinical Diagnosis and Therapeutic Strategies
Sharma, S., Sharma, U., Chaudhary, A., Naithani, M., Naithani, P., Prashar, S., Sharma, B., Nagar, P. K., Bhukya, P. L., halerao, U. B., et al. (2021) · Journal of Immunological Sciences · doi:10.29245/2578-3009/2021/2.1207 · Cited by 5
Modeling the SARS-CoV-2 nsp1–5’-UTR complex via extended ensemble simulationsPreprint
Sakuraba, S., Qilin, X., Kasahara, K., Iwakiri, J., & Kono, H. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.02.24.432807 · Cited by 5
The preference signature of the SARS-CoV-2 Nucleocapsid NTD for its 5’-genomic RNA elementsPreprint
Korn, S. M., Dhamotharan, K., & Schlundt, A. (2022) · Research Square · doi:10.21203/rs.3.rs-1445747/v1 · Cited by 5
Universal features of Nsp1-mediated translational shutdown by coronaviruses
Schubert, K., Karousis, E. D., Ban, I., Lapointe, C. P., Leibundgut, M., Bäumlin, E., Kummerant, E., Scaiola, A., Schönhut, T., Ziegelmüller, J., et al. (2023) · doi:10.1101/2023.05.31.543022 · Cited by 5
Failing to account for RNA quantity inflates background and leads to the misleading appearance that PRC2 and GFP bind to RNA in vivoPreprint
Guo, J. K., Blanco, M. R., & Guttman, M. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.11.02.621417 · Cited by 5
Self-citation
Genome-wide mapping of mesoscale neuronal RNA organization and condensationPreprint
Becker, L. A., Quinodoz, S. A., Comi, T. J., Kimchi, O., Knowles, D. A., & Brangwynne, C. P. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.19.649570 · Cited by 5
Self-citation
Predict SARS-CoV-2 genome interactions based on RNA language models
Shen, W.-W., Li, Y.-X., Zhu, L.-C., & Huang, T. (2025) · Biosafety and Health · doi:10.1016/j.bsheal.2025.09.006 · Cited by 2
Viral Modulation of Host Splicing
Begg, B. E., Ferretti, M., Tracey, M. P., & Lynch, K. W. (2025) · Annual Review of Virology · doi:10.1146/annurev-virology-092623-102539 · Cited by 5
Systems-wide view of host-pathogen interactions across COVID-19 severities using integrated omics analysis
Singh, M. S., Pyati, A., Rubi, R. D., Subramanian, R., Muley, V. Y., Ansari, M. A., & Yellaboina, S. (2024) · iScience · doi:10.1016/j.isci.2024.109087 · Cited by 4
Dissecting infectious bronchitis virus-induced host shutoff at the translation level
Zhao, Y., Huang, Y., Liukang, C., Yang, R., Tang, L., Sun, L., Zhao, Y., & Zhang, G. (2024) · Journal of Virology · doi:10.1128/jvi.00830-24 · Cited by 4
Broad‐Spectrum Antiviral Agents against SARS‐CoV‐2 Variants Inhibit the Conserved Viral Protein Nsp1–RNA Interaction
Byun, W. G., Lee, M., Ko, M., Lee, J. H., Yi, S., Lee, J., Kim, S., & Park, S. B. (2024) · Angewandte Chemie International Edition · doi:10.1002/anie.202405472 · Cited by 5
Differentially expressed ncRNAs as key regulators in infection of human bronchial epithelial cells by the SARS-CoV-2 Delta variant
Ranches, G., Hackl, H., Zaderer, V., Ploner, M., Posch, W., Wilflingseder, D., Kummer, K. K., & Hüttenhofer, A. (2025) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2025.102559 · Cited by 4
Altered DNA Methylation Pattern Contributes to Differential Epigenetic Immune Signaling in the Upper Respiratory Airway of Unvaccinated COVID-19 Patients
Govender, M., Das, J., Hopkins, F. R., Svanberg, C., Nordgren, J., Hagbom, M., Klingström, J., Nilsdotter-Augustinsson, Å., Yong, Y., Velu, V., et al. (2025) · Cells · doi:10.3390/cells14211673 · Cited by 3
RNA–protein interactomes as invaluable resources to study RNA viruses: Insights from SARS CoV‐2 studies
Koliński, M., Kałużna, E. M., & Piwecka, M. (2022) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1727 · Cited by 6
COVID-19 mortality is associated with pre-existing impaired innate immunity in health conditions
Lee, M. E., Chang, Y., Ahmadinejad, N., Johnson-Agbakwu, C., Bailey, C. V., & Liu, L. (2022) · PeerJ · doi:10.7717/peerj.13227 · Cited by 3
Non-structure protein ORF1ab (NSP8) in SARS-CoV-2 contains potential γδT cell epitopes
Du, B., Guo, Y., Li, G., Zhu, Y., Wang, Y., & Xi, X. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.936272 · Cited by 4
Alternative splicing in Atlantic salmon head kidney and SHK-1 cell line during the Piscirickettsia salmonis infection: A comparative transcriptome survey
Leal, Y., Valenzuela‐Muñoz, V., & Gallardo‐Escárate, C. (2023) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2023.109127 · Cited by 4
Harnessing ZIKV NS2A RNA for alleviating acute hepatitis and cytokine release storm by targeting translation machinery
Zhu, J., Wu, R., Yang, T., Yuan, Y., Liu, G., Chen, S., Chen, Z., Liu, S., Wang, S., Li, D., et al. (2024) · Hepatology · doi:10.1097/hep.0000000000001101 · Cited by 4
Collection of Monoclonal Antibodies Targeting SARS-CoV-2 Proteins
Matešić, M. P., Brlić, P. K., Roviš, T. L., Šafranko, Ž. M., Chaouat, A., Miklić, K., Malić, S., Ivanković, N., Schubert, M., Bertoglio, F., et al. (2022) · Viruses · doi:10.3390/v14020443 · Cited by 4
Uncovering the geometry of protein interaction network: The case of SARS-CoV-2 protein interactome
Lecca, P. (2023) · AIP conference proceedings · doi:10.1063/5.0163052 · Cited by 4
Subgenomic and negative sense RNAs are not markers of active replication of SARS-CoV-2 in nasopharyngeal swabsPreprint
Chamings, A., Bhatta, T. R., & Alexandersen, S. (2021) · medRxiv · doi:10.1101/2021.06.29.21259511 · Cited by 4
Xist spatially amplifies SHARP recruitment to balance chromosome-wide silencing and specificity to the X chromosomePreprint
Jachowicz, J. W., Strehle, M. M., Banerjee, A. K., Thai, J., Blanco, M. R., & Guttman, M. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.10.27.466149 · Cited by 4
Self-citation
System-wide hematopoietic and immune signaling aberrations in COVID-19 revealed by deep proteome and phosphoproteome analysisPreprint
Kaneko, T., Esmail, S., Voss, C., Martin, C. M., Slessarev, M., Hovey, O. F. J., Liu, X., Ye, M., Kim, S. H., Fraser, D. D., et al. (2021) · medRxiv · doi:10.1101/2021.03.19.21253675 · Cited by 4
SARS-CoV-2 nsp16 is regulated by host E3 ubiquitin ligases, UBR5 and MARCHF7Preprint
Tian, L., Zhao, Z., Gao, W., Liu, Z., Li, X., Zhang, W., & Li, Z. (2024) · eLife · doi:10.7554/elife.102277 · Cited by 4
Recognition and cleavage of human tRNA methyltransferase TRMT1 by the SARS-CoV-2 main protease
D'Oliviera, A., Dai, X., Mottaghinia, S., Olson, S., Geissler, E. P., Etienne, L., Zhang, Y., & Mugridge, J. S. (2025) · eLife · doi:10.7554/elife.91168.3 · Cited by 13
Binding of SARS-CoV-2 Nonstructural Protein 1 to 40S Ribosome Inhibits mRNA Translation
Nguyen, H. V., Nguyen, H. L., & Li, M. S. (2024) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.4c01391 · Cited by 3
Escape from SARS-CoV-2 Nsp1-mediated host shutoff by TIAR transcript reveals general features of Nsp1 resistance
Galbraith, C., Stolz, M., Tersteeg, S., Andrews, E., Patel, T. R., & Khaperskyy, D. A. (2025) · RNA · doi:10.1261/rna.080715.125 · Cited by 3
The Coronavirus Replication–Transcription Complex
Madhugiri, R., Slanina, H., Saleem-Batcha, R., & Ziebuhr, J. (2026) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-052621-091439 · Cited by 3
SARS-CoV-2 and MERS-CoV disrupt host protein synthesis via nsp1 with differential effects on the integrated stress response
Parenti, N. A., Cusic, R., Renner, D. M., Jackson, N. D., Ye, C., Tan, L. H., Pfannenstiel, J. J., Fehr, A. R., Cohen, N. A., Martínez‐Sobrido, L., et al. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2536296123 · Cited by 2
Redundant and distinct mechanisms suppress innate immune activation during SARS-CoV-2 infection
Zhou, F., Periasamy, S., Jackson, N. D., Cheng, W. S., Soto-Acosta, R., Tripathi, A., Kedarinath, K., Ilinykh, P. A., Ye, C., Chauhan, S., et al. (2026) · PLoS Biology · doi:10.1371/journal.pbio.3003808 · Cited by 3
Suppression of interferon α and γ response by Huwe1-mediated Miz1 degradation promotes SARS-CoV-2 replication
Arunagiri, V., Cooper, L. M., Dong, H., Class, J., Biswas, I., Vahora, S., Deshpande, R., Gopani, K. H., Hu, G., Richner, J. M., et al. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1388517 · Cited by 3
A Primer on Proteomic Characterization of Intercellular Communication in a Virus Microenvironment
Kostas, J. C., Brainard, C. S., & Cristea, I. M. (2025) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2025.100913 · Cited by 4
Anti-interferon armamentarium of human coronaviruses
Khatun, O., Kaur, S., & Tripathi, S. (2025) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-025-05605-z · Cited by 3
Impact of nutrition on long COVID
Thangaleela, S., & Wang, C. (2025) · Sports Medicine and Health Science · doi:10.1016/j.smhs.2025.09.002 · Cited by 3
scMOVIR: a single-cell multi-omics database for human viral infections and immune responses
Zhang, X., Yang, S., Xu, X., Lin, Y., Sun, H., Zhu, B., Zhao, W., Zhou, B., Lou, Y., Wang, X., et al. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf1153 · Cited by 3
Herpes simplex virus 1 fluidizes the nucleus, enabling condensate formation
Herzog, N. L., Shu, T., Kidiyoor, G. R., Keegan, S., Korchi, F., Chenoweth, D. M., Zhang, H., Mohr, I., Wilson, A. C., & Holt, L. J. (2026) · Molecular Cell · doi:10.1016/j.molcel.2026.02.005 · Cited by 3
The Potential of Eukaryotic Cell-Free Systems as a Rapid Response to Novel Zoonotic Pathogens: Analysis of SARS-CoV-2 Viral Proteins
Ramm, F., Dondapati, S. K., Trinh, H. A., Wenzel, D., Walter, R. M., Zemella, A., & Kubick, S. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.896751 · Cited by 3
An Updated and Focused Review on Heterocyclic Inhibitors for SARSCoV and SARS-CoV-2 3CLpro
Alam, O., Manaithiya, A., Mittal, S., Naim, M. J., Imran, M., Alshrari, A. S., Sheikh, A. A., & Khan, I. A. (2022) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557522666220511125102 · Cited by 3
The Landscape of Expressed Chimeric Transcripts in the Blood of Severe COVID-19 Infected Patients
Mukherjee, S. B., Detroja, R., Mukherjee, S., & Frenkel‐Morgenstern, M. (2023) · Viruses · doi:10.3390/v15020433 · Cited by 3
Regulating Select Agent Chimeras: Defining the Problem(s) Through the Lens of SARS-CoV-1/SARS-CoV-2 Chimeric Viruses
Wells, E. W., & Parker, M. T. (2023) · Health Security · doi:10.1089/hs.2023.0008 · Cited by 3
Aminoacyl-tRNA synthetase interactions in SARS-CoV-2 infection
Khan, D., & Fox, P. L. (2023) · Biochemical Society Transactions · doi:10.1042/bst20230527 · Cited by 3
Viral RNA Is a Hub for Critical Host–Virus Interactions
Castelló, A., & Iselin, L. (2023) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-40086-5_13 · Cited by 3
NSP6 inhibits the production of ACE2-containing exosomes to promote SARS-CoV-2 infectivity
Lv, X., Chen, R., Liang, T., Peng, H., Fang, Q., Xiao, S., Liu, S., Hu, M., Yu, F., Cao, L., et al. (2024) · mBio · doi:10.1128/mbio.03358-23 · Cited by 3
Peptide nucleic acids can form hairpins and bind RNA-binding proteins
Zhong, Y., Wilkinson‐White, L. E., Zhang, E., Mohanty, B., Zhang, B. B., McRae, M. S., Luo, R., Allport, T. A., Duff, A. P., Zhao, J., et al. (2024) · PLoS ONE · doi:10.1371/journal.pone.0310565 · Cited by 3
Interactions of SARS-CoV-2 with Human Target Cells—A Metabolic View
Eisenreich, W., Leberfing, J., Rudel, T., Heesemann, J., & Goebel, W. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25189977 · Cited by 3
Longitudinal Assessment of Nasopharyngeal Biomarkers Post-COVID-19: Unveiling Persistent Markers and Severity Correlations
Calvo, F. J. R., Rabanal‐Ruiz, Y., Verdugo-Moreno, G., Ramírez, N. B., Bodoque-Villar, R., Durán‐Prado, M., Illescas, S., Chicano‐Gálvez, E., Romero, F. J. G., Martínez-Alarcón, J., et al. (2024) · Journal of Proteome Research · doi:10.1021/acs.jproteome.4c00536 · Cited by 3
Inference of differential kinase interaction networks with KINference
Meyerhöfer, N., Krogan, N. J., Polacco, B. J., & Blumenthal, D. B. (2025) · Bioinformatics · doi:10.1093/bioinformatics/btaf349 · Cited by 3

Authors: Banerjee, A. K., Blanco, M. R., Bruce, E. A., Honson, D. D., Chen, L. M., Chow, A., Bhat, P., Ollikainen, N., Quinodoz, S. A., Loney, C., Thai, J., Miller, Z. D., Lin, A. E., Schmidt, M. M., Stewart, D. G., Goldfarb, D., De Lorenzo, G., Rihn, S. J., Voorhees, R. M., Botten, J. W., Majumdar, D., & Guttman, M.
Affiliations: University of Southern California (US)
California Institute of Technology (US)
University of Vermont (US)
MRC University of Glasgow Centre for Virus Research (GB)
Broad Institute (US)
Corresponding author: Majumdar, Devdoot
Guttman, Mitchell
ORCID: Banerjee, Abhik K.
Blanco, Mario R.
Bruce, Emily A.
Honson, Drew D.
Chen, Linlin M.
Chow, Amy
Bhat, Prashant
Ollikainen, Noah
Quinodoz, Sofia A.
Loney, Colin
Miller, Zachary D.
Lin, Aaron E.
Schmidt, Madaline M.
Stewart, Douglas G.
Goldfarb, Daniel
De Lorenzo, Giuditta
Rihn, Suzannah J.
Voorhees, Rebecca M.
Botten, Jason W.
Majumdar, Devdoot
Guttman, Mitchell
Venue: Cell
Publisher: Elsevier BV
Published: 2020-11
Volume: 183
Issue: 5
Pages: 1325-1339.e21
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/j.cell.2020.10.004
PMC: PMC7543886
OpenAlex: W3092296275
Cited by: 583
References: 100
Citations by year: 2026: 40 · 2025: 64 · 2024: 80 · 2023: 106 · 2022: 149 · 2021: 129 · 2020: 15
FWCI: 13.29
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor)
Locations: Cell (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (acceptedVersion, cc-by-sa)
CaltechAUTHORS (California Institute of Technology) (submittedVersion, cc-by)
Funders: Wellcome Trust
University of Vermont
Heritage Medical Research Institute
American Cancer Society
Foundation for the National Institutes of Health
Chan Zuckerberg Initiative
California Institute of Technology
New York Stem Cell Foundation
Topics: Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
Keywords: SARS-CoV-2, COVID-19 pandemic, host-virus interaction, nsp16, Nsp1, 18S rRNA, mRNA translation inhibition, nsp8, nsp9, 7SL RNA, signal recognition particle, protein trafficking, viral pathogenesis
MeSH terms: A549 Cells, COVID-19, SARS-CoV-2, Animals, Chlorocebus aethiops, Humans, Interferons, RNA Splicing, RNA, Messenger, RNA, Ribosomal, 18S, Protein Biosynthesis, Vero Cells, Viral Nonstructural Proteins, Signal Recognition Particle, RNA, Small Cytoplasmic, Protein Transport, Host-Pathogen Interactions, HEK293 Cells

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

SARS-CoV-2 Disrupts Splicing, Translation, and Protein Trafficking to Suppress Host Defenses

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks