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 accessAbstract
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.
Overview
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
Cites
Statistics
Verification
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?
In the citing paper
“A predominant strategy appears to be the inhibition of the type I interferon response58–60 at multiple points, including impaired recognition of viral RNA61,62, decreased nuclear translocation of pro-inflammatory transcription factors (such as IRF3, IRF7 and STAT1)61,63 and suppression of STAT1 and STAT2 phosphorylation64,65.”
From Immunological mechanisms of vaccine-induced protection against COVID-19 in humans (2021) · cites this paper as [61]
In the citing paper
“SARS-CoV-2-derived non-structural protein 16 (NSP16) suppresses global mRNA splicing and diminishes recognition of viral RNA by intracellular helicase receptors, NSP1 leads to global inhibition of mRNA translation by binding to the 18S ribosomal RNA in the mRNA entry channel, and NSP8 and NSP9 interfere with protein trafficking to the cell membrane; all three mechanisms independently leading to”
From COVID-19 and the human innate immune system (2021) · cites this paper as Banerjee et al., 2020
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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
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
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-citationThe 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
4 of the 100 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 401–500 of 590
Dysregulation of ion transport in the lung epithelium infected with SARS-CoV-2
Dada, L. A., Vagin, O., & Sznajder, J. I. (2021) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00170.2021 · Cited by 3
Gankovskaya, L. V., Zinina, E., Ганковский, В. А., & Semushkin, A. R. (2021) · Immunologiya · doi:10.33029/0206-4952-2021-42-3-222-231 · Cited by 3
Achour, A. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111722 · Cited by 3
Detecting and Profiling Endogenous RNA G-Quadruplexes in the Human Transcriptome
Zhang, R., Liu, Y., Zhang, X., Xiao, K., Hou, Y., Liu, H., & Sun, X. S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158012 · Cited by 3
Antiviral Immunity in SARS-CoV-2 Infection: From Protective to Deleterious Responses
Mihăescu, G., Chifiriuc, M. C., Vrâncianu, C. O., Constantin, M., Filip, R., Popescu, M. R., Burlibaşa, L., Nicoară, A. C., Bolocan, A., Iliescu, C., et al. (2021) · Microorganisms · doi:10.3390/microorganisms9122578 · Cited by 3
Genetic Engineering Systems to Study Human Viral Pathogens from the Coronaviridae Family
Galkin, S., Anisenko, A. N., Shadrina, O., & Gottikh, M. (2022) · Molecular Biology · doi:10.1134/s0026893322010022 · Cited by 3
Pan, Y., Chandrashekaran, I. R., Tennant, L., Rossjohn, J., & Littler, D. R. (2023) · PLoS ONE · doi:10.1371/journal.pone.0283194 · Cited by 3
Charles L Christian: model physician scientist and mentor
Crow, M. K. (2021) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2019-216630 · Cited by 3
Searching and Analyzing Patent-Relevant Information for Evaluating COVID-19 InnovationPreprint
Falciola, L., & Barbieri, M. (2020) · SSRN Electronic Journal · doi:10.2139/ssrn.3771756 · Cited by 3
Stewart, R., Yan, K., Ellis, S. A., Bishop, C., Dumenil, T. D., Tang, B., Nguyen, W., Larcher, T., Parry, R. H., Sng, J. D. J., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.12.22.521696 · Cited by 3
Increased neurovirulence of omicron BA.5 over BA.1 in human brain organoids and K18-hACE2 micePreprint
Stewart, R., Ellis, S. A., Yan, K., Dumenil, T. D., Bishop, C., Tang, B., Nguyen, W., Larcher, T., Sullivan, R., Lor, M., et al. (2023) · Research Square · doi:10.21203/rs.3.rs-2702556/v1 · Cited by 2
Synergy Between TNFα and Proteostatic Stress Drives Cell Death and Guard ImmunityPreprint
Sonnett, M., Centofanti, E., Boersma, S., Brambach, M., Peshkin, L., Tatavosian, R., Oyler‐Yaniv, A., & Oyler, J. E. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.12.598679 · Cited by 4
Altina, N. H., Maranon, D. G., Anderson, J. R., Donaldson, M. K., Elmegerhi, S., Clair, L. A. S., Perera, R. M., Geiss, B. J., & Wilusz, J. (2024) · Virology · doi:10.1016/j.virol.2024.109986 · Cited by 3
Structure–function mapping and mechanistic insights on the SARS CoV2 Nsp1
Salgueiro, B. A., Saramago, M., Tully, M. D., Arraiano, C. M., Moe, E., Matos, R. G., Matias, P. M., & Romão, C. V. (2024) · Protein Science · doi:10.1002/pro.5228 · Cited by 2
E3 Ligases and COVID-19: Insights into Viral Control and Therapeutic Potential
Mishra, M., Islam, S., & Khan, D. (2025) · Biocell · doi:10.32604/biocell.2025.058038 · Cited by 2
SARS-CoV-2 nsp16 is regulated by host E3 ubiquitin ligases, UBR5 and MARCHF7
Tian, L., Zhao, Z., Gao, W., Liu, Z., Li, X., Zhang, W., & Li, Z. (2025) · eLife · doi:10.7554/elife.102277.4 · Cited by 2
Thakur, N., Chakraborty, P., Tufariello, J. M., & Basler, C. F. (2025) · mBio · doi:10.1128/mbio.01071-25 · Cited by 2
SARS-CoV-2 Nsp1 Is a Major Suppressor of HLA Class I and Class II Expression
Schirmeister, I., Eckert, N., Weigang, S., Fuchs, J., Kern, L., Kochs, G., & Halenius, A. (2025) · Viruses · doi:10.3390/v17081083 · Cited by 2
Yang, X., Shen, Y., Tang, B., Zhu, J., Wang, B., Wang, Q., Tian, W., Wuchty, S., Zhang, Z., Liang, Z., et al. (2025) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2025.101068 · Cited by 2
Yao, Y., Huang, N., Huang, X., Yuan, M., Li, K., Ma, Y., Han, J., Zhang, G., & Liu, P. (2025) · mBio · doi:10.1128/mbio.02904-25 · Cited by 3
Nan, J., Shuai, H., Qiao, J., Zeng, R., Du, L., Chen, Y., Yoon, C., Hu, J., Guo, W., Wang, L., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-68795-5 · Cited by 2
Fan, L., Gao, X., Feng, W., Huang, Q., Wei, X., Yang, C., Wu, Y., Shen, X., Zhao, J., Zhou, Y., et al. (2026) · Journal of Virology · doi:10.1128/jvi.00186-26 · Cited by 2
Singh, N. K., Tyagi, A., Ganesh, B., Kaushik, R., Zowalaty, M. E. E., Dhama, K., & Malik, Y. S. (2024) · Elsevier eBooks · doi:10.1016/b978-0-12-818619-0.00090-3 · Cited by 2
Myelin basic protein antagonizes the SARS-CoV-2 protein ORF3a-induced autophagy inhibition
Saratov, G. A., Belogurov, A. A., & Kudriaeva, A. A. (2024) · Biochimie · doi:10.1016/j.biochi.2024.04.011 · Cited by 2
A nanobody interaction with SARS-COV-2 Spike allows the versatile targeting of lentivirus vectors
Alfadhli, A., Bates, T. A., Barklis, R. L., Romanaggi, C., Tafesse, F., & Barklis, E. (2024) · Journal of Virology · doi:10.1128/jvi.00795-24 · Cited by 2
The SARS-CoV-2 ORF6 protein inhibits nuclear export of mRNA and spliceosomal U snRNA
Taniguchi, I. (2024) · PLoS ONE · doi:10.1371/journal.pone.0312098 · Cited by 2
Coronaviruses: Pandemic SARS-CoV-2
Cowling, B. J., & Wong, S. (2024) · Springer eBooks · doi:10.1007/978-1-4939-9544-8_68-1 · Cited by 2
Probiotics mediated control and immunomodulation of SARS-CoV-2 associated pathological conditions
Kumari, P. S., Viswapriya, V., Rajakumari, M. L., & Murugan, S. (2021) · Annals of Phytomedicine An International Journal · doi:10.21276/ap.covid19.2021.10.1.16 · Cited by 1
Ghosh, A., Bhattacharyya, C., Biswas, N. K., & Das, A. K. (2021) · Springer eBooks · doi:10.1007/978-981-33-6827-9_25 · Cited by 2
Immunoediting in SARS-CoV-2: Mutual relationship between the virus and the host
Kheshtchin, N., Bakhshi, P., Arab, S., & Nourizadeh, M. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.108531 · Cited by 2
Xiao, Y., Li, W., Wang, J., Wu, X., & Sheng, B. (2023) · IEEE Transactions on Computational Biology and Bioinformatics · doi:10.1109/tcbb.2023.3283534 · Cited by 2
Research progress on post-transcriptional regulation of antiviral innate immunity
ShaoChun, Y. U. A. N., Yong, G. E., Tao, L. I. N. G., & AnLong, X. U. (2023) · Scientia Sinica Vitae · doi:10.1360/ssv-2023-0138 · Cited by 2
Chen, S. (2020) · DNA and Cell Biology · doi:10.1089/dna.2020.6278 · Cited by 2
SARS-CoV-2 Immunity: Review of Immune Response to Infection and Vaccination
Ahmad, R. (2021) · Bangladesh Journal of Medical Science · doi:10.3329/bjms.v20i5.55398 · Cited by 2
Discovery and Functional Interrogation of the Virus and Host RNA Interactome of SARS-Cov-2 ProteinsPreprint
Xiang, J. S., Mueller, J. R., Luo, E., Yee, B. A., Schafer, D. M., Schmok, J. C., Tan, F. E., Her, H.-L., Chen, C.-Y., Brannan, K. W., et al. (2021) · SSRN Electronic Journal · doi:10.2139/ssrn.3867726 · Cited by 2
Enguita, F. J., Leitão, A. L., McDonald, J. T., Zaksas, V., Das, S., Galeano, D., Taylor, D. M., Wurtele, E. S., Saravia-Butler, A., Baylin, S. B., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.26.485903 · Cited by 2
Maurina, S. F., O'Sullivan, J. P., Sharma, G., Rodríguez, D., MacFadden, A., Cendali, F. I., Henen, M. A., Kieft, J. S., Glasgow, A. A., & Steckelberg, A. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.06.07.544141 · Cited by 2
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 · Cited by 2
MDA5 guards against infection by surveying cellular RNA homeostasisPreprint
Sampaio, N. G., Gearing, L. J., Dias, A. G., Chauveau, L., Odon, V., Cursi, C., Mayer, A., Ratnadiwakara, M., Änkö, M., Hertzog, P. J., et al. (2025) · Research Square · doi:10.21203/rs.3.rs-6466919/v1 · Cited by 2
Yin, L., Liu, M., Shi, Y., Qiu, J., & So, H.-C. (2024) · medRxiv · doi:10.1101/2024.08.29.24312763 · Cited by 2
De novo design of anti-variant COVID-19 vaccine
Goswami, A., Kumar, M., Ullah, S., & Gore, M. M. (2023) · Biology Methods and Protocols · doi:10.1093/biomethods/bpad021 · Cited by 2
Organ‐specific immune response in lethal SARS‐CoV‐2 infection by deep spatial phenotyping
Balachander, A., Lee, B. T. K., Biswas, S. K., Lye, D. C., Lin, R. T. P., Leo, Y., Chui, P., Ng, L. F. P., & Rénia, L. (2022) · Clinical & Translational Immunology · doi:10.1002/cti2.1384 · Cited by 1
Dual transcriptomics data and detection of host-pathogen interactions
Eldem, V., Çınar, Y. U., Çay, S. B., Kuralay, S. C., Kayalar, Ö., Zararsız, G., Bakır, Y., & Dikmen, F. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-95890-5.00012-0 · Cited by 1
Utilizing viral RNA fragments to limit acute inflammation
Zhao, C., & Zhao, W. (2024) · Hepatology · doi:10.1097/hep.0000000000001165 · Cited by 1
Structural Biology of the SARS-CoV-2 replication–transcription complex
Fyfe, C. D., Rogers, C., Payne, A. M., von Soosten, L. C., Santoni, G., & Thorn, A. (2024) · Crystallography Reviews · doi:10.1080/0889311x.2025.2458340 · Cited by 1
Relevance of Antibody-Dependent Enhancement in COVID-19
Rodríguez‐Pinto, D., & Mendoza-Ruiz, M. S. (2025) · Immuno · doi:10.3390/immuno5020020 · Cited by 1
Innate immunity, therapeutic targets and monoclonal antibodies in SARS-CoV-2 infection
Nazir, M., Mir, I. R., Lone, S. A., Muteeb, G., Alam, R., Fomda, A. B., Khan, N., Azhar, A., Fomda, B. A., & Khan, W. H. (2025) · PeerJ · doi:10.7717/peerj.19462 · Cited by 1
Abdallah, A. M., Ansari, H., Shuaib, M., Doudin, A., Yassine, H. M., Shah, S. S. U. D., Mir, F., Emara, M., Elzouki, A.-N., & Cyprian, F. (2025) · Scientific Reports · doi:10.1038/s41598-025-04837-0 · Cited by 1
Characterization of Gene Expression Suppression by Bovine Coronavirus Non-Structural Protein 1
Ohkami, T., Kitashin, I., Kawashima, R., Yoshida, A., Saito, T., Takashima, Y., Kamitani, W., & Nakagawa, K. (2025) · Viruses · doi:10.3390/v17070978 · Cited by 1
The C-terminal Domain of SARS-CoV-2 nsp8 is a Molten Globule in the Absence of Binding Partners
Kurauskas, V., Tonelli, M., Kirchdoerfer, R. N., & Henzler‐Wildman, K. A. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169400 · Cited by 1
Global Evolutionary and Transmission Dynamics of Transmissible Gastroenteritis Virus, 1952–20231
Wang, W., Zhao, Q., Zhu, Z., Wen, W., & Li, X. (2025) · Journal of Integrative Agriculture · doi:10.1016/j.jia.2025.09.026 · Cited by 1
Legionella effector Ceg10 acetylates RPS20 to inhibit host translation and induce cell cycle arrest
Gao, J., Xu, W., Zhou, Z., Lu, L., Ge, Z., Wang, W., YongJun, L. U., & Ge, H. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2517995123 · Cited by 1
Host Responses to SARS-CoV-2 with an Emphasis on Cytokines
Hayashi, H., Kubo, Y., & Tanaka, Y. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27020664 · Cited by 1
CovInter 2.0: Comprehensive Molecular Interactome of Coronavirus Infection
Lu, W., Zhang, Y., Amahong, K., Zhu, S., Li, X., Zhou, Y., Zhu, F., & Tao, L. (2026) · Journal of Molecular Biology · doi:10.1016/j.jmb.2026.169633 · Cited by 1
Strategic variations in sarbecovirus and merbecovirus Nsp1 linker regions for translation inhibition
Yan, R., Wu, M., Ge, X., Jin, Q., Wang, M., Zhou, H., Li, Y., Wang, Y., & Yuan, S. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag017 · Cited by 1
A bacterial translation activator with an intrinsically disordered RNA-binding region
Basu, P., Farland, E. A., Charity, J. C., Townsend, K. A., & Dove, S. L. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2519770123 · Cited by 1
Schoth, J., Schwedt, I., Philipp, S., Toews, S., Schübel, L., Wacker, A., Schwalbe, H., & Weigand, J. E. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag364 · Cited by 1
Jia, Y., & Wang, Y. (2026) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2026.1777403 · Cited by 1
Loss of cellular RNA homeostasis contributes to MDA5 activation during virus infection
Sampaio, N. G., Davis, T., Gearing, L. J., Dias, A. G., Chauveau, L., Wray‐McCann, G., Odon, V., Liudkovska, V., McAllan, A. L., Cursi, C., et al. (2026) · Nature Immunology · doi:10.1038/s41590-026-02614-3 · Cited by 1
Mani, G., El‐Kamand, S., Wang, B., Baker, D. L., Ataide, S. F., Artsimovitch, I., Cubeddu, L., & Gamsjaeger, R. (2023) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26630 · Cited by 1
Variant- and vaccination-specific alternative splicing profiles in SARS-CoV-2 infections
Lee, S., Furth, P. A., Hennighausen, L. G., & Lee, H. (2024) · iScience · doi:10.1016/j.isci.2024.109177 · Cited by 1
Cytokine regulation disbalance: the basis for COVID-19 immunopathogenesis
Simbirtsev, A. S. (2023) · Cytokines and inflammation · doi:10.17816/ci627301 · Cited by 1
Deletion of 82–85 N-Terminal Residues in SARS-CoV-2 Nsp1 Restricts Virus Replication
Savellini, G. G., Anichini, G., Manetti, F., Trivisani, C. I., & Cusi, M. G. (2024) · Viruses · doi:10.3390/v16050689 · Cited by 1
Prospects for cytokine therapy in acute respiratory viral infections, including COVID-19
Simbirtsev, A. S. (2024) · Cytokines and inflammation · doi:10.17816/ci636443 · Cited by 1
Lopez-Munoz, C., Bowers, N. J., & Marchianò, S. (2025) · Current Treatment Options in Cardiovascular Medicine · doi:10.1007/s11936-025-01079-1 · Cited by 1
RNA viruses: from RNA processing and interaction mechanisms to new prevention and control strategies
ZHANG, F., Tang, Y., Yu, J. I. A., & Zhou, Y. (2025) · Scientia Sinica Vitae · doi:10.1360/ssv-2024-0100 · Cited by 1
Tougeron, D., Seitz‐Polski, B., Hentzien, M., Bani‐Sadr, F., Bourhis, J., Ducreux, M. P., Gaujoux, S., Gorphe, P., Guiu, B., Bessard, A. C. H., et al. (2021) · Bulletin du Cancer · doi:10.1016/j.bulcan.2021.03.009 · Cited by 1
Lopes, L. R. (2021) · Brazilian Journal of Microbiology · doi:10.1007/s42770-021-00497-0 · Cited by 1
Beeckmans, S., & DRIESSCHE, E. V. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.671923 · Cited by 1
Adhiyanto, C., Hendarmin, L. A., Suwarsono, E. A., Harriyati, Z., Suryani, S., Puspitaningrum, R., & Nurjadi, D. (2021) · Journal of Pure and Applied Microbiology · doi:10.22207/jpam.15.2.52 · Cited by 1
Shiao, Y. (2022) · Life · doi:10.3390/life12020203 · Cited by 1
Flattening The Epidemic Curve from a Statistical and Epidemiological Approach in Malaysia
Ibrahim, N. A. B. (2023) · Berkala Kedokteran · doi:10.20527/jbk.v19i1.15724
Mendez, A. S., Ly, M., González-Sánchez, A. M., Hartenian, E., Ingolia, N. T., Cate, J. H. D., & Glaunsinger, B. A. (2021) · SSRN Electronic Journal · doi:10.2139/ssrn.3867728 · Cited by 1
Liang, X., Xiao, J. H., Li, X., Wen, Y., Che, X., Ma, Y., Zhang, X., Zhang, Y., Jian, D., Wang, P., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.24.485560 · Cited by 1
Broderick, C. M., Calle, I. R., Gómez‐Carballa, A., Rial, J. G., Li, H. K., Mehta, R., Jackson, H., Salas, A., Martinón‐Torres, F., Sriskandan, S., et al. (2022) · medRxiv · doi:10.1101/2022.05.26.22274729 · Cited by 1
Discovering host protein interactions specific for SARS-CoV-2 RNA genomePreprint
Giambruno, R., Zacco, E., Ugolini, C., Vandelli, A., Mulroney, L., D’Onghia, M., Giuliani, B., Criscuolo, E., Castelli, M., Clementi, N., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.07.18.499583 · Cited by 1
Binding of SARS-CoV-2 non-structured protein 1 to 40S ribosome inhibits mRNA translationPreprint
Nguyen, H. V., Nguyen, H. L., & Li, M. S. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.02.24.529933 · Cited by 1
SARS-CoV-2 nsp16 is regulated by host E3 ubiquitin ligases, UBR5 and MARCHF7Preprint
Li, T. X., Liu, Z., Gao, W., Zhao, Z., Li, X., Zhang, W., & Li, Z. (2024) · eLife · doi:10.7554/elife.102277.1 · Cited by 1
Benoit, J. M., & Dennis, J. H. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.22.639619 · Cited by 1
Amahong, K., Liu, Y., Zhang, Z., Tao, L., Sarshad, A. A., & Zhu, F. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.07.642080 · Cited by 1
Ye, C., Ezzatpour, S., Imbiakha, B., Jackson, N. D., Çağatay, T., Čupić, A., Miorin, L., Choi, A., Buchholz, D. W., Carter, J., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.16.649178 · Cited by 1
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. (2025) · eLife · doi:10.7554/elife.102277.3 · Cited by 1
LABORATORY TESTING AND SCREENING FOR SARS-CoV-2: A REVIEW OF CURRENT METHODS
Marjanović, D., Primorac, D., Matišić, V., Perić, V., Molnar, V., & Zadro, R. (2020) · Genetics & Applications · doi:10.31383/ga.vol4iss2pp1-9
SARS-CoV-2 Infection Causes Strong mTORC1 Inhibition and Massive Polysome CollapsePreprint
Parthasarathy, H., Gupta, D., Tandel, D., Sah, V., Siddiqui, A. H., Suresh, A. P., & Harshan, K. H. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.08.443207
Guerrero, C. (2021) · ACTA SCIENTIFIC MICROBIOLOGY · doi:10.31080/asmi.2021.04.0857
Godbole, I., Ciminski, K., Yousefi, O. S., Pathan-Chhatbar, S., Saltukoglu, D., Vesper, N., Salavei, P., Strietz, J., Gensch, N., Reth, M. G., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.06.25.449871
Mapping the host protein interactome of non-coding regions in SARS-CoV-2 genomePreprint
Jiang, L., Xiao, M., Liao, Q., Zheng, L., Li, C., Liu, Y., Yang, B., Ren, A., Jiang, C., & Feng, X. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.06.19.449092
Hiba, O. E., Chatoui, H., Zouhairi, N., Bahi, L., Ammouta, L., Balzano, T., Hidan, M. A. E., Isbaine, F., Jayakumar, A. R., Norenberg, M. D., et al. (2021) · Advances in medical diagnosis, treatment, and care (AMDTC) book series · doi:10.4018/978-1-7998-8225-1.ch007
Insights into Molecular Mechanisms Underlying COVID-19 Pathogenesis and Potential Therapeutics
Ravula, S., Mullaguri, S. C., Akula, S., Silveri, R., & Kancha, R. K. (2021) · Indian Journal of Pharmaceutical Sciences · doi:10.36468/pharmaceutical-sciences.839
Liu, J., Zhang, Y., Wu, S., Han, L., Wang, C., Liu, S., Simpson, E. R., Liu, Y., Wang, Y., Shou, W., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.20.477147
The SARS-CoV-2 protein NSP2 impairs the microRNA-induced silencing capacity of human cellsPreprint
Zou, L., Moch, C., Graille, M., & Chapat, C. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.25.477753
Possible Mechanism of SARS-CoV-2 Nsp1-Mediated Control of Viral Gene Expression
Zhao, T., Ren, Y., Wu, J., & Zhang, Q. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.881749
Louten, J. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-90565-7.00014-9
Perspective Chapter: Tracking Trails of SARS CoV-2 – Variants to Therapy
Kumar, A., Pai, M. O., Badoni, G., Singh, A., Agrawal, A., & Omar, B. J. (2022) · Infectious diseases · doi:10.5772/intechopen.106472
SARS-CoV-2 Protein Nsp2 Stimulates Translation Under Normal and Hypoxic ConditionsPreprint
Korneeva, N. L., Khalil, M. I., Ghosh, I., Fan, R., Arnold, T., & Benedetti, A. D. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.09.13.507829
Metadata
- 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)
- 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
- 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