The DOI matches its Crossref record; 51 of the 53 references it cites were found in a registry or an index.
Proteomics of SARS-CoV-2-infected host cells reveals therapy targets
Open accessPublished version of a preprint
Abstract
A new coronavirus was recently discovered and named severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Infection with SARS-CoV-2 in humans causes coronavirus disease 2019 (COVID-19) and has been rapidly spreading around the globe 1,2. SARS-CoV-2 shows some similarities to other coronaviruses; however, treatment options and an understanding of how SARS-CoV-2 infects cells are lacking. Here we identify the host cell pathways that are modulated by SARS-CoV-2 and show that inhibition of these pathways prevents viral replication in human cells. We established a human cell-culture model for infection with a clinical isolate of SARS-CoV-2. Using this cell-culture system, we determined the infection profile of SARS-CoV-2 by translatome 3 and proteome proteomics at different times after infection. These analyses revealed that SARS-CoV-2 reshapes central cellular pathways such as translation, splicing, carbon metabolism, protein homeostasis (proteostasis) and nucleic acid metabolism. Small-molecule inhibitors that target these pathways prevented viral replication in cells. Our results reveal the cellular infection profile of SARS-CoV-2 and have enabled the identification of drugs that inhibit viral replication. We anticipate that our results will guide efforts to understand the molecular mechanisms that underlie the modulation of host cells after infection with SARS-CoV-2. Furthermore, our findings provide insights for the development of therapies for the treatment of COVID-19.
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
“Clinical isolate infection models have been developed using Caco-2 cells154 with temporal proteome changes identified during infection using multiplexed MS by combining metabolic labelling with tandem mass tagging methods.”
From A high-stringency blueprint of the human proteome (2020) · cites this paper as [154]
In the citing paper
“Building on this knowledge of coronavirus infection, recent proteomics studies have focused on SARS-CoV-2, uncovering additional potential therapeutic targets154,155.”
From A high-stringency blueprint of the human proteome (2020) · cites this paper as [154]
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
Cytoscape: A software Environment for integrated models of biomolecular interaction networks
Shannon, P., Markiel, A., Ozier, O., Baliga, N. S., Wang, J. T., Ramage, D., Amin, N., Schwikowski, B., & Ideker, T. (2003) · Genome Research · doi:10.1101/gr.1239303 · Cited by 51,888
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
Chen, N., Zhou, M., Dong, X., Qu, J., Gong, F., Han, Y., Qiu, Y., Wang, J., Liu, Y., Wei, Y., et al. (2020) · The Lancet · doi:10.1016/s0140-6736(20)30211-7 · Cited by 21,415
La certeza de lo impredecible: Cultura Educación y Sociedad en tiempos de COVID19
Martínez González, M. (2020) · DSPACE System - Metalibrary (University of the Coast) · Cited by 18,463
Data Structures for Statistical Computing in Python
McKinney, W. (2010) · Proceedings of the Python in Science Conferences · doi:10.25080/majora-92bf1922-00a · Cited by 12,930
The NumPy Array: A Structure for Efficient Numerical Computation
van der Walt, S., Colbert, S. C., & Varoquaux, G. (2011) · Computing in Science & Engineering · doi:10.1109/mcse.2011.37 · Cited by 9,381
The Perseus computational platform for comprehensive analysis of (prote)omics data
Tyanova, S., Temu, T., Sinitcyn, P., Carlson, A., Hein, M. Y., Geiger, T., Mann, M., & Cox, J. (2016) · Nature Methods · doi:10.1038/nmeth.3901 · Cited by 8,803
Chan, J., Yuan, S.-F., Kok, K.-H., To, K., Chu, H., Yang, J., Xing, F., Liu, J.-L., Yip, C., Poon, R., et al. (2020) · The Lancet · doi:10.1016/s0140-6736(20)30154-9 · Cited by 8,450
A scaling normalization method for differential expression analysis of RNA-seq data
Robinson, M. D., & Oshlack, A. (2010) · Genome Biology · doi:10.1186/gb-2010-11-3-r25 · Cited by 7,876
Cited by
Sorted by citations
Items 601–700 of 998
Short-term ex vivo tissue culture models help study human lung infectionsA review
Xia, J., Zeng, Y., Wu, X., & Xu, F. (2023) · Medicine · doi:10.1097/md.0000000000032589 · Cited by 7
Circulating Peptidome Is Strongly Altered in COVID-19 Patients
Baldanzi, G., Purghè, B., Ragnoli, B., Sainaghi, P. P., Rolla, R., Chiocchetti, A., Manfredi, M., & Malerba, M. (2023) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph20021564 · Cited by 7
Frasson, I., Diamante, L., Zangrossi, M., Carbognin, E., Pietà, A. D., Penna, A., Rosato, A., Verin, R., Torrigiani, F., Salata, C., et al. (2024) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjae004 · Cited by 8
Mapping the immunopeptidome of seven SARS-CoV-2 antigens across common HLA haplotypes
Braun, A., Rowntree, L. C., Huang, Z., Pandey, K., Thuesen, N. H., Li, C., Petersen, J., Littler, D. R., Raji, S., Nguyen, T. H. O., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-51959-6 · Cited by 9
Transcriptomics-inferred dynamics of SARS-CoV-2 interactions with host epithelial cells
Adam, L., Stanifer, M. L., Springer, F., Mathony, J., Brune, M., Ponzio, C. D., Eils, R., Boulant, S., Niopek, D., & Kallenberger, S. M. (2023) · Science Signaling · doi:10.1126/scisignal.abl8266 · Cited by 7
SARSCOVIDB─A New Platform for the Analysis of the Molecular Impact of SARS-CoV-2 Viral Infection
da Rosa, R. L., Yang, T. S., Cagnini, E. F. T., Saciloto-de-Oliveira, L. R., Moraes, A. N. S., Tatara, J. M., Costa, R. P., Borges, J. S., Innocente-Alves, C., Berger, M., et al. (2021) · ACS Omega · doi:10.1021/acsomega.0c05701 · Cited by 6
Postmortem Tissue Proteomics Reveals the Pathogenesis of Multiorgan Injuries of COVID-19Preprint
Qiu, Y., Wu, D., Ning, W., Zhang, J., Shu, T., Huang, C., Chen, R., Huang, M., Xu, J., Yang, Q., et al. (2020) · doi:10.21203/rs.3.rs-38091/v1 · Cited by 7
The Great Deceiver: miR-2392’s Hidden Role in Driving SARS-CoV-2 InfectionPreprint
McDonald, J., Enguita, F. J., Taylor, D. M., Griffin, R. J., Priebe, W., Emmett, M. R., Sajadi, M. M., Harris, A. D., Clement, J., Dybas, J. M., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.23.441024 · Cited by 7
Malgotra, V., & Sharma, V. (2021) · Preprints.org · doi:10.20944/preprints202106.0333.v1 · Cited by 6
Malgotra, V., & Sharma, V. (2021) · Preprints.org · doi:10.20944/preprints202106.0333.v2 · Cited by 6
Kelch, M. A., Vera-Guapi, A., Beder, T., Oswald, M., Hiemisch, A., Beil, N., Wajda, P., Ciesek, S., Erfle, H., Toptan, T., et al. (2023) · Frontiers in Microbiology · doi:10.3389/fmicb.2023.1193320 · Cited by 6
Self-citationDinda, 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
Xie, J., Jia, Z., Li, Y., Liao, L., Zhu, Z., Wang, Y., & Huang, R. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252111852 · Cited by 6
Ma, Y., Yang, J.-M., Mei, H.-T., Zeng, L., Yang, G., Wang, J., Ming, S., & Chu, B. (2025) · Virulence · doi:10.1080/21505594.2025.2585639 · Cited by 6
MacMahon, M., Hwang, W., Yim, S., MacMahon, E., Abraham, A., Barton, J., Tharmakulasingam, M., Bilokon, P., Gaddi, V. P., & Han, N. (2023) · Informatics in Medicine Unlocked · doi:10.1016/j.imu.2023.101387 · Cited by 6
Does oncolytic viruses‐mediated metabolic reprogramming benefit or harm the immune microenvironment?
Peng, C., Xiao, P., & Li, N. (2024) · The FASEB Journal · doi:10.1096/fj.202301947rr · Cited by 6
Applications of high performance liquid chromatography-mass spectrometry in proteomics
Wei, L. I. U., Weng, L., Gao, M., & Zhang, X. (2024) · Chinese Journal of Chromatography · doi:10.3724/sp.j.1123.2023.11006 · Cited by 6
The TOM complex from an evolutionary perspective and the functions of TOMM70
Özdemir, M., & Dennerlein, S. (2024) · Biological Chemistry · doi:10.1515/hsz-2024-0043 · Cited by 6
Mallick, M., Boehm, V., Xue, G., Blackstone, M. E., Gehring, N. H., & Chakrabarti, S. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae829 · Cited by 6
Protein turnover regulation is critical for influenza A virus infection
Huang, Y., Urban, C., Hubel, P., Stukalov, A., & Pichlmair, A. (2024) · Cell Systems · doi:10.1016/j.cels.2024.09.004 · Cited by 6
Feng, F., Chen, J., Li, R., Zhu, Y., Ma, Y., Wang, Z., Wang, Y., Gao, Z., Yang, L., Yin, Y., et al. (2025) · mBio · doi:10.1128/mbio.00385-25 · Cited by 5
Pérez‐Pulido, A. J., Cortés, G. A., Brokate-Llanos, A. M., Brea‐Calvo, G., Rodríguez-Griñolo, R., Garzón, A., & Muñoz, M. J. (2020) · Briefings in Bioinformatics · doi:10.1093/bib/bbaa419 · Cited by 6
A Multiallelic Molecular Beacon-Based Real-Time RT-PCR Assay for the Detection of SARS-CoV-2
Chrysostomou, A. C., Rodosthenous, J. H., Topcu, C., Papa, C., Aristokleous, A., Stathi, G., Christodoulou, C., Eleftheriou, C., Stylianou, D. C., & Kostrikis, L. G. (2021) · Life · doi:10.3390/life11111146 · Cited by 6
Deb, B., O’Brien, D. R., Chunawala, Z. S., & Bharucha, A. E. (2022) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/clinem/dgac038 · Cited by 6
Access to the Phospho-proteome via the Mitigation of Peptide-Metal Interactions
Hughes, C. J., Gethings, L. A., Wilson, I. D., & Plumb, R. S. (2022) · Journal of Chromatography A · doi:10.1016/j.chroma.2022.463024 · Cited by 6
Khurana, P., Varshney, R. K., & Gupta, A. (2022) · Heliyon · doi:10.1016/j.heliyon.2022.e09387 · Cited by 6
Grikscheit, K., Rabenau, H. F., Ghodratian, Z., Widera, M., Wilhelm, A., Toptan, T., Hoehl, S., Layer, E., Helfritz, F., & Ciesek, S. (2022) · Vaccines · doi:10.3390/vaccines10071163 · Cited by 7
Self-citationProgress on COVID-19 Chemotherapeutics Discovery and Novel Technology
Zhou, Y., Wang, H., Li, Y., & Wang, Q. (2022) · Molecules · doi:10.3390/molecules27238257 · Cited by 6
Lactate is useful for the efficient replication of porcine epidemic diarrhea virus in cell culture
Wuri, N., Gou, H., Zhang, B., Wang, M., Wang, S., Zhang, W., He, H., Fan, X. H., Zhang, C., Liu, Z., et al. (2023) · Frontiers in Veterinary Science · doi:10.3389/fvets.2023.1116695 · Cited by 6
Metzler, M., Tharyan, R. G., Klann, K., Grikscheit, K., Bojková, D., Cinatl, J. J., Tascher, G., Ciesek, S., & Münch, C. (2023) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2023.100537 · Cited by 5
Self-citationNano-based techniques: A revolutionary approach to prevent covid-19 and enhancing human awareness
Asaikkutti, A., Vimala, K., Dhineshkumar, E., Cheruparambath, P., Balakrishnan, K., & Arul, V. (2023) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2023.104567 · Cited by 7
Ratishvili, T., Quach, H. Q., Haralambieva, I. H., Suryawanshi, Y. R., Ovsyannikova, I. G., Kennedy, R. B., & Poland, G. A. (2023) · Vaccine · doi:10.1016/j.vaccine.2023.12.024 · Cited by 6
Aprotinin (II): Inhalational Administration for the Treatment of COVID-19 and Other Viral Conditions
Padín, J. F., Pérez‐Ortiz, J. M., & Calvo, F. J. R. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25137209 · Cited by 7
Overlapping host pathways between SARS-CoV-2 and its potential copathogens: An in silico analysis
Vavougios, G. D. (2020) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2020.104602 · Cited by 6
The chemical biology of coronavirus host–cell interactions
Datta, S., Hett, E. C., Vora, K. A., Hazuda, D. J., Oslund, R., Fadeyi, O., & Emili, A. (2020) · RSC Chemical Biology · doi:10.1039/d0cb00197j · Cited by 6
Gour, S., & Yadav, J. K. (2021) · Journal of Proteins and Proteomics · doi:10.1007/s42485-021-00057-y · Cited by 5
SUMO: a novel target for anti-coronavirus therapy
Ryu, H. (2021) · Pathogens and Global Health · doi:10.1080/20477724.2021.1906562 · Cited by 6
A Resource for the Network Representation of Cell Perturbations Caused by SARS-CoV-2 Infection
Perfetto, L., Micarelli, E., Iannuccelli, M., Surdo, P. L., Giuliani, G., Latini, S., Pugliese, G. M., Massacci, G., Vumbaca, S., Riccio, F., et al. (2021) · Genes · doi:10.3390/genes12030450 · Cited by 6
Can proteomics-based approaches further help COVID-19 prevention and therapy?
Kumar, V. (2021) · Expert Review of Proteomics · doi:10.1080/14789450.2021.1924684 · Cited by 6
Inactivation of Coronaviruses during Sample Preparation for Proteomics Experiments
Grossegesse, M., Leupold, P., Doellinger, J., Schaade, L., & Nitsche, A. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.1c00320 · 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
East meets West in COVID-19 therapeutics
Wang, S., Zeng, X. L., Wang, Y., Zhao, Y., Chen, W., & Chen, Y. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105008 · Cited by 6
Vavougios, G. D. (2021) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2021.104733 · Cited by 6
Reina, J. (2021) · Revista Española de Quimioterapia · doi:10.37201/req/042.2021 · Cited by 6
Wang, J. Y., Zhang, W., Roehrl, M. H. A., Roehrl, M. H. A., & Roehrl, M. H. A. (2023) · Australian Journal of Chemistry · doi:10.1071/ch22268 · Cited by 6
Screening of candidate host cell membrane proteins involved in SARS-CoV-2 entryPreprint
Kotani, N., Nakano, T., & Kuwahara, R. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.09.09.289488 · Cited by 6
Interferon alpha-based combinations suppress SARS-CoV-2 infection in vitro and in vivoPreprint
Ianevski, A., Yao, R., Zusinaite, E., Lello, L. S., Wang, S., Jo, E., Yang, J., Ravlo, E., Wang, W., Lysvand, H., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.01.05.425331 · Cited by 6
Costa, J. H., Mohanapriya, G., Bharadwaj, R., Noceda, C., Thiers, K. L. L., Aziz, S., Srivastava, S., Oliveira, M., Gupta, K. J., Kumari, A., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.06.08.447491 · 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
Bischof, T., Gsöellpointner, M., Kovacevic, K. D., Moser, M. M., Dizdarevic, A. M., Gualdoni, G. A., Gorki, A.-D., Nicolodi, C., Chou, S., Radivojev, S., et al. (2025) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2025.107069 · Cited by 5
Mitochondrial Dysfunction in Aging, HIV, and Long COVID: Mechanisms and Therapeutic Opportunities
Delpino, M. V., & Quarleri, J. F. (2025) · Pathogens · doi:10.3390/pathogens14101045 · Cited by 7
Airway immunometabolic responses during pulmonary bacterial and viral infections
Wadhwa, R., Tang, E. W., Wong, L. Y. R., & Lung, T. W. F. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116614 · Cited by 5
Sidorenko, V. S., Cohen, I. S., Dorjee, K., Minetti, C. A. S. A., Remeta, D. P., Gao, J., Potapova, I. A., Wang, H.-Z., Hearing, J. C., Yen, W.-Y., et al. (2024) · Virus Research · doi:10.1016/j.virusres.2024.199322 · Cited by 5
Predicting host-based, synthetic lethal antiviral targets from omics data
Staheli, J. P., Neal, M. L., Navare, A., Mast, F. D., & Aitchison, J. D. (2024) · NAR Molecular Medicine · doi:10.1093/narmme/ugad001 · Cited by 6
SARS-CoV-2 and UPS with potentials for therapeutic interventions
Ferdoush, J., Kadir, R. A., Kaplanoğlu, S., & Osborn, M. (2024) · Gene · doi:10.1016/j.gene.2024.148377 · Cited by 5
Güven, E. (2021) · Gene Reports · doi:10.1016/j.genrep.2021.101169 · Cited by 5
Looking at COVID-19 from a Systems Biology Perspective
Turilli-Ghisolfi, E. S., Lualdi, M., & Fasano, M. (2022) · Biomolecules · doi:10.3390/biom12020188 · Cited by 5
Kanduri, S. R., Ramanand, A., Varghese, V., Wen, Y., Mohamed, M. M. B., & Velez, J. C. Q. (2022) · Kidney360 · doi:10.34067/kid.0001632022 · Cited by 5
Protein Arginylation Is Regulated during SARS-CoV-2 Infection
Macedo-da-Silva, J., Rosa-Fernandes, L., Gomes, V. M., Santiago, V. F., Santos, D. M., Molnár, C. M. S., Barboza, B. R., de Souza, E. E., Marques, R. F., Boscardin, S. B., et al. (2023) · Viruses · doi:10.3390/v15020290 · Cited by 6
Elsebai, M. F., & Habib, E. E. (2023) · Archiv der Pharmazie · doi:10.1002/ardp.202200558 · Cited by 5
Drugs for COVID-19 Treatment: A New Challenge
Talukder, P., Saha, A., Roy, S., Ghosh, G., Roy, D. D., & Barua, S. (2023) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-023-04439-4 · Cited by 5
Antigen-Specific Antibody Signature Is Associated with COVID-19 Outcome
Salgado, B. B., Jordão, M. F., de Morais, T. B. D. N., da Silva, D. S. S., Filho, I. V. P., Sobrinho, W. B. S., Carvalho, N. O., dos Santos, R. O., Forato, J., Barbosa, P. P., et al. (2023) · Viruses · doi:10.3390/v15041018 · Cited by 7
Glycolytic stress deteriorates 229E virulence to improve host defense response
Kaushik, N., Patel, P., Bhartiya, P., Shin, Y., Kim, J. H., Choi, E. H., & Kaushik, N. K. (2023) · Microbes and Infection · doi:10.1016/j.micinf.2023.105150 · Cited by 5
Aguirre, J., & Guantes, R. (2023) · bioRxiv · doi:10.1016/j.isci.2023.108475 · Cited by 5
Oktavianawati, I., Santoso, M., Bakar, M. F. A., Kim, Y., & Fatmawati, S. (2023) · Applied Biological Chemistry · doi:10.1186/s13765-023-00842-x · Cited by 6
Unraveling flavivirus pathogenesis: from bulk to single-cell RNA-sequencing strategies
Kim, D., Jeong, S., & Park, S. (2024) · Korean Journal of Physiology and Pharmacology · doi:10.4196/kjpp.2024.28.5.403 · Cited by 5
Wang, Z., Li, L., Yang, S., Li, Z., Zhang, P., Shi, R., Zhou, X., Tang, X., & Li, Q. (2024) · Frontiers in Microbiology · doi:10.3389/fmicb.2024.1470953 · Cited by 5
St‐Germain, J. R., Astori, A., & Raught, B. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.1c00048 · Cited by 5
An overview of proteomic methods for the study of ‘cytokine storms’
David, P., Hansen, F. J., Bhat, A., & Weber, G. F. (2021) · Expert Review of Proteomics · doi:10.1080/14789450.2021.1911652 · Cited by 5
Toptan, T., Ciesek, S., & Hoehl, S. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-63761-3_12 · Cited by 6
Self-citationIcard, P., Simula, L., Rei, J., Fournel, L., Pauw, V. D., & Alifano, M. (2021) · Biochimie · doi:10.1016/j.biochi.2021.09.009 · Cited by 5
Wang, S., Zeng, X. L., Wang, Y., Dongzhi, Z., Zhao, Y., & Chen, Y. (2022) · Chinese Journal of Integrative Medicine · doi:10.1007/s11655-022-3573-0 · Cited by 5
Telek, E., Ujfalusi, Z., Kemenesi, G., Zana, B., Jakab, F., Hild, G., Lukács, A., & Hild, G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23116189 · Cited by 3
Pohler, A., Abdelfatah, S., Riedl, M., Meesters, C., Hildebrandt, A., & Efferth, T. (2022) · Pharmaceuticals · doi:10.3390/ph15091046 · Cited by 5
Wang, J., Liu, J., Luo, M., Cui, H. S., Zhang, W., Zhao, K., Dai, H., Song, F., Chen, K., Yu, Y., et al. (2022) · iScience · doi:10.1016/j.isci.2022.105348 · Cited by 5
Späth, J., Wang, R., Humphrey, M., Baumbach, J., & Loscalzo, J. (2023) · CPT Pharmacometrics & Systems Pharmacology · doi:10.1002/psp4.13076 · Cited by 5
Nayak, T., De, D., & Dhal, P. K. (2021) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2021.104892 · Cited by 5
Kulus, J., Kulus, M., Stefańska, K., Sobolewski, J., Piotrowska‐Kempisty, H., Mozdziak, P. E., & Kempisty, B. (2021) · Vaccines · doi:10.3390/vaccines9060639 · Cited by 6
The future of sepsis research: time to think differently?
Bastarache, J. A. (2020) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00368.2020 · Cited by 5
Lyu, L., Feng, R., Zhang, M., Gong, Q., Liao, Y., Zhou, Y., Guo, X., Su, B., Dorsett, Y., & Chen, L. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.04.16.043224 · Cited by 5
Srivastava, R., Daulatabad, S. V., Srivastava, M., & Janga, S. C. (2020) · Purdue University Indianapolis (Indiana University) · doi:10.1101/2020.07.06.190348 · Cited by 5
Vavougios, G. D. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.07.014 · Cited by 5
RetractedKee, J., Thudium, S., Renner, D. M., Glastad, K. M., Palozola, K. C., Zhang, Z., Li, Y., Cesare, J., Lan, Y., Truitt, R., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.11.10.468057 · Cited by 4
Zhang, M., Qian, B., Kunec, D., & Veit, M. (2025) · npj Viruses · doi:10.1038/s44298-025-00148-3 · Cited by 4
Bie, Z.-Y., Tan, Y., Ye, C., & Wei, K. (2025) · Frontiers in Microbiology · doi:10.3389/fmicb.2025.1690133 · Cited by 4
Chung, C. W., Irudayaraj, P., Lallow, E. O., Xu, Z., Park, Y. K., Kudchodkar, S. B., Montaner, L. J., Srinivasan, A., & Muthumani, K. (2024) · Frontiers in Virology · doi:10.3389/fviro.2024.1399993 · Cited by 5
Subbarayan, K., Al‐Samadi, A., Schäfer, H., Massa, C., Salo, T. A., Biehl, K., Vaxevanis, C., Ulagappan, K., Wahbi, W., Reimers, M., et al. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05520-9 · Cited by 4
Ibrahim, H. A. A. (2021) · Egyptian Journal of Chemistry · doi:10.21608/ejchem.2021.87893.4234 · Cited by 4
Revisiting potential value of antitumor drugs in the treatment of COVID-19
Zheng, W., Zeng, Z., Lin, S., & Hou, P. (2022) · Cell & Bioscience · doi:10.1186/s13578-022-00899-z · Cited by 5
Leukocyte metabolism in obese type 2 diabetic individuals associated with COVID-19 severity
Lobato, T. B., Gennari-Felipe, M., Pauferro, J. R. B., Correa, I. S., Santos, B. F., Dias, B. B., Borges, J. C. D. O., dos Santos, C. S., Santos, E. S. D. S., de Araújo, M. J. L., et al. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.1037469 · Cited by 4
2-Deoxy-d-Glucose: A Repurposed Drug for COVID-19 Treatment
Chopra, S., Dahiya, A., Nair, A., Sharma, N., & Sharma, R. K. (2023) · Springer eBooks · doi:10.1007/978-981-19-5399-6_20 · Cited by 4
Chen, R., Fulton, K. M., Tran, A., Duque, D., Kovalchik, K. A., Caron, É., Twine, S. M., & Li, J. (2023) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2023.100645 · Cited by 4
The role of chemical biology in the fight against SARS-CoV-2
Burslem, G. M. (2021) · Biochemical Journal · doi:10.1042/bcj20200514 · Cited by 4
multiomics: A user-friendly multi-omics data harmonisation R pipeline
Chen, T., Abadi, A. J., Cao, K. L., & Tyagi, S. (2021) · F1000Research · doi:10.12688/f1000research.53453.1 · Cited by 13
Final results of BIRCOV trial (ARB, ACEI, DRi in COVID-19)
Ivanov, D. D., Ivanova, M. D., & Crestanello, T. (2021) · KIDNEYS · doi:10.22141/2307-1257.10.3.2021.239591 · Cited by 4
Revolution in microbial bioprospecting via the development of omics-based technologies
Bansal, M., Tiwari, N., & Sharma, J. G. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-90958-7.00008-x · Cited by 4
Tolerance of Human Fibroblasts to Benfo-Oxythiamine In Vitro
Yan, M., Smeets, R., Gosau, M., Vollkommer, T., Fuest, S., Stetzer, E., Kluwe, L., Coy, J., & Burg, S. (2022) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph19074112 · Cited by 4
Interferon Signaling-Dependent Contribution of Glycolysis to Rubella Virus Infection
Schilling, E., Wald, M. E., Schulz, J., Werner, L. E., & Claus, C. (2022) · Pathogens · doi:10.3390/pathogens11050537 · Cited by 4
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
Rise of the SARS-CoV-2 Variants: can proteomics be the silver bullet?
Acharjee, A., Kingsly, J. S., Kamat, M., Kurlawala, V., Chakraborty, A., Vyas, P., Vaishnav, R., & Srivastava, S. (2022) · Expert Review of Proteomics · doi:10.1080/14789450.2022.2085564 · Cited by 4
Metadata
- Authors
- Bojkova, D., Klann, K., Koch, B., Widera, M., Krause, D., Ciesek, S., Cinatl, J., & Münch, C.
- Affiliations
- Goethe University Frankfurt (DE)
- University Hospital Frankfurt (DE)
- Corresponding author
- Cinatl, Jindrich
- Münch, Christian
- ORCID
- Venue
- Nature
- Published
- 2020-05-14
- Volume
- 583
- Issue
- 7816
- Pages
- 469-472
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC7616921
- OpenAlex
- W3026002191
- Cited by
- 1,010
- References
- 53
- Citations by year
- 2026: 25 · 2025: 58 · 2024: 86 · 2023: 118 · 2022: 198 · 2021: 347 · 2020: 177
- FWCI
- 27.46
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Nature (publishedVersion)
- Research Square (acceptedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Publikationsdatenbank der Fraunhofer-Gesellschaft (Fraunhofer-Gesellschaft) (submittedVersion)
- Fraunhofer-Publica (Fraunhofer-Gesellschaft) (submittedVersion)
- Zenodo (CERN European Organization for Nuclear Research) (submittedVersion, cc-by)
- Funders
- Frankfurter Stiftung für krebskranke Kinder
- Hilfe für krebskranke Kinder Frankfurt
- European Commission
- Deutsche Forschungsgemeinschaft (ERC StG 803565, MU 4216/1-1, CRC 1177)
- Aventis Foundation
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Health Sciences › Medicine › Infectious Diseases › COVID-19 Clinical Research Studies
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Keywords
- SARS-CoV-2, COVID-19 pandemic, viral replication, host-pathogen interaction, translation (biology), splicing, carbon metabolism, proteostasis, nucleic acid metabolism, small molecule inhibitors, antiviral drug targets, proteome, translatome
- MeSH terms
- Betacoronavirus, Proteostasis, COVID-19, SARS-CoV-2, COVID-19 Drug Treatment, Carbon, Drug Evaluation, Preclinical, Humans, Kinetics, Pneumonia, Viral, RNA Splicing, Time Factors, Protein Biosynthesis, Virus Replication, Coronavirus Infections, Caco-2 Cells, Proteome, Proteomics, Host-Pathogen Interactions, Pandemics, Molecular Targeted Therapy, In Vitro Techniques
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
