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
A SARS-CoV-2 protein interaction map reveals targets for drug repurposing
Gordon, D. E., Jang, G. M., Bouhaddou, M., Xu, J., Obernier, K., White, K. M., O’Meara, M. J., Rezelj, V. V., Guo, J. Z., Swaney, D. L., et al. (2020) · Nature · doi:10.1038/s41586-020-2286-9 · Cited by 4,405
Coronavirus biology and replication: implications for SARS-CoV-2
V’kovski, P., Kratzel, A., Steiner, S., Stalder, H., & Thiel, V. (2020) · Nature Reviews Microbiology · doi:10.1038/s41579-020-00468-6 · Cited by 3,371
Papain-like protease regulates SARS-CoV-2 viral spread and innate immunity
Shin, D., Mukherjee, R., Grewe, D., Bojková, D., Baek, K., Bhattacharya, A., Schulz, L., Widera, M., Mehdipour, A. R., Tascher, G., et al. (2020) · Nature · doi:10.1038/s41586-020-2601-5 · Cited by 1,213
Self-citationCodo, A. C., Davanzo, G. G., Monteiro, L. D. B., de Souza, G. F., Muraro, S. P., Virgilio-da-Silva, J. V., Prodonoff, J. S., Carregari, V. C., de Biagi Junior, C. A. O., Crunfli, F., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.07.007 · Cited by 733
The coding capacity of SARS-CoV-2
Finkel, Y., Mizrahi, O., Nachshon, A., Weingarten-Gabbay, S., Morgenstern, D., Yahalom-Ronen, Y., Tamir, H., Achdout, H., Stein, D., Israeli, O., et al. (2021) · Nature · doi:10.1038/s41586-020-2739-1 · Cited by 644
Multilevel proteomics reveals host perturbations by SARS-CoV-2 and SARS-CoV
Stukalov, A., Girault, V., Grass, V., Karayel, Ö., Bergant, V., Urban, C., Haas, D. A., Huang, Y., Oubraham, L., Wang, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03493-4 · Cited by 656
SARS-CoV-2 binds platelet ACE2 to enhance thrombosis in COVID-19
Zhang, S., Liu, Y., Wang, X., Li, H., Li, H., Wang, Y., Liu, M., Zhao, X., Xie, Y., Yang, Y., et al. (2020) · Journal of Hematology & Oncology · doi:10.1186/s13045-020-00954-7 · Cited by 673
In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges
Turoňová, B., Sikora, M., Schürmann, C., Hagen, W. J. H., Welsch, S., Blanc, F. E. C., von Bülow, S., Gecht, M., Bagola, K., Hörner, C., et al. (2020) · Science · doi:10.1126/science.abd5223 · Cited by 641
Malone, B. F., Urakova, N., Snijder, E. J., & Campbell, E. A. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00432-z · Cited by 583
The ORF8 protein of SARS-CoV-2 mediates immune evasion through down-regulating MHC-Ι
Zhang, Y., Chen, Y., Li, Y., Huang, F., Luo, B., Yuan, Y., Xia, B., Ma, X., Yang, T., Yu, F., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2024202118 · Cited by 553
Davidson, A. D., Williamson, M. K., Lewis, S., Shoemark, D., Carroll, M. W., Heesom, K. J., Zambon, M., Ellis, J., Lewis, P. A., Hiscox, J. A., et al. (2020) · Genome Medicine · doi:10.1186/s13073-020-00763-0 · Cited by 457
Role of Structural and Non-Structural Proteins and Therapeutic Targets of SARS-CoV-2 for COVID-19
Yadav, R., Chaudhary, J. K., Jain, N. K., Chaudhary, P. K., Khanra, S., Dhamija, P., Sharma, A., Kumar, A., & Handu, S. S. (2021) · Cells · doi:10.3390/cells10040821 · Cited by 486
Reduced Neutralization of SARS-CoV-2 Omicron Variant by Vaccine Sera and Monoclonal Antibodies
Wilhelm, A., Widera, M., Grikscheit, K., Toptan, T., Schenk, B., Pallas, C., Metzler, M., Kohmer, N., Hoehl, S., Helfritz, F. A., et al. (2021) · doi:10.1101/2021.12.07.21267432 · Cited by 440
Self-citationMulti-organ proteomic landscape of COVID-19 autopsies
Nie, X., Qian, L., Sun, R., Huang, B., Dong, X., Xiao, Q., Zhang, Q., Lu, T., Yue, L., Chen, S., et al. (2021) · Cell · doi:10.1016/j.cell.2021.01.004 · Cited by 403
Gordon, D. E., Jang, G. Μ., Bouhaddou, M., Xu, J., Obernier, K., O’Meara, M. J., Guo, J. Z., Swaney, D. L., Tummino, T. A., Hüttenhain, R., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.22.002386 · Cited by 419
Li, J., Guo, M., Tian, X., Wang, X., Yang, X., Wu, P., Liu, C., Xiao, Z., Qu, Y., Yin, Y., et al. (2020) · Med · doi:10.1016/j.medj.2020.07.002 · Cited by 361
Plitidepsin has potent preclinical efficacy against SARS-CoV-2 by targeting the host protein eEF1A
White, K. M., Rosales, R., Yildiz, S., Kehrer, T., Miorin, L., Moreno, E., Jangra, S., Uccellini, M. B., Rathnasinghe, R., Coughlan, L., et al. (2021) · Science · doi:10.1126/science.abf4058 · Cited by 348
Morphological, cellular and molecular basis of brain infection in COVID-19 patients
Crunfli, F., Carregari, V. C., Veras, F. P., Vendramini, P. H., Valença, A. G. F., Antunes, A. S. L. M., Brandão-Teles, C., da Silva Zuccoli, G., Reis-de-Oliveira, G., Silva-Costa, L. C., et al. (2020) · doi:10.1101/2020.10.09.20207464 · Cited by 331
The SARS-CoV-2 RNA–protein interactome in infected human cells
Schmidt, N., Lareau, C. A., Keshishian, H., Ganskih, S., Schneider, C., Hennig, T., Melanson, R., Werner, S., Wei, Y., Zimmer, M., et al. (2020) · Nature Microbiology · doi:10.1038/s41564-020-00846-z · Cited by 319
A metabolic handbook for the COVID-19 pandemic
Ayres, J. S. (2020) · Nature Metabolism · doi:10.1038/s42255-020-0237-2 · Cited by 293
Yeung, M. L., Teng, J. L. L., Jia, L., Zhang, C., Huang, C., Cai, J., Zhou, R., Chan, K., Zhao, H., Zhu, L., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.053 · Cited by 276
Trougakos, I. P., Stamatelopoulos, K. S., Terpos, E., Tsitsilonis, O., Aivalioti, E., Paraskevis, D. N., Kastritis, E., Pavlakis, G. N., & Dimopoulos, M. A. (2021) · Journal of Biomedical Science · doi:10.1186/s12929-020-00703-5 · Cited by 305
Appelberg, S., Gupta, S., Akusjärvi, S. S., Ambikan, A. T., Mikaeloff, F., Saccon, E., Végvári, Á., Benfeitas, R., Sperk, M., Ståhlberg, M., et al. (2020) · Emerging Microbes & Infections · doi:10.1080/22221751.2020.1799723 · Cited by 276
Li, N., Hui, H., Bray, B., Gonzalez, G. M., Zeller, M., Anderson, K. G., Knight, R. D., Smith, D. M., Wang, Y., Carlin, A. F., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109091 · Cited by 283
SARS-CoV-2 infects and induces cytotoxic effects in human cardiomyocytes
Bojkova, D., Wagner, J. U. G., Shumliakivska, M., Aslan, G. S., Saleem, U., Hansen, A., Luxán, G., Günther, S., Pham, M. D., Krishnan, J., et al. (2020) · Cardiovascular Research · doi:10.1093/cvr/cvaa267 · Cited by 257
Self-citationWu, J., Shi, Y., Pan, X., Wu, S., Hou, R., Zhang, Y., Zhong, T., Tang, H., Du, W., Wang, L., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108761 · Cited by 278
SARS-CoV-2 uses a multipronged strategy to impede host protein synthesis
Finkel, Y., Gluck, A., Nachshon, A., Winkler, R., Fisher, T., Rozman, B., Mizrahi, O., Lubelsky, Y., Zuckerman, B., Slobodin, B., et al. (2021) · Nature · doi:10.1038/s41586-021-03610-3 · Cited by 253
Repurpose Open Data to Discover Therapeutics for COVID-19 Using Deep Learning
Zeng, X., Song, X. H., Ma, T., Pan, X., Zhou, Y., Hou, Y., Zhang, Z., Li, K., Karypis, G., & Cheng, F. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00316 · Cited by 261
HIF-1α promotes SARS-CoV-2 infection and aggravates inflammatory responses to COVID-19
Tian, M., Liu, W., Li, X., Zhao, P., Shereen, M. A., Zhu, C., Huang, S., Liu, S., Yu, X., Yue, M., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00726-w · Cited by 249
Wenzel, J., Lampe, J., Müller‐Fielitz, H., Schuster, R., Zille, M., Müller, K., Krohn, M., Körbelin, J., Zhang, L., Özorhan, Ü., et al. (2021) · Nature Neuroscience · doi:10.1038/s41593-021-00926-1 · Cited by 259
Self-citationGrowth Factor Receptor Signaling Inhibition Prevents SARS-CoV-2 Replication
Klann, K., Bojková, D., Tascher, G., Ciesek, S., Münch, C., & Cinatl, J. J. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.08.006 · Cited by 237
Self-citationSun, L., Li, P., Ju, X., Rao, J. Y., Huang, W., Ren, L., Zhang, S., Xiong, T., Xu, K., Zhou, X., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.008 · Cited by 229
A high-stringency blueprint of the human proteome
Adhikari, S., Nice, E. C., Deutsch, E. W., Lane, L., Omenn, G. S., Pennington, S. R., Paik, Y.-K., Overall, C. M., Corrales, F. J., Cristea, I. M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19045-9 · Cited by 210
Metformin in COVID-19: A possible role beyond diabetes
Sharma, S., Ray, A., & Sadasivam, B. (2020) · Diabetes Research and Clinical Practice · doi:10.1016/j.diabres.2020.108183 · Cited by 202
Zhou, Y., Liu, Y., Gupta, S., Paramo, M. I., Hou, Y., Mao, C., Luo, Y., Judd, J., Wierbowski, S. D., Bertolotti, M., et al. (2022) · Nature Biotechnology · doi:10.1038/s41587-022-01474-0 · Cited by 214
D’Alessandro, A., Thomas, T. A., Dzieciątkowska, M., Hill, R. C., Francis, R. O., Hudson, K. E., Zimring, J. C., Hod, E. A., Spitalnik, S. L., & Hansen, K. C. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00365 · Cited by 195
Murgolo, N., Therien, A. G., Howell, B. J., Klein, D. J., Koeplinger, K. A., Lieberman, L. A., Adam, G. C., Flynn, J. A., McKenna, P. M., Swaminathan, G., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009225 · Cited by 204
Core mitochondrial genes are down-regulated during SARS-CoV-2 infection of rodent and human hosts
Guarnieri, J. W., Dybas, J. M., Fazelinia, H., Kim, M. S., Frere, J. J., Zhang, Y., Albrecht, Y. E. S., Murdock, D. G., Angelin, A., Singh, L. N., et al. (2023) · Science Translational Medicine · doi:10.1126/scitranslmed.abq1533 · Cited by 235
Circulating mitochondrial DNA is an early indicator of severe illness and mortality from COVID-19
Scozzi, D., Cano, M., Ma, L., Zhou, D., Zhu, J. H., O’Halloran, J. A., Goss, C. W., Rauseo, A. M., Liu, Z., Sahu, S. K., et al. (2021) · JCI Insight · doi:10.1172/jci.insight.143299 · Cited by 181
SARS-CoV-2 gene content and COVID-19 mutation impact by comparing 44 Sarbecovirus genomes
Jungreis, I., Sealfon, R. S. G., & Kellis, M. (2021) · Nature Communications · doi:10.1038/s41467-021-22905-7 · Cited by 193
Zhou, Y., Hou, Y., Shen, J., Mehra, R., Kallianpur, A., Culver, D. A., Gack, M. U., Farha, S., Zein, J., Comhair, S., et al. (2020) · PLoS Biology · doi:10.1371/journal.pbio.3000970 · Cited by 180
The SARS-CoV-2 RNA interactome
Lee, S., Lee, Y.-S., Choi, Y., Son, A., Park, Y., Lee, K., Kim, J., Kim, J., & Kim, V. N. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.04.022 · Cited by 178
Wang, G., Zhang, Q., Zhao, X., Dong, H., Wu, C., Wu, F., Yu, B., Lv, J., Zhang, S., Wu, G., et al. (2020) · Lipids in Health and Disease · doi:10.1186/s12944-020-01382-9 · Cited by 172
Potential protective mechanisms of green tea polyphenol EGCG against COVID-19
Zhang, Z., Zhang, X., Bi, K., He, Y., Yan, W., Yang, C. S., & Zhang, J. (2021) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2021.05.023 · Cited by 173
Zhou, Y., Xu, J., Hou, Y., Leverenz, J. B., Kallianpur, A. R., Mehra, R., Liu, Y., Yu, H., Pieper, A. A., Jehi, L. E., et al. (2021) · Alzheimer s Research & Therapy · doi:10.1186/s13195-021-00850-3 · Cited by 165
Kamel, W., Noerenberg, M., Cerikan, B., Chen, H., Järvelin, A. I., Kammoun, M., Lee, Y. S., Ni, S., García-Moreno, M., Andrejeva, A., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.05.023 · Cited by 157
Comprehensive transcriptomic analysis of COVID-19 blood, lung, and airway
Daamen, A. R., Bachali, P., Owen, K. A., Kingsmore, K. M., Hubbard, E. L., Labonte, A. C., Robl, R. D., Shrotri, S., Grammer, A. C., & Lipsky, P. E. (2021) · Scientific Reports · doi:10.1038/s41598-021-86002-x · Cited by 151
Lack of antiviral activity of darunavir against SARS-CoV-2
Meyer, S. D., Bojková, D., Cinatl, J. J., Damme, E. V., Buyck, C., Loock, M. V., Woodfall, B., & Ciesek, S. (2020) · International Journal of Infectious Diseases · doi:10.1016/j.ijid.2020.05.085 · Cited by 148
Self-citationSARS-CoV-2 disrupts host epigenetic regulation via histone mimicry
Kee, J., Thudium, S., Renner, D. M., Glastad, K. M., Palozola, K. C., Zhang, Z., Li, Y., Lan, Y., Cesare, J., Poleshko, A. S., et al. (2022) · Nature · doi:10.1038/s41586-022-05282-z · Cited by 145
Systematic analysis of SARS-CoV-2 infection of an ACE2-negative human airway cell
Puray‐Chavez, M., LaPak, K. M., Schrank, T. P., Elliott, J. L., Bhatt, D. P., Agajanian, M. J., Jasuja, R., Lawson, D. Q., Davis, K., Rothlauf, P. W., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109364 · Cited by 139
The key role of Warburg effect in SARS-CoV-2 replication and associated inflammatory response
Icard, P., Lincet, H., Wu, Z., Coquerel, A., Forgez, P., Alifano, M., & Fournel, L. (2020) · Biochimie · doi:10.1016/j.biochi.2020.11.010 · Cited by 141
Multilevel proteomics reveals host perturbations by SARS-CoV-2 and SARS-CoVPreprint
Stukalov, A., Girault, V., Grass, V., Karayel, O., Bergant, V., Urban, C., Haas, D. A., Huang, Y., Oubraham, L., Wang, A., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.17.156455 · Cited by 144
Cardozo, K. H. M., Lebkuchen, A., Okai, G. G., Schuch, R. A., Viana, L. G., Olivé, A. N., Lázari, C. D. S., Fraga, A., Granato, C. F. H., Pintão, M. C. T., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19925-0 · Cited by 135
Multi-level inhibition of coronavirus replication by chemical ER stress
Shaban, M. S., Müller, C., Mayr‐Buro, C., Weiser, H., Meier‐Soelch, J., Albert, B. V., Weber, A., Linne, U., Hain, T., Babayev, I., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25551-1 · Cited by 133
S-acylation controls SARS-CoV-2 membrane lipid organization and enhances infectivity
Mesquita, F. S., Abrami, L., Sergeeva, O. A., Turelli, P., Qing, E., Kunz, B., Raclot, C., Montoya, J. P., Abriata, L. A., Gallagher, T., et al. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.09.016 · Cited by 129
Davies, J. P., Almasy, K. M., McDonald, E. F., & Plate, L. (2020) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.0c00500 · Cited by 128
Khadke, S., Ahmed, N., Ahmed, N., Ratts, R., Raju, S., Gallogly, M. M., Lima, M. J. G. D., & Sohail, M. R. (2020) · Virology Journal · doi:10.1186/s12985-020-01415-w · Cited by 127
Understanding the Role of SARS-CoV-2 ORF3a in Viral Pathogenesis and COVID-19
Zhang, J., Ejikemeuwa, A., Gerzanich, V., Nasr, M., Tang, Q., Simard, J. M., & Zhao, Y. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.854567 · Cited by 138
Zhao, M., Yu, Y., Sun, L.-M., Xing, J., Li, T., Zhu, Y., Wang, M., Yu, Y., Xue, W., Xia, T., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22297-8 · Cited by 119
The trans-omics landscape of COVID-19
Wu, P., Chen, D., Ding, W., Wu, P., Hou, H., Bai, Y., Zhou, Y., Li, K., Xiang, S., Liu, P., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24482-1 · Cited by 122
Young, S. A., Taylor, S. N., Cammarata, C. L., Varnado, K. G., Roger-Dalbert, C., Montano, A., Griego-Fullbright, C., Burgard, C., Fernandez, C., Eckert, K., et al. (2020) · Journal of Clinical Microbiology · doi:10.1128/jcm.02338-20 · Cited by 122
Wang, P., Luo, R., Zhang, M., Wang, Y., Song, T., Tao, T., Li, Z., Jin, L., Zheng, H., Chen, W., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-03252-9 · Cited by 118
A critical review on SARS-CoV-2 infectivity in water and wastewater. What do we know?
Giacobbo, A., Rodrigues, M. A. S., Ferreira, J. Z., Bernardes, A. M., & de Pinho, M. N. (2021) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2021.145721 · Cited by 122
Martínez-Colón, G. J., Ratnasiri, K., Chen, R., Jiang, S., ZANLEY, E. J., Rustagi, A., Verma, R., Chen, H. M., Andrews, J. R., Mertz, K. D., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abm9151 · Cited by 140
Actionable Cytopathogenic Host Responses of Human Alveolar Type 2 Cells to SARS-CoV-2
Hekman, R. M., Hume, A. J., Goel, R. K., Abo, K. M., Huang, J., Blum, B. C., Werder, R. B., Suder, E. L., Paul, I., Phanse, S., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.11.028 · Cited by 115
Meyer, B., Chiaravalli, J., Gellenoncourt, S., Brownridge, P., Bryne, D. P., Daly, L. A., Grauslys, A., Walter, M., Agou, F., Chakrabarti, L. A., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25796-w · Cited by 119
Metabolic Perturbation Associated With COVID-19 Disease Severity and SARS-CoV-2 Replication
Krishnan, S., Nordqvist, H., Ambikan, A. T., Gupta, S., Sperk, M., Akusjärvi, S. S., Mikaeloff, F., Benfeitas, R., Saccon, E., Ponnan, S. M., et al. (2021) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2021.100159 · Cited by 112
Sensing of cytoplasmic chromatin by cGAS activates innate immune response in SARS-CoV-2 infection
Zhou, Z. L., Zhang, X., Lei, X., Xiao, X., Jiao, T., Ma, R., Dong, X., Jiang, Q., Wang, W., Shi, Y., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00800-3 · Cited by 120
Tang, C., Chen, J., Zhang, L., Zhang, R., Zhang, S., Ye, S., Zhao, Z., & Yang, D. (2020) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2020.151435 · Cited by 117
Hu, Y., Ma, C., Szeto, T., Hurst, B. L., Tarbet, E. B., & Wang, J. (2021) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.0c00761 · Cited by 115
Zhang, S., Huang, W., Ren, L., Ju, X., Gong, M., Rao, J. Y., Sun, L., Li, P., Ding, Q., Wang, J., et al. (2021) · Cell Research · doi:10.1038/s41422-021-00581-y · Cited by 119
Mitochondria: In the Cross Fire of SARS-CoV-2 and Immunity
Burtscher, J., Cappellano, G., Omori, A., Koshiba, T., & Millet, G. P. (2020) · iScience · doi:10.1016/j.isci.2020.101631 · Cited by 110
Replication kinetics and infectivity of SARS-CoV-2 variants of concern in common cell culture models
Mautner, L., Hoyos, M., Dangel, A., Berger, C., Ehrhardt, A., & Baiker, A. E. (2022) · Virology Journal · doi:10.1186/s12985-022-01802-5 · Cited by 107
Metabolomic analyses reveal new stage-specific features of COVID-19
Jia, H.-L., Liu, C., Li, D., Huang, Q., Liu, D., Zhang, Y., Ye, C., Zhou, D., Wang, Y., Tan, Y., et al. (2021) · European Respiratory Journal · doi:10.1183/13993003.00284-2021 · Cited by 103
Tao, K., Tzou, P. L., Nouhin, J., Bonilla, H. F., Jagannathan, P., & Shafer, R. W. (2021) · Clinical Microbiology Reviews · doi:10.1128/cmr.00109-21 · Cited by 109
Gouveia, D., Miotello, G., Gallais, F., Gaillard, J., Debroas, S., Bellanger, L., Lavigne, J., Sotto, A., Grenga, L., Pible, O., et al. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00535 · Cited by 102
Poran, A., Harjanto, D., Malloy, M., Arieta, C. M., Rothenberg, D. A., Lenkala, D., van Buuren, M. M., Addona, T. A., Rooney, M. S., Srinivasan, L., et al. (2020) · Genome Medicine · doi:10.1186/s13073-020-00767-w · Cited by 101
Tran, V. V., Tran, N. H. T., Hwang, H. S., & Chang, M. (2021) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2021.113192 · Cited by 103
Direct RNA sequencing and early evolution of SARS-CoV-2Preprint
Taiaroa, G., Rawlinson, D., Featherstone, L. A., Pitt, M. E., Caly, L., Druce, J. D., Purcell, D. F. J., Harty, L., Tran, T., Roberts, J., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.05.976167 · Cited by 101
Mechanistic insight into substrate processing and allosteric inhibition of human p97
Pan, M., Yu, Y., Ai, H., Zheng, Q., Xie, Y., Liu, L., & Zhao, M. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-021-00617-2 · Cited by 89
The Mechanism of SARS-CoV-2 Nucleocapsid Protein Recognition by the Human 14-3-3 Proteins
Tugaeva, K. V., Hawkins, D. E. D. P., Smith, J. L. R., Bayfield, O. W., Ker, D.-S., Sysoev, A. A., Klychnikov, O. I., Antson, A. A., & Sluchanko, N. N. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.166875 · Cited by 95
RNA G-quadruplex in TMPRSS2 reduces SARS-CoV-2 infection
Liu, G., Du, W., Sang, X., Tong, Q., Wang, Y., Chen, G., Yuan, Y., Jiang, L., Cheng, W., Liu, D., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-29135-5 · Cited by 98
Comprehensive mapping of SARS-CoV-2 interactions in vivo reveals functional virus-host interactions
Yang, S. L., DeFalco, L., Anderson, D. E., Zhang, Y., Aw, J. G. A., Lim, S. Y., Lim, X. N., Tan, K. Y., Zhang, T., Chawla, T., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25357-1 · Cited by 94
Dynamically evolving novel overlapping gene as a factor in the SARS-CoV-2 pandemic
Nelson, C. W., Ardern, Z., Goldberg, T. L., Meng, C., Kuo, C.-H., Ludwig, C., Kolokotronis, S.-O., & Wei, X. (2020) · eLife · doi:10.7554/elife.59633 · Cited by 87
The SARS-CoV-2 ORF10 is not essential in vitro or in vivo in humans
Pancer, K., Milewska, A., Owczarek, K., Dabrowska, A., Kowalski, M., Łabaj, P. P., Branicki, W., Sanak, M., & Pyrc, K. (2020) · PLOS Pathogens · doi:10.1371/journal.ppat.1008959 · Cited by 83
Barh, D., Tiwari, S., Weener, M. E., Azevedo, V., Góes-Neto, A., Gromiha, M. M., & Ghosh, P. (2020) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2020.104051 · Cited by 90
García‐Revilla, J., Deierborg, T., Venero, J. L., & Boza‐Serrano, A. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.02069 · Cited by 92
Chen, Z., Wang, C., Feng, X., Nie, L., Tang, M., Zhang, H., Xiong, Y., Swisher, S. K., Srivastava, M., & Chen, J. (2021) · The EMBO Journal · doi:10.15252/embj.2021107776 · Cited by 103
Lv, H., Dao, F., Zulfiqar, H., & Lin, H. (2021) · Briefings in Bioinformatics · doi:10.1093/bib/bbab244 · Cited by 91
A high-resolution temporal atlas of the SARS-CoV-2 translatome and transcriptome
Kim, D., Kim, S., Park, J., Chang, H. R., Chang, J., Ahn, J., Park, H., Park, J., Son, N., Kang, G., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25361-5 · Cited by 88
The Role of Tricarboxylic Acid Cycle Metabolites in Viral Infections
Sánchez‐García, F. J., Pérez-Hernández, C. A., Rodríguez-Murillo, M., & Moreno‐Altamirano, M. M. B. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.725043 · Cited by 89
Arieta, C. M., Xie, Y. J., Rothenberg, D., Diao, H., Harjanto, D., Meda, S., Marquart, K., Koenitzer, B., Sciuto, T. E., Lobo, A., et al. (2023) · Cell · doi:10.1016/j.cell.2023.04.007 · Cited by 88
Rosa, R. B., Dantas, W. M., do Nascimento, J. C. F., da Silva, M. V., de Oliveira, R. N., & Pena, L. (2021) · Viruses · doi:10.3390/v13030379 · Cited by 89
Kumar, R., Verma, H., Singhvi, N., Sood, U., Gupta, V., Singh, M., KUMARI, R. R., Hira, P., Nagar, S., Talwar, C., et al. (2020) · mSystems · doi:10.1128/msystems.00505-20 · Cited by 81
Aprotinin Inhibits SARS-CoV-2 Replication
Bojkova, D., Bechtel, M., McLaughlin, K.-M., McGreig, J. E., Klann, K., Bellinghausen, C., Rohde, G., Jonigk, D., Braubach, P., Ciesek, S., et al. (2020) · Cells · doi:10.3390/cells9112377 · Cited by 84
Self-citationATR-FTIR spectrum analysis of saliva samples from COVID-19 positive patients
Martínez-Cuazitl, A., Vázquez-Zapién, G. J., Sánchez-Brito, M., Limón-Pacheco, J. H., Guerrero-Ruiz, M., Garibay-Gonzalez, F., Delgado-Macuil, R. J., de Jesus, M. G., Corona-Perezgrovas, M. Á., Pereyra-Talamantes, A., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-99529-w · Cited by 83
SARS-CoV-2 Disrupts Proximal Elements in the JAK-STAT Pathway
Chen, D. W., Khan, N., Close, B. J., Goel, R. K., Blum, B. C., Tavares, A. H., Kenney, D., Conway, H. L., Ewoldt, J. K., Chitalia, V. C., et al. (2021) · Journal of Virology · doi:10.1128/jvi.00862-21 · Cited by 81
Hallmarks of Metabolic Reprogramming and Their Role in Viral Pathogenesis
Allen, C. N. S., Arjona, S. P., Santerre, M., & Sawaya, B. E. (2022) · Viruses · doi:10.3390/v14030602 · Cited by 85
COVID-19 drug discovery and treatment options
Chan, J. F., Yuan, S., Chu, H., Sridhar, S., & Yuen, K. (2024) · Nature Reviews Microbiology · doi:10.1038/s41579-024-01036-y · Cited by 92
Drug targets for COVID-19 therapeutics: Ongoing global efforts
Saxena, A. (2020) · Journal of Biosciences · doi:10.1007/s12038-020-00067-w · Cited by 84
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