Proteomics of SARS-CoV-2-infected host cells reveals therapy targets
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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.
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Clinical isolate infection models have been developed using Caco-2 cells with temporal proteome changes identified during infection using multiplexed MS by combining metabolic labelling with tandem mass tagging methods.
“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]
Recent proteomics studies have focused on SARS-CoV-2, uncovering additional potential therapeutic targets.
“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]
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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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 11,511 · see citing works
The NumPy Array: A Structure for Efficient Numerical Computation
van der Walt, S., Colbert, S. C., & Varoquaux, G. P. (2011) · Computing in Science & Engineering · doi:10.1109/mcse.2011.37 · Cited by 10,444 · see citing works
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 · see citing works
The Perseus computational platform for comprehensive analysis of (prote)omics data
Tyanova, S., Temu, T., Sinitcyn, P. G., Carlson, A., Hein, M. Y., Geiger, T., Mann, M., & Cox, J. (2016) · Nature Methods · doi:10.1038/nmeth.3901 · Cited by 7,977 · see citing works
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 · see citing works
Detection of 2019 novel coronavirus (2019-nCoV) by real-time RT-PCR
Corman, V. M., Landt, O., Kaiser, M., Molenkamp, R., Meijer, A., Chu, D. K. W., Bleicker, T., Brünink, S., Schneider, J. A., Schmidt, M. L., et al. (2020) · Eurosurveillance · doi:10.2807/1560-7917.es.2020.25.3.2000045 · Cited by 7,266 · see citing works
Wang, M., Cao, R., Zhang, L., Yang, X., Liu, J., Xu, M., Shi, Z., Hú, Z., Zhong, W., & Xiao, G. (2020) · Cell Research · doi:10.1038/s41422-020-0282-0 · Cited by 6,967 · see citing works
Pérez-Riverol, Y., Csordas, A., Bai, J.-W., Bernal-Llinares, M., Hewapathirana, S., Kundu, D. J., Inuganti, A., Griss, J., Mayer, G., Eisenacher, M., et al. (2018) · Nucleic Acids Res. · doi:10.1093/nar/gky1106 · Cited by 6,216 · see citing works
Maere, S., Heymans, K., & Kuiper, M. (2005) · Bioinform. · doi:10.1093/bioinformatics/bti551 · Cited by 4,251 · see citing works
Evidence for gastrointestinal infection of SARS-CoV-2
Xiao, F., Tang, M., Zheng, X., Liu, Y., Li, X., & Shan, H. (2020) · Gastroenterology · doi:10.1053/j.gastro.2020.02.055 · Cited by 2,836 · see citing works
Jin, Y., Cai, L., Cheng, Z., Cheng, H., Deng, T., Fan, Y., Fang, C., Huang, D., Huang, L., Huang, Q., et al. (2020) · Military Medical Research · doi:10.1186/s40779-020-0233-6 · Cited by 2,255 · see citing works
Enrichment Map: A Network-Based Method for Gene-Set Enrichment Visualization and Interpretation
Merico, D., Isserlin, R., Stueker, O., Emili, A., & Bader, G. D. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013984 · Cited by 2,235 · see citing works
Epidemiologic Features and Clinical Course of Patients Infected With SARS-CoV-2 in Singapore
Young, B. E., Ong, S. W. X., Kalimuddin, S., Low, J. G. H., Tan, S. Y., Loh, J., Ng, O. T., Marimuthu, K., Ang, L. W., Mak, T. M., et al. (2020) · JAMA · doi:10.1001/jama.2020.3204 · Cited by 2,058 · see citing works
Zhao, S., Lin, Q., Ran, J., Musa, S. S., Yang, G., Wang, W., Lou, Y., Gao, D., Yang, L., He, D., et al. (2020) · International Journal of Infectious Diseases · doi:10.1016/j.ijid.2020.01.050 · Cited by 1,852 · see citing works
Glycyrrhizin, an active component of liquorice roots, and replication of SARS-associated coronavirus
Cinátl, J., Morgenstern, B., Bauer, G., Chandra, P., Rabenau, H. F., & Hw, D. (2003) · The Lancet · doi:10.1016/s0140-6736(03)13615-x · Cited by 1,163 · see citing works
Evidence of SARS-CoV-2 Infection in Returning Travelers from Wuhan, China
Hoehl, S., Rabenau, H. F., Berger, A., Kortenbusch, M., Cinatl, J. J., Bojková, D., Behrens, P., Böddinghaus, B., Götsch, U., Naujoks, F., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmc2001899 · Cited by 578 · see citing works
Self-citationTreatment of SARS with human interferons
Cinátl, J., Morgenstern, B., Bauer, G., Chandra, P., Rabenau, H. F., & Doerr, H. W. (2003) · The Lancet · doi:10.1016/s0140-6736(03)13973-6 · Cited by 472 · see citing works
Narayanan, K., Huang, C., Lokugamage, K. G., Kamitani, W., Ikegami, T., Tseng, C.-T. K., & Makino, S. (2008) · Journal of Virology · doi:10.1128/jvi.02472-07 · Cited by 421 · see citing works
A two-pronged strategy to suppress host protein synthesis by SARS coronavirus Nsp1 protein
Kamitani, W., Huang, C., Narayanan, K., Lokugamage, K. G., & Makino, S. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1680 · Cited by 410 · see citing works
2019 novel coronavirus of pneumonia in Wuhan, China: emerging attack and management strategies
She, J., Jiang, J., Ye, L., Hu, L., Bai, C., & Song, Y. (2020) · Clinical and Translational Medicine · doi:10.1186/s40169-020-00271-z · Cited by 410 · see citing works
Recent discovery and development of inhibitors targeting coronaviruses
Pillaiyar, T., Meenakshisundaram, S., & Manickam, M. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.01.015 · Cited by 361 · see citing works
Plubell, D. L., Wilmarth, P. A., Zhao, Y., Fenton, A. M., Minnier, J., Reddy, A. P., Klimek, J. E., Yang, X., David, L. L., & Pamir, N. (2017) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m116.065524 · Cited by 337 · see citing works
Ectodomain shedding of angiotensin converting enzyme 2 in human airway epithelia
Jia, H. P., Look, D. C., Tan, P., Shi, L., Hickey, M. A., Gakhar, L., Chappell, M. C., Wohlford-Lenane, C., & McCray, P. B. (2009) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00071.2009 · Cited by 329 · see citing works
High-throughput screening and identification of potent broad-spectrum inhibitors of coronaviruses.
Shen, L., Niu, J., Wang, C., Huang, B., Wang, W., Zhu, N., Deng, Y., Wang, H., Ye, F., Cen, S., et al. (2019) · Journal of Virology · doi:10.1128/jvi.00023-19 · Cited by 319 · see citing works
Tang, B., Wang, X., Li, Q., Bragazzi, N. L., Tang, S., Xiao, Y., & Wu, J. (2020) · SSRN Electronic Journal · doi:10.2139/ssrn.3525558 · Cited by 294 · see citing works
Pinkus, G. S., & SAID, J. W. (1977) · PubMed · Cited by 288 · see citing works
Yan, B., Chu, H., Yang, D., Sze, K. H., Lai, P.-M., Yuan, S., Shuai, H., Wang, Y., Kao, R. Y. T., Chan, J. F., et al. (2019) · Viruses · doi:10.3390/v11010073 · Cited by 267 · see citing works
Nucleoside analogues for the treatment of coronavirus infections
Pruijssers, A. J., & Denison, M. R. (2019) · Current Opinion in Virology · doi:10.1016/j.coviro.2019.04.002 · Cited by 196 · see citing works
Proteomics Analysis Unravels the Functional Repertoire of Coronavirus Nonstructural Protein 3
Neuman, B. W., Joseph, J. S., Saikatendu, K. S., Serrano, P., Chatterjee, A., Johnson, M. A., Liao, L., Klaus, J. P., Yates, J. R., Wüthrich, K., et al. (2008) · Journal of Virology · doi:10.1128/jvi.02631-07 · Cited by 192 · see citing works
A Mighty “Protein Extractor” of the Cell: Structure and Function of the p97/CDC48 ATPase
Ye, Y., Tang, W. K., Zhang, T., & Xia, D. (2017) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2017.00039 · Cited by 183 · see citing works
Whole-exome sequencing for finding de novo mutations in sporadic mental retardation
Robinson, P. (2010) · Genome Biology · doi:10.1186/gb-2010-11-12-144 · Cited by 180 · see citing works
Structural basis of splicing modulation by antitumor macrolide compounds
Cretu, C., Agrawal, A. A., Cook, A., Will, C. L., Fekkes, P., Smith, P. G., Lührmann, R., Larsen, N., Buonamici, S., & Pena, V. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.03.011 · Cited by 174 · see citing works
Functional Interaction Network Construction and Analysis for Disease Discovery
Wu, G., & Haw, R. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6783-4_11 · Cited by 156 · see citing works
Rhinovirus induces an anabolic reprogramming in host cell metabolism essential for viral replication
Gualdoni, G. A., Mayer, K. A., Kapsch, A., Kreuzberg, K., Puck, A., Kienzl, P., Oberndorfer, F., Frühwirth, K., Winkler, S., Blaas, D., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1800525115 · Cited by 148 · see citing works
Tippett, P. S., & Neet, K. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33591-9 · Cited by 141 · see citing works
Marcelin, J. R., Wilson, J. W., & Razonable, R. R. (2014) · Transplant Infectious Disease · doi:10.1111/tid.12194 · Cited by 101 · see citing works
Klann, K., Tascher, G., & Münch, C. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.11.010 · Cited by 95 · see citing works
Self-citationEmmott, E., Munday, D., Bickerton, E., Britton, P., Rodgers, M. A., Whitehouse, A., Zhou, E.-M., & Hiscox, J. A. (2013) · Journal of Virology · doi:10.1128/jvi.00321-13 · Cited by 93 · see citing works
Ribavirin in the treatment of chronic hepatitis C
Martin, P. B., & Jensen, D. M. (2008) · Journal of Gastroenterology and Hepatology · doi:10.1111/j.1440-1746.2008.05398.x · Cited by 88 · see citing works
SAIJO, M., MORIKAWA, S., FUKUSHI, S., MIZUTANI, T., HASEGAWA, H., NAGATA, N., IWATA, N., & KURANE, I. (2005) · Antiviral Research · doi:10.1016/j.antiviral.2005.01.003 · Cited by 82 · see citing works
Wong, H. H., Kumar, P., Tay, F. P., Moreau, D., Liu, D. X., & Bard, F. (2015) · Journal of Virology · doi:10.1128/jvi.01360-15 · Cited by 75 · see citing works
Chen, J.-Y., Chen, W.-N., Poon, V. K., Zheng, B.-J., Lin, X., Wang, Y.-X., & Wen, Y. (2009) · Archives of Virology · doi:10.1007/s00705-009-0323-y · Cited by 57 · see citing works
Song, T., Fang, L., Wang, D., Zhang, R., Zeng, S., An, K., Chen, H., & Xiao, S. (2016) · Journal of Proteomics · doi:10.1016/j.jprot.2016.05.009 · Cited by 55 · see citing works
Jourdan, S. S., Osorio, F. A., & Hiscox, J. A. (2012) · PROTEOMICS · doi:10.1002/pmic.201100469 · Cited by 42 · see citing works
Wu, L. S., Rower, J. E., Burton, J. R., Anderson, P. L., Hammond, K. P., Baouchi‐Mokrane, F., Everson, G. T., Urban, T. J., D’Argenio, D. Z., & Kiser, J. J. (2015) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.04618-14 · Cited by 33 · see citing works
Zhang, J., Hu, Y., Hau, R. K., Musharrafieh, R. G., Ma, C., Zhou, X., Chen, Y., & Wang, J. (2019) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2019.03.020 · Cited by 28 · see citing works
Flagged first, then by citations
2 of the 53 references couldn’t be matched to a known paper.
Cited by
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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 · see citing works
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 3,175 · see citing works
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 1,194 · see citing works
Self-citationCodo, A. C., Davanzo, G. G., Monteiro, L. D. B., de Souza, G. F., Muraro, S. P., Virgílio-da-Silva, J. V., Prodonoff, J. S., Carregari, V. C., de Biagi, C. A. O., Crunfli, F., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.07.007 · Cited by 908 · see citing works
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 · see citing works
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 686 · see citing works
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 662 · see citing works
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 630 · see citing works
Malone, B., Urakova, N., Snijder, E. J., & Campbell, E. A. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00432-z · Cited by 538 · see citing works
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 528 · see citing works
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 · see citing works
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 452 · see citing works
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 · see citing works
Self-citationMulti-organ proteomic landscape of COVID-19 autopsies
Nie, X., Qian, L.-J., Sun, R., Huang, B., Dong, X., Xiao, Q., Zhang, Q.-S., Lu, T., Yue, L., Chen, S., et al. (2020) · medRxiv · doi:10.1016/j.cell.2021.01.004 · Cited by 373 · see citing works
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 · see citing works
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 352 · see citing works
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 · see citing works
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 · see citing works
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. M., et al. (2020) · Nature Microbiology · doi:10.1038/s41564-020-00846-z · Cited by 320 · see citing works
A metabolic handbook for the COVID-19 pandemic
Ayres, J. S. (2020) · Nature Metabolism · doi:10.1038/s42255-020-0237-2 · Cited by 289 · see citing works
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 273 · see citing works
Trougakos, I., Stamatelopoulos, K., Terpos, E., Tsitsilonis, O., Aivalioti, E., Paraskevis, D., Kastritis, E., Pavlakis, G., & Dimopoulos, M. (2021) · Journal of Biomedical Sciences · doi:10.1186/s12929-020-00703-5 · Cited by 241 · see citing works
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 277 · see citing works
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 277 · see citing works
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 · see citing works
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 264 · see citing works
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 260 · see citing works
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 258 · see citing works
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 · see citing works
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 252 · see citing works
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 · see citing works
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 224 · see citing works
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 · see citing works
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 203 · see citing works
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 203 · see citing works
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 198 · see citing works
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 189 · see citing works
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 191 · see citing works
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 179 · see citing works
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 182 · see citing works
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 · see citing works
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 175 · see citing works
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 168 · see citing works
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 171 · see citing works
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 161 · see citing works
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 · see citing works
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 147 · see citing works
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 · see citing works
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 143 · see citing works
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 131 · see citing works
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 140 · see citing works
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 136 · see citing works
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 · see citing works
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 131 · see citing works
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 126 · see citing works
Davies, J. P., Almasy, K. M., McDonald, E. F., & Plate, L. (2020) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.0c00500 · Cited by 129 · see citing works
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 · see citing works
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 125 · see citing works
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 123 · see citing works
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 117 · see citing works
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 · see citing works
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 · see citing works
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 121 · see citing works
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 136 · see citing works
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 119 · see citing works
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 116 · see citing works
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 118 · see citing works
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 118 · see citing works
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 · see citing works
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 112 · see citing works
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 115 · see citing works
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 107 · see citing works
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 104 · see citing works
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 105 · see citing works
Tao, K., Tzou, P. L., Nouhin, J., Bonilla, H., Jagannathan, P., & Shafer, R. (2021) · Clinical Microbiology Reviews · doi:10.1128/cmr.00109-21 · Cited by 72 · see citing works
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 · see citing works
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 102 · see citing works
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 101 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 95 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
García‐Revilla, J., Deierborg, T., Venero, J. L., & Boza‐Serrano, A. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.02069 · Cited by 91 · see citing works
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 102 · see citing works
Lv, H., Dao, F., Zulfiqar, H., & Lin, H. (2021) · Briefings in Bioinformatics · doi:10.1093/bib/bbab244 · Cited by 91 · see citing works
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 90 · see citing works
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 90 · see citing works
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 85 · see citing works
Rosa, R. B., Dantas, W., Nascimento, J. C. F. D., da Silva, M. V., de Oliveira, R. D., & Pena, L. (2021) · Viruses · doi:10.3390/v13030379 · Cited by 77 · see citing works
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 · see citing works
Aprotinin Inhibits SARS-CoV-2 Replication
Bojková, D., Bechtel, M., McLaughlin, K.-M., McGreig, J. E., Klann, K., Bellinghausen, C., Rohde, G. G. U., Jonigk, D. D., Braubach, P., Ciesek, S., et al. (2020) · Cells · doi:10.3390/cells9112377 · Cited by 83 · see citing works
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 · see citing works
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 79 · see citing works
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 83 · see citing works
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 87 · see citing works
Drug targets for COVID-19 therapeutics: Ongoing global efforts
Saxena, A. (2020) · Journal of Biosciences · doi:10.1007/s12038-020-00067-w · Cited by 82 · see citing works
- 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
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