SARS-CoV-2 infection induces DNA damage, through CHK1 degradation and impaired 53BP1 recruitment, and cellular senescence
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Ana C. Henriques | C. Tripodo | F. d’Adda di Fagagna | A. Marcello | Z. Lavagnino | S. Zacchigna | S. Sepe | M. Iannacone | Ubaldo Gioia | R. Bussani | S. Tavella | F. Pisati | C. Rampazzo | S. Barozzi | Marta Ceccon | A. Paldino | P. Cavalcante | M. Conte | S. Rajasekharan | Tea Carletti | Valeria Fumagalli | P. Martínez-Orellana | M. C. Volpe | A. Colliva | Valentina Matti | Giada Cicio | Matteo Cabrini | Nicola Iacomino | E. Presot | Alessia Paldino | Sreejith Rajasekharan
[1] F. Slack,et al. Severe COVID-19 is associated with molecular signatures of aging in the human brain. , 2022, Nature aging.
[2] Soyoung Lee,et al. COVID-19 and cellular senescence , 2022, Nature reviews. Immunology.
[3] B. Stripp,et al. Pulmonary infection by SARS-CoV-2 induces senescence accompanied by an inflammatory phenotype in severe COVID-19: possible implications for viral mutagenesis , 2022, European Respiratory Journal.
[4] Tokiko Watanabe,et al. SARS-CoV-2 infection triggers paracrine senescence and leads to a sustained senescence-associated inflammatory response , 2022, Nature Aging.
[5] Chao Sui,et al. SARS-CoV-2 NSP13 Inhibits Type I IFN Production by Degradation of TBK1 via p62-Dependent Selective Autophagy , 2022, The Journal of Immunology.
[6] J. Shay,et al. DNA damage response at telomeres boosts the transcription of SARS‐CoV‐2 receptor ACE2 during aging , 2021, EMBO reports.
[7] R. De Francesco,et al. Administration of aerosolized SARS-CoV-2 to K18-hACE2 mice uncouples respiratory infection from fatal neuroinvasion , 2021, Science Immunology.
[8] A. Poso,et al. SARS‐CoV‐2–host proteome interactions for antiviral drug discovery , 2021, Molecular systems biology.
[9] W. Travis,et al. Lung epithelial and endothelial damage, loss of tissue repair, inhibition of fibrinolysis, and cellular senescence in fatal COVID-19 , 2021, Science Translational Medicine.
[10] Hongyan Huang,et al. Micronucleus production, activation of DNA damage response and cGAS-STING signaling in syncytia induced by SARS-CoV-2 infection , 2021, Biology direct.
[11] Y. Mei,et al. SARS–CoV–2 Spike Impairs DNA Damage Repair and Inhibits V(D)J Recombination In Vitro , 2021, Viruses.
[12] D. Bernard,et al. Evidence That SARS-CoV-2 Induces Lung Cell Senescence: Potential Impact on COVID-19 Lung Disease , 2021, American journal of respiratory cell and molecular biology.
[13] Z. Rao,et al. Structural biology of SARS-CoV-2 and implications for therapeutic development , 2021, Nature Reviews Microbiology.
[14] R. Eils,et al. Virus-induced senescence is a driver and therapeutic target in COVID-19 , 2021, Nature.
[15] Nimrat Chatterjee,et al. SARS-CoV-2 triggers DNA damage response in Vero E6 cells , 2021, bioRxiv.
[16] T. Pan,et al. Targeting liquid–liquid phase separation of SARS-CoV-2 nucleocapsid protein promotes innate antiviral immunity by elevating MAVS activity , 2021, Nature Cell Biology.
[17] M. Kohanski,et al. SARS-CoV-2 induces double-stranded RNA-mediated innate immune responses in respiratory epithelial-derived cells and cardiomyocytes , 2021, Proceedings of the National Academy of Sciences.
[18] D. Brodie,et al. Post-acute COVID-19 syndrome , 2021, Nature Medicine.
[19] R. Bartenschlager,et al. Antiviral drug screen identifies DNA-damage response inhibitor as potent blocker of SARS-CoV-2 replication , 2021, Cell Reports.
[20] G. Zimmer,et al. A genome-wide CRISPR screen identifies interactors of the autophagy pathway as conserved coronavirus targets , 2021, bioRxiv.
[21] Zhengfan Jiang,et al. Sensing of cytoplasmic chromatin by cGAS activates innate immune response in SARS-CoV-2 infection , 2021, Signal Transduction and Targeted Therapy.
[22] Jia Wang,et al. SARS-CoV-2 nucleocapsid protein undergoes liquid–liquid phase separation into stress granules through its N-terminal intrinsically disordered region , 2021, Cell discovery.
[23] Mark R. Marten,et al. Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)1 , 2021, Autophagy.
[24] S. Moradi,et al. In silico analysis suggests the RNAi-enhancing antibiotic enoxacin as a potential inhibitor of SARS-CoV-2 infection , 2020, Scientific Reports.
[25] E. Lander,et al. The SARS-CoV-2 RNA–protein interactome in infected human cells , 2020, Nature Microbiology.
[26] D. Baker,et al. Cellular senescence in ageing: from mechanisms to therapeutic opportunities , 2020, Nature Reviews Molecular Cell Biology.
[27] Nicolas L. Fawzi,et al. SARS‐CoV‐2 nucleocapsid protein phase‐separates with RNA and with human hnRNPs , 2020, The EMBO journal.
[28] L. Zentilin,et al. Persistence of viral RNA, pneumocyte syncytia and thrombosis are hallmarks of advanced COVID-19 pathology , 2020, EBioMedicine.
[29] V. Thiel,et al. Coronavirus biology and replication: implications for SARS-CoV-2 , 2020, Nature Reviews Microbiology.
[30] S. Chanda,et al. SARS-CoV-2 Orf6 hijacks Nup98 to block STAT nuclear import and antagonize interferon signaling , 2020, Proceedings of the National Academy of Sciences.
[31] M. Guttman,et al. SARS-CoV-2 Disrupts Splicing, Translation, and Protein Trafficking to Suppress Host Defenses , 2020, Cell.
[32] J. Lou,et al. Liquid–liquid phase separation by SARS-CoV-2 nucleocapsid protein and RNA , 2020, Cell Research.
[33] D. A. Stein,et al. TMPRSS2 and furin are both essential for proteolytic activation of SARS-CoV-2 in human airway cells , 2020, Life Science Alliance.
[34] Andrew R. Leach,et al. The Global Phosphorylation Landscape of SARS-CoV-2 Infection , 2020, Cell.
[35] Eugene V. Koonin,et al. Genomic determinants of pathogenicity in SARS-CoV-2 and other human coronaviruses , 2020, Proceedings of the National Academy of Sciences.
[36] R. Schwartz,et al. Imbalanced Host Response to SARS-CoV-2 Drives Development of COVID-19 , 2020, Cell.
[37] Benjamin J. Polacco,et al. A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug-Repurposing , 2020, Nature.
[38] B. Deplancke,et al. Disparate temperature-dependent virus–host dynamics for SARS-CoV-2 and SARS-CoV in the human respiratory epithelium , 2020, bioRxiv.
[39] Hyeshik Chang,et al. The Architecture of SARS-CoV-2 Transcriptome , 2020, Cell.
[40] F. d’Adda di Fagagna,et al. Functional transcription promoters at DNA double-strand breaks mediate RNA-driven phase separation of damage response factors , 2019, Nature Cell Biology.
[41] V. Gottifredi,et al. Chk1 loss creates replication barriers that compromise cell survival independently of excess origin firing , 2019, The EMBO journal.
[42] M. Altmeyer,et al. Phase separation of 53BP1 determines liquid‐like behavior of DNA repair compartments , 2019, The EMBO journal.
[43] S. Francia,et al. Pharmacological boost of DNA damage response and repair by enhanced biogenesis of DNA damage response RNAs , 2019, Scientific Reports.
[44] A. Venkitaraman,et al. BRCA2 controls DNA:RNA hybrid level at DSBs by mediating RNase H2 recruitment , 2018, Nature Communications.
[45] Zhijian J. Chen,et al. The cGAS–cGAMP–STING pathway connects DNA damage to inflammation, senescence, and cancer , 2018, The Journal of experimental medicine.
[46] Younho Choi,et al. Autophagy during viral infection — a double-edged sword , 2018, Nature Reviews Microbiology.
[47] G. Shivashankar,et al. Damage-induced lncRNAs control the DNA damage response through interaction with DDRNAs at individual double-strand breaks , 2017, Nature Cell Biology.
[48] Dennis E Discher,et al. Mitotic progression following DNA damage enables pattern recognition within micronuclei , 2017, Nature.
[49] Jessica K De Freitas,et al. WRN regulates pathway choice between classical and alternative non-homologous end joining , 2016, Nature Communications.
[50] G. Lenzi,et al. HPV31 utilizes the ATR-Chk1 pathway to maintain elevated RRM2 levels and a replication-competent environment in differentiating Keratinocytes. , 2016, Virology.
[51] J. Mikkelsen,et al. Lack of immunological DNA sensing in hepatocytes facilitates hepatitis B virus infection , 2016, Hepatology.
[52] Marco Y. Hein,et al. p53 down-regulates SARS coronavirus replication and is targeted by the SARS-unique domain and PLpro via E3 ubiquitin ligase RCHY1 , 2016, Proceedings of the National Academy of Sciences.
[53] H. Qi,et al. ATR-CHK1-E2F3 signaling transactivates human ribonucleotide reductase small subunit M2 for DNA repair induced by the chemical carcinogen MNNG. , 2016, Biochimica et biophysica acta.
[54] R. Hollingworth,et al. Activation of the DNA Damage Response by RNA Viruses , 2016, Biomolecules.
[55] Honglin Luo. Interplay between the virus and the ubiquitin–proteasome system: molecular mechanism of viral pathogenesis , 2015, Current Opinion in Virology.
[56] F. d’Adda di Fagagna,et al. Irreparable telomeric DNA damage and persistent DDR signalling as a shared causative mechanism of cellular senescence and ageing , 2014, Current opinion in genetics & development.
[57] D. Green,et al. To Be or Not to Be? How Selective Autophagy and Cell Death Govern Cell Fate , 2014, Cell.
[58] Michal Zimmermann,et al. 53BP1: pro choice in DNA repair. , 2014, Trends in cell biology.
[59] Benjamin G. Bitler,et al. Suppression of nucleotide metabolism underlies the establishment and maintenance of oncogene-induced senescence. , 2013, Cell reports.
[60] R. Grand,et al. DNA viruses and the cellular DNA-damage response. , 2012, The Journal of general virology.
[61] P. Reichard,et al. Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells , 2012, Proceedings of the National Academy of Sciences.
[62] Piero Carninci,et al. Site-specific DICER and DROSHA RNA products control the DNA damage response , 2012, Nature.
[63] F. D. D. Fagagna,et al. Telomeric DNA damage is irreparable and causes persistent DNA-damage-response activation , 2012, Nature Cell Biology.
[64] S. Jackson,et al. Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications. , 2011, Genes & development.
[65] C. Lilley,et al. Genomes in conflict: maintaining genome integrity during virus infection. , 2010, Annual review of microbiology.
[66] C. Lilley,et al. A viral E3 ligase targets RNF8 and RNF168 to control histone ubiquitination and DNA damage responses , 2010, The EMBO journal.
[67] P. Reichard,et al. Quantitation of cellular deoxynucleoside triphosphates , 2009, Nucleic acids research.
[68] J. Bartek,et al. The DNA-damage response in human biology and disease , 2009, Nature.
[69] J. Campisi,et al. Persistent DNA damage signaling triggers senescence-associated inflammatory cytokine secretion , 2009, Nature Cell Biology.
[70] H. Niida,et al. Essential role of Chk1 in S phase progression through regulation of RNR2 expression. , 2008, Biochemical and biophysical research communications.
[71] F. D. D. Fagagna. Living on a break: cellular senescence as a DNA-damage response , 2008, Nature Reviews Cancer.
[72] C. Lilley,et al. Using or abusing: viruses and the cellular DNA damage response. , 2007, Trends in microbiology.
[73] A. Amsterdam,et al. DTL/CDT2 is essential for both CDT1 regulation and the early G2/M checkpoint. , 2006, Genes & development.
[74] S. Bekker-Jensen,et al. Dynamic assembly and sustained retention of 53BP1 at the sites of DNA damage are controlled by Mdc1/NFBD1 , 2005, The Journal of cell biology.
[75] Ying Zhu,et al. Nuclear/nucleolar localization properties of C-terminal nucleocapsid protein of SARS coronavirus , 2005, Virus Research.
[76] C. McCall,et al. Targeted ubiquitination of CDT1 by the DDB1–CUL4A–ROC1 ligase in response to DNA damage , 2004, Nature Cell Biology.
[77] J. Gautier,et al. Regulation of DNA replication by ATR: signaling in response to DNA intermediates. , 2004, DNA repair.
[78] Jianyu Zheng,et al. Radiation-mediated proteolysis of CDT1 by CUL4–ROC1 and CSN complexes constitutes a new checkpoint , 2003, Nature Cell Biology.
[79] Jeffrey M. Trimarchi,et al. Transcription: Sibling rivalry in the E2F family , 2002, Nature Reviews Molecular Cell Biology.
[80] C Roskelley,et al. A biomarker that identifies senescent human cells in culture and in aging skin in vivo. , 1995, Proceedings of the National Academy of Sciences of the United States of America.