{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T06:08:55Z","timestamp":1790834935882,"version":"4.1.0"},"update-to":[{"DOI":"10.1371\/journal.ppat.1010173","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2022,1,3]],"date-time":"2022-01-03T00:00:00Z","timestamp":1641168000000}}],"reference-count":66,"publisher":"Public Library of Science (PLoS)","issue":"12","license":[{"start":{"date-parts":[[2021,12,20]],"date-time":"2021-12-20T00:00:00Z","timestamp":1639958400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001665","name":"Agence Nationale de la Recherche","doi-asserted-by":"publisher","award":["ANR-10-LABX-62-EIBID"],"award-info":[{"award-number":["ANR-10-LABX-62-EIBID"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001665","name":"Agence Nationale de la Recherche","doi-asserted-by":"publisher","award":["ANR-17-CE12-0007"],"award-info":[{"award-number":["ANR-17-CE12-0007"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002915","name":"Fondation pour la Recherche M\u00e9dicale","doi-asserted-by":"publisher","award":["EQU202003010152"],"award-info":[{"award-number":["EQU202003010152"]}],"id":[{"id":"10.13039\/501100002915","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Fondation iXCore-iXLife"},{"name":"Pasteur-Weizmann foundation"}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p>\n                    For many intracellular bacterial pathogens manipulating host cell survival is essential for maintaining their replicative niche, and is a common strategy used to promote infection. The bacterial pathogen\n                    <jats:italic>Listeria monocytogenes<\/jats:italic>\n                    is well known to hijack host machinery for its own benefit, such as targeting the host histone H3 for modification by SIRT2. However, by what means this modification benefits infection, as well as the molecular players involved, were unknown. Here we show that SIRT2 activity supports\n                    <jats:italic>Listeria<\/jats:italic>\n                    intracellular survival by maintaining genome integrity and host cell viability. This protective effect is dependent on H3K18 deacetylation, which safeguards the host genome by counteracting infection-induced DNA damage. Mechanistically, infection causes SIRT2 to interact with the nucleic acid binding protein TDP-43 and localise to genomic R-loops, where H3K18 deacetylation occurs. This work highlights novel functions of TDP-43 and R-loops during bacterial infection and identifies the mechanism through which\n                    <jats:italic>L<\/jats:italic>\n                    .\n                    <jats:italic>monocytogenes<\/jats:italic>\n                    co-opts SIRT2 to allow efficient infection.\n                  <\/jats:p>","DOI":"10.1371\/journal.ppat.1010173","type":"journal-article","created":{"date-parts":[[2021,12,20]],"date-time":"2021-12-20T14:08:58Z","timestamp":1640009338000},"page":"e1010173","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":23,"title":["Histone H3 deacetylation promotes host cell viability for efficient infection by Listeria monocytogenes"],"prefix":"10.1371","volume":"17","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6538-4012","authenticated-orcid":true,"given":"Matthew J. G.","family":"Eldridge","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5078-4083","authenticated-orcid":true,"given":"M\u00e9lanie A.","family":"Hamon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2021,12,20]]},"reference":[{"key":"ppat.1010173.ref001","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1038\/nrm3293","article-title":"Sirtuins as regulators of metabolism and healthspan","volume":"13","author":"RH Houtkooper","year":"2012","journal-title":"Nat Rev Mol Cell Biol"},{"key":"ppat.1010173.ref002","doi-asserted-by":"crossref","first-page":"756","DOI":"10.1016\/j.tips.2015.08.001","article-title":"Emerging Role of Sirtuin 2 in the Regulation of Mammalian Metabolism","volume":"36","author":"P Gomes","year":"2015","journal-title":"Trends Pharmacol Sci"},{"key":"ppat.1010173.ref003","doi-asserted-by":"crossref","first-page":"1238858","DOI":"10.1126\/science.1238858","article-title":"A Role for SIRT2-Dependent Histone H3K18 Deacetylation in Bacterial Infection","volume":"341","author":"HA Eskandarian","year":"2013","journal-title":"Science (80-)"},{"key":"ppat.1010173.ref004","doi-asserted-by":"crossref","first-page":"1124","DOI":"10.1016\/j.celrep.2018.03.116","article-title":"Infection Reveals a Modification of SIRT2 Critical for Chromatin Association","volume":"23","author":"JM Pereira","year":"2018","journal-title":"Cell Rep"},{"key":"ppat.1010173.ref005","first-page":"1","article-title":"Active nuclear import of the deacetylase Sirtuin-2 is controlled by its C-terminus and importins","volume":"10","author":"MJG Eldridge","year":"2020","journal-title":"Sci Rep"},{"key":"ppat.1010173.ref006","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1016\/j.ccr.2008.09.001","article-title":"Impaired DNA Damage Response, Genome Instability, and Tumorigenesis in SIRT1 Mutant Mice","volume":"14","author":"RH Wang","year":"2008","journal-title":"Cancer Cell"},{"key":"ppat.1010173.ref007","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1038\/emm.2007.2","article-title":"SIRT1 promotes DNA repair activity and deacetylation of Ku70","volume":"39","author":"J Jeong","year":"2007","journal-title":"Exp Mol Med"},{"key":"ppat.1010173.ref008","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1046\/j.1474-9728.2003.00052.x","article-title":"WRN, the protein deficient in Werner syndrome, plays a critical structural role in optimizing DNA repair","volume":"2","author":"L Chen","year":"2003","journal-title":"Aging Cell"},{"key":"ppat.1010173.ref009","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/j.molcel.2010.07.006","article-title":"SIRT1 regulates UV-induced DNA repair through deacetylating XPA","volume":"39","author":"W Fan","year":"2010","journal-title":"Mol Cell"},{"key":"ppat.1010173.ref010","article-title":"SIRT6 is a DNA double-strand break sensor","volume":"9","author":"L Onn","year":"2020","journal-title":"Elife"},{"key":"ppat.1010173.ref011","doi-asserted-by":"crossref","first-page":"434","DOI":"10.1038\/nsmb.3202","article-title":"SIRT6 deacetylates H3K18ac at pericentric chromatin to prevent mitotic errors and cellular senescence","volume":"23","author":"L Tasselli","year":"2016","journal-title":"Nat Struct Mol Biol"},{"key":"ppat.1010173.ref012","doi-asserted-by":"crossref","first-page":"1488","DOI":"10.15252\/embj.201593499","article-title":"SIRT 7 promotes genome integrity and modulates non-homologous end joining DNA repair","volume":"35","author":"BN Vazquez","year":"2016","journal-title":"EMBO J"},{"key":"ppat.1010173.ref013","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.ccr.2009.11.023","article-title":"SIRT3 Is a Mitochondria-Localized Tumor Suppressor Required for Maintenance of Mitochondrial Integrity and Metabolism during Stress","volume":"17","author":"HS Kim","year":"2010","journal-title":"Cancer Cell"},{"key":"ppat.1010173.ref014","doi-asserted-by":"crossref","first-page":"e731","DOI":"10.1038\/cddis.2013.254","article-title":"Interaction of Sirt3 with OGG1 contributes to repair of mitochondrial DNA and protects from apoptotic cell death under oxidative stress","volume":"4","author":"Y Cheng","year":"2013","journal-title":"Cell Death Dis"},{"key":"ppat.1010173.ref015","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1016\/j.ccr.2013.02.024","article-title":"SIRT4 has tumor-suppressive activity and regulates the cellular metabolic response to dna damage by inhibiting mitochondrial glutamine metabolism","volume":"23","author":"SM Jeong","year":"2013","journal-title":"Cancer Cell"},{"key":"ppat.1010173.ref016","doi-asserted-by":"crossref","first-page":"4105","DOI":"10.1093\/hmg\/ddx298","article-title":"The NAD+-dependent deacetylase SIRT2 attenuates oxidative stress and mitochondrial dysfunction and improves insulin sensitivity in hepatocytes","volume":"26","author":"V Lemos","year":"2017","journal-title":"Hum Mol Genet"},{"key":"ppat.1010173.ref017","doi-asserted-by":"crossref","first-page":"82","DOI":"10.3389\/fphar.2012.00082","article-title":"SIRT2 as a Therapeutic Target for Age-Related Disorders","volume":"3","author":"RM de Oliveira","year":"2012","journal-title":"Front Pharmacol"},{"key":"ppat.1010173.ref018","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1101\/gad.211342.112","article-title":"The tumor suppressor SirT2 regulates cell cycle progression and genome stability by modulating the mitotic deposition of H4K20 methylation","volume":"27","author":"L Serrano","year":"2013","journal-title":"Genes Dev"},{"key":"ppat.1010173.ref019","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1016\/j.ccr.2011.09.004","article-title":"SIRT2 Maintains Genome Integrity and Suppresses Tumorigenesis through Regulating APC\/C Activity","volume":"20","author":"HS Kim","year":"2011","journal-title":"Cancer Cell"},{"key":"ppat.1010173.ref020","doi-asserted-by":"crossref","first-page":"13546","DOI":"10.1073\/pnas.1301463110","article-title":"SIRT2 directs the replication stress response through CDK9 deacetylation","volume":"110","author":"H Zhang","year":"2013","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ppat.1010173.ref021","doi-asserted-by":"crossref","first-page":"928","DOI":"10.4161\/cc.27780","article-title":"Listeria monocytogenes induces host DNA damage and delays the host cell cycle to promote infection","volume":"13","author":"E Leit\u00e3o","year":"2014","journal-title":"Cell Cycle"},{"key":"ppat.1010173.ref022","doi-asserted-by":"crossref","first-page":"1004470","DOI":"10.1371\/journal.ppat.1004470","article-title":"Listeria monocytogenes Dampens the DNA Damage Response","volume":"10","author":"A Samba-Louaka","year":"2014","journal-title":"PLoS Pathog"},{"key":"ppat.1010173.ref023","doi-asserted-by":"crossref","first-page":"931","DOI":"10.1083\/jcb.201108081","article-title":"Cell death and infection: A double-edged sword for host and pathogen survival","volume":"195","author":"H Ashida","year":"2011","journal-title":"J Cell Biol"},{"key":"ppat.1010173.ref024","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/j.mib.2017.03.001","article-title":"Modulation of host cell apoptotic pathways by intracellular pathogens","volume":"35","author":"A Friedrich","year":"2017","journal-title":"Curr Opin Microbiol"},{"key":"ppat.1010173.ref025","first-page":"31495","article-title":"The Secreted Protease Factor CPAF Is Responsible for Degrading Pro-apoptotic BH3-only Proteins in Chlamydia trachomatis-infected Cells","volume":"281","author":"M Pirbhai","year":"2006","journal-title":"J Biol Chem"},{"key":"ppat.1010173.ref026","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.coi.2019.05.007","article-title":"Apoptosis inhibition by intracellular bacteria and its consequence on host immunity","volume":"60","author":"SM Behar","year":"2019","journal-title":"Curr Opin Immunol"},{"key":"ppat.1010173.ref027","doi-asserted-by":"crossref","first-page":"9058","DOI":"10.1074\/jbc.M412588200","article-title":"The Salmonella effector protein SopB protects epithelial cells from apoptosis by sustained activation of Akt","volume":"280","author":"LA Knodler","year":"2005","journal-title":"J Biol Chem"},{"key":"ppat.1010173.ref028","doi-asserted-by":"crossref","first-page":"1297","DOI":"10.1053\/j.gastro.2008.12.059","article-title":"Epidermal Growth Factor Receptor Activation Protects Gastric Epithelial Cells From Helicobacter pylori-Induced Apoptosis","volume":"136","author":"F Yan","year":"2009","journal-title":"Gastroenterology"},{"key":"ppat.1010173.ref029","first-page":"e51043","article-title":"Imaging InlC Secretion to Investigate Cellular Infection by the Bacterial Pathogen Listeria monocytogenes","author":"A K\u00fchbacher","year":"2013","journal-title":"JoVE (Journal Vis Exp"},{"key":"ppat.1010173.ref030","doi-asserted-by":"crossref","first-page":"D794","DOI":"10.1093\/nar\/gkx1081","article-title":"The Encyclopedia of DNA elements (ENCODE): data portal update","volume":"46","author":"CA Davis","year":"2018","journal-title":"Nucleic Acids Res"},{"key":"ppat.1010173.ref031","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.24655","article-title":"A type I IFN-dependent DNA damage response regulates the genetic program and inflammasome activation in macrophages","volume":"6","author":"AJ Morales","year":"2017","journal-title":"Elife"},{"key":"ppat.1010173.ref032","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.bbrep.2018.03.009","article-title":"Analysis of the substrate recognition state of TDP-43 to single-stranded DNA using fluorescence correlation spectroscopy","volume":"14","author":"A Kitamura","year":"2018","journal-title":"Biochem Biophys Reports"},{"key":"ppat.1010173.ref033","doi-asserted-by":"crossref","first-page":"4712","DOI":"10.1093\/nar\/gkt1407","article-title":"The crystal structure of TDP-43 RRM1-DNA complex reveals the specific recognition for UG- and TG-rich nucleic acids","volume":"42","author":"PH Kuo","year":"2014","journal-title":"Nucleic Acids Res"},{"key":"ppat.1010173.ref034","doi-asserted-by":"crossref","first-page":"1322","DOI":"10.1086\/420978","article-title":"Nuclear factor TDP-43 binds to the polymorphic TG repeats in CFTR intron 8 and causes skipping of exon 9: A functional link with disease penetrance","volume":"74","author":"E Buratti","year":"2004","journal-title":"Am J Hum Genet"},{"key":"ppat.1010173.ref035","doi-asserted-by":"crossref","first-page":"36337","DOI":"10.1074\/jbc.M104236200","article-title":"Characterization and Functional Implications of the RNA Binding Properties of Nuclear Factor TDP-43, a Novel Splicing Regulator of CFTR Exon 9","volume":"276","author":"E Buratti","year":"2001","journal-title":"J Biol Chem"},{"key":"ppat.1010173.ref036","doi-asserted-by":"crossref","first-page":"1774","DOI":"10.1093\/emboj\/20.7.1774","article-title":"Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping","volume":"20","author":"E Buratti","year":"2001","journal-title":"EMBO J"},{"key":"ppat.1010173.ref037","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1016\/j.neuron.2013.12.018","article-title":"Axonal Transport of TDP-43 mRNA Granules Is Impaired by ALS-Causing Mutations","volume":"81","author":"NH Alami","year":"2014","journal-title":"Neuron"},{"key":"ppat.1010173.ref038","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1093\/hmg\/ddq137","article-title":"TDP-43 and FUS\/TLS: Emerging roles in RNA processing and neurodegeneration","volume":"19","author":"C Lagier-Tourenne","year":"2010","journal-title":"Hum Mol Genet"},{"key":"ppat.1010173.ref039","doi-asserted-by":"crossref","first-page":"3584","DOI":"10.1128\/jvi.69.6.3584-3596.1995","article-title":"Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs","volume":"69","author":"SH Ou","year":"1995","journal-title":"J Virol"},{"key":"ppat.1010173.ref040","doi-asserted-by":"crossref","first-page":"10970","DOI":"10.1074\/jbc.M110.166587","article-title":"TDP-43 is a transcriptional repressor: The testis-specific mouse acrv1 gene is a TDP-43 target in vivo","volume":"286","author":"AS Lalmansingh","year":"2011","journal-title":"J Biol Chem"},{"key":"ppat.1010173.ref041","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1016\/j.bbrc.2012.07.071","article-title":"The N-terminus of TDP-43 promotes its oligomerization and enhances DNA binding affinity","volume":"425","author":"C Chang ke","year":"2012","journal-title":"Biochem Biophys Res Commun"},{"key":"ppat.1010173.ref042","first-page":"1","article-title":"Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation","volume":"8","author":"T Afroz","year":"2017","journal-title":"Nat Commun 2017 81"},{"key":"ppat.1010173.ref043","doi-asserted-by":"crossref","first-page":"1652","DOI":"10.1038\/s12276-020-00513-7","article-title":"The role of TDP-43 propagation in neurodegenerative diseases: integrating insights from clinical and experimental studies","volume":"52","author":"M Jo","year":"2020","journal-title":"Exp Mol Med"},{"key":"ppat.1010173.ref044","doi-asserted-by":"crossref","first-page":"4696","DOI":"10.1073\/pnas.1818415116","article-title":"Motor neuron disease-associated loss of nuclear TDP-43 is linked to DNA double-strand break repair defects","volume":"116","author":"J Mitra","year":"2019","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ppat.1010173.ref045","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s13024-020-00386-4","article-title":"Impaired NHEJ repair in amyotrophic lateral sclerosis is associated with TDP-43 mutations","volume":"15","author":"A Konopka","year":"2020","journal-title":"Mol Neurodegener"},{"key":"ppat.1010173.ref046","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1038\/s41556-021-00663-4","article-title":"R-loops as Janus-faced modulators of DNA repair","volume":"23","author":"A Marnef","year":"2021","journal-title":"Nat Cell Biol"},{"key":"ppat.1010173.ref047","doi-asserted-by":"crossref","first-page":"398","DOI":"10.1016\/j.molcel.2019.01.024","article-title":"R-Loops as Cellular Regulators and Genomic Threats","volume":"73","author":"MP Crossley","year":"2019","journal-title":"Mol Cell"},{"key":"ppat.1010173.ref048","article-title":"Regulatory R-loops as facilitators of gene expression and genome stability","author":"C Niehrs","year":"2020","journal-title":"Nat Rev Mol Cell Biol"},{"key":"ppat.1010173.ref049","doi-asserted-by":"crossref","first-page":"2041","DOI":"10.1101\/gad.17010011","article-title":"R-loop-mediated genomic instability is caused by impairment of replication fork progression","volume":"25","author":"W Gan","year":"2011","journal-title":"Genes Dev"},{"key":"ppat.1010173.ref050","doi-asserted-by":"crossref","first-page":"3167","DOI":"10.1016\/j.celrep.2019.08.041","article-title":"Dual Processing of R-Loops and Topoisomerase I Induces Transcription-Dependent DNA Double-Strand Breaks","volume":"28","author":"A Cristini","year":"2019","journal-title":"Cell Rep"},{"key":"ppat.1010173.ref051","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/ncomms13049","article-title":"Classical non-homologous end-joining pathway utilizes nascent RNA for error-free double-strand break repair of transcribed genes","volume":"7","author":"A Chakraborty","year":"2016","journal-title":"Nat Commun"},{"key":"ppat.1010173.ref052","doi-asserted-by":"crossref","first-page":"558","DOI":"10.1016\/j.cell.2018.08.056","article-title":"Human Rad52 Promotes XPG-Mediated R-loop Processing to Initiate Transcription-Associated Homologous Recombination Repair","volume":"175","author":"T Yasuhara","year":"2018","journal-title":"Cell"},{"key":"ppat.1010173.ref053","doi-asserted-by":"crossref","first-page":"e1009260","DOI":"10.1371\/journal.pgen.1009260","article-title":"TDP-43 mutations link Amyotrophic Lateral Sclerosis with R-loop homeostasis and R loopmediated DNA damage","volume":"16","author":"M Gianini","year":"2020","journal-title":"PLoS Genet"},{"key":"ppat.1010173.ref054","author":"T Mosler","year":"2021","journal-title":"R-loop proximity proteomics identifies a role of DDX41 in transcription-1 associated genomic instability"},{"key":"ppat.1010173.ref055","doi-asserted-by":"crossref","first-page":"1891","DOI":"10.1016\/j.celrep.2018.04.025","article-title":"RNA\/DNA Hybrid Interactome Identifies DXH9 as a Molecular Player in Transcriptional Termination and R-Loop-Associated DNA Damage","volume":"23","author":"A Cristini","year":"2018","journal-title":"Cell Rep"},{"key":"ppat.1010173.ref056","doi-asserted-by":"crossref","first-page":"7870","DOI":"10.1093\/nar\/gkz519","article-title":"SIRT7 mediates L1 elements transcriptional repression and their association with the nuclear lamina","volume":"47","author":"BN Vazquez","year":"2019","journal-title":"Nucleic Acids Res"},{"key":"ppat.1010173.ref057","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1016\/j.molcel.2019.10.020","article-title":"TFIIIC Binding to Alu Elements Controls Gene Expression via Chromatin Looping and Histone Acetylation","volume":"77","author":"R Ferrari","year":"2020","journal-title":"Mol Cell"},{"key":"ppat.1010173.ref058","doi-asserted-by":"crossref","first-page":"11242","DOI":"10.1074\/jbc.AC118.003325","article-title":"The epigenetic regulator SIRT7 guards against mammalian cellular senescence induced by ribosomal DNA instability","volume":"293","author":"S Paredes","year":"2018","journal-title":"J Biol Chem"},{"key":"ppat.1010173.ref059","doi-asserted-by":"crossref","first-page":"1","DOI":"10.7554\/eLife.55415","article-title":"Host sirtuin 2 as an immunotherapeutic target against tuberculosis","volume":"9","author":"A Bhaskar","year":"2020","journal-title":"Elife"},{"key":"ppat.1010173.ref060","doi-asserted-by":"crossref","DOI":"10.1101\/pdb.prot083733","article-title":"Rapid Isolation of Nuclei from Cells In Vitro","volume":"2015","author":"A Nabbi","year":"2015","journal-title":"Cold Spring Harb Protoc"},{"key":"ppat.1010173.ref061","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1038\/s41564-020-00805-8","article-title":"The histone demethylase KDM6B fine-tunes the host response to Streptococcus pneumoniae","volume":"6","author":"MG Connor","year":"2021","journal-title":"Nat Microbiol"},{"key":"ppat.1010173.ref062","doi-asserted-by":"crossref","first-page":"5440","DOI":"10.1128\/AEM.00844-12","article-title":"One-step sequence- and ligation-independent cloning as a rapid and versatile cloning method for functional genomics studies","volume":"78","author":"J-Y Jeong","year":"2012","journal-title":"Appl Environ Microbiol"},{"key":"ppat.1010173.ref063","doi-asserted-by":"crossref","first-page":"41469","DOI":"10.1074\/jbc.M112.367847","article-title":"Oncogene Ras\/phosphatidylinositol 3-kinase signaling targets histone H3 acetylation at lysine 56","volume":"287","author":"Y Liu","year":"2012","journal-title":"J Biol Chem"},{"key":"ppat.1010173.ref064","doi-asserted-by":"crossref","first-page":"e15878","DOI":"10.1371\/journal.pone.0015878","article-title":"The C-terminal TDP-43 fragments have a high aggregation propensity and harm neurons by a dominant-negative mechanism","volume":"5","author":"C","year":"2010","journal-title":"PLoS One"},{"key":"ppat.1010173.ref065","doi-asserted-by":"crossref","first-page":"9047","DOI":"10.1093\/nar\/gku601","article-title":"DNA damage triggers SAF-A and RNA biogenesis factors exclusion from chromatin coupled to R-loops removal","volume":"42","author":"S Britton","year":"2014","journal-title":"Nucleic Acids Res"},{"key":"ppat.1010173.ref066","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1016\/S0003-2697(03)00286-0","article-title":"Site-directed mutagenesis using a single mutagenic oligonucleotide and DpnI digestion of template DNA","volume":"319","author":"AR Shenoy","year":"2003","journal-title":"Anal Biochem"}],"updated-by":[{"DOI":"10.1371\/journal.ppat.1010173","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2022,1,3]],"date-time":"2022-01-03T00:00:00Z","timestamp":1641168000000}}],"container-title":["PLOS Pathogens"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.ppat.1010173","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,1,3]],"date-time":"2022-01-03T13:47:19Z","timestamp":1641217639000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.ppat.1010173"}},"subtitle":[],"editor":[{"given":"Michael R.","family":"Wessels","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2021,12,20]]},"references-count":66,"journal-issue":{"issue":"12","published-online":{"date-parts":[[2021,12,20]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.ppat.1010173","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/2021.07.16.452630","asserted-by":"object"}]},"ISSN":["1553-7374"],"issn-type":[{"value":"1553-7374","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,12,20]]}}}