{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T20:28:51Z","timestamp":1790972931865,"version":"4.1.0"},"reference-count":205,"publisher":"Oxford University Press (OUP)","issue":"5","funder":[{"DOI":"10.13039\/100000002","name":"NIH","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000049","name":"National Institute on Aging","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000049","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2021,3,18]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Cockayne syndrome (CS) is a segmental premature aging syndrome caused primarily by defects in the CSA or CSB genes. In addition to premature aging, CS patients typically exhibit microcephaly, progressive mental and sensorial retardation and cutaneous photosensitivity. Defects in the CSB gene were initially thought to primarily impair transcription-coupled nucleotide excision repair (TC-NER), predicting a relatively consistent phenotype among CS patients. In contrast, the phenotypes of CS patients are pleiotropic and variable. The latter is consistent with recent work that implicates CSB in multiple cellular systems and pathways, including DNA base excision repair, interstrand cross-link repair, transcription, chromatin remodeling, RNAPII processing, nucleolin regulation, rDNA transcription, redox homeostasis, and mitochondrial function. The discovery of additional functions for CSB could potentially explain the many clinical phenotypes of CSB patients. This review focuses on the diverse roles played by CSB in cellular pathways that enhance genome stability, providing insight into the molecular features of this complex premature aging disease.<\/jats:p>","DOI":"10.1093\/nar\/gkab085","type":"journal-article","created":{"date-parts":[[2021,2,2]],"date-time":"2021-02-02T23:26:11Z","timestamp":1612308371000},"page":"2418-2434","source":"Crossref","is-referenced-by-count":65,"title":["Current and emerging roles of Cockayne syndrome group B (CSB) protein"],"prefix":"10.1093","volume":"49","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-2341-0953","authenticated-orcid":false,"given":"Vinod","family":"Tiwari","sequence":"first","affiliation":[{"name":"Laboratory of Molecular Gerontology, National Institute on Aging, National Institutes of Health, Baltimore, MD 21224, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Beverly A","family":"Baptiste","sequence":"additional","affiliation":[{"name":"Laboratory of Molecular Gerontology, National Institute on Aging, National Institutes of Health, Baltimore, MD 21224, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mustafa N","family":"Okur","sequence":"additional","affiliation":[{"name":"Laboratory of Molecular Gerontology, National Institute on Aging, National Institutes of Health, Baltimore, MD 21224, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4823-6429","authenticated-orcid":false,"given":"Vilhelm A","family":"Bohr","sequence":"additional","affiliation":[{"name":"Laboratory of Molecular Gerontology, National Institute on Aging, National Institutes of Health, Baltimore, MD 21224, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2021,2,15]]},"reference":[{"key":"2021031723301315300_B1","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1002\/(SICI)1098-1004(1999)14:1<9::AID-HUMU2>3.0.CO;2-6","article-title":"A summary of mutations in the UV-sensitive disorders: xeroderma pigmentosum, Cockayne syndrome, and trichothiodystrophy","volume":"14","author":"Cleaver","year":"1999","journal-title":"Hum. Mutat."},{"key":"2021031723301315300_B2","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1086\/301686","article-title":"Molecular analysis of mutations in the CSB (ERCC6) gene in patients with Cockayne syndrome","volume":"62","author":"Mallery","year":"1998","journal-title":"Am. J. Hum. Genet."},{"key":"2021031723301315300_B3","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1016\/0092-8674(90)90122-U","article-title":"A presumed DNA helicase encoded by ERCC-3 is involved in the human repair disorders xeroderma pigmentosum and Cockayne's syndrome","volume":"62","author":"Weeda","year":"1990","journal-title":"Cell"},{"key":"2021031723301315300_B4","first-page":"185","article-title":"Xeroderma pigmentosum complementation group G associated with Cockayne syndrome","volume":"53","author":"Vermeulen","year":"1993","journal-title":"Am. J. Hum. Genet."},{"key":"2021031723301315300_B5","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1016\/j.ajhg.2013.04.007","article-title":"Malfunction of nuclease ERCC1-XPF results in diverse clinical manifestations and causes Cockayne syndrome, xeroderma pigmentosum, and Fanconi anemia","volume":"92","author":"Kashiyama","year":"2013","journal-title":"Am. J. Hum. Genet."},{"key":"2021031723301315300_B6","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1007\/s10038-003-0107-2","article-title":"CKN1 (MIM 216400): mutations in Cockayne syndrome type A and a new common polymorphism","volume":"49","author":"Cao","year":"2004","journal-title":"J. Hum. Genet."},{"key":"2021031723301315300_B7","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/j.mad.2013.02.006","article-title":"Cockayne syndrome: the expanding clinical and mutational spectrum","volume":"134","author":"Laugel","year":"2013","journal-title":"Mech. Ageing Dev."},{"key":"2021031723301315300_B8","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1002\/ajmg.1320420115","article-title":"Cockayne syndrome: review of 140 cases","volume":"42","author":"Nance","year":"1992","journal-title":"Am. J. Med. Genet."},{"key":"2021031723301315300_B9","doi-asserted-by":"crossref","first-page":"744","DOI":"10.1016\/j.dnarep.2008.01.014","article-title":"Incidence of DNA repair deficiency disorders in western Europe: Xeroderma pigmentosum, Cockayne syndrome and trichothiodystrophy","volume":"7","author":"Kleijer","year":"2008","journal-title":"DNA Repair (Amst.)"},{"key":"2021031723301315300_B10","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1038\/gim.2015.110","article-title":"The Cockayne Syndrome Natural History (CoSyNH) study: clinical findings in 102 individuals and recommendations for care","volume":"18","author":"Wilson","year":"2016","journal-title":"Genet. Med."},{"key":"2021031723301315300_B11","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1111\/ped.12635","article-title":"Nationwide survey of Cockayne syndrome in Japan: Incidence, clinical course and prognosis","volume":"57","author":"Kubota","year":"2015","journal-title":"Pediatr. Int."},{"key":"2021031723301315300_B12","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1016\/0092-8674(95)90028-4","article-title":"The Cockayne syndrome group A gene encodes a WD repeat protein that interacts with CSB protein and a subunit of RNA polymerase II TFIIH","volume":"82","author":"Henning","year":"1995","journal-title":"Cell"},{"key":"2021031723301315300_B13","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1007\/s13238-011-1018-1","article-title":"Structure and function of WD40 domain proteins","volume":"2","author":"Xu","year":"2011","journal-title":"Protein Cell"},{"key":"2021031723301315300_B14","doi-asserted-by":"crossref","first-page":"1024","DOI":"10.1016\/j.cell.2011.10.035","article-title":"The molecular basis of CRL4DDB2\/CSA ubiquitin ligase architecture, targeting, and activation","volume":"147","author":"Fischer","year":"2011","journal-title":"Cell"},{"key":"2021031723301315300_B15","doi-asserted-by":"crossref","first-page":"a012625","DOI":"10.1101\/cshperspect.a012625","article-title":"Mammalian transcription-coupled excision repair","volume":"5","author":"Vermeulen","year":"2013","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"2021031723301315300_B16","doi-asserted-by":"crossref","first-page":"1429","DOI":"10.1101\/gad.378206","article-title":"CSA-dependent degradation of CSB by the ubiquitin-proteasome pathway establishes a link between complementation factors of the Cockayne syndrome","volume":"20","author":"Groisman","year":"2006","journal-title":"Genes Dev."},{"key":"2021031723301315300_B17","doi-asserted-by":"crossref","first-page":"1228","DOI":"10.1016\/j.cell.2020.02.010","article-title":"Ubiquitination of DNA damage-stalled RNAPII promotes transcription-coupled repair","volume":"180","author":"Nakazawa","year":"2020","journal-title":"Cell"},{"key":"2021031723301315300_B18","first-page":"231","article-title":"Transcription-coupled nucleotide excision repair is coordinated by ubiquitin and SUMO in response to ultraviolet irradiation","volume":"48","author":"Liebelt","year":"2020","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B19","doi-asserted-by":"crossref","first-page":"5806","DOI":"10.1128\/MCB.10.11.5806","article-title":"Molecular cloning of the human DNA excision repair gene ERCC-6","volume":"10","author":"Troelstra","year":"1990","journal-title":"Mol. Cell. Biol."},{"key":"2021031723301315300_B20","doi-asserted-by":"crossref","first-page":"3583","DOI":"10.1091\/mbc.10.11.3583","article-title":"The ATPase domain but not the acidic region of Cockayne syndrome group B gene product is essential for DNA repair","volume":"10","author":"Brosh","year":"1999","journal-title":"Mol. Biol. Cell"},{"key":"2021031723301315300_B21","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1016\/S0092-8674(00)81918-2","article-title":"SWI2\/SNF2 and related proteins: ATP-driven motors that disrupt protein-DNA interactions","volume":"88","author":"Pazin","year":"1997","journal-title":"Cell"},{"key":"2021031723301315300_B22","doi-asserted-by":"crossref","first-page":"1885","DOI":"10.1074\/jbc.272.3.1885","article-title":"Human transcription-repair coupling factor CSB\/ERCC6 is a DNA-stimulated ATPase but is not a helicase and does not disrupt the ternary transcription complex of stalled RNA polymerase II","volume":"272","author":"Selby","year":"1997","journal-title":"J. Biol. Chem."},{"key":"2021031723301315300_B23","doi-asserted-by":"crossref","first-page":"7643","DOI":"10.1128\/MCB.20.20.7643-7653.2000","article-title":"ATP-dependent chromatin remodeling by the Cockayne syndrome B DNA repair-transcription-coupling factor","volume":"20","author":"Citterio","year":"2000","journal-title":"Mol. Cell. Biol."},{"key":"2021031723301315300_B24","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1093\/nar\/gkj410","article-title":"Cockayne syndrome group B protein has novel strand annealing and exchange activities","volume":"34","author":"Muftuoglu","year":"2006","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B25","doi-asserted-by":"crossref","first-page":"3784","DOI":"10.1093\/nar\/gkz081","article-title":"Structural basis of ubiquitin recognition by the winged-helix domain of Cockayne syndrome group B protein","volume":"47","author":"Takahashi","year":"2019","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B26","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1016\/j.molcel.2010.04.017","article-title":"A ubiquitin-binding domain in Cockayne syndrome B required for transcription-coupled nucleotide excision repair","volume":"38","author":"Anindya","year":"2010","journal-title":"Mol. Cell"},{"key":"2021031723301315300_B27","doi-asserted-by":"crossref","first-page":"2104","DOI":"10.1038\/s41467-020-15903-8","article-title":"The cooperative action of CSB, CSA, and UVSSA target TFIIH to DNA damage-stalled RNA polymerase II","volume":"11","author":"van\u00a0der\u00a0Weegen","year":"2020","journal-title":"Nat. Commun."},{"key":"2021031723301315300_B28","doi-asserted-by":"crossref","first-page":"4306","DOI":"10.1111\/j.1742-4658.2005.04844.x","article-title":"The Cockayne syndrome group B protein is a functional dimer","volume":"272","author":"Christiansen","year":"2005","journal-title":"FEBS J."},{"key":"2021031723301315300_B29","doi-asserted-by":"crossref","first-page":"4722","DOI":"10.1074\/jbc.M409147200","article-title":"The CSB protein actively wraps DNA","volume":"280","author":"Beerens","year":"2005","journal-title":"J. Biol. Chem."},{"key":"2021031723301315300_B30","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1016\/j.ajhg.2019.06.005","article-title":"DNA damage and associated DNA repair defects in disease and premature aging","volume":"105","author":"Tiwari","year":"2019","journal-title":"Am. J. Hum. Genet."},{"key":"2021031723301315300_B31","doi-asserted-by":"crossref","first-page":"e20190085","DOI":"10.1590\/1678-4685-gmb-2019-0085","article-title":"Cockayne syndrome: the many challenges and approaches to understand a multifaceted disease","volume":"43","author":"Vessoni","year":"2020","journal-title":"Genet Mol Biol"},{"key":"2021031723301315300_B32","doi-asserted-by":"crossref","first-page":"4707","DOI":"10.1073\/pnas.87.12.4707","article-title":"The genetic defect in Cockayne syndrome is associated with a defect in repair of UV-induced DNA damage in transcriptionally active DNA","volume":"87","author":"Venema","year":"1990","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021031723301315300_B33","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.mad.2013.12.008","article-title":"Cockayne syndrome group B protein stimulates NEIL2 DNA glycosylase activity","volume":"135","author":"Aamann","year":"2014","journal-title":"Mech. Ageing Dev."},{"key":"2021031723301315300_B34","doi-asserted-by":"crossref","first-page":"2029","DOI":"10.4161\/cc.29018","article-title":"Cockayne syndrome protein A is a transcription factor of RNA polymerase I and stimulates ribosomal biogenesis and growth","volume":"13","author":"Koch","year":"2014","journal-title":"Cell Cycle"},{"key":"2021031723301315300_B35","doi-asserted-by":"crossref","first-page":"e113914","DOI":"10.1371\/journal.pone.0113914","article-title":"Identification of two missense mutations of ERCC6 in three Chinese sisters with Cockayne syndrome by whole exome sequencing","volume":"9","author":"Yu","year":"2014","journal-title":"PLoS One"},{"key":"2021031723301315300_B36","doi-asserted-by":"crossref","first-page":"34931","DOI":"10.1074\/jbc.M004936200","article-title":"XAB2, a novel tetratricopeptide repeat protein involved in transcription-coupled DNA repair and transcription","volume":"275","author":"Nakatsu","year":"2000","journal-title":"J. Biol. Chem."},{"key":"2021031723301315300_B37","doi-asserted-by":"crossref","first-page":"6209","DOI":"10.1073\/pnas.0902113106","article-title":"A UV-sensitive syndrome patient with a specific CSA mutation reveals separable roles for CSA in response to UV and oxidative DNA damage","volume":"106","author":"Nardo","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021031723301315300_B38","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1016\/j.mad.2013.03.009","article-title":"Multiple interaction partners for Cockayne syndrome proteins: implications for genome and transcriptome maintenance","volume":"134","author":"Aamann","year":"2013","journal-title":"Mech. Ageing Dev."},{"key":"2021031723301315300_B39","doi-asserted-by":"crossref","first-page":"2473","DOI":"10.1093\/nar\/gkz1242","article-title":"Cockayne syndrome group A and B proteins function in rRNA transcription through nucleolin regulation","volume":"48","author":"Okur","year":"2020","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B40","doi-asserted-by":"crossref","first-page":"939","DOI":"10.1016\/0092-8674(92)90390-X","article-title":"ERCC6, a member of a subfamily of putative helicases, is involved in Cockayne's syndrome and preferential repair of active genes","volume":"71","author":"Troelstra","year":"1992","journal-title":"Cell"},{"key":"2021031723301315300_B41","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/S0378-1119(00)00172-4","article-title":"Genomic heterogeneity of nucleotide excision repair","volume":"250","author":"Balajee","year":"2000","journal-title":"Gene"},{"key":"2021031723301315300_B42","doi-asserted-by":"crossref","first-page":"e9","DOI":"10.1074\/jbc.O110.000232","article-title":"Discovery and characterization of DNA excision repair pathways: the work of Philip Courtland Hanawalt","volume":"285","author":"Kresge","year":"2010","journal-title":"J. Biol. Chem."},{"key":"2021031723301315300_B43","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1038\/ng.2230","article-title":"UV-sensitive syndrome protein UVSSA recruits USP7 to regulate transcription-coupled repair","volume":"44","author":"Schwertman","year":"2012","journal-title":"Nat. Genet."},{"key":"2021031723301315300_B44","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/S1097-2765(01)00281-7","article-title":"Sequential assembly of the nucleotide excision repair factors in vivo","volume":"8","author":"Volker","year":"2001","journal-title":"Mol. Cell"},{"key":"2021031723301315300_B45","doi-asserted-by":"crossref","first-page":"9870","DOI":"10.1074\/jbc.275.13.9870","article-title":"The xeroderma pigmentosum group C protein complex XPC-HR23B plays an important role in the recruitment of transcription factor IIH to damaged DNA","volume":"275","author":"Yokoi","year":"2000","journal-title":"J. Biol. Chem."},{"key":"2021031723301315300_B46","doi-asserted-by":"crossref","first-page":"5293","DOI":"10.1093\/emboj\/cdg489","article-title":"The comings and goings of nucleotide excision repair factors on damaged DNA","volume":"22","author":"Riedl","year":"2003","journal-title":"EMBO J."},{"key":"2021031723301315300_B47","doi-asserted-by":"crossref","first-page":"6669","DOI":"10.1073\/pnas.95.12.6669","article-title":"Assembly, subunit composition, and footprint of human DNA repair excision nuclease","volume":"95","author":"Wakasugi","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021031723301315300_B48","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1111\/php.12647","article-title":"Nucleotide excision repair: finely tuned molecular orchestra of early pre-incision events","volume":"93","author":"Zhu","year":"2017","journal-title":"Photochem. Photobiol."},{"key":"2021031723301315300_B49","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1038\/nrm3822","article-title":"Understanding nucleotide excision repair and its roles in cancer and ageing","volume":"15","author":"Marteijn","year":"2014","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2021031723301315300_B50","doi-asserted-by":"crossref","first-page":"5011","DOI":"10.1021\/bi00015a012","article-title":"Nucleotide excision repair DNA synthesis by DNA polymerase epsilon in the presence of PCNA, RFC, and RPA","volume":"34","author":"Shivji","year":"1995","journal-title":"Biochemistry"},{"key":"2021031723301315300_B51","doi-asserted-by":"crossref","first-page":"6803","DOI":"10.1128\/MCB.17.12.6803","article-title":"Recruitment of the putative transcription-repair coupling factor CSB\/ERCC6 to RNA polymerase II elongation complexes","volume":"17","author":"Tantin","year":"1997","journal-title":"Mol. Cell. Biol."},{"key":"2021031723301315300_B52","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/j.molcel.2005.09.022","article-title":"Recognition of RNA polymerase II and transcription bubbles by XPG, CSB, and TFIIH: insights for transcription-coupled repair and Cockayne Syndrome","volume":"20","author":"Sarker","year":"2005","journal-title":"Mol. Cell"},{"key":"2021031723301315300_B53","doi-asserted-by":"crossref","first-page":"5955","DOI":"10.1093\/emboj\/16.19.5955","article-title":"The Cockayne syndrome B protein, involved in transcription-coupled DNA repair, resides in an RNA polymerase II-containing complex","volume":"16","author":"van\u00a0Gool","year":"1997","journal-title":"EMBO J."},{"key":"2021031723301315300_B54","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1038\/nature24658","article-title":"Structural basis for the initiation of eukaryotic transcription-coupled DNA repair","volume":"551","author":"Xu","year":"2017","journal-title":"Nature"},{"key":"2021031723301315300_B55","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.dnarep.2018.06.004","article-title":"Efficient UV repair requires disengagement of the CSB winged helix domain from the CSB ATPase domain","volume":"68","author":"Batenburg","year":"2018","journal-title":"DNA Repair (Amst.)"},{"key":"2021031723301315300_B56","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1016\/j.molcel.2009.10.027","article-title":"UV-induced association of the CSB remodeling protein with chromatin requires ATP-dependent relief of N-terminal autorepression","volume":"37","author":"Lake","year":"2010","journal-title":"Mol. Cell"},{"key":"2021031723301315300_B57","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1083\/jcb.200401056","article-title":"DNA damage stabilizes interaction of CSB with the transcription elongation machinery","volume":"166","author":"van\u00a0den\u00a0Boom","year":"2004","journal-title":"J. Cell Biol."},{"key":"2021031723301315300_B58","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1016\/S0092-8674(03)00316-7","article-title":"The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage","volume":"113","author":"Groisman","year":"2003","journal-title":"Cell"},{"key":"2021031723301315300_B59","doi-asserted-by":"crossref","first-page":"4011","DOI":"10.1093\/nar\/gkz055","article-title":"FACT subunit Spt16 controls UVSSA recruitment to lesion-stalled RNA Pol II and stimulates TC-NER","volume":"47","author":"Wienholz","year":"2019","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B60","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1038\/ng.2228","article-title":"Mutations in UVSSA cause UV-sensitive syndrome and destabilize ERCC6 in transcription-coupled DNA repair","volume":"44","author":"Zhang","year":"2012","journal-title":"Nat. Genet."},{"key":"2021031723301315300_B61","doi-asserted-by":"crossref","first-page":"586","DOI":"10.1038\/ng.2229","article-title":"Mutations in UVSSA cause UV-sensitive syndrome and impair RNA polymerase IIo processing in transcription-coupled nucleotide-excision repair","volume":"44","author":"Nakazawa","year":"2012","journal-title":"Nat. Genet."},{"key":"2021031723301315300_B62","doi-asserted-by":"crossref","first-page":"11004","DOI":"10.18632\/oncotarget.14205","article-title":"UV-induced proteolysis of RNA polymerase II is mediated by VCP\/p97 segregase and timely orchestration by Cockayne syndrome B protein","volume":"8","author":"He","year":"2017","journal-title":"Oncotarget"},{"key":"2021031723301315300_B63","doi-asserted-by":"crossref","first-page":"1245","DOI":"10.1016\/j.cell.2020.02.009","article-title":"Regulation of the RNAPII pool is integral to the DNA damage response","volume":"180","author":"Tufegd\u017ei\u0107\u00a0Vidakovi\u0107","year":"2020","journal-title":"Cell"},{"key":"2021031723301315300_B64","doi-asserted-by":"crossref","first-page":"194659","DOI":"10.1016\/j.bbagrm.2020.194659","article-title":"Molecular basis of transcriptional pausing, stalling, and transcription-coupled repair initiation","volume":"1864","author":"Oh","year":"2021","journal-title":"Biochim. Biophys. Acta Gene Regul. Mech."},{"key":"2021031723301315300_B65","doi-asserted-by":"crossref","first-page":"766","DOI":"10.1038\/s41580-019-0169-4","article-title":"The DNA damage response to transcription stress","volume":"20","author":"Lans","year":"2019","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2021031723301315300_B66","doi-asserted-by":"crossref","first-page":"102661","DOI":"10.1016\/j.dnarep.2019.102661","article-title":"Non-canonical DNA\/RNA structures during transcription-coupled double-strand break repair: roadblocks or bona fide repair intermediates","volume":"81","author":"Puget","year":"2019","journal-title":"DNA Repair (Amst.)"},{"key":"2021031723301315300_B67","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1016\/j.tibs.2018.02.010","article-title":"The cellular response to transcription-blocking DNA damage","volume":"43","author":"Gregersen","year":"2018","journal-title":"Trends Biochem. Sci."},{"key":"2021031723301315300_B68","doi-asserted-by":"crossref","first-page":"4093","DOI":"10.1016\/j.jmb.2019.05.040","article-title":"Transcription-coupled repair: from cells to single molecules and back again","volume":"431","author":"Strick","year":"2019","journal-title":"J. Mol. Biol."},{"key":"2021031723301315300_B69","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1177\/0960327112444476","article-title":"Impact of DNA polymorphisms in key DNA base excision repair proteins on cancer risk","volume":"31","author":"Karahalil","year":"2012","journal-title":"Hum. Exp. Toxicol."},{"key":"2021031723301315300_B70","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/j.dnarep.2018.08.013","article-title":"DNA scanning by base excision repair enzymes and implications for pathway coordination","volume":"71","author":"Howard","year":"2018","journal-title":"DNA Repair (Amst.)"},{"key":"2021031723301315300_B71","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1016\/j.tibs.2019.04.006","article-title":"Emerging roles of DNA glycosylases and the base excision repair pathway","volume":"44","author":"Mullins","year":"2019","journal-title":"Trends Biochem. Sci."},{"key":"2021031723301315300_B72","doi-asserted-by":"crossref","first-page":"a012583","DOI":"10.1101\/cshperspect.a012583","article-title":"Base excision repair","volume":"5","author":"Krokan","year":"2013","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"2021031723301315300_B73","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/j.mrrev.2017.02.001","article-title":"Repair of oxidatively induced DNA damage by DNA glycosylases: mechanisms of action, substrate specificities and excision kinetics","volume":"771","author":"Dizdaroglu","year":"2017","journal-title":"Mutat. Res."},{"key":"2021031723301315300_B74","doi-asserted-by":"crossref","first-page":"678","DOI":"10.1089\/ars.2013.5492","article-title":"Human apurinic\/apyrimidinic endonuclease 1","volume":"20","author":"Li","year":"2014","journal-title":"Antioxid. Redox. Signal."},{"key":"2021031723301315300_B75","doi-asserted-by":"crossref","first-page":"1365","DOI":"10.1093\/nar\/27.5.1365","article-title":"Repair of 8-oxoguanine in DNA is deficient in Cockayne syndrome group B cells","volume":"27","author":"Dianov","year":"1999","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B76","doi-asserted-by":"crossref","first-page":"668","DOI":"10.1096\/fj.02-0851com","article-title":"Primary fibroblasts of Cockayne syndrome patients are defective in cellular repair of 8-hydroxyguanine and 8-hydroxyadenine resulting from oxidative stress","volume":"17","author":"Tuo","year":"2003","journal-title":"FASEB J."},{"key":"2021031723301315300_B77","doi-asserted-by":"crossref","first-page":"30832","DOI":"10.1074\/jbc.M204814200","article-title":"The cockayne syndrome group B gene product is involved in cellular repair of 8-hydroxyadenine in DNA","volume":"277","author":"Tuo","year":"2002","journal-title":"J. Biol. Chem."},{"key":"2021031723301315300_B78","doi-asserted-by":"crossref","first-page":"45772","DOI":"10.1074\/jbc.M107888200","article-title":"The Cockayne syndrome group B gene product is involved in general genome base excision repair of 8-hydroxyguanine in DNA","volume":"276","author":"Tuo","year":"2001","journal-title":"J. Biol. Chem."},{"key":"2021031723301315300_B79","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/S0378-1119(01)00870-8","article-title":"Phenotypic consequences of mutations in the conserved motifs of the putative helicase domain of the human Cockayne syndrome group B gene","volume":"283","author":"Muftuoglu","year":"2002","journal-title":"Gene"},{"key":"2021031723301315300_B80","doi-asserted-by":"crossref","first-page":"782","DOI":"10.1093\/nar\/30.3.782","article-title":"Differential requirement for the ATPase domain of the Cockayne syndrome group B gene in the processing of UV-induced DNA damage and 8-oxoguanine lesions in human cells","volume":"30","author":"Selzer","year":"2002","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B81","doi-asserted-by":"crossref","first-page":"8675","DOI":"10.1038\/sj.onc.1205994","article-title":"Mitochondrial repair of 8-oxoguanine is deficient in Cockayne syndrome group B","volume":"21","author":"Stevnsner","year":"2002","journal-title":"Oncogene"},{"key":"2021031723301315300_B82","doi-asserted-by":"crossref","first-page":"9270","DOI":"10.1074\/jbc.M807006200","article-title":"Cockayne syndrome group B protein stimulates repair of formamidopyrimidines by NEIL1 DNA glycosylase","volume":"284","author":"Muftuoglu","year":"2009","journal-title":"J. Biol. Chem."},{"key":"2021031723301315300_B83","doi-asserted-by":"crossref","first-page":"3","DOI":"10.2174\/1874467211205010003","article-title":"Overview of base excision repair biochemistry","volume":"5","author":"Kim","year":"2012","journal-title":"Curr Mol Pharmacol"},{"key":"2021031723301315300_B84","doi-asserted-by":"crossref","first-page":"6530","DOI":"10.1093\/emboj\/20.22.6530","article-title":"XRCC1 coordinates the initial and late stages of DNA abasic site repair through protein-protein interactions","volume":"20","author":"Vidal","year":"2001","journal-title":"EMBO J."},{"key":"2021031723301315300_B85","doi-asserted-by":"crossref","first-page":"4103","DOI":"10.1093\/nar\/gkm404","article-title":"Cockayne syndrome B protein stimulates apurinic endonuclease 1 activity and protects against agents that introduce base excision repair intermediates","volume":"35","author":"Wong","year":"2007","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B86","doi-asserted-by":"crossref","first-page":"3811","DOI":"10.1093\/nar\/gkz120","article-title":"Poly(ADP-ribosyl)ation by PARP1: reaction mechanism and regulatory proteins","volume":"47","author":"Alemasova","year":"2019","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B87","doi-asserted-by":"crossref","first-page":"610","DOI":"10.1038\/nrm.2017.53","article-title":"The multifaceted roles of PARP1 in DNA repair and chromatin remodelling","volume":"18","author":"Ray\u00a0Chaudhuri","year":"2017","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2021031723301315300_B88","doi-asserted-by":"crossref","first-page":"7625","DOI":"10.1128\/MCB.25.17.7625-7636.2005","article-title":"Cooperation of the Cockayne syndrome group B protein and poly(ADP-ribose) polymerase 1 in the response to oxidative stress","volume":"25","author":"Thorslund","year":"2005","journal-title":"Mol. Cell. Biol."},{"key":"2021031723301315300_B89","doi-asserted-by":"crossref","first-page":"17863","DOI":"10.1074\/jbc.RA118.004548","article-title":"Poly(ADP-ribose) polymerase 1 (PARP1) promotes oxidative stress-induced association of Cockayne syndrome group B protein with chromatin","volume":"293","author":"Boetefuer","year":"2018","journal-title":"J. Biol. Chem."},{"key":"2021031723301315300_B90","doi-asserted-by":"crossref","first-page":"5332","DOI":"10.1093\/nar\/gkg715","article-title":"Poly(ADP-ribosyl)ation accelerates DNA repair in a pathway dependent on Cockayne syndrome B protein","volume":"31","author":"Flohr","year":"2003","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B91","doi-asserted-by":"crossref","first-page":"840","DOI":"10.1016\/j.cmet.2014.10.005","article-title":"A high-fat diet and NAD(+) activate Sirt1 to rescue premature aging in cockayne syndrome","volume":"20","author":"Scheibye-Knudsen","year":"2014","journal-title":"Cell Metab."},{"key":"2021031723301315300_B92","doi-asserted-by":"crossref","first-page":"7747","DOI":"10.1093\/nar\/gky579","article-title":"The transcription-coupled DNA repair-initiating protein CSB promotes XRCC1 recruitment to oxidative DNA damage","volume":"46","author":"Menoni","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B93","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1016\/j.dnarep.2017.06.010","article-title":"Taming Tricky DSBs: ATM on duty","volume":"56","author":"Clouaire","year":"2017","journal-title":"DNA Repair (Amst.)"},{"key":"2021031723301315300_B94","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1146\/annurev-genet-110410-132435","article-title":"Double-strand break end resection and repair pathway choice","volume":"45","author":"Symington","year":"2011","journal-title":"Annu. Rev. Genet."},{"key":"2021031723301315300_B95","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1038\/nature06337","article-title":"Human CtIP promotes DNA end resection","volume":"450","author":"Sartori","year":"2007","journal-title":"Nature"},{"key":"2021031723301315300_B96","doi-asserted-by":"crossref","first-page":"7713","DOI":"10.1074\/jbc.M710245200","article-title":"Cell cycle-dependent complex formation of BRCA1.CtIP.MRN is important for DNA double-strand break repair","volume":"283","author":"Chen","year":"2008","journal-title":"J. Biol. Chem."},{"key":"2021031723301315300_B97","doi-asserted-by":"crossref","first-page":"e1169343","DOI":"10.1080\/23723556.2016.1169343","article-title":"BRCA1-CtIP interaction in the repair of DNA double-strand breaks","volume":"3","author":"Aparicio","year":"2016","journal-title":"Mol Cell Oncol"},{"key":"2021031723301315300_B98","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1146\/annurev-biochem-062917-012415","article-title":"The MRE11-RAD50-NBS1 complex conducts the orchestration of damage signaling and outcomes to stress in DNA replication and repair","volume":"87","author":"Syed","year":"2018","journal-title":"Annu. Rev. Biochem."},{"key":"2021031723301315300_B99","doi-asserted-by":"crossref","first-page":"1840","DOI":"10.1111\/j.1349-7006.2011.02037.x","article-title":"BRCA1 contributes to transcription-coupled repair of DNA damage through polyubiquitination and degradation of Cockayne syndrome B protein","volume":"102","author":"Wei","year":"2011","journal-title":"Cancer Sci."},{"key":"2021031723301315300_B100","doi-asserted-by":"crossref","first-page":"1921","DOI":"10.1038\/s41467-017-02114-x","article-title":"ATM and CDK2 control chromatin remodeler CSB to inhibit RIF1 in DSB repair pathway choice","volume":"8","author":"Batenburg","year":"2017","journal-title":"Nat. Commun."},{"key":"2021031723301315300_B101","doi-asserted-by":"crossref","first-page":"10678","DOI":"10.1093\/nar\/gkz784","article-title":"CSB interacts with BRCA1 in late S\/G2 to promote MRN- and CtIP-mediated DNA end resection","volume":"47","author":"Batenburg","year":"2019","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B102","doi-asserted-by":"crossref","first-page":"1399","DOI":"10.15252\/embj.201490041","article-title":"Cockayne syndrome group B protein regulates DNA double-strand break repair and checkpoint activation","volume":"34","author":"Batenburg","year":"2015","journal-title":"EMBO J."},{"key":"2021031723301315300_B103","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1038\/nrc3088","article-title":"DNA interstrand crosslink repair and cancer","volume":"11","author":"Deans","year":"2011","journal-title":"Nat. Rev. Cancer"},{"key":"2021031723301315300_B104","first-page":"4899","article-title":"Transcription-coupled nucleotide excision repair as a determinant of cisplatin sensitivity of human cells","volume":"62","author":"Furuta","year":"2002","journal-title":"Cancer Res."},{"key":"2021031723301315300_B105","doi-asserted-by":"crossref","first-page":"6805","DOI":"10.1038\/sj.onc.1204901","article-title":"P53 plays a protective role against UV- and cisplatin-induced apoptosis in transcription-coupled repair proficient fibroblasts","volume":"20","author":"McKay","year":"2001","journal-title":"Oncogene"},{"key":"2021031723301315300_B106","doi-asserted-by":"crossref","first-page":"8953","DOI":"10.1093\/nar\/gks670","article-title":"Repair of cisplatin-induced DNA interstrand crosslinks by a replication-independent pathway involving transcription-coupled repair and translesion synthesis","volume":"40","author":"Enoiu","year":"2012","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B107","doi-asserted-by":"crossref","first-page":"5382","DOI":"10.1093\/nar\/gki851","article-title":"Triplex targeted genomic crosslinks enter separable deletion and base substitution pathways","volume":"33","author":"Richards","year":"2005","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B108","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1016\/j.jmb.2015.11.020","article-title":"Elements that regulate the DNA damage response of proteins defective in cockayne syndrome","volume":"428","author":"Iyama","year":"2016","journal-title":"J. Mol. Biol."},{"key":"2021031723301315300_B109","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1093\/nar\/gku1279","article-title":"CSB interacts with SNM1A and promotes DNA interstrand crosslink processing","volume":"43","author":"Iyama","year":"2015","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B110","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1093\/nar\/gkg164","article-title":"Functional consequences of mutations in the conserved SF2 motifs and post-translational phosphorylation of the CSB protein","volume":"31","author":"Christiansen","year":"2003","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B111","doi-asserted-by":"crossref","first-page":"4941","DOI":"10.1093\/nar\/gkm386","article-title":"Cockayne syndrome protein B interacts with and is phosphorylated by c-Abl tyrosine kinase","volume":"35","author":"Imam","year":"2007","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B112","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1038\/sj.onc.1203372","article-title":"Role of the ATPase domain of the Cockayne syndrome group B protein in UV induced apoptosis","volume":"19","author":"Balajee","year":"2000","journal-title":"Oncogene"},{"key":"2021031723301315300_B113","doi-asserted-by":"crossref","first-page":"913","DOI":"10.1016\/S1568-7864(02)00116-7","article-title":"Functional crosstalk between hOgg1 and the helicase domain of Cockayne syndrome group B protein","volume":"1","author":"Tuo","year":"2002","journal-title":"DNA Repair (Amst.)"},{"key":"2021031723301315300_B114","doi-asserted-by":"crossref","first-page":"3151","DOI":"10.1093\/nar\/28.16.3151","article-title":"Molecular characterization of an acidic region deletion mutant of Cockayne syndrome group B protein","volume":"28","author":"Sunesen","year":"2000","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B115","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/S0921-8777(98)00051-2","article-title":"Efficient PCNA complex formation is dependent upon both transcription coupled repair and genome overall repair","volume":"409","author":"Balajee","year":"1998","journal-title":"Mutat. Res."},{"key":"2021031723301315300_B116","doi-asserted-by":"crossref","first-page":"4476","DOI":"10.1093\/nar\/27.22.4476","article-title":"Oxidative damage-induced PCNA complex formation is efficient in xeroderma pigmentosum group A but reduced in Cockayne syndrome group B cells","volume":"27","author":"Balajee","year":"1999","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B117","doi-asserted-by":"crossref","first-page":"e1003407","DOI":"10.1371\/journal.pgen.1003407","article-title":"ATP-dependent chromatin remodeling by Cockayne syndrome protein B and NAP1-like histone chaperones is required for efficient transcription-coupled DNA repair","volume":"9","author":"Cho","year":"2013","journal-title":"PLoS Genet."},{"key":"2021031723301315300_B118","doi-asserted-by":"crossref","first-page":"4696","DOI":"10.1093\/nar\/gkx188","article-title":"NAP1L1 accelerates activation and decreases pausing to enhance nucleosome remodeling by CSB","volume":"45","author":"Lee","year":"2017","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B119","doi-asserted-by":"crossref","first-page":"8548","DOI":"10.1093\/nar\/gkz568","article-title":"Cockayne syndrome group B deficiency reduces H3K9me3 chromatin remodeler SETDB1 and exacerbates cellular aging","volume":"47","author":"Lee","year":"2019","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B120","doi-asserted-by":"crossref","first-page":"5247","DOI":"10.3934\/mbe.2019262","article-title":"CSB modulates the competition between HIF-1 and p53 upon hypoxia","volume":"16","author":"Ye","year":"2019","journal-title":"Math Biosci Eng"},{"key":"2021031723301315300_B121","doi-asserted-by":"crossref","first-page":"1665","DOI":"10.1093\/emboj\/cdg142","article-title":"Chromosomal protein HMGN1 enhances the rate of DNA repair in chromatin","volume":"22","author":"Birger","year":"2003","journal-title":"EMBO J."},{"key":"2021031723301315300_B122","doi-asserted-by":"crossref","first-page":"2545","DOI":"10.1038\/emboj.2008.180","article-title":"CSB protein is (a direct target of HIF-1 and) a critical mediator of the hypoxic response","volume":"27","author":"Filippi","year":"2008","journal-title":"EMBO J."},{"key":"2021031723301315300_B123","doi-asserted-by":"crossref","first-page":"9613","DOI":"10.1073\/pnas.0510909103","article-title":"Cockayne syndrome group B protein (CSB) plays a general role in chromatin maintenance and remodeling","volume":"103","author":"Newman","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021031723301315300_B124","doi-asserted-by":"crossref","first-page":"4306","DOI":"10.1073\/pnas.94.9.4306","article-title":"Reduced RNA polymerase II transcription in intact and permeabilized Cockayne syndrome group B cells","volume":"94","author":"Balajee","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021031723301315300_B125","doi-asserted-by":"crossref","first-page":"3636","DOI":"10.1093\/nar\/25.18.3636","article-title":"Reduced RNA polymerase II transcription in extracts of cockayne syndrome and xeroderma pigmentosum\/Cockayne syndrome cells","volume":"25","author":"Dianov","year":"1997","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B126","doi-asserted-by":"crossref","first-page":"14454","DOI":"10.1073\/pnas.1412569111","article-title":"Dysregulation of gene expression as a cause of Cockayne syndrome neurological disease","volume":"111","author":"Wang","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021031723301315300_B127","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.1038\/sj.onc.1206187","article-title":"The transcriptional response after oxidative stress is defective in Cockayne syndrome group B cells","volume":"22","author":"Kyng","year":"2003","journal-title":"Oncogene"},{"key":"2021031723301315300_B128","doi-asserted-by":"crossref","first-page":"7475","DOI":"10.1093\/nar\/gkm744","article-title":"Two faces of p53: aging and tumor suppression","volume":"35","author":"Rodier","year":"2007","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B129","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1038\/ng0695-188","article-title":"p53 modulation of TFIIH-associated nucleotide excision repair activity","volume":"10","author":"Wang","year":"1995","journal-title":"Nat. Genet."},{"key":"2021031723301315300_B130","doi-asserted-by":"crossref","first-page":"693","DOI":"10.4161\/cc.8.5.7754","article-title":"Cockayne syndrome B protein (CSB): linking p53, HIF-1 and p300 to robustness, lifespan, cancer and cell fate decisions","volume":"8","author":"Frontini","year":"2009","journal-title":"Cell Cycle"},{"key":"2021031723301315300_B131","doi-asserted-by":"crossref","first-page":"89","DOI":"10.18632\/aging.100439","article-title":"Interaction between the Cockayne syndrome B and p53 proteins: implications for aging","volume":"4","author":"Frontini","year":"2012","journal-title":"Aging (Albany NY)"},{"key":"2021031723301315300_B132","doi-asserted-by":"crossref","first-page":"1389","DOI":"10.1073\/pnas.0610619104","article-title":"Increased apoptosis, p53 up-regulation, and cerebellar neuronal degeneration in repair-deficient Cockayne syndrome mice","volume":"104","author":"Laposa","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021031723301315300_B133","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/S1568-7864(01)00017-9","article-title":"Transcription coupled repair efficiency determines the cell cycle progression and apoptosis after UV exposure in hamster cells","volume":"1","author":"Proietti\u00a0De\u00a0Santis","year":"2002","journal-title":"DNA Repair (Amst.)"},{"key":"2021031723301315300_B134","doi-asserted-by":"crossref","first-page":"3719","DOI":"10.4161\/cc.10.21.17905","article-title":"CSA and CSB proteins interact with p53 and regulate its Mdm2-dependent ubiquitination","volume":"10","author":"Latini","year":"2011","journal-title":"Cell Cycle"},{"key":"2021031723301315300_B135","doi-asserted-by":"crossref","first-page":"11205","DOI":"10.1073\/pnas.94.21.11205","article-title":"Cockayne syndrome group B protein enhances elongation by RNA polymerase II","volume":"94","author":"Selby","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021031723301315300_B136","doi-asserted-by":"crossref","first-page":"e1004284","DOI":"10.1371\/journal.pgen.1004284","article-title":"The sequence-specific transcription factor c-Jun targets Cockayne syndrome protein B to regulate transcription and chromatin structure","volume":"10","author":"Lake","year":"2014","journal-title":"PLoS Genet."},{"key":"2021031723301315300_B137","doi-asserted-by":"crossref","first-page":"2125","DOI":"10.1093\/nar\/gkv1219","article-title":"The CSB chromatin remodeler and CTCF architectural protein cooperate in response to oxidative stress","volume":"44","author":"Lake","year":"2016","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B138","doi-asserted-by":"crossref","first-page":"30906","DOI":"10.1074\/jbc.R111.324962","article-title":"Genome-wide studies of CCCTC-binding factor (CTCF) and cohesin provide insight into chromatin structure and regulation","volume":"287","author":"Lee","year":"2012","journal-title":"J. Biol. Chem."},{"key":"2021031723301315300_B139","first-page":"1473","article-title":"Failure of RNA synthesis to recover after UV irradiation: an early defect in cells from individuals with Cockayne's syndrome and xeroderma pigmentosum","volume":"42","author":"Mayne","year":"1982","journal-title":"Cancer Res."},{"key":"2021031723301315300_B140","doi-asserted-by":"crossref","first-page":"4155","DOI":"10.1093\/emboj\/16.14.4155","article-title":"Cockayne syndrome: defective repair of transcription","volume":"16","author":"van\u00a0Gool","year":"1997","journal-title":"EMBO J."},{"key":"2021031723301315300_B141","doi-asserted-by":"crossref","first-page":"1915","DOI":"10.1038\/sj.emboj.7601071","article-title":"Cockayne syndrome B protein regulates the transcriptional program after UV irradiation","volume":"25","author":"Proietti-De-Santis","year":"2006","journal-title":"EMBO J."},{"key":"2021031723301315300_B142","doi-asserted-by":"crossref","first-page":"10503","DOI":"10.1073\/pnas.180169797","article-title":"UV-induced inhibition of transcription involves repression of transcription initiation and phosphorylation of RNA polymerase II","volume":"97","author":"Rockx","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021031723301315300_B143","doi-asserted-by":"crossref","first-page":"1054","DOI":"10.1016\/j.molcel.2017.11.009","article-title":"Cockayne's Syndrome A and B proteins regulate transcription arrest after genotoxic stress by promoting ATF3 degradation","volume":"68","author":"Epanchintsev","year":"2017","journal-title":"Mol. Cell"},{"key":"2021031723301315300_B144","doi-asserted-by":"crossref","first-page":"E2261","DOI":"10.1073\/pnas.1220071110","article-title":"Regulatory interplay of Cockayne syndrome B ATPase and stress-response gene ATF3 following genotoxic stress","volume":"110","author":"Kristensen","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021031723301315300_B145","doi-asserted-by":"crossref","first-page":"1105","DOI":"10.1038\/s41598-020-57999-4","article-title":"Defective transcription of ATF3 responsive genes, a marker for Cockayne Syndrome","volume":"10","author":"Epanchintsev","year":"2020","journal-title":"Sci. Rep."},{"key":"2021031723301315300_B146","doi-asserted-by":"crossref","first-page":"E3495","DOI":"10.1073\/pnas.1507105112","article-title":"DNA damage during the G0\/G1 phase triggers RNA-templated, Cockayne syndrome B-dependent homologous recombination","volume":"112","author":"Wei","year":"2015","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021031723301315300_B147","doi-asserted-by":"crossref","first-page":"4235","DOI":"10.1038\/sj.onc.1206611","article-title":"Induction of ATF3 by ionizing radiation is mediated via a signaling pathway that includes ATM, Nibrin1, stress-induced MAPkinases and ATF-2","volume":"22","author":"Kool","year":"2003","journal-title":"Oncogene"},{"key":"2021031723301315300_B148","doi-asserted-by":"crossref","first-page":"386","DOI":"10.1016\/j.molcel.2007.10.008","article-title":"Damage-induced ubiquitylation of human RNA polymerase II by the ubiquitin ligase Nedd4, but not Cockayne syndrome proteins or BRCA1","volume":"28","author":"Anindya","year":"2007","journal-title":"Mol. Cell"},{"key":"2021031723301315300_B149","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1016\/j.cell.2008.04.026","article-title":"A metabolic throttle regulates the epigenetic state of rDNA","volume":"133","author":"Grummt","year":"2008","journal-title":"Cell"},{"key":"2021031723301315300_B150","doi-asserted-by":"crossref","first-page":"17490","DOI":"10.1038\/s41598-018-36027-6","article-title":"Regulation of the Intranuclear Distribution of the Cockayne Syndrome Proteins","volume":"8","author":"Iyama","year":"2018","journal-title":"Sci. Rep."},{"key":"2021031723301315300_B151","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1016\/S1097-2765(02)00678-0","article-title":"CSB is a component of RNA pol I transcription","volume":"10","author":"Bradsher","year":"2002","journal-title":"Mol. Cell"},{"key":"2021031723301315300_B152","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1146\/annurev.cellbio.24.110707.175259","article-title":"The epigenetics of rRNA genes: from molecular to chromosome biology","volume":"24","author":"McStay","year":"2008","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"2021031723301315300_B153","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1016\/j.molcel.2007.06.021","article-title":"Activation of RNA polymerase I transcription by cockayne syndrome group B protein and histone methyltransferase G9a","volume":"27","author":"Yuan","year":"2007","journal-title":"Mol. Cell"},{"key":"2021031723301315300_B154","doi-asserted-by":"crossref","first-page":"4892","DOI":"10.1093\/emboj\/20.17.4892","article-title":"NoRC\u2013a novel member of mammalian ISWI-containing chromatin remodeling machines","volume":"20","author":"Strohner","year":"2001","journal-title":"EMBO J."},{"key":"2021031723301315300_B155","doi-asserted-by":"crossref","first-page":"12502","DOI":"10.1073\/pnas.1610198113","article-title":"Cockayne syndrome group A and B proteins converge on transcription-linked resolution of non-B DNA","volume":"113","author":"Scheibye-Knudsen","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021031723301315300_B156","doi-asserted-by":"crossref","first-page":"1217","DOI":"10.1086\/380399","article-title":"Cockayne syndrome group B cellular and biochemical functions","volume":"73","author":"Licht","year":"2003","journal-title":"Am. J. Hum. Genet."},{"key":"2021031723301315300_B157","doi-asserted-by":"crossref","first-page":"111207","DOI":"10.1016\/j.mad.2020.111207","article-title":"Mitophagy and DNA damage signaling in human aging","volume":"186","author":"Babbar","year":"2020","journal-title":"Mech. Ageing Dev."},{"key":"2021031723301315300_B158","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1016\/j.mad.2013.02.007","article-title":"Mitochondrial deficiency in Cockayne syndrome","volume":"134","author":"Scheibye-Knudsen","year":"2013","journal-title":"Mech. Ageing Dev."},{"key":"2021031723301315300_B159","doi-asserted-by":"crossref","first-page":"e13268","DOI":"10.1111\/acel.13268","article-title":"Cockayne syndrome proteins CSA and CSB maintain mitochondrial homeostasis through NAD+ signaling","volume":"19","author":"Okur","year":"2020","journal-title":"Aging Cell"},{"key":"2021031723301315300_B160","doi-asserted-by":"crossref","first-page":"1189","DOI":"10.1016\/S0531-5565(02)00142-0","article-title":"Mitochondrial repair of 8-oxoguanine and changes with aging","volume":"37","author":"Stevnsner","year":"2002","journal-title":"Exp. Gerontol."},{"key":"2021031723301315300_B161","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.cmet.2016.09.017","article-title":"Mammalian mitochondria and aging: an update","volume":"25","author":"Kauppila","year":"2017","journal-title":"Cell Metab."},{"key":"2021031723301315300_B162","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1016\/S0079-6603(01)68107-8","article-title":"Base excision repair in nuclear and mitochondrial DNA","volume":"68","author":"Dianov","year":"2001","journal-title":"Prog. Nucleic Acid Res. Mol. Biol."},{"key":"2021031723301315300_B163","doi-asserted-by":"crossref","first-page":"1194","DOI":"10.1016\/j.cell.2013.05.039","article-title":"The hallmarks of aging","volume":"153","author":"L\u00f3pez-Ot\u00edn","year":"2013","journal-title":"Cell"},{"key":"2021031723301315300_B164","doi-asserted-by":"crossref","first-page":"2334","DOI":"10.1096\/fj.09-147991","article-title":"Cockayne syndrome group B protein promotes mitochondrial DNA stability by supporting the DNA repair association with the mitochondrial membrane","volume":"24","author":"Aamann","year":"2010","journal-title":"FASEB J."},{"key":"2021031723301315300_B165","doi-asserted-by":"crossref","first-page":"192","DOI":"10.18632\/aging.100546","article-title":"A novel diagnostic tool reveals mitochondrial pathology in human diseases and aging","volume":"5","author":"Scheibye-Knudsen","year":"2013","journal-title":"Aging (Albany NY)"},{"key":"2021031723301315300_B166","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1016\/j.mad.2008.04.009","article-title":"The role of Cockayne syndrome group B (CSB) protein in base excision repair and aging","volume":"129","author":"Stevnsner","year":"2008","journal-title":"Mech. Ageing Dev."},{"key":"2021031723301315300_B167","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41514-019-0040-z","article-title":"Short-term NAD(+) supplementation prevents hearing loss in mouse models of Cockayne syndrome","volume":"6","author":"Okur","year":"2020","journal-title":"NPJ Aging Mech Dis"},{"key":"2021031723301315300_B168","doi-asserted-by":"crossref","first-page":"1468","DOI":"10.4161\/auto.29321","article-title":"Contribution of defective mitophagy to the neurodegeneration in DNA repair-deficient disorders","volume":"10","author":"Scheibye-Knudsen","year":"2014","journal-title":"Autophagy"},{"key":"2021031723301315300_B169","doi-asserted-by":"crossref","first-page":"1098","DOI":"10.1016\/j.dnarep.2008.03.011","article-title":"Mitochondrial DNA, base excision repair and neurodegeneration","volume":"7","author":"de\u00a0Souza-Pinto","year":"2008","journal-title":"DNA Repair (Amst.)"},{"key":"2021031723301315300_B170","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1093\/carcin\/bgn250","article-title":"Base excision repair of oxidative DNA damage and association with cancer and aging","volume":"30","author":"Maynard","year":"2009","journal-title":"Carcinogenesis"},{"key":"2021031723301315300_B171","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/S1568-7864(02)00003-4","article-title":"Repair of 8-oxoG is slower in endogenous nuclear genes than in mitochondrial DNA and is without strand bias","volume":"1","author":"Thorslund","year":"2002","journal-title":"DNA Repair (Amst.)"},{"key":"2021031723301315300_B172","doi-asserted-by":"crossref","first-page":"3722","DOI":"10.1093\/nar\/gki683","article-title":"Localization of mitochondrial DNA base excision repair to an inner membrane-associated particulate fraction","volume":"33","author":"Stuart","year":"2005","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B173","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1084\/jem.20111721","article-title":"Cockayne syndrome group B protein prevents the accumulation of damaged mitochondria by promoting mitochondrial autophagy","volume":"209","author":"Scheibye-Knudsen","year":"2012","journal-title":"J. Exp. Med."},{"key":"2021031723301315300_B174","doi-asserted-by":"crossref","first-page":"520","DOI":"10.1111\/j.1474-9726.2012.00815.x","article-title":"An altered redox balance mediates the hypersensitivity of Cockayne syndrome primary fibroblasts to oxidative stress","volume":"11","author":"Pascucci","year":"2012","journal-title":"Aging Cell"},{"key":"2021031723301315300_B175","doi-asserted-by":"crossref","first-page":"1058","DOI":"10.1111\/febs.14663","article-title":"Toward understanding genomic instability, mitochondrial dysfunction and aging","volume":"286","author":"Fakouri","year":"2019","journal-title":"FEBS J."},{"key":"2021031723301315300_B176","doi-asserted-by":"crossref","first-page":"948","DOI":"10.1016\/j.bbagrm.2012.04.002","article-title":"Human mitochondrial RNA polymerase: structure-function, mechanism and inhibition","volume":"1819","author":"Arnold","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"2021031723301315300_B177","doi-asserted-by":"crossref","first-page":"8392","DOI":"10.1093\/nar\/gks565","article-title":"Human Cockayne syndrome B protein reciprocally communicates with mitochondrial proteins and promotes transcriptional elongation","volume":"40","author":"Berquist","year":"2012","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B178","doi-asserted-by":"crossref","first-page":"820","DOI":"10.1016\/j.jmb.2009.06.078","article-title":"Nucleic acid binding activity of human Cockayne syndrome B protein and identification of Ca(2+) as a novel metal cofactor","volume":"391","author":"Berquist","year":"2009","journal-title":"J. Mol. Biol."},{"key":"2021031723301315300_B179","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1038\/nrm.2016.14","article-title":"Nuclear DNA damage signalling to mitochondria in ageing","volume":"17","author":"Fang","year":"2016","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2021031723301315300_B180","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1016\/j.freeradbiomed.2016.11.050","article-title":"DNA damage related crosstalk between the nucleus and mitochondria","volume":"107","author":"Saki","year":"2017","journal-title":"Free Radic. Biol. Med."},{"key":"2021031723301315300_B181","doi-asserted-by":"crossref","first-page":"770","DOI":"10.1016\/j.freeradbiomed.2017.04.018","article-title":"PARP inhibition protects mitochondria and reduces ROS production via PARP-1-ATF4-MKP-1-MAPK retrograde pathway","volume":"108","author":"Hocsak","year":"2017","journal-title":"Free Radic. Biol. Med."},{"key":"2021031723301315300_B182","doi-asserted-by":"crossref","first-page":"31616","DOI":"10.1074\/jbc.M109.025882","article-title":"Mitochondrial localization of PARP-1 requires interaction with mitofilin and is involved in the maintenance of mitochondrial DNA integrity","volume":"284","author":"Rossi","year":"2009","journal-title":"J. Biol. Chem."},{"key":"2021031723301315300_B183","doi-asserted-by":"crossref","first-page":"13161","DOI":"10.1093\/nar\/gku1089","article-title":"Opposing roles of mitochondrial and nuclear PARP1 in the regulation of mitochondrial and nuclear DNA integrity: implications for the regulation of mitochondrial function","volume":"42","author":"Szczesny","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B184","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1016\/j.bbrc.2015.04.119","article-title":"SIRT1 deacetylates and stabilizes hypoxia-inducible factor-1\u03b1 (HIF-1\u03b1) via direct interactions during hypoxia","volume":"462","author":"Joo","year":"2015","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2021031723301315300_B185","doi-asserted-by":"crossref","first-page":"882","DOI":"10.1016\/j.cell.2014.03.026","article-title":"Defective mitophagy in XPA via PARP-1 hyperactivation and NAD(+)\/SIRT1 reduction","volume":"157","author":"Fang","year":"2014","journal-title":"Cell"},{"key":"2021031723301315300_B186","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":"Serrano","year":"2013","journal-title":"Genes Dev."},{"key":"2021031723301315300_B187","doi-asserted-by":"crossref","first-page":"516","DOI":"10.1016\/j.molmed.2012.05.004","article-title":"Metabolic regulation by SIRT3: implications for tumorigenesis","volume":"18","author":"Finley","year":"2012","journal-title":"Trends Mol. Med."},{"key":"2021031723301315300_B188","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1016\/j.cell.2005.11.044","article-title":"Genomic instability and aging-like phenotype in the absence of mammalian SIRT6","volume":"124","author":"Mostoslavsky","year":"2006","journal-title":"Cell"},{"key":"2021031723301315300_B189","doi-asserted-by":"crossref","first-page":"390","DOI":"10.1126\/science.1099196","article-title":"Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase","volume":"305","author":"Cohen","year":"2004","journal-title":"Science"},{"key":"2021031723301315300_B190","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1097\/MOL.0b013e328328d0a4","article-title":"PGC-1alpha, SIRT1 and AMPK, an energy sensing network that controls energy expenditure","volume":"20","author":"Cant\u00f3","year":"2009","journal-title":"Curr. Opin. Lipidol."},{"key":"2021031723301315300_B191","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1186\/2041-9414-4-6","article-title":"SIRT1\/PARP1 crosstalk: connecting DNA damage and metabolism","volume":"4","author":"Luna","year":"2013","journal-title":"Genome Integr"},{"key":"2021031723301315300_B192","doi-asserted-by":"crossref","first-page":"12017","DOI":"10.1073\/pnas.0705070104","article-title":"AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1alpha","volume":"104","author":"J\u00e4ger","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021031723301315300_B193","doi-asserted-by":"crossref","first-page":"E751","DOI":"10.1152\/ajpendo.00745.2009","article-title":"AMPK and SIRT1: a long-standing partnership","volume":"298","author":"Ruderman","year":"2010","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"2021031723301315300_B194","doi-asserted-by":"crossref","first-page":"e13268","DOI":"10.1111\/acel.13268","article-title":"Cockayne syndrome proteins CSA and CSB maintain mitochondrial homeostasis through NAD(+) signaling","volume":"19","author":"Okur","year":"2020","journal-title":"Aging Cell"},{"key":"2021031723301315300_B195","doi-asserted-by":"crossref","first-page":"566","DOI":"10.1016\/j.cmet.2016.09.004","article-title":"NAD(+) replenishment improves lifespan and healthspan in ataxia telangiectasia models via mitophagy and DNA repair","volume":"24","author":"Fang","year":"2016","journal-title":"Cell Metab."},{"key":"2021031723301315300_B196","doi-asserted-by":"crossref","first-page":"5284","DOI":"10.1038\/s41467-019-13172-8","article-title":"NAD(+) augmentation restores mitophagy and limits accelerated aging in Werner syndrome","volume":"10","author":"Fang","year":"2019","journal-title":"Nat. Commun."},{"key":"2021031723301315300_B197","doi-asserted-by":"crossref","first-page":"102852","DOI":"10.18632\/oncotarget.9913","article-title":"Overexpression of parkin rescues the defective mitochondrial phenotype and the increased apoptosis of Cockayne syndrome A cells","volume":"8","author":"Pascucci","year":"2017","journal-title":"Oncotarget"},{"key":"2021031723301315300_B198","doi-asserted-by":"crossref","first-page":"656","DOI":"10.1016\/j.dnarep.2013.04.018","article-title":"Blinded by the UV light: how the focus on transcription-coupled NER has distracted from understanding the mechanisms of Cockayne syndrome neurologic disease","volume":"12","author":"Brooks","year":"2013","journal-title":"DNA Repair (Amst.)"},{"key":"2021031723301315300_B199","doi-asserted-by":"crossref","first-page":"10973","DOI":"10.1093\/nar\/gkaa795","article-title":"A C. elegans model for neurodegeneration in Cockayne syndrome","volume":"48","author":"Lopes","year":"2020","journal-title":"Nucleic Acids Res."},{"key":"2021031723301315300_B200","doi-asserted-by":"crossref","first-page":"2869","DOI":"10.1016\/j.neurobiolaging.2015.06.010","article-title":"Mitochondrial decline precedes phenotype development in the complement factor H mouse model of retinal degeneration but can be corrected by near infrared light","volume":"36","author":"Calaza","year":"2015","journal-title":"Neurobiol. Aging"},{"key":"2021031723301315300_B201","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1136\/jmedgenet-2017-104877","article-title":"Functional and clinical relevance of novel mutations in a large cohort of patients with Cockayne syndrome","volume":"55","author":"Calmels","year":"2018","journal-title":"J. Med. Genet."},{"key":"2021031723301315300_B202","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1016\/j.mad.2013.04.003","article-title":"Cockayne syndrome pathogenesis: lessons from mouse models","volume":"134","author":"Jaarsma","year":"2013","journal-title":"Mech. Ageing Dev."},{"key":"2021031723301315300_B203","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1084\/jem.20091834","article-title":"Proteins of nucleotide and base excision repair pathways interact in mitochondria to protect from loss of subcutaneous fat, a hallmark of aging","volume":"207","author":"Kamenisch","year":"2010","journal-title":"J. Exp. Med."},{"key":"2021031723301315300_B204","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1016\/j.mad.2008.01.005","article-title":"Clinical implications of the basic defects in Cockayne syndrome and xeroderma pigmentosum and the DNA lesions responsible for cancer, neurodegeneration and aging","volume":"129","author":"Cleaver","year":"2008","journal-title":"Mech. Ageing Dev."},{"key":"2021031723301315300_B205","doi-asserted-by":"crossref","first-page":"1612","DOI":"10.1016\/j.celrep.2018.04.041","article-title":"Loss of proteostasis is a pathomechanism in Cockayne syndrome","volume":"23","author":"Alupei","year":"2018","journal-title":"Cell Rep."}],"container-title":["Nucleic Acids Research"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/academic.oup.com\/nar\/article-pdf\/49\/5\/2418\/36627378\/gkab085.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"http:\/\/academic.oup.com\/nar\/article-pdf\/49\/5\/2418\/36627378\/gkab085.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,3,17]],"date-time":"2021-03-17T19:32:06Z","timestamp":1616009526000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/nar\/article\/49\/5\/2418\/6137297"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,2,15]]},"references-count":205,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2021,2,15]]},"published-print":{"date-parts":[[2021,3,18]]}},"URL":"https:\/\/doi.org\/10.1093\/nar\/gkab085","relation":{},"ISSN":["0305-1048","1362-4962"],"issn-type":[{"value":"0305-1048","type":"print"},{"value":"1362-4962","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2021,3,18]]},"published":{"date-parts":[[2021,2,15]]}}}