The DNA damage response to transcription stress

The Hallmarks of Aging

López-Otín, C., Blasco, M. A., Partridge, L., Serrano, M., & Kroemer, G. (2013) · Cell · doi:10.1016/j.cell.2013.05.039 · Cited by 14,982

Instability and decay of the primary structure of DNA

Lindahl, T. (1993) · Nature · doi:10.1038/362709a0 · Cited by 5,679

Genome maintenance mechanisms for preventing cancer

Hoeijmakers, J. H. J. (2001) · Nature · doi:10.1038/35077232 · Cited by 3,939

Repair Pathway Choices and Consequences at the Double-Strand Break

Ceccaldi, R., Rondinelli, B., & D’Andrea, A. D. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.07.009 · Cited by 1,499

Targeted Apoptosis of Senescent Cells Restores Tissue Homeostasis in Response to Chemotoxicity and Aging

Baar, M. P., Brandt, R. M. C., Putavet, D. A., Klein, J. D. D., Derks, K. W. J., Bourgeois, B. R. M., Stryeck, S., Rijksen, Y., van Willigenburg, H., Feijtel, D. A., et al. (2017) · Cell · doi:10.1016/j.cell.2017.02.031 · Cited by 1,454

Direct Cellular Responses to Platinum-Induced DNA Damage

Jung, Y., & Lippard, S. J. (2007) · Chemical Reviews · doi:10.1021/cr068207j · Cited by 1,412

Understanding nucleotide excision repair and its roles in cancer and ageing

Marteijn, J. A., Lans, H., Vermeulen, W., & Hoeijmakers, J. H. J. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3822 · Cited by 1,192

Transcription-coupled DNA repair: two decades of progress and surprises

Hanawalt, P. C., & Spivak, G. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2549 · Cited by 1,081

R Loops: From Transcription Byproducts to Threats to Genome Stability

Aguilera, A., & García‐Muse, T. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.04.009 · Cited by 1,029

RNA m6A methylation regulates the ultraviolet-induced DNA damage response

Xiang, Y., Laurent, B., Hsu, C.-H., Nachtergaele, S., Lu, Z., Sheng, W., Xu, C., Chen, H., Ouyang, J., Wang, S., et al. (2017) · Nature · doi:10.1038/nature21671 · Cited by 919

Nucleotide Excision Repair in EukaryotesPreprint

Schärer, O. D. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a012609 · Cited by 863

Eukaryotic core promoters and the functional basis of transcription initiation

Haberle, V., & Stark, A. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0028-8 · Cited by 774

R-Loops as Cellular Regulators and Genomic Threats

Crossley, M. P., Bocek, M. J., & Cimprich, K. A. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.01.024 · Cited by 771

The Ubiquitin Ligase Activity in the DDB2 and CSA Complexes Is Differentially Regulated by the COP9 Signalosome in Response to DNA Damage

Groisman, R., Polanowska, J., Kuraoka, I., Sawada, J.-I., Saijo, M., Drapkin, R., Kisselev, A. F., Tanaka, K., & Nakatani, Y. (2003) · Cell · doi:10.1016/s0092-8674(03)00316-7 · Cited by 756

ERCC6, a member of a subfamily of putative helicases, is involved in Cockayne's syndrome and preferential repair of active genes

Troelstra, C., van Gool, A., de Wit, J., Vermeulen, W., Bootsma, D., & Hoeijmakers, J. H. J. (1992) · Cell · doi:10.1016/0092-8674(92)90390-x · Cited by 729

7SK small nuclear RNA binds to and inhibits the activity of CDK9/cyclin T complexes

Nguyen, V. T., Kiss, T., Michels, A. A., & Bensaude, O. (2001) · Nature · doi:10.1038/35104581 · Cited by 708

A Slow RNA Polymerase II Affects Alternative Splicing In Vivo

de la Mata, M., Alonso, C. R., Kadener, S., Fededa, J. P., Blaustein, M., Pelisch, F., Cramer, P., Bentley, D., & Kornblihtt, A. R. (2003) · Molecular Cell · doi:10.1016/j.molcel.2003.08.001 · Cited by 683

Transcription-Replication Conflict Orientation Modulates R-Loop Levels and Activates Distinct DNA Damage Responses

Hamperl, S., Bocek, M. J., Saldivar, J. C., Swigut, T., & Cimprich, K. A. (2017) · Cell · doi:10.1016/j.cell.2017.07.043 · Cited by 678

A new progeroid syndrome reveals that genotoxic stress suppresses the somatotroph axis

Niedernhofer, L. J., Garinis, G. A., Raams, A., Lalai, A. S., Robinson, A. R., Appeldoorn, E., Odijk, H., Oostendorp, R., Ahmad, A., van Leeuwen, W., et al. (2006) · Nature · doi:10.1038/nature05456 · Cited by 669

RNA Polymerase II Elongation Control

Zhou, Q., Li, T., & Price, D. H. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-052610-095910 · Cited by 590

Premature Aging in Mice Deficient in DNA Repair and Transcription

de Boer, J., Andressoo, J. O., de Wit, J., Huijmans, J., Beems, R. B., van Steeg, H., Weeda, G., van der Horst, G. T. J., van Leeuwen, W., Themmen, A. P. N., et al. (2002) · Science · doi:10.1126/science.1070174 · Cited by 545

Inhibition of transcription by platinum antitumor compounds

Todd, R. C., & Lippard, S. J. (2009) · Metallomics · doi:10.1039/b907567d · Cited by 539

A chromatin localization screen reveals poly (ADP ribose)-regulated recruitment of the repressive polycomb and NuRD complexes to sites of DNA damage

Chou, D. M., Adamson, B., Dephoure, N. E., Tan, X., Nottke, A. C., Hurov, K. E., Gygi, S. P., Colaiácovo, M. P., & Elledge, S. J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1012946107 · Cited by 529

The Cockayne syndrome group A gene encodes a WD repeat protein that interacts with CSB protein and a subunit of RNA polymerase II TFIIH

Henning, K. A., Li, L., Iyer, N., McDaniel, L. D., Reagan, M. S., Legerski, R., Schultz, R. A., Stefanini, M., Lehmann, A. R., Mayne, L. V., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90028-4 · Cited by 507

The Molecular Basis of CRL4DDB2/CSA Ubiquitin Ligase Architecture, Targeting, and Activation

Fischer, E. S., Scrima, A., Böhm, K., Matsumoto, S., Lingaraju, G. M., Faty, M., Yasuda, T., Cavadini, S., Wakasugi, M., Hanaoka, F., et al. (2011) · Cell · doi:10.1016/j.cell.2011.10.035 · Cited by 460

Born to run: control of transcription elongation by RNA polymerase II

Chen, F. X., Smith, E. R., & Shilatifard, A. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0010-5 · Cited by 447

Xeroderma pigmentosum, trichothiodystrophy and Cockayne syndrome: A complex genotype–phenotype relationship

Kraemer, K. H., Patronas, N. J., Schiffmann, R., Brooks, B. P., Tamura, D., & DiGiovanna, J. J. (2007) · Neuroscience · doi:10.1016/j.neuroscience.2006.12.020 · Cited by 443

Failure of RNA synthesis to recover after UV irradiation; An early defect in cells from individuals with Cockayne syndrome and xeroderma pigmentosum

Mayne, L. V., & Lehmann, A. R. (1982) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/0027-5107(82)90047-1 · Cited by 420

Mechanisms of Oncogene-Induced Replication Stress: Jigsaw Falling into Place

Kotsantis, P., Petermann, E., & Boulton, S. J. (2018) · Cancer Discovery · doi:10.1158/2159-8290.cd-17-1461 · Cited by 416

Base excision repair: A critical player in many games

Wallace, S. S. (2014) · DNA Repair · doi:10.1016/j.dnarep.2014.03.030 · Cited by 401

Alcohol and endogenous aldehydes damage chromosomes and mutate stem cells

Garaycoechea, J. I., Crossan, G. P., Langevin, F., Mulderrig, L., Louzada, S., Yang, F., Guilbaud, G., Park, N., Roerink, S. F., Nik‐Zainal, S., et al. (2018) · Nature · doi:10.1038/nature25154 · Cited by 397

XPD Helicase Structures and Activities: Insights into the Cancer and Aging Phenotypes from XPD Mutations

Fan, L., Fuss, J. O., Cheng, Q. J., Arvai, A. S., Hammel, M., Roberts, V. A., Cooper, P. K., & Tainer, J. A. (2008) · Cell · doi:10.1016/j.cell.2008.04.030 · Cited by 369

TFIIH: when transcription met DNA repair

Compe, E., & Egly, J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3350 · Cited by 357

A high-fat diet and NAD(+) activate Sirt1 to rescue premature aging in Cockayne syndrome

Scheibye-Knudsen, M., Mitchell, S. J., Fang, E. F., Iyama, T., Ward, T., Wang, J., Dunn, C. A., Singh, N., Veith, S., Hasan-Olive, M. M., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.10.005 · Cited by 352

Transcription-coupled nucleotide excision repair as a determinant of cisplatin sensitivity of human cells.

Furuta, T., Ueda, T., Aune, G. J., Sarasin, A. R., Kraemer, K. H., & Pommier, Y. G. (2002) · PubMed · Cited by 349

Blockage of RNA polymerase as a possible trigger for u.v. light-induced apoptosis.

Ljungman, M. E., & Zhang, F. (1996) · PubMed · Cited by 331

UV-induced ubiquitination of RNA polymerase II: a novel modification deficient in Cockayne syndrome cells.

Bregman, D. B., Halaban, R., van Gool, A. J., Henning, K. A., Friedberg, E. C., & Warren, S. L. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.21.11586 · Cited by 331

Neurotoxicity of oxaliplatin and cisplatin for dorsal root ganglion neurons correlates with platinum–DNA binding

Ta, L. E., Espeset, L., Podratz, J. L., & Windebank, A. J. (2006) · NeuroToxicology · doi:10.1016/j.neuro.2006.04.010 · Cited by 327

Restricted diet delays accelerated ageing and genomic stress in DNA-repair-deficient mice

Vermeij, W. P., Dollé, M. E. T., Reiling, E., Jaarsma, D., Payan-Gomez, C., Bombardieri, C. R., Wu, H., Roks, A. J. M., Botter, S. M., van der Eerden, B. C., et al. (2016) · Nature · doi:10.1038/nature19329 · Cited by 315

DNA Damage Regulates Alternative Splicing through Inhibition of RNA Polymerase II Elongation

Muñoz, M. J., Perez-Santángelo, S., Paronetto, M. P., de la Mata, M., Pelisch, F., Boireau, S., Glover-Cutter, K. M., Ben-Dov, C., Blaustein, M., Lozano, J. J., et al. (2009) · Cell · doi:10.1016/j.cell.2009.03.010 · Cited by 310

Cockayne syndrome group B protein enhances elongation by RNA polymerase II

Selby, C. P., & Sancar, A. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.21.11205 · Cited by 309

Transcription Recovery after DNA Damage Requires Chromatin Priming by the H3.3 Histone Chaperone HIRA

Adam, S., Polo, S. E., & Almouzni, G. (2013) · Cell · doi:10.1016/j.cell.2013.08.029 · Cited by 309

E. coli Transcription Repair Coupling Factor (Mfd Protein) Rescues Arrested Complexes by Promoting Forward Translocation

Park, J., Marr, M. T., & Roberts, J. W. (2002) · Cell · doi:10.1016/s0092-8674(02)00769-9 · Cited by 306

The Oxidative DNA Lesion 8,5′-(S)-Cyclo-2′-deoxyadenosine Is Repaired by the Nucleotide Excision Repair Pathway and Blocks Gene Expression in Mammalian Cells

Brooks, P. J., Wise, D. S., Berry, D. A., Kosmoski, J. V., Smerdon, M. J., Somers, R. L., Mackie, H., Spoonde, A. Y., Ackerman, E. J., Coleman, K. G., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002259200 · Cited by 298

Pre-mRNA splicing is facilitated by an optimal RNA polymerase II elongation rate

Fong, N., Kim, H., Zhou, Y., Ji, X., Qiu, J., Saldi, T., Diener, K., Jones, K., Fu, X.-D., & Bentley, D. L. (2014) · Genes & Development · doi:10.1101/gad.252106.114 · Cited by 287

A single-molecule view of transcription reveals convoys of RNA polymerases and multi-scale bursting

Tantale, K., Mueller, F., Kozulic-Pirher, A., Lesne, A., Victor, J., Robert, M.-C., Capozi, S., Chouaib, R., Baecker, V., Langerak, J. M., et al. (2016) · Nature Communications · doi:10.1038/ncomms12248 · Cited by 286

Conflict Resolution in the Genome: How Transcription and Replication Make It Work

Hamperl, S., & Cimprich, K. A. (2016) · Cell · doi:10.1016/j.cell.2016.09.053 · Cited by 285

UV-sensitive syndrome protein UVSSA recruits USP7 to regulate transcription-coupled repair

Schwertman, P., Lagarou, A., Dekkers, D. H. W., Raams, A., van der Hoek, A. C., Laffeber, C., Hoeijmakers, J. H. J., Demmers, J. A. A., Fousteri, M., Vermeulen, W., et al. (2012) · Nature Genetics · doi:10.1038/ng.2230 · Cited by 279

RNA Polymerase Backtracking in Gene Regulation and Genome Instability

Nudler, E. (2012) · Cell · doi:10.1016/j.cell.2012.06.003 · Cited by 273

CSA-dependent degradation of CSB by the ubiquitin-proteasome pathway establishes a link between complementation factors of the Cockayne syndrome.

Groisman, R., Kuraoka, I., Chevallier, O., Gaye, N., Magnaldo, T., Tanaka, K., Kisselev, A. F., Harel-Bellan, A., & Nakatani, Y. (2006) · Genes & Development · doi:10.1101/gad.378206 · Cited by 268

Transcription-replication encounters, consequences and genomic instability

Helmrich, A., Ballarino, M., Nudler, E., & Tora, L. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2543 · Cited by 267

The Cockayne syndrome B protein, involved in transcription‐coupled DNA repair, resides in an RNA polymerase II‐containing complex

van Gool, A. J., Citterio, E., Rademakers, S., Os, R. I. V. R.-V., Vermeulen, W., Constantinou, A., Egly, J., Bootsma, D., & Hoeijmakers, J. H. J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.19.5955 · Cited by 261

Translesion DNA polymerases in eukaryotes: what makes them tick?

Vaisman, A., & Woodgate, R. (2017) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2017.1291576 · Cited by 261

Replication-Transcription Conflicts Generate R-Loops that Orchestrate Bacterial Stress Survival and Pathogenesis

Lang, K. S., Hall, A. N., Merrikh, C. N., Ragheb, M. N., Tabakh, H., Pollock, A. J., Woodward, J. J., Dreifus, J. E., & Merrikh, H. (2017) · Cell · doi:10.1016/j.cell.2017.07.044 · Cited by 260

CPD Damage Recognition by Transcribing RNA Polymerase II

Brueckner, F., Hennecke, U., Carell, T., & Cramer, P. (2007) · Science · doi:10.1126/science.1135400 · Cited by 257

Genome-wide analysis of human global and transcription-coupled excision repair of UV damage at single-nucleotide resolutionPreprint

Hu, J., Adar, S., Selby, C. P., Lieb, J. D., & Sancar, A. (2015) · Genes & Development · doi:10.1101/gad.261271.115 · Cited by 254

The core spliceosome as target and effector of non-canonical ATM signalling

Tresini, M., Warmerdam, D. O., Kolovos, P., Snijder, L., Vrouwe, M. G., Demmers, J. A. A., van IJcken, W. F. J., Grosveld, F. G., Medema, R. H., Hoeijmakers, J. H. J., et al. (2015) · Nature · doi:10.1038/nature14512 · Cited by 252

Ataxia telangiectasia mutated activation by transcription‐ and topoisomerase I‐induced DNA double‐strand breaks

Sordet, O., Redon, C. E., Guirouilh‐Barbat, J., Smith, S. H., Solier, S., Douarre, C., Conti, C., Nakamura, A., Das, B. B., Nicolas, E., et al. (2009) · EMBO Reports · doi:10.1038/embor.2009.97 · Cited by 245

Transcription‐coupled repair removes both cyclobutane pyrimidine dimers and 6‐4 photoproducts with equal efficiency and in a sequential way from transcribed DNA in xeroderma pigmentosum group C fibroblasts.

van Hoffen, A., Venema, J., Meschini, R., van Zeeland, A. A., & Mullenders, L. H. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07010.x · Cited by 242

Impaired Genome Maintenance Suppresses the Growth Hormone–Insulin-Like Growth Factor 1 Axis in Mice with Cockayne Syndrome

van der Pluijm, I., Garinis, G. A., Brandt, R. M. C., Gorgels, T. G. M. F., Wijnhoven, S., Diderich, K. E. M., de Wit, J., Mitchell, J. R., van Oostrom, C., Beems, R. B., et al. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0050002 · Cited by 240

Platinum-Induced Neurotoxicity and Preventive Strategies: Past, Present, and Future

Avan, A., Postma, T. J., Ceresa, C., Avan, A., Cavaletti, G., Giovannetti, E., & Peters, G. J. (2015) · The Oncologist · doi:10.1634/theoncologist.2014-0044 · Cited by 239

Cockayne syndrome: The expanding clinical and mutational spectrum

Laugel, V. (2013) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2013.02.006 · Cited by 239

DNAPKcs-dependent arrest of RNA polymerase II transcription in the presence of DNA breaks

Pankotai, T., Bonhomme, C., Chen, D., & Soutoglou, E. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2224 · Cited by 239

How Slow RNA Polymerase II Elongation Favors Alternative Exon Skipping

Dujardin, G., Lafaille, C., de la Mata, M., Marasco, L. E., Muñoz, M. J., Jossic-Corcos, C. L., Corcos, L., & Kornblihtt, A. R. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.044 · Cited by 236

A Rad26–Def1 complex coordinates repair and RNA pol II proteolysis in response to DNA damage

Woudstra, E. C., Gilbert, C., Fellows, J., Jansen, L. E. T., Brouwer, J., Erdjument‐Bromage, H., Tempst, P., & Svejstrup, J. Q. (2002) · Nature · doi:10.1038/415929a · Cited by 234

Structure of hsDDB1-drDDB2 bound to a 13 bp CPD-duplex (purine at D-1 position) at 3.0 A resolution (CPD 1)

Scrima, A., Fischer, E. S., Iwai, S., Gut, H., & Thomä, N. H. (2011) · Worldwide Protein Data Bank · doi:10.2210/pdb4a08/pdb · Cited by 233

Ultraviolet Radiation-induced Ubiquitination and Proteasomal Degradation of the Large Subunit of RNA Polymerase II

Ratner, J. N., Balasubramanian, B., Corden, J., Warren, S. L., & Bregman, D. B. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.9.5184 · Cited by 233

ATP-dependent chromatin remodeling in the DNA-damage response

Lans, H., Marteijn, J. A. F., & Vermeulen, W. (2012) · Epigenetics & Chromatin · doi:10.1186/1756-8935-5-4 · Cited by 230

DNA repair in terminally differentiated cells

Nouspikel, T. (2002) · DNA repair · doi:10.1016/s1568-7864(01)00005-2 · Cited by 228

Cisplatin preferentially binds to DNA in dorsal root ganglion neurons in vitro and in vivo: a potential mechanism for neurotoxicity

McDonald, E. S., Randon, K. R., Knight, A., & Windebank, A. J. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2004.09.013 · Cited by 227

Recognition of RNA Polymerase II and Transcription Bubbles by XPG, CSB, and TFIIH: Insights for Transcription-Coupled Repair and Cockayne Syndrome

Sarker, A. H., Tsutakawa, S. E., Kostek, S. A., Ng, C., Shin, D. S., Peris, M., Campeau, E., Tainer, J. A., Nogales, E., & Cooper, P. K. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.09.022 · Cited by 224

Damage-Induced Ubiquitylation of Human RNA Polymerase II by the Ubiquitin Ligase Nedd4, but Not Cockayne Syndrome Proteins or BRCA1

Anindya, R., Aygün, O., & Svejstrup, J. Q. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.10.008 · Cited by 222

H2AX phosphorylation after UV irradiation is triggered by DNA repair intermediates and is mediated by the ATR kinase

Hanasoge, S., & Ljungman, M. (2007) · Carcinogenesis · doi:10.1093/carcin/bgm157 · Cited by 216

Mutations in UVSSA cause UV-sensitive syndrome and impair RNA polymerase IIo processing in transcription-coupled nucleotide-excision repair

Nakazawa, Y., Sasaki, K., Mitsutake, N., Matsuse, M., Shimada, M., Nardò, T., Takahashi, Y., Ohyama, K., Ito, K., Mishima, H., et al. (2012) · Nature Genetics · doi:10.1038/ng.2229 · Cited by 213

Malfunction of Nuclease ERCC1-XPF Results in Diverse Clinical Manifestations and Causes Cockayne Syndrome, Xeroderma Pigmentosum, and Fanconi Anemia

Kashiyama, K., Nakazawa, Y., Pilz, D. T., Guo, C., Shimada, M., Sasaki, K., Fawcett, H., Wing, J., Lewin, S. O., Carr, L., et al. (2013) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2013.04.007 · Cited by 212

Two-step recognition of DNA damage for mammalian nucleotide excision repair: Directional binding of the XPC complex and DNA strand scanning

Sugasawa, K., Akagi, J.-I., Nishi, R., Iwai, S., & Hanaoka, F. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.035 · Cited by 205

UV-induced inhibition of transcription involves repression of transcription initiation and phosphorylation of RNA polymerase II

Rockx, D., Mason, R. S., van Hoffen, A., Barton, M. C., Citterio, E., Bregman, D. B., van Zeeland, A. A., Vrieling, H., & Mullenders, L. H. F. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.180169797 · Cited by 203

Local UV‐induced DNA damage in cell nuclei results in local transcription inhibition

Moné, M. J., Volker, M., Nikaido, O., Mullenders, L. H. F., van Zeeland, A. A., Verschure, P. J., Manders, E. M. M., & DRIEL, R. V. (2001) · EMBO Reports · doi:10.1093/embo-reports/kve224 · Cited by 202

Recruitment of the Putative Transcription-Repair Coupling Factor CSB/ERCC6 to RNA Polymerase II Elongation Complexes

Tantin, D. R., Kansal, A., & Carey, M. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.12.6803 · Cited by 202

Structural basis for the initiation of eukaryotic transcription-coupled DNA repair

Xu, J., Lahiri, I., Wang, W., Wier, A. D., Cianfrocco, M. A., Chong, J. P. C., Hare, A. A., Dervan, P. B., DiMaio, F., Leschziner, A. E., et al. (2017) · Nature · doi:10.1038/nature24658 · Cited by 202

UV Irradiation Induces a Non-coding RNA that Functionally Opposes the Protein Encoded by the Same Gene

Williamson, L. M., Saponaro, M., Boeing, S., East, P., Mitter, R., Kantidakis, T., Kelly, G. P., Lobley, A., Walker, J., Spencer‐Dene, B., et al. (2017) · Cell · doi:10.1016/j.cell.2017.01.019 · Cited by 201

Mutations in UVSSA cause UV-sensitive syndrome and destabilize ERCC6 in transcription-coupled DNA repair.

Zhang, X., Horibata, K., Saijo, M., Ishigami, C., Ukai, A., Kanno, S.-I., Tahara, H., Neilan, E. G., Honma, M., Nohmi, T., et al. (2012) · Nature Genetics · doi:10.1038/ng.2228 · Cited by 201

Ubiquitylation and degradation of elongating RNA polymerase II: The last resort

Wilson, M. D., Harreman, M. T., & Svejstrup, J. Q. (2012) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2012.08.002 · Cited by 200

Cdc48/p97 mediates UV-dependent turnover of RNA Pol II

Verma, R., Oania, R., Fang, R., Smith, G. T., & Deshaies, R. J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2010.12.017 · Cited by 196

Repair of cisplatin-induced DNA interstrand crosslinks by a replication-independent pathway involving transcription-coupled repair and translesion synthesis

Enoiu, M., Jiricny, J., & Schärer, O. D. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks670 · Cited by 192

RNA polymerase II bypass of oxidative DNA damage is regulated by transcription elongation factors

Charlet‐Berguerand, N., Feuerhahn, S., Kong, S. E., Ziserman, H., Conaway, J. W., Conaway, R., & Egly, J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601403 · Cited by 190

Nucleotide Excision Repair Driven by the Dissociation of CAK from TFIIH

Coin, F., Oksenych, V., Mocquet, V., Groh, S., Blattner, C., & Egly, J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.04.024 · Cited by 188

Transcription Dynamics in Living Cells

Lenstra, T. L., Rodriguez, J., Chen, H., & Larson, D. R. (2016) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-062215-010838 · Cited by 186

ROS-induced R loops trigger a transcription-coupled but BRCA1/2-independent homologous recombination pathway through CSB

Teng, Y., Yadav, T., Duan, M.-H., Tan, J. J., Xiang, Y., Gao, B., Xu, J., Liang, Z., Liu, Y., Nakajima, S., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06586-3 · Cited by 184

Nucleotide excision repair-induced H2A ubiquitination is dependent on MDC1 and RNF8 and reveals a universal DNA damage response

Marteijn, J. A., Bekker-Jensen, S., Mailand, N., Lans, H., Schwertman, P., Gourdin, A. M., Dantuma, N. P., Lukas, J., & Vermeulen, W. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200902150 · Cited by 184

The Ewing Sarcoma Protein Regulates DNA Damage-Induced Alternative Splicing

Paronetto, M. P., Miñana, B., & Valcárcel, J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.05.035 · Cited by 182

Proteins of nucleotide and base excision repair pathways interact in mitochondria to protect from loss of subcutaneous fat, a hallmark of aging

Kamenisch, Y., Fousteri, M. I., Knoch, J., von Thaler, A., Fehrenbacher, B., Kato, H., Becker, T., Dollé, M. E. T., Kuiper, R., Majora, M., et al. (2010) · The Journal of Experimental Medicine · doi:10.1084/jem.20091834 · Cited by 182

Complete absence of Cockayne syndrome group B gene product gives rise to UV-sensitive syndrome but not Cockayne syndrome

Horibata, K., Iwamoto, Y., Kuraoka, I., Jaspers, N. G. J., Kurimasa, A., Oshimura, M., Ichihashi, M., & Tanaka, K. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404587101 · Cited by 178

The multifunctional Ccr4–Not complex directly promotes transcription elongation

Kruk, J. A., Dutta, A., Fu, J., Gilmour, D. S., & Reese, J. C. (2011) · Genes & Development · doi:10.1101/gad.2020911 · Cited by 177

Transcription as a Threat to Genome Integrity

Gaillard, H., & Aguilera, A. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014908 · Cited by 173

Cisplatin‐ and UV‐damaged DNA lure the basal transcription factor TFIID/TBP

Vichi, P., Coin, F., Renaud, J., Vermeulen, W., Hoeijmakers, J. H. J., Moras, D., & Egly, J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.24.7444 · Cited by 172

Mechanism of transcriptional stalling at cisplatin-damaged DNA

Damsma, G. E., Alt, A., Brueckner, F., Carell, T., & Cramer, P. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1314 · Cited by 172

DNA damage stabilizes interaction of CSB with the transcription elongation machinery

van den Boom, V., Citterio, E., Hoogstraten, D., Zotter, A., Egly, J., van Cappellen, W. A., Hoeijmakers, J. H. J., Houtsmuller, A. B., & Vermeulen, W. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200401056 · Cited by 166

Oncogenic TLS/ERG and EWS/Fli-1 fusion proteins inhibit RNA splicing mediated by YB-1 protein.

Chansky, H. A., Hu, M., Hickstein, D. D., & Yang, L. (2001) · PubMed · Cited by 166

Multiplexed DNA repair assays for multiple lesions and multiple doses via transcription inhibition and transcriptional mutagenesis

Nagel, Z. D., Margulies, C. M., Chaim, I. A., McRee, S. K., Mazzucato, P., Ahmad, A., Abo, R., Butty, V. L., Forget, A. L., & Samson, L. D. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1401182111 · Cited by 165

PP2B and PP1α cooperatively disrupt 7SK snRNP to release P-TEFb for transcription in response to Ca2+signalingPreprint

Chen, R., Liu, M., Li, H., Xue, Y., Ramey, W. N., He, N., Ai, N., Luo, H., Zhu, Y., Zhou, N., et al. (2008) · Genes & Development · doi:10.1101/gad.1636008 · Cited by 164

Cotranscriptional exon skipping in the genotoxic stress response

Dutertre, M., Sanchez, G., Cian, M. D., Barbier, J., Dardenne, É., Gratadou, L., Dujardin, G., Jossic-Corcos, C. L., Corcos, L., & Auboeuf, D. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1912 · Cited by 161

Anti-tumour compounds illudin S and Irofulven induce DNA lesions ignored by global repair and exclusively processed by transcription- and replication-coupled repair pathways

Jaspers, N. G. J., Raams, A., Kelner, M. J., Ng, J. M. Y., Yamashita, Y. M., Takeda, S., McMorris, T. C., & Hoeijmakers, J. H. J. (2002) · DNA repair · doi:10.1016/s1568-7864(02)00166-0 · Cited by 161

Tripartite DNA Lesion Recognition and Verification by XPC, TFIIH, and XPA in Nucleotide Excision Repair

Li, C., Gołębiowski, F., Onishi, Y., Samara, N. L., Sugasawa, K., & Yang, W. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.08.012 · Cited by 160

The RNA Splicing Response to DNA Damage

Shkreta, L., & Chabot, B. (2015) · Biomolecules · doi:10.3390/biom5042935 · Cited by 156

Transcription-Coupled DNA Double-Strand Break Repair: Active Genes Need Special Care

Marnef, A., Cohen, S., & Legube, G. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.03.024 · Cited by 156

Repair Capacity for Platinum-DNA Adducts Determines the Severity of Cisplatin-Induced Peripheral Neuropathy

Dzagnidze, A., Katsarava, Z., Makhalova, J., Liedert, B., Yoon, M., Kaube, H., Limmroth, V., & Thomale, J. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0523-07.2007 · Cited by 152

Evidence that Transcript Cleavage Is Essential for RNA Polymerase II Transcription and Cell Viability

Sigurðsson, S., Dirac-Svejstrup, A. B., & Svejstrup, J. Q. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.02.026 · Cited by 149

Preferential Repair of Oxidized Base Damage in the Transcribed Genes of Mammalian Cells

Banerjee, D., Mandal, S. M., Das, A., Hegde, M. L., Das, S., Bhakat, K. K., Boldogh, I. R., Sarkar, P. S., MITRA, S. P., & Hazra, T. K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.198796 · Cited by 148

Structural Characterization of RNA Polymerase II Complexes Arrested by a Cyclobutane Pyrimidine Dimer in the Transcribed Strand of Template DNA

Tornaletti, S., Reines, D., & Hanawalt, P. C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.34.24124 · Cited by 147

Effects of abasic sites and DNA single-strand breaks on prokaryotic RNA polymerases.

Zhou, W., & Doetsch, P. W. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.14.6601 · Cited by 145

Enhanced Chromatin Dynamics by FACT Promotes Transcriptional Restart after UV-Induced DNA Damage

Dinant, C., Ampatziadis-Michailidis, G., Lans, H., Tresini, M., Lagarou, A., Grosbart, M., Theil, A. F., van Cappellen, W. A., Kimurâ, H., Bártek, J., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.08.007 · Cited by 145

Single-Stranded Breaks in DNA but Not Oxidative DNA Base Damages Block Transcriptional Elongation by RNA Polymerase II in HeLa Cell Nuclear Extracts

Kathe, S. D., Shen, G., & Wallace, S. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313598200 · Cited by 145

Effect of 8-oxoguanine on transcription elongation by T7 RNA polymerase and mammalian RNA polymerase II

Tornaletti, S., Maeda, L. S., Kolodner, R. D., & Hanawalt, P. C. (2004) · DNA repair · doi:10.1016/j.dnarep.2004.01.003 · Cited by 143

Cockayne syndrome group B protein promotes mitochondrial DNA stability by supporting the DNA repair association with the mitochondrial membrane

Aamann, M. D., Sorensen, M. M., Hvitby, C., Berquist, B. R., Müftüoğlu, M., Tian, J., de Souza-Pinto, N. C., Scheibye‐Knudsen, M., Wilson, D. M., Stevnsner, T., et al. (2010) · The FASEB Journal · doi:10.1096/fj.09-147991 · Cited by 142

Reduced hematopoietic reserves in DNA interstrand crosslink repair‐deficient Ercc1−/− mice

Prasher, J. M., Lalai, A. S., Heijmans‐Antonissen, C., Ploemacher, R., Hoeijmakers, J. H. J., Touw, I. P., & Niedernhofer, L. J. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600542 · Cited by 141

A UV-sensitive syndrome patient with a specific CSA mutation reveals separable roles for CSA in response to UV and oxidative DNA damage

Nardò, T., Oneda, R., Spivak, G., Vaz, B., Mortier, L., Thomas, P., Orioli, D., Laugel, V., Stary, A., Hanawalt, P. C., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902113106 · Cited by 140

A Ubiquitin-Binding Domain in Cockayne Syndrome B Required for Transcription-Coupled Nucleotide Excision Repair

Anindya, R., Mari, P., Kristensen, U., Kool, H., Giglia‐Mari, G., Mullenders, L. H. F., Fousteri, M. I., Vermeulen, W., Egly, J., & Svejstrup, J. Q. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.04.017 · Cited by 133

Translocation of Cockayne syndrome group A protein to the nuclear matrix: Possible relevance to transcription-coupled DNA repair

Kamiuchi, S., Saijo, M., Citterio, E., de Jager, M., Hoeijmakers, J. H. J., & Tanaka, K. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.012473199 · Cited by 133

Involvement of Global Genome Repair, Transcription Coupled Repair, and Chromatin Remodeling in UV DNA Damage Response Changes during Development

Lans, H., Marteijn, J. A. F., Schumacher, B., Hoeijmakers, J. H. J., Jansen, G., & Vermeulen, W. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1000941 · Cited by 131

The role of Cockayne Syndrome group B (CSB) protein in base excision repair and aging

Stevnsner, T., Müftüoğlu, M., Aamann, M. D., & Bohr, V. A. (2008) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2008.04.009 · Cited by 130

8-Oxoguanine-mediated transcriptional mutagenesis causes Ras activation in mammalian cells

Saxowsky, T. T., Meadows, K. L., Klungland, A., & Doetsch, P. W. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806464105 · Cited by 129

The 8,5′-cyclopurine-2′-deoxynucleosides: Candidate neurodegenerative DNA lesions in xeroderma pigmentosum, and unique probes of transcription and nucleotide excision repair

Brooks, P. J. (2008) · DNA repair · doi:10.1016/j.dnarep.2008.03.016 · Cited by 126

Mechanism of Translesion Transcription by RNA Polymerase II and Its Role in Cellular Resistance to DNA Damage

Walmacq, C., Cheung, A. C. M., Kireeva, M. L., Lubkowska, L., Ye, C., Gotte, D., Strathern, J. N., Carell, T., Cramer, P., & Kashlev, M. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.02.006 · Cited by 124

Common TFIIH recruitment mechanism in global genome and transcription-coupled repair subpathways

Okuda, M., Nakazawa, Y., Guo, C., Ogi, T., & Nishimura, Y. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx970 · Cited by 123

Exo1 competes with repair synthesis, converts NER intermediates to long ssDNA gaps, and promotes checkpoint activation

Giannattasio, M., Follonier, C., Tourrière, H., Puddu, F., Lazzaro, F., Pasero, P., Lopes, M., Plevani, P., & Muzi-Falconi, M. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.004 · Cited by 121

Transcriptional mutagenesis: causes and involvement in tumour development

Brégeon, D., & Doetsch, P. W. (2011) · Nature reviews. Cancer · doi:10.1038/nrc3006 · Cited by 120

Cooperation of the Cockayne Syndrome Group B Protein and Poly(ADP-Ribose) Polymerase 1 in the Response to Oxidative Stress

Thorslund, T., von Kobbe, C., Harrigan, J. A., Indig, F. E., Christiansen, M., Stevnsner, T., & Bohr, V. A. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.17.7625-7636.2005 · Cited by 118

Cockayne syndrome B protein stimulates apurinic endonuclease 1 activity and protects against agents that introduce base excision repair intermediates

Wong, H., Müftüoğlu, M., Beck, G., Imam, S. Z., Bohr, V. A., & Wilson, D. M. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm404 · Cited by 117

Base and nucleotide excision repair facilitate resolution of platinum drugs-induced transcription blockage

Slyšková, J., Sabatella, M., Ribeiro-Silva, C., Stok, C., Theil, A. F., Vermeulen, W., & Lans, H. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky764 · Cited by 117

XPA: A key scaffold for human nucleotide excision repair

Sugitani, N., Sivley, R. M., Perry, K. E., Capra, J. A., & Chazin, W. J. (2016) · DNA Repair · doi:10.1016/j.dnarep.2016.05.018 · Cited by 116

Translesion synthesis by RNA polymerases: occurrence and biological implications for transcriptional mutagenesis

Doetsch, P. W. (2002) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/s0027-5107(02)00258-0 · Cited by 112

Dysregulation of gene expression as a cause of Cockayne syndrome neurological disease

Wang, Y., Chakravarty, P., Ranes, M., Kelly, G. P., Brooks, P. J., Neilan, E. G., Stewart, A., Schiavo, G., & Svejstrup, J. Q. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1412569111 · Cited by 112

DNA repair in differentiated cells: Some new answers to old questions

Nouspikel, T. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2006.07.006 · Cited by 109

Genotoxic Stress Induces Coordinately Regulated Alternative Splicing of the p53 Modulators MDM2 and MDM4

Chandler, D. S., Singh, R. K., Caldwell, L. C., Bitler, J. L., & Lozano, G. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-4271 · Cited by 108

Nucleotide excision repair–initiating proteins bind to oxidative DNA lesions in vivo

Menoni, H., Hoeijmakers, J. H. J., & Vermeulen, W. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201205149 · Cited by 108

Lack of recognition by global-genome nucleotide excision repair accounts for the high mutagenicity and persistence of aristolactam-DNA adducts

Sidorenko, V. S., Yeo, J.-E., Bonala, R., Johnson, F., Schärer, O. D., & Grollman, A. P. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr1095 · Cited by 107

Effects of Aminofluorene and Acetylaminofluorene DNA Adducts on Transcriptional Elongation by RNA Polymerase II

Donahue, B. A., Fuchs, R. P., Reines, D., & Hanawalt, P. C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.18.10588 · Cited by 105

Cockayne’s Syndrome A and B Proteins Regulate Transcription Arrest after Genotoxic Stress by Promoting ATF3 Degradation

Epanchintsev, A., Costanzo, F., Rauschendorf, M., Caputo, M., Ye, T., Donnio, L., Proietti‐De‐Santis, L., Coin, F., Laugel, V., & Egly, J. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.11.009 · Cited by 104

An altered redox balance mediates the hypersensitivity of Cockayne syndrome primary fibroblasts to oxidative stress

Pascucci, B., Lemma, T., Iorio, E., Giovannini, S., Vaz, B., Iavarone, I., Calcagnile, A., Narciso, L., Degan, P., Podo, F., et al. (2012) · Aging Cell · doi:10.1111/j.1474-9726.2012.00815.x · Cited by 104

The emerging role of pre-messenger RNA splicing in stress responses: Sending alternative messages and silent messengers

Dutertre, M., Sanchez, G., Barbier, J., Corcos, L., & Auboeuf, D. (2011) · RNA Biology · doi:10.4161/rna.8.5.16016 · Cited by 102

Role of the DNA Base Excision Repair Protein, APE1 in Cisplatin, Oxaliplatin, or Carboplatin Induced Sensory Neuropathy

Kelley, M. R., Jiang, Y., Guo, C., Reed, A. M., Meng, H., & Vasko, M. R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0106485 · Cited by 101

8-Oxo-7,8-dihydroguanine in DNA does not constitute a barrier to transcription, but is converted into transcription-blocking damage by OGG1

Kitsera, N., Stathis, D., Lühnsdorf, B., Müller, H., Carell, T., Epe, B., & Khobta, A. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr163 · Cited by 100

P53 plays a protective role against UV- and cisplatin-induced apoptosis in transcription-coupled repair proficient fibroblasts

McKay, B. C., Becerril, C., & Ljungman, M. E. (2001) · Oncogene · doi:10.1038/sj.onc.1204901 · Cited by 98

Comet-FISH with strand-specific probes reveals transcription-coupled repair of 8-oxoGuanine in human cells

Guo, J., Hanawalt, P. C., & Spivak, G. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt524 · Cited by 98

Functional crosstalk between hOgg1 and the helicase domain of Cockayne syndrome group B protein

Tuo, J., Chen, C., Zeng, X., Christiansen, M., & Bohr, V. A. (2002) · DNA repair · doi:10.1016/s1568-7864(02)00116-7 · Cited by 97

A new UV-sensitive syndrome not belonging to any complementation groups of xeroderma pigmentosum or Cockayne syndrome: siblings showing biochemical characteristics of Cockayne syndrome without typical clinical manifestations

Itoh, T., Ono, T., & Yamaizumi, M. (1994) · Mutation Research/DNA Repair · doi:10.1016/0921-8777(94)90068-x · Cited by 97

P-TEFb Activation by RBM7 Shapes a Pro-survival Transcriptional Response to Genotoxic Stress

Bugai, A., Quaresma, A. J. C., Friedel, C. C., Lenasi, T., Düster, R., Sibley, C. R., Fujinaga, K., Kukanja, P., Hennig, T., Blasius, M., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.01.033 · Cited by 92

Effect of Thymine Glycol on Transcription Elongation by T7 RNA Polymerase and Mammalian RNA Polymerase II

Tornaletti, S., Maeda, L. S., Lloyd, D. R., Reines, D., & Hanawalt, P. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105282200 · Cited by 92

Interaction of T7 RNA polymerase with DNA in an elongation complex arrested at a specific psoralen adduct site.

Shi, Y., Gamper, H., & Hearst, J. E. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)57424-5 · Cited by 92

Transcription Arrest at an Abasic Site in the Transcribed Strand of Template DNA

Tornaletti, S., Maeda, L. S., & Hanawalt, P. C. (2006) · Chemical Research in Toxicology · doi:10.1021/tx060103g · Cited by 90

Function and Interactions of ERCC1-XPF in DNA Damage Response

Faridounnia, M., Folkers, G. E., & Boelens, R. (2018) · Molecules · doi:10.3390/molecules23123205 · Cited by 90

ATP-Dependent Chromatin Remodeling by Cockayne Syndrome Protein B and NAP1-Like Histone Chaperones Is Required for Efficient Transcription-Coupled DNA Repair

Cho, I., Tsai, P.-F., Lake, R. J., Basheer, A., & Fan, H.-Y. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003407 · Cited by 89

Three-Dimensional Visualization of Ultraviolet-Induced DNA Damage and Its Repair in Human Cell Nuclei

Nakagawa, A., Kobayashi, N., Muramatsu, T., Yamashina, Y., Shirai, T., HASHIMOTO, M. W., Ikenaga, M., & Mori, T. (1998) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.1998.00100.x · Cited by 88

DNA repair and recovery of RNA synthesis following exposure to ultraviolet light are delayed in long genes

de Andrade-Lima, L. C., Veloso, A., Paulsen, M. T., Menck, C. F. M., & Ljungman, M. E. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv148 · Cited by 88

Global unleashing of transcription elongation waves in response to genotoxic stress restricts somatic mutation rate

Lavigne, M. D., Konstantopoulos, D., Ntakou‐Zamplara, K. Z., Liakos, A., & Fousteri, M. I. (2017) · Nature Communications · doi:10.1038/s41467-017-02145-4 · Cited by 88

Nucleotide Excision Repair Disorders and the Balance Between Cancer and Aging

Andressoo, J., Hoeijmakers, J. H. J., & Mitchell, J. R. (2006) · Cell Cycle · doi:10.4161/cc.5.24.3565 · Cited by 87

UV-sensitive syndrome

Spivak, G. (2005) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2005.03.017 · Cited by 86

p38-MK2 signaling axis regulates RNA metabolism after UV-light-induced DNA damage

Borisova, M. E., Voigt, A., Tollenaere, M. A. X., Sahu, S. K., Juretschke, T., Kreim, N., Mailand, N., Choudhary, C., Bekker‐Jensen, S., Akutsu, M., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-03417-3 · Cited by 85

Xeroderma pigmentosum-Cockayne syndrome complex

Natale, V., & Raquer-McKay, H. M. (2017) · Orphanet Journal of Rare Diseases · doi:10.1186/s13023-017-0616-2 · Cited by 84

Blockage of RNA Polymerase II at a Cyclobutane Pyrimidine Dimer and 6-4 Photoproduct

Mei Kwei, J. S., Kuraoka, I., Horibata, K., Ubukata, M., Kobatake, E., Iwai, S., Handa, H., & Tanaka, K. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.06.066 · Cited by 82

Retinal Degeneration and Ionizing Radiation Hypersensitivity in a Mouse Model for Cockayne Syndrome

Gorgels, T. G. M. F., van der Pluijm, I., Brandt, R. M. C., Garinis, G. A., STEEG, H. V., van den Aardweg, G. J., Jansen, G. H., Ruijter, J. M., Bergen, A. A. B., Norren, D. V., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01037-06 · Cited by 82

Transcription activities at 8-oxoG lesions in DNA

Larsen, E., Kwon, K.-R., Coin, F., Egly, J., & Klungland, A. (2004) · DNA repair · doi:10.1016/j.dnarep.2004.06.008 · Cited by 81

Human ISWI complexes are targeted by SMARCA5 ATPase and SLIDE domains to help resolve lesion-stalled transcription

Aydın, Ö. Z., Marteijn, J. A. F., Ribeiro-Silva, C., López, A. R., Wijgers, N., Smeenk, G., van Attikum, H., Poot, R. A., Vermeulen, W., & Lans, H. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku565 · Cited by 81

Proteasome-Mediated Processing of Def1, a Critical Step in the Cellular Response to Transcription Stress

Wilson, M. D., Harreman, M. T., Taschner, M. J., Reid, J., Walker, J., Erdjument‐Bromage, H., Tempst, P., & Svejstrup, J. Q. (2013) · Cell · doi:10.1016/j.cell.2013.07.028 · Cited by 80

Human exonuclease 1 connects nucleotide excision repair (NER) processing with checkpoint activation in response to UV irradiation

Sertic, S., Pizzi, S., Cloney, R., Lehmann, A. R., Marini, F., Plevani, P., & Muzi-Falconi, M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1108547108 · Cited by 80

Histone Methyltransferase DOT1L Drives Recovery of Gene Expression after a Genotoxic Attack

Oksenych, V., Zhovmer, A. S., Ziani, S., Mari, P., Eberová, J., Nardò, T., Stefanini, M., Giglia‐Mari, G., Egly, J., & Coin, F. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003611 · Cited by 78

An Xpd mouse model for the combined xeroderma pigmentosum/Cockayne syndrome exhibiting both cancer predisposition and segmental progeria

Andressoo, J.-O., Mitchell, J. R., de Wit, J., Hoogstraten, D., Volker, M., Toussaint, W., Speksnijder, E., Beems, R. B., van Steeg, H., Jans, J., et al. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.05.027 · Cited by 78

Transcription Domain-Associated Repair in Human Cells

Nouspikel, T., Hyka‐Nouspikel, N., & Hanawalt, P. C. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01263-06 · Cited by 76

Cockayne syndrome group B protein regulates DNA double‐strand break repair and checkpoint activation

Batenburg, N. L., Thompson, E. L., Hendrickson, E. A., & Zhu, X. (2015) · The EMBO Journal · doi:10.15252/embj.201490041 · Cited by 76

The transcription-coupled DNA repair-initiating protein CSB promotes XRCC1 recruitment to oxidative DNA damage

Menoni, H., Wienholz, F., Theil, A. F., Janssens, R. C., Lans, H., Campalans, A., Radicella, J. P., Marteijn, J. A. F., & Vermeulen, W. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky579 · Cited by 75

RNA polymerase II is released from the DNA template during transcription-coupled repair in mammalian cells

Chiou, Y., Hu, J., Sancar, A., & Selby, C. P. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.000971 · Cited by 74

KIAA1530 Protein Is Recruited by Cockayne Syndrome Complementation Group Protein A (CSA) to Participate in Transcription-coupled Repair (TCR)

Fei, J., & Chen, J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.398131 · Cited by 70

Aging: not all DNA damage is equal

Vermeij, W. P., Hoeijmakers, J. H. J., & Pothof, J. (2014) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2014.06.006 · Cited by 70

Structural basis of DNA lesion recognition for eukaryotic transcription-coupled nucleotide excision repair

Wang, W., Xu, J., Chong, J. P. C., & Wang, D. (2018) · DNA repair · doi:10.1016/j.dnarep.2018.08.006 · Cited by 68

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Perlow, R. A., Kolbanovskiy, A., Hingerty, B. E., Geacintov, N. E., Broyde, S. B., & Scicchitano, D. A. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00593-4 · Cited by 66

BMI1–UBR5 axis regulates transcriptional repression at damaged chromatin

Sanchez, A. R., de Vivo, A., Uprety, N., Kim, J., Stevens, S. M., & Kee, Y. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1610735113 · Cited by 66

ATM and ATR Pathways Signal Alternative Splicing of Drosophila TAF1 Pre-mRNA in Response to DNA Damage

Katzenberger, R. J., Marengo, M. S., & Wassarman, D. A. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01125-06 · Cited by 65

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Barnhoorn, S., Uittenboogaard, L. M., Jaarsma, D., Vermeij, W. P., Tresini, M., Weymaere, M., Menoni, H., Brandt, R. M. C., de Waard, M. C., Botter, S. M., et al. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004686 · Cited by 64

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Fielden, J., Ruggiano, A., Popović, M., & Ramadan, K. (2018) · DNA repair · doi:10.1016/j.dnarep.2018.08.025 · Cited by 62

Ccr4-Not and TFIIS Function Cooperatively To Rescue Arrested RNA Polymerase II

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Heterogeneity and overlaps in nucleotide excision repair disorders

Ferri, D., Orioli, D., & Botta, E. (2019) · Clinical Genetics · doi:10.1111/cge.13545 · Cited by 61

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Giono, L. E., Moreno, N. N., Botto, A. E. C., Dujardin, G., Muñoz, M. J., & Kornblihtt, A. R. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.03.004 · Cited by 59

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Lans, H., & Vermeulen, W. (2015) · DNA repair · doi:10.1016/j.dnarep.2015.04.025 · Cited by 58

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Walmacq, C., Wang, L., Chong, J. P. C., Scibelli, K., Lubkowska, L., Gnatt, A. L., Brooks, P. J., Wang, D., & Kashlev, M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1415186112 · Cited by 48

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Pines, A., Dijk, M., Makowski, M. M., Meulenbroek, E. M., Vrouwe, M. G., van der Weegen, Y., Baltissen, M. P. A., French, P. J., van Royen, M. E., Luijsterburg, M. S., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-03484-6 · Cited by 48

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Edifizi, D., & Schumacher, B. (2015) · Biomolecules · doi:10.3390/biom5031855 · Cited by 45

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Adam, S., & Polo, S. E. (2014) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.07.017 · Cited by 45

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Wienholz, F., Zhou, D., der Velden, Y. T.-V., Schwertman, P., Tresini, M., Pines, A., van Toorn, M., Bezstarosti, K., Demmers, J., & Marteijn, J. A. F. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz055 · Cited by 44

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Labrie, M., Brugge, J. S., Mills, G. B., & Zervantonakis, I. K. (2022) · Nature reviews. Cancer · doi:10.1038/s41568-022-00454-5 · Cited by 410

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Karagöz, G. E., Acosta‐Alvear, D., & Walter, P. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033886 · Cited by 306

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Zhou, Y., Wang, T., Wu, D., Min, Z., Tan, J., & Yu, B. (2020) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-020-01714-8 · Cited by 266

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