Homolog Rekombinasyon ve DNA Tamir Mekanizmaları

Watson JD, Crick FHC. A structure for deoxyribose nucleic acid. Nature; 1953; 171: 737–738.

Nirenberg MW, Matthaei JH, Jones OW, et al. Approximation of genetic code via cell-free protein synthesis directed by template RNA. Federation Proceedings; 1963; 22; 55–61.

Leder P, Clark BFC, Sly WS, et al. Cell-free peptide synthesis dependent upon synthetic oligodeoxynucleotides. Proceedings of the National Academy of Sciences; 1963; 50: 1135–1143.

Herriott RM. Mutagenesis. Cancer Research; 1966; 26(9_Part_1): 1971–1979.

Loewe L, Hill WG. The population genetics of mutations: good, bad and indifferent. Philos Trans R Soc Lond B Biol Sci; 2010; 365(1544):1153-1167. doi: 10.1098/rstb.2009.0317

Sung P, Klein H. Mechanism of homologous recombination: mediators and helicases take on regulatory functions. Nat Rev Mol Cell Biol; 2006; 7(10): 739–750. doi: 10.1038/nrm2008

Lu X, Simon M, Chodaparambil J, et al. The effect of H3K79 dimethylation and H4K20 trimethylation on nucleosome and chromatin structure. Nat Struct Mol Biol; 2008; 15; 1122–1124. doi: 10.1038/nsmb.1489

Humphrey W, Dalke A, Schulten K. VMD-Visual Molecular Dynamics. J. Molec. Graphics; 1996; 14(1): 33-38.

Gura MA, Freiman RN. Primordial Follicle. Skinner MK (eds.) Encyclopedia of Reproduction. 2nd ed. Academic Press; 2018. p. 65-71. doi: 10.1016/B978-0-12-801238-3.64394-5

Page SL, Hawley RS. The genetics and molecular biology of the synaptonemal complex. Annu Rev Cell Dev Biol; 2004; 20:525-558. doi: 10.1146/annurev.cellbio

Moens PB. Synaptonemal Complex. Brenner S, Miller JH (eds.) Encyclopedia of Genetics. Academic Press; 2001. p. 1910-1912. doi: 10.1006/rwgn.2001.1265

Vrielynck N, Chambon A, Vezon D, et al. A DNA topoisomerase VI-like complex initiates meiotic recombination. Science; 2016; 351(6276): 939-943. doi: 10.1126/science.aad5196

Lieber MR, Gu J, Lu H, et al. Nonhomologous DNA end joining (NHEJ) and chromosomal translocations in humans. Subcell Biochem; 2010; 50: 279-296. doi: 10.1007/978-90-481-3471-7_14

Krejci L, Altmannova V, Spirek M, et al. Homologous recombination and its regulation. Nucleic Acids Res; 2012; 40(13): 5795-5818. doi: 10.1093/nar/gks270

Jasin M, Rothstein R. Repair of strand breaks by homologous recombination. Cold Spring Harb Perspect Biol; 2013; 5(11): a012740. doi: 10.1101/cshperspect.a012740

Kowalczykowski SC. An Overview of the Molecular Mechanisms of Recombinational DNA Repair. Cold Spring Harb Perspect Biol; 2015; 7(11): a016410. doi: 10.1101/cshperspect.a016410

Li X, Heyer WD. Homologous recombination in DNA repair and DNA damage tolerance. Cell Res; 2008; 18, 99–113. doi: 10.1038/cr.2008.1

San Filippo J, Sung P, Klein H. Mechanism of eukaryotic homologous recombination. Annu Rev Biochem; 2008; 77: 229-257. doi: 10.1146/annurev.biochem.77.061306.125255

Toledo LI, Altmeyer M, Rask MB, et al. ATR prohibits replication catastrophe by preventing global exhaustion of RPA. Cell; 2013; 155: 1088–1103. doi: 10.1016/j.cell.2013.10.043

Iftode C, Daniely Y, Borowiec JA. Replication protein A (RPA): the eukaryotic SSB. Crit Rev Biochem Mol Biol; 1999; 34(3):141-180. doi: 10.1080/10409239991209255

Xue C, Wang W, Crickard JB, et al. Regulatory control of Sgs1 and Dna2 during eukaryotic DNA end resection. Proc Natl Acad Sci USA; 2019; 116(13): 6091-6100. doi: 10.1073/pnas.1819276116

Bermúdez-López M, Aragon L. Smc5/6 complex regulates Sgs1 recombination functions. Curr Genet; 2017; 63(3): 381-388. doi: 10.1007/s00294-016-0648-5

Cejka P, Cannavo E, Polaczek P, et al. DNA end resection by Dna2-Sgs1-RPA and its stimulation by Top3-Rmi1 and Mre11-Rad50-Xrs2. Nature; 2010; 467: 112–116. doi: 10.1038/nature09355.

Szankasi R, Smith GR. A DNA exonuclease induced during meiosis of Schizosaccharomyces pombe. J Biol Chem; 1992; 267: 3014–3023.

Cannavo E, Cejka P, Kowalczykowski SC. Relationshipof DNA degradation by Saccharomyces cerevisiae exonuclease 1 and its stimulation by RPA and Mre11–Rad50–Xrs2 to DNA end resection. Proc Natl Acad Sci; 2013; 110(18): E1661–E1668. doi: 10.1073/pnas.1305166110

Tomimatsu N, Mukherjee B, Catherine Hardebeck M, et al. Phosphorylation of EXO1 by CDKs 1 and 2 regulates DNA end resection and repair pathway choice. Nat Commun; 2014; 5: 3561. doi: 10.1038/ncomms4561

Kim C, Paulus BF, Wold MS. Interactions of Human Replication Protein A with Oligonucleotides. Biochemistry; 1994; 33(47): 14197–14206. doi: 10.1021/bi00251a031

Bhat KP, Cortez D. RPA and RAD51: fork reversal, fork protection, and genome stability. Nat Struct Mol Biol; 2018; 25(6): 446-453. doi: 10.1038/s41594-018-0075-z

Sung P. Function of yeast Rad52 protein as a mediator between replication protein A and the Rad51 recombinase. J Biol Chem; 1997; 272(45): 28194-28197. doi: 10.1074/jbc.272.45.28194

Song B, Sung P. Functional interactions among yeast Rad51 recombinase, Rad52 mediator, and replication protein A in DNA strand exchange. J Biol Chem; 2000; 275(21):15895-15904. doi: 10.1074/jbc.M910244199

Sung P. Catalysis of ATP-dependent homologous DNA pairing and strand exchange by yeast RAD51 protein. Science; 1994; 265(5176): 1241-1243. doi: 10.1126/science.8066464

Robertson RB, Moses DN, Kwon Y, et al. Structural transitions within human Rad51 nucleoprotein filaments. Proc Natl Acad Sci USA; 2009; 106(31): 12688-12693. doi: 10.1073/pnas.0811465106

Maloisel L, Bhargava J, Roeder GS. A role for DNA polymerase delta in gene conversion and crossing over during meiosis in Saccharomyces cerevisiae. Genetics; 2004; 167(3): 1133-1142. doi: 10.1534/genetics.104.026260

McVey M, Khodaverdian VY, Meyer D, et al. Eukaryotic DNA Polymerases in Homologous Recombination. Annu Rev Genet; 2016; 50: 393-421. doi: 10.1146/annurev-genet-120215-035243

Raji H, Hartsuiker E. Double-strand break repair and homologous recombination in Schizosaccharomyces pombe. Yeast; 2006; 23(13): 963-976. doi: 10.1002/yea.1414

Muñoz-Galván S, Tous C, Blanco MG, et al. Distinct roles of Mus81, Yen1, Slx1-Slx4, and Rad1 nucleases in the repair of replication-born double-strand breaks by sister chromatid exchange. Mol Cell Biol; 2012; 32(9): 1592-1603. doi: 10.1128/MCB.00111-12

Rass U. Resolving branched DNA intermediates with structure-specific nucleases during replication in eukaryotes. Chromosoma; 2013; 122(6): 499-515. doi: 10.1007/s00412-013-0431-z

Castor D, Nair N, Déclais AC, et al. Cooperative control of holliday junction resolution and DNA repair by the SLX1 and MUS81-EME1 nucleases. Mol Cell; 2013; 52(2): 221-233. doi: 10.1016/j.molcel.2013.08.036

Wyatt HD, Sarbajna S, Matos J, et al. Coordinated actions of SLX1-SLX4 and MUS81-EME1 for Holliday junction resolution in human cells. Mol Cell; 2013; 52(2): 234-247. doi: 10.1016/j.molcel.2013.08.035

Wright WD, Shah SS, Heyer WD. Homologous recombination and the repair of DNA double-strand breaks. J Biol Chem; 2018; 293(27): 10524-10535. doi: 10.1074/jbc.TM118.000372

Morrison A, Bell JB, Kunkel TA, et al. Eukaryotic DNA polymerase amino acid sequence required for 3'----5' exonuclease activity. Proc Natl Acad Sci USA; 1991; 88(21): 9473-9477. doi: 10.1073/pnas.88.21.9473

Soriano I, Vazquez E, De Leon N, et al. Expression of the cancer-associated DNA polymerase ε P286R in fission yeast leads to translesion synthesis polymerase dependent hypermutation and defective DNA replication. PLoS Genet; 2021; 17(7): e1009526. doi: 10.1371/journal.pgen.1009526

Li GM. Mechanisms and functions of DNA mismatch repair. Cell Res; 2008; 18(1): 85-98. doi: 10.1038/cr.2007.115

Duncan BK, Miller JH. Mutagenic deamination of cytosine residues in DNA. Nature; 1980; 287(5782): 560-561. doi: 10.1038/287560a0

Nakamura J, Swenberg JA. Endogenous apurinic/apyrimidinic sites in genomic DNA of mammalian tissues. Cancer Res; 1999; 59(11): 2522–2526.

Drake JW. Spontaneous mutation. Annu Rev Genet; 1991; 25: 125-146. doi: 10.1146/annurev.ge.25.120191.001013

Turrens JF. Mitochondrial formation of reactive oxygen species. J Physiol; 2003; 552(Pt2): 335-44. doi: 10.1113/jphysiol.2003.049478

Zorov DB, Juhaszova M, Sollott SJ. Mitochondrial reactive oxygen species (ROS) and ROS-induced ROS release. Physiol Rev; 2014; 94(3): 909-950. doi: 10.1152/physrev.00026.2013

White M, Cohen J, Hummel C, et al. The Role of Oxidative Stress in Ovarian Cancer: Implications for the Treatment of Patients. Preedy V(eds.) Cancer. Academic Press; 2014. p. 41-50. doi: 10.1016/B978-0-12-405205-5.00005-2

Van Loon B, Markkanen E, Hübscher U. Oxygen as a friend and enemy: How to combat the mutational potential of 8-oxo-guanine. DNA Repair; 2010; 9(6): 604–616. doi: 10.1016/j.dnarep.2010.03.004

Chatterjee N, Walker GC. Mechanisms of DNA damage, repair, and mutagenesis. Environ Mol Mutagen; 2017; 58(5): 235-263. doi: 10.1002/em.22087

Kodym A, Afza R. Physical and chemical mutagenesis. Methods Mol Biol; 2003; 236: 189-204. doi: 10.1385/1-59259-413-1:189

Brown T, Kneale G, Hunter WN, et al. Structural characterisation of the bromouracil.guanine base pair mismatch in a Z-DNA fragment. Nucleic Acids Res; 1986; 14(4): 1801-1809. doi: 10.1093/nar/14.4.1801

Sega GA. A review of the genetic effects of ethyl methanesulfonate. Mutat Res;

1984; 134(2-3): 113-142. doi: 10.1016/0165-1110(84)90007-1

Karran P, Lindahl T. Hypoxanthine in deoxyribonucleic acid: generation by heat-induced hydrolysis of adenine residues and release in free form by a deoxyribonucleic acid glycosylase from calf thymus. Biochemistry; 1980; 19(26): 6005-6011. doi: 10.1021/bi00567a010

Kamiya H, Shimizu M, Suzuki M, et al. Mutation induced by deoxyxanthosine in codon 12 of a synthetic c-Ha-ras gene. Nucleosides Nucleotides; 1992; 11(2-4): 247-260.

Scaria PV, Shafer RH. Binding of ethidium bromide to a DNA triple helix. Evidence for intercalation. J Biol Chem; 1991; 266(9): 5417-5423.

Reisz JA, Bansal N, Qian J, et al. Effects of ionizing radiation on biological molecules--mechanisms of damage and emerging methods of detection. Antioxid Redox Signal; 2014; 21(2): 260-292. doi: 10.1089/ars.2013.5489

Kiefer J. Effects of Ultraviolet Radiation on DNA. In: Obe G, Vijayalaxmi (eds.) Chromosomal Alterations. Springer, Berlin, Heidelberg. 2007. doi: 10.1007/978-3-540-71414-9_3

House JE, House KA. Atomic and Molecular Structure. In: House JE, House KA (eds.) Descriptive Inorganic Chemistry 2nd ed. Academic Press. 2010; p. 17-61. doi: 10.1016/B978-0-12-088755-2.00002-1

Nikitaki Z, Hellweg CE, Georgakilas AG, et al. Stress-induced DNA damage biomarkers: applications and limitations. Front Chem; 2015; 3: 35. doi: 10.3389/fchem.2015.00035

Wang JY. DNA damage and apoptosis. Cell Death Differ; 2001; 8(11): 1047-8. doi: 10.1038/sj.cdd.4400938

Chromosome Breakage. In: Encyclopedia of Genetics, Genomics, Proteomics and Informatics. Springer, Dordrecht. 2008; doi: 10.1007/978-1-4020-6754-9_2969

Funk RK, Stockham AL, Laack NNI. Basics of Radiation Therapy. In: Herrmann J (eds.) Clinical Cardio-Oncology Elsevier. 2016; p. 39-60. doi: 10.1016/B978-0-323-44227-5.00003-X

Rastogi RP, Richa, Kumar A. Molecular mechanisms of ultraviolet radiation-induced DNA damage and repair. J Nucleic Acids; 2010; 2010: 592980. doi: 10.4061/2010/592980

Zhu Y, Zhang Y, He Z, et al. Detrimental Effects of Multiple Mutations in Position 240 of Fusarium graminearum β2-Tubulin. Phytopathology; 2020; 110(9): 1522-1529. doi: 10.1094/PHYTO-11-19-0409-R

Hanahan D, Weinberg RA. Hallmarks of cancer: the next generation. Cell; 2011; 144(5): 646-674. doi: 10.1016/j.cell.2011.02.013

Pećina-Šlaus N, Kafka A, Salamon I, et al. Mismatch Repair Pathway, Genome Stability and Cancer. Front Mol Biosci; 2020; 7:122. doi: 10.3389/fmolb.2020.00122

Iyer RR, Pluciennik A, Burdett V, et al. DNA mismatch repair: functions and mechanisms. Chem Rev; 2006; 106(2): 302-323. doi: 10.1021/cr0404794

Fishel R, Wilson T. MutS homologs in mammalian cells. Curr Opin Genet Dev; 1997; 7(1): 105-113. doi: 10.1016/s0959-437x(97)80117-7

Habraken Y, Sung P, Prakash L, et al. Binding of insertion/deletion DNA mismatches by the heterodimer of yeast mismatch repair proteins MSH2 and MSH3. Curr Biol; 1996; 6(9): 1185-7. doi: 10.1016/s0960-9822(02)70686-6

Li, GM. Mismatch Repair. In: Bell, E. (eds) Molecular Life Sciences. Springer; 2014. doi: 10.1007/978-1-4614-6436-5_64-2

Keijzers G, Bakula D, Petr MA, et al. Human Exonuclease 1 (EXO1) Regulatory Functions in DNA Replication with Putative Roles in Cancer. Int J Mol Sci; 2018; 20(1): 74. doi: 10.3390/ijms20010074

Krokan HE, Bjørås M. Base excision repair. Cold Spring Harb Perspect Biol; 2013; 5(4): a012583. doi: 10.1101/cshperspect.a012583

Zharkov DO. Base excision DNA repair. Cell Mol Life Sci; 2008; 65(10): 1544-65. doi: 10.1007/s00018-008-7543-2

Sancar A, Lindsey-Boltz LA, Unsal-Kaçmaz K, et al. Molecular mechanisms of mammalian DNA repair and the DNA damage checkpoints. Annu Rev Biochem; 2004; 73: 39-85. doi: 10.1146/annurev.biochem.73.011303.073723

Sancar A. DNA repair in humans. Annu Rev Genet; 1995; 29:69-105. doi: 10.1146/annurev.ge.29.120195.000441

Lindahl T. DNA glycosylases, endonucleases for apurinic/apyrimidinic sites, and base excision-repair. Prog Nucleic Acid Res Mol Biol; 1979; 22: 135-192. doi: 10.1016/s0079-6603(08)60800-4

Girard PM, D'Ham C, Cadet J, et al. Opposite base-dependent excision of 7,8-dihydro-8-oxoadenine by the Ogg1 protein of Saccharomyces cerevisiae. Carcinogenesis; 1998; 19(7): 1299-1305. doi: 10.1093/carcin/19.7.1299

Lindahl T. An N-glycosidase from Escherichia coli that releases free uracil from DNA containing deaminated cytosine residues. Proc Natl Acad Sci USA; 1974; 71(9): 3649-3653. doi: 10.1073/pnas.71.9.3649

Olsen LC, Aasland R, Wittwer CU, et al. Molecular cloning of human uracil-DNA glycosylase, a highly conserved DNA repair enzyme. EMBO J; 1989; 8(10): 3121-5. doi: 10.1002/j.1460-2075.1989.tb08464.x

Richardson CC, Kornberg A. A Deoxyribonucleic acid phosphatase-exonuclease from escherichia coli. i. purification of the enzyme and characterization of the phosphatase activity. J Biol Chem; 1964; 239:242-50

Demple B, Herman T, Chen DS. Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: definition of a family of DNA repair enzymes. Proc Natl Acad Sci USA; 1991; 88(24): 11450-4. doi: 10.1073/pnas.88.24.11450

Masuda Y, Bennett RA, Demple B. Dynamics of the interaction of human apurinic endonuclease (Ape1) with its substrate and product. J Biol Chem; 1998; 273(46): 30352-9. doi: 10.1074/jbc.273.46.30352

McCullough AK, Sanchez A, Dodson ML, et al. The reaction mechanism of DNA glycosylase/AP lyases at abasic sites. Biochemistry; 2001; 40(2): 561-8. doi: 10.1021/bi002404+

Pheiffer BH, Zimmerman SB. 3'-Phosphatase activity of the DNA kinase from rat liver. Biochem Biophys Res Commun; 1982; 109(4): 1297-302. doi: 10.1016/0006-291x(82)91918-0

Weinfeld M, Mani RS, Abdou I, et al. Tidying up loose ends: the role of polynucleotide kinase/phosphatase in DNA strand break repair. Trends Biochem Sci; 2011; 36(5): 262-271. doi: 10.1016/j.tibs.2011.01.006

Dianova II, Sleeth KM, Allinson SL, et al. XRCC1-DNA polymerase beta interaction is required for efficient base excision repair. Nucleic Acids Res; 2004; 32(8): 2550-2555. doi: 10.1093/nar/gkh567

Mortusewicz O, Rothbauer U, Cardoso MC, et al. Differential recruitment of DNA Ligase I and III to DNA repair sites. Nucleic Acids Res; 2006; 34(12): 3523-3532. doi: 10.1093/nar/gkl492

Robertson AB, Klungland A, Rognes T, et al. DNA repair in mammalian cells: Base excision repair: the long and short of it. Cell Mol Life Sci; 2009; 66(6): 981-993. doi: 10.1007/s00018-009-8736-z

Koellner CM, Mensink KA, Highsmith WE. Basic Concepts in Human Molecular Genetics. Coleman WB, Tsongalis GJ (eds.) Molecular Pathology. 2nd ed. Academic Press; 2018. p. 99-120. doi: 10.1016/B978-0-12-802761-5.00005-5

Dasari S, Tchounwou PB. Cisplatin in cancer therapy: molecular mechanisms of action. Eur J Pharmacol; 2014; 740: 364-378. doi: 10.1016/j.ejphar.2014.07.025

Sancar A, Tang MS. Nucleotide excision repair. Photochem Photobiol; 1993; 57(5): 905-921. doi: 10.1111/j.1751-1097.1993.tb09233.x

Reardon JT, Sancar A. Nucleotide excision repair. Prog Nucleic Acid Res Mol Biol; 2005; 79: 183-235. doi: 10.1016/S0079-6603(04)79004-2

Reardon JT, Sancar A. Purification and characterization of Escherichia coli and human nucleotide excision repair enzyme systems. Methods Enzymol; 2006; 408: 189-213. doi: 10.1016/S0076-6879(06)08012-8

Sugasawa K. Mechanism and regulation of DNA damage recognition in mammalian nucleotide excision repair. Enzymes; 2019; 45: 99-138. doi: 10.1016/bs.enz.2019.06.004

Schärer OD. Nucleotide excision repair in eukaryotes. Cold Spring Harb Perspect Biol; 2013; 5(10): a012609. doi: 10.1101/cshperspect.a012609

Marteijn JA, Lans H, Vermeulen W, et al. Understanding nucleotide excision repair and its roles in cancer and ageing. Nat Rev Mol Cell Biol; 2014; 15(7): 465-481. doi: 10.1038/nrm3822

Prakash S, Prakash L. Nucleotide excision repair in yeast. Mutat Res. 2000; 451(1-2): 13-24. doi: 10.1016/s0027-5107(00)00037-3

Gillet LC, Schärer OD. Molecular mechanisms of mammalian global genome nucleotide excision repair. Chem Rev; 2006; 106(2): 253-276. doi: 10.1021/cr040483f

Spivak G. Transcription-coupled repair: an update. Arch Toxicol; 2016; 90(11): 2583-2594. doi: 10.1007/s00204-016-1820-x

Araki M, Masutani C, Takemura M, et al. Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair. J Biol Chem; 2001; 276(22): 18665-72. doi: 10.1074/jbc.M100855200

Nishi R, Okuda Y, Watanabe E, et al. Centrin 2 stimulates nucleotide excision repair by interacting with xeroderma pigmentosum group C protein. Mol Cell Biol; 2005; 25(13): 5664-74. doi: 10.1128/MCB.25.13.5664-5674

Masutani C, Sugasawa K, Yanagisawa J, et al. Purification and cloning of a nucleotide excision repair complex involving the xeroderma pigmentosum group C protein and a human homologue of yeast RAD23. EMBO J; 1994; 13(8): 1831-1843. doi: 10.1002/j.1460-2075.1994.tb06452.x

Ng JM, Vermeulen W, van der Horst GT, et al. A novel regulation mechanism of DNA repair by damage-induced and RAD23-dependent stabilization of xeroderma pigmentosum group C protein. Genes Dev; 2003; 17(13): 1630-1645. doi: 10.1101/gad.260003

Fei J, Kaczmarek N, Luch A, et al. Regulation of nucleotide excision repair by UV-DDB: prioritization of damage recognition to internucleosomal DNA. PLoS Biol; 2011; 9(10): e1001183. doi: 10.1371/journal.pbio.1001183

Kokic G, Chernev A, Tegunov D, et al. Structural basis of TFIIH activation for nucleotide excision repair. Nat Commun; 2019; 10(1): 2885. doi: 10.1038/s41467-019-10745-5

Rimel JK, Taatjes DJ. The essential and multifunctional TFIIH complex. Protein Sci; 2018; 27(6): 1018-1037. doi: 10.1002/pro.3424

Overmeer RM, Moser J, Volker M, et al. Replication protein A safeguards genome integrity by controlling NER incision events. J Cell Biol; 2011; 192(3): 401-415. doi: 10.1083/jcb.201006011

Vermeulen W, Fousteri M. Mammalian transcription-coupled excision repair. Cold Spring Harb Perspect Biol; 2013; 5(8): a012625. doi: 10.1101/cshperspect.a012625

Svejstrup JQ. Mechanisms of transcription-coupled DNA repair. Nat Rev Mol Cell Biol; 2002; 3(1):21-29. doi: 10.1038/nrm703

Hanawalt PC, Spivak G. Transcription-coupled DNA repair: two decades of progress and surprises. Nat Rev Mol Cell Biol; 2008; 9(12): 958-970. doi: 10.1038/nrm2549

Fousteri M, Mullenders LH. Transcription-coupled nucleotide excision repair in mammalian cells: molecular mechanisms and biological effects. Cell Res; 2008; 18(1): 73-84. doi: 10.1038/cr.2008.6

van Gool AJ, Citterio E, Rademakers S, et al. The Cockayne syndrome B protein, involved in transcription-coupled DNA repair, resides in an RNA polymerase II-containing complex. EMBO J; 1997; 16(19): 5955-5965. doi: 10.1093/emboj/16.19.5955

Henning KA, Li L, Iyer N, et al. The Cockayne syndrome group A gene encodes a WD repeat protein that interacts with CSB protein and a subunit of RNA polymerase II TFIIH. Cell; 1995; 82(4): 555-564. doi: 10.1016/0092-8674(95)90028-4

van der Weegen Y, Golan-Berman H, Mevissen TET, et al. The cooperative action of CSB, CSA, and UVSSA target TFIIH to DNA damage-stalled RNA polymerase II. Nat Commun; 2020; 11(1): 2104. doi: 10.1038/s41467-020-15903-8. Erratum in: Nat Commun; 2020; 11(1): 5734

Nakatsu Y, Asahina H, Citterio E, et al. XAB2, a novel tetratricopeptide repeat protein involved in transcription-coupled DNA repair and transcription. J Biol Chem; 2000; 275(45): 34931-34937. doi: 10.1074/jbc.M004936200

Schwertman P, Lagarou A, Dekkers DH, et al. UV-sensitive syndrome protein UVSSA recruits USP7 to regulate transcription-coupled repair. Nat Genet; 2012; 44(5): 598-602. doi: 10.1038/ng.2230

Groisman R, Kuraoka I, Chevallier O, et al. CSA-dependent degradation of CSB by the ubiquitin-proteasome pathway establishes a link between complementation factors of the Cockayne syndrome. Genes Dev; 2006; 20(11): 1429-34. doi: 10.1101/gad.378206

Groisman R, Polanowska J, Kuraoka I, et al. The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage. Cell; 2003; 113(3): 357-367. doi: 10.1016/s0092-8674(03)00316-7

Watson JD, Crick FHC. A structure for deoxyribose nucleic acid. Nature; 1953; 171: 737–738.

Nirenberg MW, Matthaei JH, Jones OW, et al. Approximation of genetic code via cell-free protein synthesis directed by template RNA. Federation Proceedings; 1963; 22; 55–61.

Leder P, Clark BFC, Sly WS, et al. Cell-free peptide synthesis dependent upon synthetic oligodeoxynucleotides. Proceedings of the National Academy of Sciences; 1963; 50: 1135–1143.

Herriott RM. Mutagenesis. Cancer Research; 1966; 26(9_Part_1): 1971–1979.

Loewe L, Hill WG. The population genetics of mutations: good, bad and indifferent. Philos Trans R Soc Lond B Biol Sci; 2010; 365(1544):1153-1167. doi: 10.1098/rstb.2009.0317

Sung P, Klein H. Mechanism of homologous recombination: mediators and helicases take on regulatory functions. Nat Rev Mol Cell Biol; 2006; 7(10): 739–750. doi: 10.1038/nrm2008

Lu X, Simon M, Chodaparambil J, et al. The effect of H3K79 dimethylation and H4K20 trimethylation on nucleosome and chromatin structure. Nat Struct Mol Biol; 2008; 15; 1122–1124. doi: 10.1038/nsmb.1489

Humphrey W, Dalke A, Schulten K. VMD-Visual Molecular Dynamics. J. Molec. Graphics; 1996; 14(1): 33-38.

Gura MA, Freiman RN. Primordial Follicle. Skinner MK (eds.) Encyclopedia of Reproduction. 2nd ed. Academic Press; 2018. p. 65-71. doi: 10.1016/B978-0-12-801238-3.64394-5

Page SL, Hawley RS. The genetics and molecular biology of the synaptonemal complex. Annu Rev Cell Dev Biol; 2004; 20:525-558. doi: 10.1146/annurev.cellbio

Moens PB. Synaptonemal Complex. Brenner S, Miller JH (eds.) Encyclopedia of Genetics. Academic Press; 2001. p. 1910-1912. doi: 10.1006/rwgn.2001.1265

Vrielynck N, Chambon A, Vezon D, et al. A DNA topoisomerase VI-like complex initiates meiotic recombination. Science; 2016; 351(6276): 939-943. doi: 10.1126/science.aad5196

Lieber MR, Gu J, Lu H, et al. Nonhomologous DNA end joining (NHEJ) and chromosomal translocations in humans. Subcell Biochem; 2010; 50: 279-296. doi: 10.1007/978-90-481-3471-7_14

Krejci L, Altmannova V, Spirek M, et al. Homologous recombination and its regulation. Nucleic Acids Res; 2012; 40(13): 5795-5818. doi: 10.1093/nar/gks270

Jasin M, Rothstein R. Repair of strand breaks by homologous recombination. Cold Spring Harb Perspect Biol; 2013; 5(11): a012740. doi: 10.1101/cshperspect.a012740

Kowalczykowski SC. An Overview of the Molecular Mechanisms of Recombinational DNA Repair. Cold Spring Harb Perspect Biol; 2015; 7(11): a016410. doi: 10.1101/cshperspect.a016410

Li X, Heyer WD. Homologous recombination in DNA repair and DNA damage tolerance. Cell Res; 2008; 18, 99–113. doi: 10.1038/cr.2008.1

San Filippo J, Sung P, Klein H. Mechanism of eukaryotic homologous recombination. Annu Rev Biochem; 2008; 77: 229-257. doi: 10.1146/annurev.biochem.77.061306.125255

Toledo LI, Altmeyer M, Rask MB, et al. ATR prohibits replication catastrophe by preventing global exhaustion of RPA. Cell; 2013; 155: 1088–1103. doi: 10.1016/j.cell.2013.10.043

Iftode C, Daniely Y, Borowiec JA. Replication protein A (RPA): the eukaryotic SSB. Crit Rev Biochem Mol Biol; 1999; 34(3):141-180. doi: 10.1080/10409239991209255

Xue C, Wang W, Crickard JB, et al. Regulatory control of Sgs1 and Dna2 during eukaryotic DNA end resection. Proc Natl Acad Sci USA; 2019; 116(13): 6091-6100. doi: 10.1073/pnas.1819276116

Bermúdez-López M, Aragon L. Smc5/6 complex regulates Sgs1 recombination functions. Curr Genet; 2017; 63(3): 381-388. doi: 10.1007/s00294-016-0648-5

Cejka P, Cannavo E, Polaczek P, et al. DNA end resection by Dna2-Sgs1-RPA and its stimulation by Top3-Rmi1 and Mre11-Rad50-Xrs2. Nature; 2010; 467: 112–116. doi: 10.1038/nature09355.

Szankasi R, Smith GR. A DNA exonuclease induced during meiosis of Schizosaccharomyces pombe. J Biol Chem; 1992; 267: 3014–3023.

Cannavo E, Cejka P, Kowalczykowski SC. Relationshipof DNA degradation by Saccharomyces cerevisiae exonuclease 1 and its stimulation by RPA and Mre11–Rad50–Xrs2 to DNA end resection. Proc Natl Acad Sci; 2013; 110(18): E1661–E1668. doi: 10.1073/pnas.1305166110

Tomimatsu N, Mukherjee B, Catherine Hardebeck M, et al. Phosphorylation of EXO1 by CDKs 1 and 2 regulates DNA end resection and repair pathway choice. Nat Commun; 2014; 5: 3561. doi: 10.1038/ncomms4561

Kim C, Paulus BF, Wold MS. Interactions of Human Replication Protein A with Oligonucleotides. Biochemistry; 1994; 33(47): 14197–14206. doi: 10.1021/bi00251a031

Bhat KP, Cortez D. RPA and RAD51: fork reversal, fork protection, and genome stability. Nat Struct Mol Biol; 2018; 25(6): 446-453. doi: 10.1038/s41594-018-0075-z

Sung P. Function of yeast Rad52 protein as a mediator between replication protein A and the Rad51 recombinase. J Biol Chem; 1997; 272(45): 28194-28197. doi: 10.1074/jbc.272.45.28194

Song B, Sung P. Functional interactions among yeast Rad51 recombinase, Rad52 mediator, and replication protein A in DNA strand exchange. J Biol Chem; 2000; 275(21):15895-15904. doi: 10.1074/jbc.M910244199

Sung P. Catalysis of ATP-dependent homologous DNA pairing and strand exchange by yeast RAD51 protein. Science; 1994; 265(5176): 1241-1243. doi: 10.1126/science.8066464

Robertson RB, Moses DN, Kwon Y, et al. Structural transitions within human Rad51 nucleoprotein filaments. Proc Natl Acad Sci USA; 2009; 106(31): 12688-12693. doi: 10.1073/pnas.0811465106

Maloisel L, Bhargava J, Roeder GS. A role for DNA polymerase delta in gene conversion and crossing over during meiosis in Saccharomyces cerevisiae. Genetics; 2004; 167(3): 1133-1142. doi: 10.1534/genetics.104.026260

McVey M, Khodaverdian VY, Meyer D, et al. Eukaryotic DNA Polymerases in Homologous Recombination. Annu Rev Genet; 2016; 50: 393-421. doi: 10.1146/annurev-genet-120215-035243

Raji H, Hartsuiker E. Double-strand break repair and homologous recombination in Schizosaccharomyces pombe. Yeast; 2006; 23(13): 963-976. doi: 10.1002/yea.1414

Muñoz-Galván S, Tous C, Blanco MG, et al. Distinct roles of Mus81, Yen1, Slx1-Slx4, and Rad1 nucleases in the repair of replication-born double-strand breaks by sister chromatid exchange. Mol Cell Biol; 2012; 32(9): 1592-1603. doi: 10.1128/MCB.00111-12

Rass U. Resolving branched DNA intermediates with structure-specific nucleases during replication in eukaryotes. Chromosoma; 2013; 122(6): 499-515. doi: 10.1007/s00412-013-0431-z

Castor D, Nair N, Déclais AC, et al. Cooperative control of holliday junction resolution and DNA repair by the SLX1 and MUS81-EME1 nucleases. Mol Cell; 2013; 52(2): 221-233. doi: 10.1016/j.molcel.2013.08.036

Wyatt HD, Sarbajna S, Matos J, et al. Coordinated actions of SLX1-SLX4 and MUS81-EME1 for Holliday junction resolution in human cells. Mol Cell; 2013; 52(2): 234-247. doi: 10.1016/j.molcel.2013.08.035

Wright WD, Shah SS, Heyer WD. Homologous recombination and the repair of DNA double-strand breaks. J Biol Chem; 2018; 293(27): 10524-10535. doi: 10.1074/jbc.TM118.000372

Morrison A, Bell JB, Kunkel TA, et al. Eukaryotic DNA polymerase amino acid sequence required for 3'----5' exonuclease activity. Proc Natl Acad Sci USA; 1991; 88(21): 9473-9477. doi: 10.1073/pnas.88.21.9473

Soriano I, Vazquez E, De Leon N, et al. Expression of the cancer-associated DNA polymerase ε P286R in fission yeast leads to translesion synthesis polymerase dependent hypermutation and defective DNA replication. PLoS Genet; 2021; 17(7): e1009526. doi: 10.1371/journal.pgen.1009526

Li GM. Mechanisms and functions of DNA mismatch repair. Cell Res; 2008; 18(1): 85-98. doi: 10.1038/cr.2007.115

Duncan BK, Miller JH. Mutagenic deamination of cytosine residues in DNA. Nature; 1980; 287(5782): 560-561. doi: 10.1038/287560a0

Nakamura J, Swenberg JA. Endogenous apurinic/apyrimidinic sites in genomic DNA of mammalian tissues. Cancer Res; 1999; 59(11): 2522–2526.

Drake JW. Spontaneous mutation. Annu Rev Genet; 1991; 25: 125-146. doi: 10.1146/annurev.ge.25.120191.001013

Turrens JF. Mitochondrial formation of reactive oxygen species. J Physiol; 2003; 552(Pt2): 335-44. doi: 10.1113/jphysiol.2003.049478

Zorov DB, Juhaszova M, Sollott SJ. Mitochondrial reactive oxygen species (ROS) and ROS-induced ROS release. Physiol Rev; 2014; 94(3): 909-950. doi: 10.1152/physrev.00026.2013

White M, Cohen J, Hummel C, et al. The Role of Oxidative Stress in Ovarian Cancer: Implications for the Treatment of Patients. Preedy V(eds.) Cancer. Academic Press; 2014. p. 41-50. doi: 10.1016/B978-0-12-405205-5.00005-2

Van Loon B, Markkanen E, Hübscher U. Oxygen as a friend and enemy: How to combat the mutational potential of 8-oxo-guanine. DNA Repair; 2010; 9(6): 604–616. doi: 10.1016/j.dnarep.2010.03.004

Chatterjee N, Walker GC. Mechanisms of DNA damage, repair, and mutagenesis. Environ Mol Mutagen; 2017; 58(5): 235-263. doi: 10.1002/em.22087

Kodym A, Afza R. Physical and chemical mutagenesis. Methods Mol Biol; 2003; 236: 189-204. doi: 10.1385/1-59259-413-1:189

Brown T, Kneale G, Hunter WN, et al. Structural characterisation of the bromouracil.guanine base pair mismatch in a Z-DNA fragment. Nucleic Acids Res; 1986; 14(4): 1801-1809. doi: 10.1093/nar/14.4.1801

Sega GA. A review of the genetic effects of ethyl methanesulfonate. Mutat Res;

1984; 134(2-3): 113-142. doi: 10.1016/0165-1110(84)90007-1

Karran P, Lindahl T. Hypoxanthine in deoxyribonucleic acid: generation by heat-induced hydrolysis of adenine residues and release in free form by a deoxyribonucleic acid glycosylase from calf thymus. Biochemistry; 1980; 19(26): 6005-6011. doi: 10.1021/bi00567a010

Kamiya H, Shimizu M, Suzuki M, et al. Mutation induced by deoxyxanthosine in codon 12 of a synthetic c-Ha-ras gene. Nucleosides Nucleotides; 1992; 11(2-4): 247-260.

Scaria PV, Shafer RH. Binding of ethidium bromide to a DNA triple helix. Evidence for intercalation. J Biol Chem; 1991; 266(9): 5417-5423.

Reisz JA, Bansal N, Qian J, et al. Effects of ionizing radiation on biological molecules--mechanisms of damage and emerging methods of detection. Antioxid Redox Signal; 2014; 21(2): 260-292. doi: 10.1089/ars.2013.5489

Kiefer J. Effects of Ultraviolet Radiation on DNA. In: Obe G, Vijayalaxmi (eds.) Chromosomal Alterations. Springer, Berlin, Heidelberg. 2007. doi: 10.1007/978-3-540-71414-9_3

House JE, House KA. Atomic and Molecular Structure. In: House JE, House KA (eds.) Descriptive Inorganic Chemistry 2nd ed. Academic Press. 2010; p. 17-61. doi: 10.1016/B978-0-12-088755-2.00002-1

Nikitaki Z, Hellweg CE, Georgakilas AG, et al. Stress-induced DNA damage biomarkers: applications and limitations. Front Chem; 2015; 3: 35. doi: 10.3389/fchem.2015.00035

Wang JY. DNA damage and apoptosis. Cell Death Differ; 2001; 8(11): 1047-8. doi: 10.1038/sj.cdd.4400938

Chromosome Breakage. In: Encyclopedia of Genetics, Genomics, Proteomics and Informatics. Springer, Dordrecht. 2008; doi: 10.1007/978-1-4020-6754-9_2969

Funk RK, Stockham AL, Laack NNI. Basics of Radiation Therapy. In: Herrmann J (eds.) Clinical Cardio-Oncology Elsevier. 2016; p. 39-60. doi: 10.1016/B978-0-323-44227-5.00003-X

Rastogi RP, Richa, Kumar A. Molecular mechanisms of ultraviolet radiation-induced DNA damage and repair. J Nucleic Acids; 2010; 2010: 592980. doi: 10.4061/2010/592980

Zhu Y, Zhang Y, He Z, et al. Detrimental Effects of Multiple Mutations in Position 240 of Fusarium graminearum β2-Tubulin. Phytopathology; 2020; 110(9): 1522-1529. doi: 10.1094/PHYTO-11-19-0409-R

Hanahan D, Weinberg RA. Hallmarks of cancer: the next generation. Cell; 2011; 144(5): 646-674. doi: 10.1016/j.cell.2011.02.013

Pećina-Šlaus N, Kafka A, Salamon I, et al. Mismatch Repair Pathway, Genome Stability and Cancer. Front Mol Biosci; 2020; 7:122. doi: 10.3389/fmolb.2020.00122

Iyer RR, Pluciennik A, Burdett V, et al. DNA mismatch repair: functions and mechanisms. Chem Rev; 2006; 106(2): 302-323. doi: 10.1021/cr0404794

Fishel R, Wilson T. MutS homologs in mammalian cells. Curr Opin Genet Dev; 1997; 7(1): 105-113. doi: 10.1016/s0959-437x(97)80117-7

Habraken Y, Sung P, Prakash L, et al. Binding of insertion/deletion DNA mismatches by the heterodimer of yeast mismatch repair proteins MSH2 and MSH3. Curr Biol; 1996; 6(9): 1185-7. doi: 10.1016/s0960-9822(02)70686-6

Li, GM. Mismatch Repair. In: Bell, E. (eds) Molecular Life Sciences. Springer; 2014. doi: 10.1007/978-1-4614-6436-5_64-2

Keijzers G, Bakula D, Petr MA, et al. Human Exonuclease 1 (EXO1) Regulatory Functions in DNA Replication with Putative Roles in Cancer. Int J Mol Sci; 2018; 20(1): 74. doi: 10.3390/ijms20010074

Krokan HE, Bjørås M. Base excision repair. Cold Spring Harb Perspect Biol; 2013; 5(4): a012583. doi: 10.1101/cshperspect.a012583

Zharkov DO. Base excision DNA repair. Cell Mol Life Sci; 2008; 65(10): 1544-65. doi: 10.1007/s00018-008-7543-2

Sancar A, Lindsey-Boltz LA, Unsal-Kaçmaz K, et al. Molecular mechanisms of mammalian DNA repair and the DNA damage checkpoints. Annu Rev Biochem; 2004; 73: 39-85. doi: 10.1146/annurev.biochem.73.011303.073723

Sancar A. DNA repair in humans. Annu Rev Genet; 1995; 29:69-105. doi: 10.1146/annurev.ge.29.120195.000441

Lindahl T. DNA glycosylases, endonucleases for apurinic/apyrimidinic sites, and base excision-repair. Prog Nucleic Acid Res Mol Biol; 1979; 22: 135-192. doi: 10.1016/s0079-6603(08)60800-4

Girard PM, D'Ham C, Cadet J, et al. Opposite base-dependent excision of 7,8-dihydro-8-oxoadenine by the Ogg1 protein of Saccharomyces cerevisiae. Carcinogenesis; 1998; 19(7): 1299-1305. doi: 10.1093/carcin/19.7.1299

Lindahl T. An N-glycosidase from Escherichia coli that releases free uracil from DNA containing deaminated cytosine residues. Proc Natl Acad Sci USA; 1974; 71(9): 3649-3653. doi: 10.1073/pnas.71.9.3649

Olsen LC, Aasland R, Wittwer CU, et al. Molecular cloning of human uracil-DNA glycosylase, a highly conserved DNA repair enzyme. EMBO J; 1989; 8(10): 3121-5. doi: 10.1002/j.1460-2075.1989.tb08464.x

Richardson CC, Kornberg A. A Deoxyribonucleic acid phosphatase-exonuclease from escherichia coli. i. purification of the enzyme and characterization of the phosphatase activity. J Biol Chem; 1964; 239:242-50

Demple B, Herman T, Chen DS. Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: definition of a family of DNA repair enzymes. Proc Natl Acad Sci USA; 1991; 88(24): 11450-4. doi: 10.1073/pnas.88.24.11450

Masuda Y, Bennett RA, Demple B. Dynamics of the interaction of human apurinic endonuclease (Ape1) with its substrate and product. J Biol Chem; 1998; 273(46): 30352-9. doi: 10.1074/jbc.273.46.30352

McCullough AK, Sanchez A, Dodson ML, et al. The reaction mechanism of DNA glycosylase/AP lyases at abasic sites. Biochemistry; 2001; 40(2): 561-8. doi: 10.1021/bi002404+

Pheiffer BH, Zimmerman SB. 3'-Phosphatase activity of the DNA kinase from rat liver. Biochem Biophys Res Commun; 1982; 109(4): 1297-302. doi: 10.1016/0006-291x(82)91918-0

Weinfeld M, Mani RS, Abdou I, et al. Tidying up loose ends: the role of polynucleotide kinase/phosphatase in DNA strand break repair. Trends Biochem Sci; 2011; 36(5): 262-271. doi: 10.1016/j.tibs.2011.01.006

Dianova II, Sleeth KM, Allinson SL, et al. XRCC1-DNA polymerase beta interaction is required for efficient base excision repair. Nucleic Acids Res; 2004; 32(8): 2550-2555. doi: 10.1093/nar/gkh567

Mortusewicz O, Rothbauer U, Cardoso MC, et al. Differential recruitment of DNA Ligase I and III to DNA repair sites. Nucleic Acids Res; 2006; 34(12): 3523-3532. doi: 10.1093/nar/gkl492

Robertson AB, Klungland A, Rognes T, et al. DNA repair in mammalian cells: Base excision repair: the long and short of it. Cell Mol Life Sci; 2009; 66(6): 981-993. doi: 10.1007/s00018-009-8736-z

Koellner CM, Mensink KA, Highsmith WE. Basic Concepts in Human Molecular Genetics. Coleman WB, Tsongalis GJ (eds.) Molecular Pathology. 2nd ed. Academic Press; 2018. p. 99-120. doi: 10.1016/B978-0-12-802761-5.00005-5

Dasari S, Tchounwou PB. Cisplatin in cancer therapy: molecular mechanisms of action. Eur J Pharmacol; 2014; 740: 364-378. doi: 10.1016/j.ejphar.2014.07.025

Sancar A, Tang MS. Nucleotide excision repair. Photochem Photobiol; 1993; 57(5): 905-921. doi: 10.1111/j.1751-1097.1993.tb09233.x

Reardon JT, Sancar A. Nucleotide excision repair. Prog Nucleic Acid Res Mol Biol; 2005; 79: 183-235. doi: 10.1016/S0079-6603(04)79004-2

Reardon JT, Sancar A. Purification and characterization of Escherichia coli and human nucleotide excision repair enzyme systems. Methods Enzymol; 2006; 408: 189-213. doi: 10.1016/S0076-6879(06)08012-8

Sugasawa K. Mechanism and regulation of DNA damage recognition in mammalian nucleotide excision repair. Enzymes; 2019; 45: 99-138. doi: 10.1016/bs.enz.2019.06.004

Schärer OD. Nucleotide excision repair in eukaryotes. Cold Spring Harb Perspect Biol; 2013; 5(10): a012609. doi: 10.1101/cshperspect.a012609

Marteijn JA, Lans H, Vermeulen W, et al. Understanding nucleotide excision repair and its roles in cancer and ageing. Nat Rev Mol Cell Biol; 2014; 15(7): 465-481. doi: 10.1038/nrm3822

Prakash S, Prakash L. Nucleotide excision repair in yeast. Mutat Res. 2000; 451(1-2): 13-24. doi: 10.1016/s0027-5107(00)00037-3

Gillet LC, Schärer OD. Molecular mechanisms of mammalian global genome nucleotide excision repair. Chem Rev; 2006; 106(2): 253-276. doi: 10.1021/cr040483f

Spivak G. Transcription-coupled repair: an update. Arch Toxicol; 2016; 90(11): 2583-2594. doi: 10.1007/s00204-016-1820-x

Araki M, Masutani C, Takemura M, et al. Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair. J Biol Chem; 2001; 276(22): 18665-72. doi: 10.1074/jbc.M100855200

Nishi R, Okuda Y, Watanabe E, et al. Centrin 2 stimulates nucleotide excision repair by interacting with xeroderma pigmentosum group C protein. Mol Cell Biol; 2005; 25(13): 5664-74. doi: 10.1128/MCB.25.13.5664-5674

Masutani C, Sugasawa K, Yanagisawa J, et al. Purification and cloning of a nucleotide excision repair complex involving the xeroderma pigmentosum group C protein and a human homologue of yeast RAD23. EMBO J; 1994; 13(8): 1831-1843. doi: 10.1002/j.1460-2075.1994.tb06452.x

Ng JM, Vermeulen W, van der Horst GT, et al. A novel regulation mechanism of DNA repair by damage-induced and RAD23-dependent stabilization of xeroderma pigmentosum group C protein. Genes Dev; 2003; 17(13): 1630-1645. doi: 10.1101/gad.260003

Fei J, Kaczmarek N, Luch A, et al. Regulation of nucleotide excision repair by UV-DDB: prioritization of damage recognition to internucleosomal DNA. PLoS Biol; 2011; 9(10): e1001183. doi: 10.1371/journal.pbio.1001183

Kokic G, Chernev A, Tegunov D, et al. Structural basis of TFIIH activation for nucleotide excision repair. Nat Commun; 2019; 10(1): 2885. doi: 10.1038/s41467-019-10745-5

Rimel JK, Taatjes DJ. The essential and multifunctional TFIIH complex. Protein Sci; 2018; 27(6): 1018-1037. doi: 10.1002/pro.3424

Overmeer RM, Moser J, Volker M, et al. Replication protein A safeguards genome integrity by controlling NER incision events. J Cell Biol; 2011; 192(3): 401-415. doi: 10.1083/jcb.201006011

Vermeulen W, Fousteri M. Mammalian transcription-coupled excision repair. Cold Spring Harb Perspect Biol; 2013; 5(8): a012625. doi: 10.1101/cshperspect.a012625

Svejstrup JQ. Mechanisms of transcription-coupled DNA repair. Nat Rev Mol Cell Biol; 2002; 3(1):21-29. doi: 10.1038/nrm703

Hanawalt PC, Spivak G. Transcription-coupled DNA repair: two decades of progress and surprises. Nat Rev Mol Cell Biol; 2008; 9(12): 958-970. doi: 10.1038/nrm2549

Fousteri M, Mullenders LH. Transcription-coupled nucleotide excision repair in mammalian cells: molecular mechanisms and biological effects. Cell Res; 2008; 18(1): 73-84. doi: 10.1038/cr.2008.6

van Gool AJ, Citterio E, Rademakers S, et al. The Cockayne syndrome B protein, involved in transcription-coupled DNA repair, resides in an RNA polymerase II-containing complex. EMBO J; 1997; 16(19): 5955-5965. doi: 10.1093/emboj/16.19.5955

Henning KA, Li L, Iyer N, et al. The Cockayne syndrome group A gene encodes a WD repeat protein that interacts with CSB protein and a subunit of RNA polymerase II TFIIH. Cell; 1995; 82(4): 555-564. doi: 10.1016/0092-8674(95)90028-4

van der Weegen Y, Golan-Berman H, Mevissen TET, et al. The cooperative action of CSB, CSA, and UVSSA target TFIIH to DNA damage-stalled RNA polymerase II. Nat Commun; 2020; 11(1): 2104. doi: 10.1038/s41467-020-15903-8. Erratum in: Nat Commun; 2020; 11(1): 5734

Nakatsu Y, Asahina H, Citterio E, et al. XAB2, a novel tetratricopeptide repeat protein involved in transcription-coupled DNA repair and transcription. J Biol Chem; 2000; 275(45): 34931-34937. doi: 10.1074/jbc.M004936200

Schwertman P, Lagarou A, Dekkers DH, et al. UV-sensitive syndrome protein UVSSA recruits USP7 to regulate transcription-coupled repair. Nat Genet; 2012; 44(5): 598-602. doi: 10.1038/ng.2230

Groisman R, Kuraoka I, Chevallier O, et al. CSA-dependent degradation of CSB by the ubiquitin-proteasome pathway establishes a link between complementation factors of the Cockayne syndrome. Genes Dev; 2006; 20(11): 1429-34. doi: 10.1101/gad.378206

Groisman R, Polanowska J, Kuraoka I, et al. The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage. Cell; 2003; 113(3): 357-367. doi: 10.1016/s0092-8674(03)00316-7