{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T19:13:39Z","timestamp":1791400419100,"version":"4.3.3"},"reference-count":211,"publisher":"MDPI AG","issue":"23","license":[{"start":{"date-parts":[[2022,11,22]],"date-time":"2022-11-22T00:00:00Z","timestamp":1669075200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100012190","name":"Ministry of Science and Higher Education of the Russian Federation","doi-asserted-by":"publisher","award":["075-15-2022-263"],"award-info":[{"award-number":["075-15-2022-263"]}],"id":[{"id":"10.13039\/501100012190","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cells"],"abstract":"<jats:p>Nucleotide excision repair (NER) is a central DNA repair pathway responsible for removing a wide variety of DNA-distorting lesions from the genome. The highly choreographed cascade of core NER reactions requires more than 30 polypeptides. The xeroderma pigmentosum group A (XPA) protein plays an essential role in the NER process. XPA interacts with almost all NER participants and organizes the correct NER repair complex. In the absence of XPA\u2019s scaffolding function, no repair process occurs. In this review, we briefly summarize our current knowledge about the XPA protein structure and analyze the formation of contact with its protein partners during NER complex assembling. We focus on different ways of regulation of the XPA protein\u2019s activity and expression and pay special attention to the network of post-translational modifications. We also discuss the data that is not in line with the currently accepted hypothesis about the functioning of the XPA protein.<\/jats:p>","DOI":"10.3390\/cells11233723","type":"journal-article","created":{"date-parts":[[2022,11,23]],"date-time":"2022-11-23T03:15:24Z","timestamp":1669173324000},"page":"3723","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":12,"title":["The XPA Protein\u2014Life under Precise Control"],"prefix":"10.3390","volume":"11","author":[{"given":"Yuliya S.","family":"Krasikova","sequence":"first","affiliation":[{"name":"Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of Russian Academy of Sciences, Novosibirsk 630090, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5980-8889","authenticated-orcid":false,"given":"Olga I.","family":"Lavrik","sequence":"additional","affiliation":[{"name":"Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of Russian Academy of Sciences, Novosibirsk 630090, Russia"},{"name":"Department of Natural Sciences, Novosibirsk State University, Novosibirsk 630090, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7496-7527","authenticated-orcid":false,"given":"Nadejda I.","family":"Rechkunova","sequence":"additional","affiliation":[{"name":"Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of Russian Academy of Sciences, Novosibirsk 630090, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,11,22]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1021\/cr040483f","article-title":"Molecular mechanisms of mammalian global genome nucleotide excision repair","volume":"106","author":"Gillet","year":"2006","journal-title":"Chem Rev."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.dnarep.2018.08.005","article-title":"Molecular basis for damage recognition and verification by XPC-RAD23B and TFIIH in nucleotide excision repair","volume":"71","author":"Mu","year":"2018","journal-title":"DNA Repair"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1186\/s41021-019-0119-6","article-title":"Mechanism and regulation of DNA damage recognition in nucleotide excision repair","volume":"41","author":"Kusakabe","year":"2019","journal-title":"Genes Environ."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1442","DOI":"10.1212\/WNL.55.10.1442","article-title":"Cockayne syndrome and xeroderma pigmentosum","volume":"55","author":"Rapin","year":"2000","journal-title":"Neurology"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1038\/jid.2011.426","article-title":"Shining a light on xeroderma pigmentosum","volume":"132","author":"DiGiovanna","year":"2012","journal-title":"J. Invest. Dermatol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1236","DOI":"10.1073\/pnas.1519444113","article-title":"Deep phenotyping of 89 xeroderma pigmentosum patients reveals unexpected heterogeneity dependent on the precise molecular defect","volume":"113","author":"Fassihi","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Krasikova, Y., Rechkunova, N., and Lavrik, O. (2021). Nucleotide Excision Repair: From Molecular Defects to Neurological Abnormalities. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22126220"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/bj3280001","article-title":"The DNA damage-recognition problem in human and other eukaryotic cells: The XPA damage binding protein","volume":"328","author":"Cleaver","year":"1997","journal-title":"Biochem. J."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"18759","DOI":"10.1074\/jbc.274.26.18759","article-title":"Order of assembly of human DNA repair excision nuclease","volume":"274","author":"Wakasugi","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1002\/mc.10143","article-title":"Critical DNA damage recognition functions of XPC-hHR23B and XPA-RPA in nucleotide excision repair","volume":"38","author":"Thoma","year":"2003","journal-title":"Mol. Carcinog."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1016\/j.molcel.2015.08.012","article-title":"Tripartite DNA Lesion Recognition and Verification by XPC, TFIIH, and XPA in Nucleotide Excision Repair","volume":"59","author":"Li","year":"2015","journal-title":"Mol. Cell"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.dnarep.2016.05.018","article-title":"XPA: A key scaffold for human nucleotide excision repair","volume":"44","author":"Sugitani","year":"2016","journal-title":"DNA Repair"},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Borsz\u00e9kov\u00e1 Pulzov\u00e1, L., Ward, T.A., and Chovanec, M. (2020). XPA: DNA Repair Protein of Significant Clinical Importance. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21062182"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"701","DOI":"10.1038\/1400","article-title":"Solution structure of the DNA- and RPA-binding domain of the human repair factor XPA","volume":"5","author":"Ikegami","year":"1998","journal-title":"Nat. Struct. Biol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"15116","DOI":"10.1021\/bi991755p","article-title":"Interactions of human nucleotide excision repair protein XPA with DNA and RPA70 Delta C327: Chemical shift mapping and 15N NMR relaxation studies","volume":"38","author":"Buchko","year":"1999","journal-title":"Biochemistry"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"985","DOI":"10.1016\/j.bbrc.2019.05.050","article-title":"Structural characterization of the redefined DNA-binding domain of human XPA","volume":"514","author":"Lian","year":"2019","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"466","DOI":"10.1016\/j.ijbiomac.2020.01.169","article-title":"New structural insights into the recognition of undamaged splayed-arm DNA with a single pair of non-complementary nucleotides by human nucleotide excision repair protein XPA","volume":"148","author":"Lian","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"8272","DOI":"10.1073\/pnas.1508509112","article-title":"Structural insights into the recognition of cisplatin and AAF-dG lesion by Rad14 (XPA)","volume":"112","author":"Koch","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"10782","DOI":"10.1002\/chem.201602438","article-title":"Structural basis for bulky-Adduct DNA-lesion recognition by the nucleotide excision repair protein Rad14","volume":"22","author":"Simon","year":"2016","journal-title":"Chemistry"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1379","DOI":"10.1002\/cbic.201700169","article-title":"Structural insights into the recognition of N(2) -Aryl- and C8-Aryl DNA lesions by the repair protein XPA\/ Rad14","volume":"18","author":"Ebert","year":"2017","journal-title":"Chembiochem"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"2885","DOI":"10.1038\/s41467-019-10745-5","article-title":"Structural basis of TFIIH activation for nucleotide excision repair","volume":"10","author":"Kokic","year":"2019","journal-title":"Nat. Commun."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"8083","DOI":"10.1093\/nar\/gkq649","article-title":"Localization of xeroderma pigmentosum group A protein and replication protein A on damaged DNA in nucleotide excision repair","volume":"38","author":"Krasikova","year":"2010","journal-title":"Nucleic Acids Res."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1038\/nrm3920","article-title":"Intrinsically disordered proteins in cellular signalling and regulation","volume":"16","author":"Wright","year":"2015","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"5129","DOI":"10.1111\/j.1742-4658.2005.04948.x","article-title":"Flexible nets. The roles of intrinsic disorder in protein interaction networks","volume":"272","author":"Dunker","year":"2005","journal-title":"FEBS J."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1038\/msb.2008.16","article-title":"The role of disorder in interaction networks: A structural analysis","volume":"4","author":"Kim","year":"2008","journal-title":"Mol. Syst. Biol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"12182","DOI":"10.1016\/S0021-9258(19)49821-9","article-title":"Mutational analysis of the structure and function of the xeroderma pigmentosum group A complementing protein. Identification of essential domains for nuclear localization and DNA excision repair","volume":"267","author":"Miyamoto","year":"1992","journal-title":"J. Biol. Chem."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"854745","DOI":"10.1155\/2013\/854745","article-title":"Structural and Sequence Similarities of Hydra Xeroderma Pigmentosum A Protein to Human Homolog Suggest Early Evolution and Conservation","volume":"2013","author":"Barve","year":"2013","journal-title":"BioMed Res. Int."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1038\/348073a0","article-title":"Analysis of a human DNA excision repair gene involved in group A xeroderma pigmentosum and containing a zinc-finger domain","volume":"348","author":"Tanaka","year":"1990","journal-title":"Nature"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"2635","DOI":"10.1093\/nar\/29.12.2635","article-title":"DNA-XPA interactions: A 31P NMP and molecular modeling study of dCCAATTAACC association with the minimal DNA-binding domain (M98-F219) of the Nucleotide Excision Repair protein XPA","volume":"29","author":"Buchko","year":"2001","journal-title":"Nucleic Acids Res."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1016\/j.ab.2007.05.019","article-title":"Quantitative electrospray ionization mass spectrometry of zinc finger oxidation: The reaction of XPA zinc finger with H(2)O(2)","volume":"369","author":"Smirnova","year":"2007","journal-title":"Anal Biochem"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1016\/0921-8777(95)00038-0","article-title":"Identification of a damaged-DNA binding domain of the XPA protein","volume":"362","author":"Kuraoka","year":"1996","journal-title":"Mutat. Res."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"2779","DOI":"10.1093\/nar\/26.11.2779","article-title":"Structural features of the minimal DNA binding domain (M98-F219) of human nucleotide excision repair protein XPA","volume":"26","author":"Buchko","year":"1998","journal-title":"Nucleic Acids Res."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"e00162","DOI":"10.1042\/BSR20140158","article-title":"A new structural insight into XPA-DNA interactions","volume":"34","author":"Hilton","year":"2014","journal-title":"Biosci. Rep."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"10830","DOI":"10.1021\/ja503020f","article-title":"Redefining the DNA-binding domain of human XPA","volume":"136","author":"Sugitani","year":"2014","journal-title":"J. Am. Chem. Soc."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"16847","DOI":"10.1074\/jbc.M117.800078","article-title":"Analysis of DNA binding by human factor xeroderma pigmentosum complementation group A (XPA) provides insight into its interactions with nucleotide excision repair substrates","volume":"292","author":"Sugitani","year":"2017","journal-title":"J. Biol. Chem."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"3554","DOI":"10.1093\/emboj\/20.13.3554","article-title":"Double-check probing of DNA bending and unwinding by XPA-RPA: An architectural function in DNA repair","volume":"20","author":"Missura","year":"2001","journal-title":"EMBO J."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1038\/nsmb1061","article-title":"Recognition of helical kinks by xeroderma pigmentosum group A protein triggers DNA excision repair","volume":"13","author":"Camenisch","year":"2006","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"15921","DOI":"10.1021\/bi061626q","article-title":"Specific and efficient binding of xeroderma pigmentosum complementation group A to double-strand\/single-strand DNA junctions with 3'- and\/or 5'-ssDNA branches","volume":"45","author":"Yang","year":"2006","journal-title":"Biochemistry"},{"key":"ref_39","doi-asserted-by":"crossref","unstructured":"Krasikova, Y.S., Rechkunova, N.I., Maltseva, E.A., and Lavrik, O.I. (2018). RPA and XPA interaction with DNA structures mimicking intermediates of the late stages in nucleotide excision repair. PLoS ONE, 13.","DOI":"10.1371\/journal.pone.0190782"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1356","DOI":"10.1038\/s41467-020-15168-1","article-title":"Single molecule analysis reveals monomeric XPA bends DNA and undergoes episodic linear diffusion during damage search","volume":"11","author":"Beckwitt","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"516","DOI":"10.1093\/nar\/gkn964","article-title":"Physical and functional interaction between DDB and XPA in nucleotide excision repair","volume":"37","author":"Wakasugi","year":"2009","journal-title":"Nucleic Acids Res."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"4762","DOI":"10.1038\/s41467-022-31820-4","article-title":"XPC-PARP complexes engage the chromatin remodeler ALC1 to catalyze global genome DNA damage repair","volume":"13","author":"Blessing","year":"2022","journal-title":"Nat. Commun."},{"key":"ref_43","first-page":"a012609","article-title":"Nucleotide excision repair in eukaryotes","volume":"5","year":"2013","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"14965","DOI":"10.1021\/bi061370o","article-title":"Biochemical and structural domain analysis of xeroderma pigmentosum complementation group C protein","volume":"45","author":"Bunick","year":"2006","journal-title":"Biochemistry"},{"key":"ref_45","first-page":"886","article-title":"Interaction of nucleotide excision repair factors XPC-HR23B, XPA, and RPA with damaged DNA","volume":"73","author":"Krasikova","year":"2008","journal-title":"Biochemistry"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"102972","DOI":"10.1016\/j.dnarep.2020.102972","article-title":"Envisioning how the prototypic molecular machine TFIIH functions in transcription initiation and DNA repair","volume":"96","author":"Tsutakawa","year":"2020","journal-title":"DNA Repair"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"4896","DOI":"10.1074\/jbc.270.9.4896","article-title":"The general transcription-repair factor TFIIH is recruited to the excision repair complex by the XPA protein independent of the TFIIE transcription factor","volume":"270","author":"Park","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"1156","DOI":"10.1002\/bies.201400107","article-title":"Replication protein A: Single-stranded DNA's first responder: Dynamic DNA-interactions allow replication protein A to direct single-strand DNA intermediates into different pathways for synthesis or repair","volume":"36","author":"Chen","year":"2014","journal-title":"Bioessays"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1146\/annurev.biochem.66.1.61","article-title":"Replication protein A: A heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism","volume":"66","author":"Wold","year":"1997","journal-title":"Annu. Rev. Biochem."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1134\/S0026893316030080","article-title":"Replication protein A as a major eukaryotic single-stranded DNA-binding protein and its role in DNA repair","volume":"50","author":"Krasikova","year":"2016","journal-title":"Mol. Biol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"2173","DOI":"10.1093\/nar\/gkz1231","article-title":"A key interaction with RPA orients XPA in NER complexes","volume":"48","author":"Sugitani","year":"2020","journal-title":"Nucleic Acids Res."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"e2207408119","DOI":"10.1073\/pnas.2207408119","article-title":"Two interaction surfaces between XPA and RPA organize the preincision complex in nucleotide excision repair","volume":"119","author":"Kim","year":"2022","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"5012","DOI":"10.1073\/pnas.91.11.5012","article-title":"Specific association between the human DNA repair proteins XPA and ERCC1","volume":"91","author":"Li","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"5017","DOI":"10.1073\/pnas.91.11.5017","article-title":"Formation of a ternary complex by human XPA, ERCC1, and ERCC4(XPF) excision repair proteins","volume":"91","author":"Park","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"4768","DOI":"10.1038\/sj.emboj.7601894","article-title":"Structural basis for the recruitment of ERCC1-XPF to nucleotide excision repair complexes by XPA","volume":"26","author":"Tsodikov","year":"2007","journal-title":"EMBO J."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1016\/j.dnarep.2008.01.018","article-title":"DNA repair gets physical: Mapping an XPA-binding site on ERCC1","volume":"7","author":"Croteau","year":"2008","journal-title":"DNA Repair"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"2503","DOI":"10.1016\/j.bpj.2013.04.023","article-title":"Conformational determinants for the recruitment of ERCC1 by XPA in the nucleotide excision repair (NER) Pathway: Structure and dynamics of the XPA binding motif","volume":"104","author":"Fadda","year":"2013","journal-title":"Biophys J."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1083\/jcb.200903138","article-title":"Identification of a novel, widespread, and functionally important PCNA-binding motif","volume":"186","author":"Gilljam","year":"2009","journal-title":"J. Cell Biol."},{"key":"ref_59","doi-asserted-by":"crossref","unstructured":"Gilljam, K.M., M\u00fcller, R., Liabakk, N.B., and Otterlei, M. (2012). Nucleotide excision repair is associated with the replisome and its efficiency depends on a direct interaction between XPA and PCNA. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0049199"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1107\/S2053230X18003242","article-title":"Structure of proliferating cell nuclear antigen (PCNA) bound to an APIM peptide reveals the universality of PCNA interaction","volume":"74","author":"Hara","year":"2018","journal-title":"Acta Cryst. F Struct. Biol. Commun."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"13012","DOI":"10.1021\/bi026064z","article-title":"Dimerization of human XPA and formation of XPA(2)-RPA protein complex","volume":"41","author":"Yang","year":"2002","journal-title":"Biochemistry"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"5755","DOI":"10.1128\/MCB.23.16.5755-5767.2003","article-title":"Xeroderma pigmentosum group A protein loads as a separate factor onto DNA lesions","volume":"23","author":"Rademakers","year":"2003","journal-title":"Mol. Cell. Biol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"3322","DOI":"10.1080\/07391102.2018.1517051","article-title":"Investigation of the probable homo-dimer model of the Xeroderma pigmentosum complementation group A (XPA) protein to represent the DNA-binding core","volume":"37","author":"Pradhan","year":"2019","journal-title":"J. Biomol. Struct. Dyn."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1007\/s00018-022-04194-5","article-title":"XPG: A multitasking genome caretaker","volume":"79","author":"Theil","year":"2022","journal-title":"Cell Mol. Life Sci."},{"key":"ref_65","doi-asserted-by":"crossref","unstructured":"Park, J.M., and Kang, T.H. (2016). Transcriptional and posttranslational regulation of nucleotide excision repair: The guardian of the genome against ultraviolet radiation. Int. J. Mol. Sci., 17.","DOI":"10.3390\/ijms17111840"},{"key":"ref_66","first-page":"1008","article-title":"Post-translational Modifications of Nucleotide Excision Repair Proteins and Their Role in the DNA Repair","volume":"84","author":"Rechkunova","year":"2019","journal-title":"Biochemistry"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"24213","DOI":"10.1074\/jbc.M109.000745","article-title":"Checkpoint kinase ATR promotes nucleotide excision repair of UV-induced DNA damage via physical interaction with xeroderma pigmentosum group A","volume":"284","author":"Shell","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"655","DOI":"10.4161\/cc.8.4.7844","article-title":"UV-dependent interaction between Cep164 and XPA mediates localization of Cep164 at sites of DNA damage and UV sensitivity","volume":"8","author":"Pan","year":"2009","journal-title":"Cell Cycle"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"4212","DOI":"10.1093\/nar\/28.21.4212","article-title":"A novel cytoplasmic GTPase XAB1 interacts with DNA repair protein XPA","volume":"28","author":"Nitta","year":"2000","journal-title":"Nucleic Acids Res."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"34931","DOI":"10.1074\/jbc.M004936200","article-title":"XAB2, a novel tetratricopeptide repeat protein involved in transcription-coupled DNA repair and transcription","volume":"275","author":"Nakatsu","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"940","DOI":"10.1074\/jbc.M706647200","article-title":"Isolation of XAB2 complex involved in pre-mRNA splicing, transcription, and transcription-coupled repair","volume":"283","author":"Kuraoka","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"8239","DOI":"10.1093\/nar\/gkz532","article-title":"XAB2 depletion induces intron retention in POLR2A to impair global transcription and promote cellular senescence","volume":"47","author":"Hou","year":"2019","journal-title":"Nucleic Acids Res."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"5702","DOI":"10.1093\/nar\/gkw275","article-title":"Tetratricopeptide repeat factor XAB2 mediates the end resection step of homologous recombination","volume":"44","author":"Onyango","year":"2016","journal-title":"Nucleic Acids Res."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"3153","DOI":"10.1038\/s41467-021-23505-1","article-title":"The splicing factor XAB2 interacts with ERCC1-XPF and XPG for R-loop processing","volume":"12","author":"Goulielmaki","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"e77094","DOI":"10.7554\/eLife.77094","article-title":"XAB2 dynamics during DNA damage-dependent transcription inhibition","volume":"11","author":"Donnio","year":"2022","journal-title":"Elife"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"15933","DOI":"10.1073\/pnas.0403664101","article-title":"In vivo dynamics of chromatin-associated complex formation in mammalian nucleotide excision repair","volume":"101","author":"Bernas","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"570","DOI":"10.1038\/nature06155","article-title":"Recognition of DNA damage by the Rad4 nucleotide excision repair protein","volume":"449","author":"Min","year":"2007","journal-title":"Nature"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"6015","DOI":"10.1093\/nar\/gkz359","article-title":"Structure and mechanism of pyrimidine-pyrimidone (6-4) photoproduct recognition by the Rad4\/XPC nucleotide excision repair complex","volume":"47","author":"Paul","year":"2019","journal-title":"Nucleic Acids Res."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"8337","DOI":"10.1093\/nar\/gkz629","article-title":"Single-molecule visualization reveals the damage search mechanism for the human NER protein XPC-RAD23B","volume":"47","author":"Cheon","year":"2019","journal-title":"Nucleic Acids Res."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"12348","DOI":"10.1093\/nar\/gkaa909","article-title":"Tethering- facilitated DNA 'opening' and complementary roles of \u03b2-hairpin motifs in the Rad4\/XPC DNA damage sensor protein","volume":"48","author":"Paul","year":"2020","journal-title":"Nucleic Acids Res."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"4868","DOI":"10.1038\/s41467-020-18705-0","article-title":"Ubiquitin and TFIIH-stimulated DDB2 dissociation drives DNA damage handover in nucleotide excision repair","volume":"11","author":"Sabatella","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"3338","DOI":"10.1038\/s41467-021-23684-x","article-title":"Cryo-EM structure of TFIIH\/Rad4-Rad23-Rad33 in damaged DNA opening in nucleotide excision repair","volume":"12","author":"Shim","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"3811","DOI":"10.1093\/nar\/gkz120","article-title":"Poly(ADP-ribosyl)ation by PARP1: Reaction mechanism and regulatory proteins","volume":"47","author":"Alemasova","year":"2019","journal-title":"Nucleic Acids Res."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"1228","DOI":"10.1016\/j.cell.2020.02.010","article-title":"Ubiquitination of DNA Damage-Stalled RNAPII Promotes Transcription-Coupled Repair","volume":"180","author":"Nakazawa","year":"2020","journal-title":"Cell"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"1039","DOI":"10.1016\/j.cell.2020.02.053","article-title":"Repair, Removal, and Shutdown: It All Hinges on RNA Polymerase II Ubiquitylation","volume":"180","author":"Son","year":"2020","journal-title":"Cell"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"2104","DOI":"10.1038\/s41467-020-15903-8","article-title":"The cooperative action of CSB, CSA, and UVSSA target TFIIH to DNA damage-stalled RNA polymerase II","volume":"11","author":"Mevissen","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"14127","DOI":"10.1073\/pnas.1921311117","article-title":"Human XPG nuclease structure, assembly, and activities with insights for neurodegeneration and cancer from pathogenic mutations","volume":"117","author":"Tsutakawa","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1038\/nature17970","article-title":"Near-atomic resolution visualization of human transcription promoter opening","volume":"533","author":"He","year":"2016","journal-title":"Nature"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1038\/nature24282","article-title":"Structures of transcription pre-initiation complex with TFIIH and Mediator","volume":"551","author":"Schilbach","year":"2017","journal-title":"Nature"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1073\/pnas.1213981110","article-title":"ARCH domain of XPD, an anchoring platform for CAK that conditions TFIIH DNA repair and transcription activities","volume":"110","author":"Abdulrahman","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"414","DOI":"10.1038\/nature23903","article-title":"The cryo-electron microscopy structure of human transcription factor IIH","volume":"549","author":"Greber","year":"2017","journal-title":"Nature"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"e44771","DOI":"10.7554\/eLife.44771","article-title":"The complete structure of the human TFIIH core complex","volume":"8","author":"Greber","year":"2019","journal-title":"Elife"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"zcaa022","DOI":"10.1093\/narcan\/zcaa022","article-title":"Replication protein A: A multifunctional protein with roles in DNA replication, repair and beyond","volume":"2","author":"Dueva","year":"2020","journal-title":"NAR Cancer"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"3908","DOI":"10.1074\/jbc.M111.287441","article-title":"Repair-specific functions of replication protein A","volume":"287","author":"Hass","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1093\/nar\/29.2.373","article-title":"Polarity of human replication protein A binding to DNA","volume":"29","author":"Kolpashchikov","year":"2001","journal-title":"Nucleic Acids Res."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"2337","DOI":"10.1101\/gad.194787.112","article-title":"Structure and conformational change of a replication protein A heterotrimer bound to ssDNA","volume":"26","author":"Fan","year":"2012","journal-title":"Genes Dev."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1016\/j.jmb.2011.08.034","article-title":"Role of interaction of XPF with RPA in nucleotide excision repair","volume":"413","author":"Fisher","year":"2011","journal-title":"J. Mol. Biol."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1016\/j.dnarep.2011.04.022","article-title":"Regulation of endonuclease activity in human nucleotide excision repair","volume":"10","author":"Fagbemi","year":"2011","journal-title":"DNA Repair"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"1111","DOI":"10.1038\/emboj.2009.49","article-title":"Coordination of dual incision and repair synthesis in human nucleotide excision repair","volume":"28","author":"Staresincic","year":"2009","journal-title":"EMBO J."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"5293","DOI":"10.1093\/emboj\/cdg489","article-title":"The comings and goings of nucleotide excision repair factors on damaged DNA","volume":"22","author":"Riedl","year":"2003","journal-title":"EMBO J."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1038\/sj.emboj.7601948","article-title":"Sequential recruitment of the repair factors during NER: The role of XPG in initiating the resynthesis step","volume":"27","author":"Mocquet","year":"2008","journal-title":"EMBO J."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1083\/jcb.201006011","article-title":"Replication protein A safeguards genome integrity by controlling NER incision events","volume":"192","author":"Overmeer","year":"2011","journal-title":"J. Cell Biol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1016\/j.molcel.2007.06.014","article-title":"Sealing of chromosomal DNA nicks during nucleotide excision repair requires XRCC1 and DNA ligase III alpha in a cell-cycle-specific manner","volume":"27","author":"Moser","year":"2007","journal-title":"Mol. Cell"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"26574","DOI":"10.1074\/jbc.M114.597088","article-title":"DNA repair synthesis and ligation affect the processing of excised oligonucleotides generated by human nucleotide excision repair","volume":"289","author":"Kemp","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"22889","DOI":"10.1074\/jbc.M112.374447","article-title":"Mechanism of release and fate of excised oligonucleotides during nucleotide excision repair","volume":"287","author":"Kemp","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1016\/j.dnarep.2005.12.001","article-title":"XPA protein as a limiting factor for nucleotide excision repair and UV sensitivity in human cells","volume":"5","author":"Roginskaya","year":"2006","journal-title":"DNA Repair"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"2281","DOI":"10.1128\/MCB.21.7.2281-2291.2001","article-title":"Strong functional interactions of TFIIH with XPC and XPG in human DNA nucleotide excision repair, without a preassembled repairosome","volume":"21","author":"Nigg","year":"2001","journal-title":"Mol. Cell. Biol."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1083\/jcb.200909175","article-title":"Stochastic and reversible assembly of a multiprotein DNA repair complex ensures accurate target site recognition and efficient repair","volume":"189","author":"Luijsterburg","year":"2010","journal-title":"J. Cell Biol."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"7147","DOI":"10.1016\/S0021-9258(18)53158-6","article-title":"Replication protein A is the major single-stranded DNA binding protein detected in mammalian cell extracts by gel retardation assays and UV cross-linking of long and short single-stranded DNA molecules","volume":"268","author":"Seroussi","year":"1993","journal-title":"J. Biol. Chem."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1002\/mc.20418","article-title":"Elevation of XPA protein level in testis tumor cells without increasing resistance to cisplatin or UV radiation","volume":"47","author":"Roginskaya","year":"2008","journal-title":"Mol. Carcinog."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"2864","DOI":"10.1073\/pnas.0812638106","article-title":"Circadian oscillation of nucleotide excision repair in mammalian brain","volume":"106","author":"Kang","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"4890","DOI":"10.1073\/pnas.0915085107","article-title":"Circadian control of XPA and excision repair of cisplatin-DNA damage by cryptochrome and HERC2 ubiquitin ligase","volume":"107","author":"Kang","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"18790","DOI":"10.1073\/pnas.1115249108","article-title":"Control of skin cancer by the circadian rhythm","volume":"108","author":"Gaddameedhi","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"3176","DOI":"10.1093\/nar\/gkq1318","article-title":"Regulation of nucleotide excision repair activity by transcriptional and post-transcriptional control of the XPA protein","volume":"39","author":"Kang","year":"2010","journal-title":"Nucleic Acids Res."},{"key":"ref_115","first-page":"6152","article-title":"Overexpression of the XPA repair gene increases resistance to ultraviolet radiation in human cells by selective repair of DNA damage","volume":"55","author":"Cleaver","year":"1995","journal-title":"Cancer Res."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"1039","DOI":"10.1093\/carcin\/23.6.1039","article-title":"Low amounts of the DNA repair XPA protein are sufficient to recover UV-resistance","volume":"23","author":"Muotri","year":"2002","journal-title":"Carcinogenesis"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.dnarep.2017.10.004","article-title":"XPA is primarily cytoplasmic but is transported into the nucleus upon UV damage in a cell cycle dependent manner","volume":"60","author":"Musich","year":"2017","journal-title":"DNA Repair"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1038\/sj.onc.1209828","article-title":"ATR-dependent checkpoint modulates XPA nuclear import in response to UV irradiation","volume":"26","author":"Wu","year":"2007","journal-title":"Oncogene"},{"key":"ref_119","doi-asserted-by":"crossref","unstructured":"Li, Z., Musich, P.R., Cartwright, B.M., Wang, H., and Zou, Y. (2013). UV-induced nuclear import of XPA is mediated by importin-\u03b14 in an ATR-dependent manner. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0068297"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/j.dnarep.2018.01.002","article-title":"Response to \u201cXPA is primarily cytoplasmic but is transported into the nucleus upon UV damage\u201d","volume":"62","author":"Wood","year":"2018","journal-title":"DNA Repair"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"17896","DOI":"10.1073\/pnas.0801585105","article-title":"ATR kinase is required for global genomic nucleotide excision repair exclusively during S phase in human cells","volume":"105","author":"Auclair","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_122","doi-asserted-by":"crossref","unstructured":"Li, Z., Musich, P.R., Serrano, M.A., Dong, Z., and Zou, Y. (2011). XPA-mediated regulation of global nucleotide excision repair by ATR Is p53-dependent and occurs primarily in S-phase. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0028326"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1007\/978-3-319-56017-5_4","article-title":"Xeroderma PigmentosaGroup A (XPA), Nucleotide Excision Repair and Regulation by ATR in Response to Ultraviolet Irradiation","volume":"996","author":"Musich","year":"2017","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/0378-1119(96)00510-0","article-title":"Molecular cloning, expression and chromosomal localization of a human gene encoding a 33 kDa putative metallopeptidase (PRSM1)","volume":"174","author":"Scott","year":"1996","journal-title":"Gene"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/S0092-8674(00)80407-9","article-title":"GRASP65, a protein involved in the stacking of Golgi cisternae","volume":"91","author":"Barr","year":"1997","journal-title":"Cell"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"R93","DOI":"10.1530\/JME-19-0153","article-title":"Circadian clock genes and the transcriptional architecture of the clock mechanism","volume":"63","author":"Cox","year":"2019","journal-title":"J. Mol. Endocrinol."},{"key":"ref_127","doi-asserted-by":"crossref","unstructured":"Kang, T.-H. (2021). Circadian Rhythm of NER and ATR Pathways. Biomolecules, 11.","DOI":"10.3390\/biom11050715"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"14524","DOI":"10.18632\/oncotarget.24539","article-title":"The circadian clock regulates cisplatin-induced toxicity and tumor regression in melanoma mouse and human models","volume":"9","author":"Dakup","year":"2018","journal-title":"Oncotarget"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"296","DOI":"10.1111\/php.12662","article-title":"Impact of the Circadian Clock on UV-Induced DNA Damage Response and Photocarcinogenesis","volume":"93","author":"Dakup","year":"2017","journal-title":"Photochem Photobiol."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1038\/onc.2012.539","article-title":"Coordinated regulation of XPA stability by ATR and HERC2 during nucleotide excision repair","volume":"33","author":"Lee","year":"2014","journal-title":"Oncogene"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"912","DOI":"10.1111\/j.1365-2958.2008.06574.x","article-title":"Controlled degradation by ClpXP protease tunes the levels of the excision repair protein UvrA to the extent of DNA damage","volume":"71","author":"Pruteanu","year":"2009","journal-title":"Mol. Microbiol."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/j.addr.2016.10.002","article-title":"Molecular Targeting of Hypoxia in Radiotherapy","volume":"109","author":"Rey","year":"2017","journal-title":"Adv. Drug Deliv."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1038\/nrc3958","article-title":"The Tumour Microenvironment After Radiotherapy: Mechanisms of Resistance and Recurrence","volume":"15","author":"Barker","year":"2015","journal-title":"Nat. Rev. Cancer"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"742215","DOI":"10.3389\/fendo.2021.742215","article-title":"Hypoxia in Solid Tumors: How Low Oxygenation Impacts the \"Six Rs\" of Radiotherapy","volume":"12","author":"Rakotomalala","year":"2021","journal-title":"Front. Endocrinol."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"1187","DOI":"10.1093\/carcin\/bgs142","article-title":"HIF1\u03b1 regulated expression of XPA contributes to cisplatin resistance in lung cancer","volume":"33","author":"Liu","year":"2012","journal-title":"Carcinogenesis"},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"797","DOI":"10.1093\/nar\/gkp1072","article-title":"Hypoxia-inducible factor-1alpha regulates the expression of nucleotide excision repair proteins in keratinocytes","volume":"38","author":"Rezvani","year":"2010","journal-title":"Nucleic Acids Res."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"364","DOI":"10.18632\/aging.202137","article-title":"Enhancer-bound Nrf2 licenses HIF-1\u03b1 transcription under hypoxia to promote cisplatin resistance in hepatocellular carcinoma cells","volume":"13","author":"Jin","year":"2020","journal-title":"Aging"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1016\/j.dnarep.2015.09.015","article-title":"High mobility group (HMG) proteins: Modulators of chromatin structure and DNA repair in mammalian cells","volume":"36","author":"Reeves","year":"2015","journal-title":"DNA Repair"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"911152","DOI":"10.3389\/fimmu.2022.911152","article-title":"High Mobility Group Proteins in Sepsis","volume":"13","author":"Liang","year":"2022","journal-title":"Front. Immunol."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"32184","DOI":"10.1074\/jbc.M505600200","article-title":"Inhibition of nucleotide excision repair by high mobility group protein HMGA1","volume":"280","author":"Adair","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"6044","DOI":"10.1158\/0008-5472.CAN-06-1689","article-title":"High-mobility group A1 proteins inhibit expression of nucleotide excision repair factor xeroderma pigmentosum group A","volume":"67","author":"Adair","year":"2007","journal-title":"Cancer Res."},{"key":"ref_142","doi-asserted-by":"crossref","unstructured":"Jiang, Y., Zhang, C., Chen, K., Chen, Z., Sun, Z., Zhang, Z., Ding, D., Ren, S., and Zuo, Y. (2014). The clinical significance of DC-SIGN and DC-SIGNR, which are novel markers expressed in human colon cancer. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0114748"},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1007\/s11010-015-2465-4","article-title":"Low expression of dendritic cell-specific intercellular adhesion molecule-grabbing nonintegrin-related protein in lung cancer and significant correlations with brain metastasis and natural killer cells","volume":"407","author":"Liu","year":"2015","journal-title":"Mol. Cell Biochem."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1186\/s13045-016-0383-x","article-title":"Novel roles of DC-SIGNR in colon cancer cell adhesion, migration, invasion, and liver metastasis","volume":"10","author":"Na","year":"2017","journal-title":"J. Hematol. Oncol."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1186\/s12943-017-0639-2","article-title":"DC\u2014SIGNR by influencing the lncRNA HNRNPKP2 upregulates the expression of CXCR4 in gastric cancer liver metastasis","volume":"16","author":"Zhang","year":"2017","journal-title":"Mol. Cancer"},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"681372","DOI":"10.3389\/fcell.2021.681372","article-title":"CLEC4s as Potential Therapeutic Targets in Hepatocellular Carcinoma Microenvironment","volume":"9","author":"Zhang","year":"2021","journal-title":"Front. Cell Dev. Biol."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"6374","DOI":"10.7150\/jca.30139","article-title":"CLEC4M is associated with poor prognosis and promotes cisplatin resistance in NSCLC patients","volume":"10","author":"Tan","year":"2019","journal-title":"J. Cancer"},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"54","DOI":"10.3109\/08830185.2013.834897","article-title":"DC-SIGN, DC-SIGNR and LSECtin: C-type lectins for infection","volume":"33","author":"Zhang","year":"2014","journal-title":"Int. Rev. Immunol."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1007\/s00109-008-0350-2","article-title":"DC-SIGN and L-SIGN: The SIGNs for infection","volume":"86","author":"Khoo","year":"2008","journal-title":"J. Mol. Med."},{"key":"ref_150","first-page":"1711","article-title":"High expression levels of CLEC4M indicate poor prognosis in patients with hepatocellular carcinoma","volume":"19","author":"Luo","year":"2020","journal-title":"Oncol. Lett."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"2245","DOI":"10.3892\/mmr.2020.11336","article-title":"CLEC4M overexpression inhibits progression and is associated with a favorable prognosis in hepatocellular carcinoma","volume":"22","author":"Yu","year":"2020","journal-title":"Mol. Med. Rep."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"a012716","DOI":"10.1101\/cshperspect.a012716","article-title":"DNA damage sensing by the ATM and ATR kinases","volume":"5","author":"Zou","year":"2013","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"ref_153","first-page":"238","article-title":"Bringing It All Together: Coupling Excision Repair to the DNA Damage Checkpoint","volume":"93","year":"2016","journal-title":"Photochem. Photobiol."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1038\/cr.2014.147","article-title":"RPA-coated single-stranded DNA as a platform for post-translational modifications in the DNA damage response","volume":"25","author":"Zou","year":"2015","journal-title":"Cell Res."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1038\/s41594-018-0181-y","article-title":"Dynamics and selective remodeling of the DNA-binding domains of RPA","volume":"26","author":"Pokhrel","year":"2019","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1016\/S0076-6879(05)09007-5","article-title":"Recruitment of ATR-ATRIP, Rad17, and 9-1-1 complexes to DNA damage","volume":"409","author":"Yang","year":"2006","journal-title":"Methods Enzymol."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"4728","DOI":"10.1038\/sj.onc.1208674","article-title":"Interaction and colocalization of Rad9\/Rad1\/Hus1 checkpoint complex with replication protein A in human cells","volume":"24","author":"Wu","year":"2005","journal-title":"Oncogene"},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1016\/j.dnarep.2013.01.003","article-title":"NER initiation factors, DDB2 and XPC, regulate UV radiation response by recruiting ATR and ATM kinases to DNA damage sites","volume":"12","author":"Ray","year":"2013","journal-title":"DNA Repair"},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"5074","DOI":"10.1074\/jbc.M113.542787","article-title":"Coupling of human DNA excision repair and the DNA damage checkpoint in a defined in vitro system","volume":"289","author":"Kemp","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_160","doi-asserted-by":"crossref","unstructured":"Ray, A., Blevins, C., Wani, G., and Wani, A.A. (2016). ATR- and ATM-Mediated DNA damage response is dependent on excision repair assembly during G1 but bot in S phase of cell cycle. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0159344"},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1101\/gad.1627708","article-title":"Cep164 is a mediator protein required for the maintenance of genomic stability through modulation of MDC1, RPA and CHK1","volume":"22","author":"Sivasubramaniam","year":"2008","journal-title":"Genes Dev."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.bbapap.2007.07.017","article-title":"Mammalian NDR protein kinases: From regulation to a role in centrosome duplication","volume":"1784","author":"Hergovich","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1016\/j.bbrc.2015.04.071","article-title":"NDR1 modulates the UV-induced DNA-damage checkpoint and nucleotide excision repair","volume":"461","author":"Park","year":"2015","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"5664","DOI":"10.1128\/MCB.25.13.5664-5674.2005","article-title":"Centrin 2 stimulates nucleotide excision repair by interacting with xeroderma pigmentosum group C protein","volume":"25","author":"Nishi","year":"2005","journal-title":"Mol. Cell. Biol."},{"key":"ref_165","first-page":"346","article-title":"Influence of centrin 2 on the interaction of nucleotide excision repair factors with damaged DNA","volume":"77","author":"Krasikova","year":"2012","journal-title":"Biochemistry"},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"21892","DOI":"10.1039\/D2RA03402F","article-title":"Phosphorylation promotes the endonuclease-like activity of human centrin 2","volume":"12","author":"Yang","year":"2022","journal-title":"RSC Adv."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"813","DOI":"10.1016\/j.dnarep.2010.04.005","article-title":"The oncogenic phosphatase WIP1 negatively regulates nucleotide excision repair","volume":"9","author":"Nguyen","year":"2010","journal-title":"DNA Repair"},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/j.molcel.2010.07.006","article-title":"SIRT1 regulates UV-induced DNA repair through deacetylating XPA","volume":"39","author":"Fan","year":"2010","journal-title":"Mol. Cell"},{"key":"ref_169","doi-asserted-by":"crossref","unstructured":"Alves-Fernandes, D.K., and Jasiulionis, M.G. (2019). The Role of SIRT1 on DNA Damage Response and Epigenetic Alterations in Cancer. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20133153"},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"1008","DOI":"10.1038\/nn.3460","article-title":"SIRT1 collaborates with ATM and HDAC1 to maintain genomic stability in neurons","volume":"16","author":"Dobbin","year":"2013","journal-title":"Nat. Neurosci."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1128\/MCB.00202-14","article-title":"The RASSF1A tumor suppressor regulates XPA-mediated DNA repair","volume":"35","author":"Donninger","year":"2015","journal-title":"Mol. Cell. Biol."},{"key":"ref_172","doi-asserted-by":"crossref","unstructured":"Garc\u00eda-Guti\u00e9rrez, L., McKenna, S., Kolch, W., and Matallanas, D. (2020). RASSF1A Tumour Suppressor: Target the Network for Effective Cancer Therapy. Cancers, 12.","DOI":"10.3390\/cancers12010229"},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"365213","DOI":"10.1155\/2012\/365213","article-title":"RASSF1 Polymorphisms in Cancer","volume":"2012","author":"Gordon","year":"2012","journal-title":"Mol. Biol. Int."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"962","DOI":"10.1038\/ncb3035","article-title":"RASSF1A-LATS1 signalling stabilizes replication forks by restricting CDK2-mediated phosphorylation of BRCA2","volume":"16","author":"Pefani","year":"2014","journal-title":"Nat. Cell Biol."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"1889","DOI":"10.1016\/j.cub.2008.10.060","article-title":"NDR kinase is activated by RASSF1A\/MST1 in response to Fas receptor stimulation and promotes apoptosis","volume":"18","author":"Vichalkovski","year":"2008","journal-title":"Curr. Biol."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"2010","DOI":"10.1016\/j.celrep.2017.08.016","article-title":"UV-Induced RPA1 Acetylation Promotes Nucleotide Excision Repair","volume":"20","author":"He","year":"2017","journal-title":"Cell Rep."},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"1997","DOI":"10.1016\/j.celrep.2017.08.015","article-title":"PCAF\/GCN5-mediated acetylation of RPA1 promotes nucleotide excision repair","volume":"20","author":"Zhao","year":"2017","journal-title":"Cell Rep."},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"22623","DOI":"10.1073\/pnas.1010377108","article-title":"Regulation of global genome nucleotide excision repair by SIRT1 through xeroderma pigmentosum C","volume":"107","author":"Ming","year":"2010","journal-title":"Proc. Natl. Acad. Sci USA"},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1038\/onc.2013.583","article-title":"Dual role of SIRT1 in UVB-induced skin tumorigenesis","volume":"34","author":"Ming","year":"2015","journal-title":"Oncogene"},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"22575","DOI":"10.18632\/oncotarget.4610","article-title":"Enhanced nucleotide excision repair capacity in lung cancer cells by preconditioning with DNA-damaging agents","volume":"6","author":"Choi","year":"2015","journal-title":"Oncotarget"},{"key":"ref_181","first-page":"5233","article-title":"Recent advances of SIRT1 and implications in chemotherapeutics resistance in cancer","volume":"11","author":"Yousafzai","year":"2021","journal-title":"Am. J. Cancer Res."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"321653","DOI":"10.1155\/2012\/321653","article-title":"Pleiotropic cellular functions of PARP1 in longevity and aging: Genome maintenance meets inflammation","volume":"2012","author":"Mangerich","year":"2012","journal-title":"Oxidative Med. Cell. Longev."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"1658","DOI":"10.1073\/pnas.1209507110","article-title":"Role of poly(ADP-ribose) polymerase-1 in the removal of UV-induced DNA lesions by nucleotide excision repair","volume":"110","author":"Robu","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1134\/S0026893316040038","article-title":"Poly(ADP-ribose) polymerase 1 as a key regulator of DNA repair","volume":"50","author":"Khodyreva","year":"2016","journal-title":"Mol. Biol."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"8129","DOI":"10.1093\/nar\/gkx565","article-title":"The role of poly ADP-ribosylation in the first wave of DNA damage response","volume":"45","author":"Liu","year":"2017","journal-title":"Nucleic Acids Res."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1134\/S0026893321020126","article-title":"Interactome of Base and Nucleotide Excision DNA Repair Systems","volume":"55","author":"Rechkunova","year":"2021","journal-title":"Mol. Biol."},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.1016\/j.mam.2012.12.005","article-title":"Reprogramming cellular events by poly(ADP-ribose)-binding proteins","volume":"34","author":"Krietsch","year":"2013","journal-title":"Mol. Asp. Med."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"4","DOI":"10.32607\/20758251-2017-9-2-4-16","article-title":"At the Interface of Three Nucleic Acids: The Role of RNA-Binding Proteins and Poly(ADP-ribose) in DNA Repair","volume":"9","author":"Alemasova","year":"2017","journal-title":"Acta Nat."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"19020","DOI":"10.1038\/srep19020","article-title":"Characterization of the interactions of PARP-1 with UV-damaged DNA in vivo and in vitro","volume":"6","author":"Purohit","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"E6847","DOI":"10.1073\/pnas.1706981114","article-title":"Poly(ADP-ribose) polymerase 1 escorts XPC to UV-induced DNA lesions during nucleotide excision repair","volume":"114","author":"Robu","year":"2017","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"590242","DOI":"10.3389\/fcell.2020.590242","article-title":"Methods to Study Intracellular Movement and Localization of the Nucleotide Excision Repair Proteins at the DNA Lesions in Mammalian Cells","volume":"8","author":"Robu","year":"2020","journal-title":"Front. Cell Dev. Biol."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"39824","DOI":"10.1074\/jbc.M112.393504","article-title":"Poly(ADP-ribose) contributes to an association between poly(ADP-ribose) polymerase-1 and xeroderma pigmentosum complementation group A in nucleotide excision repair","volume":"287","author":"King","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"3625","DOI":"10.1111\/febs.12885","article-title":"Poly(ADP-ribose)-mediated interplay of XPA and PARP1 leads to reciprocal regulation of protein function","volume":"281","author":"Fischer","year":"2014","journal-title":"FEBS J."},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"40974","DOI":"10.1074\/jbc.M006520200","article-title":"Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins","volume":"275","author":"Pleschke","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"e143","DOI":"10.1093\/nar\/gkm944","article-title":"Quantitative analysis of the binding affinity of poly(ADP-ribose) to specific binding proteins as a function of chain length","volume":"35","author":"Fahrer","year":"2007","journal-title":"Nucleic Acids Res."},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"1809","DOI":"10.1016\/j.celrep.2019.04.031","article-title":"PARP-1 Activation Directs FUS to DNA Damage Sites to Form PARG-Reversible Compartments Enriched in Damaged DNA","volume":"27","author":"Singatulina","year":"2019","journal-title":"Cell Rep."},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"873","DOI":"10.4161\/cc.5.8.2690","article-title":"Control of AIF-mediated cell death by the functional interplay of SIRT1 and PARP-1 in response to DNA damage","volume":"5","author":"Dantzer","year":"2006","journal-title":"Cell Cycle"},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"43121","DOI":"10.1074\/jbc.M506162200","article-title":"Poly(ADP-ribose) polymerase-1-dependent cardiac myocyte cell death during heart failure is mediated by NAD+ depletion and reduced Sir2alpha deacetylase activity","volume":"280","author":"Pillai","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1073\/pnas.0610590104","article-title":"Metabolic regulation of SIRT1 transcription via a HIC1:CtBP corepressor complex","volume":"104","author":"Zhang","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"4116","DOI":"10.1128\/MCB.00121-09","article-title":"SIRT1 promotes cell survival under stress by deacetylation-dependent deactivation of poly(ADP-ribose) polymerase 1","volume":"29","author":"Rajamohan","year":"2009","journal-title":"Mol. Cell. Biol."},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"882","DOI":"10.1016\/j.cell.2014.03.026","article-title":"Defective mitophagy in XPA via PARP-1 hyperactivation and NAD(+)\/SIRT1 reduction","volume":"157","author":"Fang","year":"2014","journal-title":"Cell"},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/j.dnarep.2018.09.010","article-title":"Replication protein A as a modulator of the poly(ADP-ribose)polymerase 1 activity","volume":"72","author":"Maltseva","year":"2018","journal-title":"DNA Repair"},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"7625","DOI":"10.1128\/MCB.25.17.7625-7636.2005","article-title":"Cooperation of the Cockayne syndrome group B protein and poly(ADP-ribose) polymerase 1 in the response to oxidative stress","volume":"25","author":"Thorslund","year":"2005","journal-title":"Mol. Cell. Biol."},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1083\/jcb.201112132","article-title":"PARP1 promotes nucleotide excision repair through DDB2 stabilization and recruitment of ALC1","volume":"199","author":"Pines","year":"2012","journal-title":"J. Cell Biol."},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"7925","DOI":"10.1007\/s00018-021-03984-7","article-title":"Nucleotide excision repair leaves a mark on chromatin: DNA damage detection in nucleosomes","volume":"78","author":"Apelt","year":"2021","journal-title":"Cell Mol. Life Sci."},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1038\/nrd1691","article-title":"Cellular processing of platinum anticancer drugs","volume":"4","author":"Wang","year":"2005","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/j.canlet.2014.01.005","article-title":"Nucleotide excision repair: Why is it not used to predict response to platinum-based chemotherapy?","volume":"346","author":"Bowden","year":"2014","journal-title":"Cancer Lett."},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"2313","DOI":"10.1002\/cncr.21031","article-title":"Expression of xeroderma pigmentosum A protein predicts improved outcome in metastatic ovarian carcinoma","volume":"103","author":"Stevens","year":"2005","journal-title":"Cancer"},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1002\/ijc.20134","article-title":"Reduced levels of XPA, ERCC1 and XPF DNA repair proteins in testis tumor cell lines","volume":"110","author":"Welsh","year":"2004","journal-title":"Int. J. Cancer"},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1038\/bjc.2013.303","article-title":"Association between ERCC1 and XPA expression and polymorphisms and the response to cisplatin in testicular germ cell tumours","volume":"109","author":"Mendoza","year":"2013","journal-title":"Br. J. Cancer"},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1124\/pr.116.013441","article-title":"Systems Chronotherapeutics","volume":"69","author":"Ballesta","year":"2017","journal-title":"Pharmacol. Rev."}],"container-title":["Cells"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2073-4409\/11\/23\/3723\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T01:24:31Z","timestamp":1760145871000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2073-4409\/11\/23\/3723"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,11,22]]},"references-count":211,"journal-issue":{"issue":"23","published-online":{"date-parts":[[2022,12]]}},"alternative-id":["cells11233723"],"URL":"https:\/\/doi.org\/10.3390\/cells11233723","relation":{},"ISSN":["2073-4409"],"issn-type":[{"value":"2073-4409","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,11,22]]}}}