{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,15]],"date-time":"2026-07-15T02:02:11Z","timestamp":1784080931875,"version":"3.55.0"},"reference-count":67,"publisher":"Oxford University Press (OUP)","issue":"4","license":[{"start":{"date-parts":[[2026,2,5]],"date-time":"2026-02-05T00:00:00Z","timestamp":1770249600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"funder":[{"name":"The Korean Institute for Basic Science","award":["IBS-R022-A1"],"award-info":[{"award-number":["IBS-R022-A1"]}]},{"DOI":"10.13039\/100000054","name":"National Cancer Institute","doi-asserted-by":"publisher","award":["P01 CA092584"],"award-info":[{"award-number":["P01 CA092584"]}],"id":[{"id":"10.13039\/100000054","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R35 GM118089"],"award-info":[{"award-number":["R35 GM118089"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000066","name":"National Institute of Environmental Health Sciences","doi-asserted-by":"publisher","award":["R01 ES032786"],"award-info":[{"award-number":["R01 ES032786"]}],"id":[{"id":"10.13039\/100000066","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003725","name":"National Research Foundation of Korea","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003725","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100009122","name":"Ministry of Education","doi-asserted-by":"publisher","award":["RS-2023-00274772"],"award-info":[{"award-number":["RS-2023-00274772"]}],"id":[{"id":"10.13039\/100009122","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,2,5]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Nucleotide excision repair (NER) is the key pathway for the removal of DNA damage induced by UV irradiation and chemotherapeutic reagents. Protein\u2013protein interactions are crucial for the dynamic and coordinated assembly of the proteins involved in DNA lesions. Here we focus on the role of interactions between the multi-subunit helicase\/translocase complex TFIIH and the 3\u2032 endonuclease XPG. We show that XPG interacts with the p62 and XPD subunits of TFIIH through its long spacer region bridging its split active site. We show that interactions between three acidic regions of XPG and the Pleckstrin homology (PH) domain of p62 are of moderate importance for NER, while defects in the interactions with XPD fail to pull-down TFIIH and strongly reduce NER activity. These p62 and XPD interface mutations additively reduce NER activity. Unexpectedly, we show that these interactions did not impair the recruitment of XPG but instead were defective in the formation of a catalytically competent NER complex and in triggering the incision 5\u2032 to the lesion by ERCC1\u2013XPF. Our studies provide fundamental insights into how interactions between TFIIH and XPG contribute to the NER pathway and, more generally, how modular protein\u2013protein interactions control each step along the NER reaction coordinate.<\/jats:p>","DOI":"10.1093\/nar\/gkag078","type":"journal-article","created":{"date-parts":[[2026,1,23]],"date-time":"2026-01-23T12:44:19Z","timestamp":1769172259000},"source":"Crossref","is-referenced-by-count":2,"title":["The interaction of XPG with TFIIH through p62 and XPD is required for the completion of nucleotide excision repair"],"prefix":"10.1093","volume":"54","author":[{"given":"Mihyun","family":"Kim","sequence":"first","affiliation":[{"name":"Center for Genomic Integrity, Institute for Basic Science , Ulsan ,","place":["Republic of Korea"]},{"name":"Department of Biological Sciences, College of Information-Bio Convergence Engineering, Ulsan National Institute of Science and Technology , Ulsan ,","place":["Republic of Korea"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eunwoo","family":"Jeong","sequence":"additional","affiliation":[{"name":"Center for Genomic Integrity, Institute for Basic Science , Ulsan ,","place":["Republic of Korea"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jiyoung","family":"Park","sequence":"additional","affiliation":[{"name":"Center for Genomic Integrity, Institute for Basic Science , Ulsan ,","place":["Republic of Korea"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Areetha","family":"D\u2019Souza","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Vanderbilt University , Nashville, TN 37240-7917 ,","place":["United States"]},{"name":"Center for Structural Biology, Vanderbilt University , Nashville, TN 37240-7917 ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Miaw-Sheue","family":"Tsai","sequence":"additional","affiliation":[{"name":"Biological Systems and Engineering Division, Lawrence Berkeley National Laboratory , Berkeley, CA ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chunli","family":"Yan","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Georgia State University , Atlanta, GA ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5306-1005","authenticated-orcid":false,"given":"Ivaylo","family":"Ivanov","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Georgia State University , Atlanta, GA ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Walter J","family":"Chazin","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Vanderbilt University , Nashville, TN 37240-7917 ,","place":["United States"]},{"name":"Center for Structural Biology, Vanderbilt University , Nashville, TN 37240-7917 ,","place":["United States"]},{"name":"Department of Chemistry, Vanderbilt University , Nashville, TN 37232-7917 ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hyun Suk","family":"Kim","sequence":"additional","affiliation":[{"name":"Center for Genomic Integrity, Institute for Basic Science , Ulsan ,","place":["Republic of Korea"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2425-2715","authenticated-orcid":false,"given":"Orlando D","family":"Sch\u00e4rer","sequence":"additional","affiliation":[{"name":"Center for Genomic Integrity, Institute for Basic Science , Ulsan ,","place":["Republic of Korea"]},{"name":"Department of Biological Sciences, College of Information-Bio Convergence Engineering, Ulsan National Institute of Science and Technology , Ulsan ,","place":["Republic of Korea"]},{"name":"Graduate School of Health Science and Technology, College of Information-Bio Convergence Engineering, Ulsan National Institute of Science and Technology , Ulsan ,","place":["Republic of Korea"]},{"name":"UPMC Hillman Cancer Center & Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine , Pittsburgh, PA 15213-1863 ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2026,2,5]]},"reference":[{"key":"2026020505452439500_B1","doi-asserted-by":"publisher","first-page":"465","DOI":"10.1038\/nrm3822","article-title":"Understanding nucleotide excision repair and its roles in cancer and ageing","volume":"15","author":"Marteijn","year":"2014","journal-title":"Nat Rev Mol Cell Biol"},{"key":"2026020505452439500_B2","doi-asserted-by":"publisher","first-page":"a012609","DOI":"10.1101\/cshperspect.a012609","article-title":"Nucleotide excision repair in eukaryotes","volume":"5","author":"Sch\u00e4rer","year":"2013","journal-title":"Cold Spring Harb Perspect Biol"},{"key":"2026020505452439500_B3","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1016\/S1097-2765(01)00281-7","article-title":"Sequential assembly of the nucleotide excision repair factors in vivo","volume":"8","author":"Volker","year":"2001","journal-title":"Mol Cell"},{"key":"2026020505452439500_B4","doi-asserted-by":"publisher","first-page":"223","DOI":"10.1016\/S1097-2765(00)80132-X","article-title":"Xeroderma pigmentosum group C protein complex is the initiator of global genome nucleotide excision repair","volume":"2","author":"Sugasawa","year":"1998","journal-title":"Mol Cell"},{"key":"2026020505452439500_B5","doi-asserted-by":"publisher","first-page":"595","DOI":"10.1038\/s41556-021-00688-9","article-title":"ELOF1 is a transcription-coupled DNA repair factor that directs RNA polymerase II ubiquitylation","volume":"23","author":"van\u00a0der\u00a0Weegen","year":"2021","journal-title":"Nat Cell Biol"},{"key":"2026020505452439500_B6","doi-asserted-by":"publisher","first-page":"2104","DOI":"10.1038\/s41467-020-15903-8","article-title":"The cooperative action of CSB, CSA, and UVSSA target TFIIH to DNA damage-stalled RNA polymerase II","volume":"11","author":"van\u00a0der\u00a0Weegen","year":"2020","journal-title":"Nat Commun"},{"key":"2026020505452439500_B7","doi-asserted-by":"publisher","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":"2026020505452439500_B8","doi-asserted-by":"publisher","first-page":"586","DOI":"10.1038\/ng.2229","article-title":"Mutations in UVSSA cause UV-sensitive syndrome and impair RNA polymerase IIo processing in transcription-coupled nucleotide-excision repair","volume":"44","author":"Nakazawa","year":"2012","journal-title":"Nat Genet"},{"key":"2026020505452439500_B9","doi-asserted-by":"publisher","first-page":"608","DOI":"10.1038\/s41556-021-00692-z","article-title":"Elongation factor ELOF1 drives transcription-coupled repair and prevents genome instability","volume":"23","author":"Geijer","year":"2021","journal-title":"Nat Cell Biol"},{"key":"2026020505452439500_B10","doi-asserted-by":"publisher","first-page":"7091","DOI":"10.1016\/j.cell.2024.10.020","article-title":"STK19 positions TFIIH for cell-free transcription-coupled DNA repair","volume":"187","author":"Mevissen","year":"2024","journal-title":"Cell"},{"key":"2026020505452439500_B11","doi-asserted-by":"publisher","first-page":"4740","DOI":"10.1016\/j.molcel.2024.10.030","article-title":"STK19 drives transcription-coupled repair by stimulating repair complex stability, RNA Pol II ubiquitylation, and TFIIH recruitment","volume":"84","author":"Ramadhin","year":"2024","journal-title":"Mol Cell"},{"key":"2026020505452439500_B12","doi-asserted-by":"publisher","first-page":"12767","DOI":"10.1093\/nar\/gkae787","article-title":"STK19 is a transcription-coupled repair factor that participates in UVSSA ubiquitination and TFIIH loading","volume":"52","author":"Tan","year":"2024","journal-title":"Nucleic Acids Res"},{"key":"2026020505452439500_B13","doi-asserted-by":"publisher","first-page":"7107","DOI":"10.1016\/j.cell.2024.10.018","article-title":"STK19 facilitates the clearance of lesion-stalled RNAPII during transcription-coupled DNA repair","volume":"187","author":"van\u00a0den\u00a0Heuvel","year":"2024","journal-title":"Cell"},{"key":"2026020505452439500_B14","doi-asserted-by":"publisher","first-page":"6559","DOI":"10.1093\/emboj\/16.21.6559","article-title":"Mechanism of open complex and dual incision formation by human nucleotide excision repair factors","volume":"16","author":"Evans","year":"1997","journal-title":"EMBO J"},{"key":"2026020505452439500_B15","doi-asserted-by":"publisher","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":"2026020505452439500_B16","doi-asserted-by":"publisher","first-page":"17545","DOI":"10.1073\/pnas.1004339107","article-title":"Strand- and site-specific DNA lesion demarcation by the xeroderma pigmentosum group D helicase","volume":"107","author":"Mathieu","year":"2010","journal-title":"Proc Natl Acad Sci USA"},{"key":"2026020505452439500_B17","doi-asserted-by":"publisher","first-page":"9","DOI":"10.1016\/j.molcel.2008.04.024","article-title":"Nucleotide excision repair driven by the dissociation of CAK from TFIIH","volume":"31","author":"Coin","year":"2008","journal-title":"Mol Cell"},{"key":"2026020505452439500_B18","doi-asserted-by":"publisher","first-page":"2971","DOI":"10.1038\/emboj.2009.230","article-title":"Molecular insights into the recruitment of TFIIH to sites of DNA damage","volume":"28","author":"Oksenych","year":"2009","journal-title":"EMBO J"},{"key":"2026020505452439500_B19","doi-asserted-by":"publisher","first-page":"1580","DOI":"10.1038\/s41594-024-01323-5","article-title":"XPD stalled on cross-linked DNA provides insight into damage verification","volume":"31","author":"Kuper","year":"2024","journal-title":"Nat Struct Mol Biol"},{"key":"2026020505452439500_B20","doi-asserted-by":"publisher","first-page":"6669","DOI":"10.1073\/pnas.95.12.6669","article-title":"Assembly, subunit composition, and footprint of human DNA repair excision nuclease","volume":"95","author":"Wakasugi","year":"1998","journal-title":"Proc Natl Acad Sci USA"},{"key":"2026020505452439500_B21","doi-asserted-by":"publisher","first-page":"349","DOI":"10.1101\/gad.14.3.349","article-title":"Nucleotide excision repair of DNA with recombinant human proteins: definition of the minimal set of factors, active forms of TFIIH, and modulation by CAK","volume":"14","author":"Araujo","year":"2000","journal-title":"Genes Dev"},{"key":"2026020505452439500_B22","doi-asserted-by":"publisher","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":"2026020505452439500_B23","doi-asserted-by":"publisher","first-page":"714","DOI":"10.1016\/j.molcel.2010.02.009","article-title":"Three DNA polymerases, recruited by different mechanisms, carry out NER repair synthesis in human cells","volume":"37","author":"Ogi","year":"2010","journal-title":"Mol Cell"},{"key":"2026020505452439500_B24","doi-asserted-by":"publisher","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":"2026020505452439500_B25","doi-asserted-by":"publisher","first-page":"103728","DOI":"10.1016\/j.dnarep.2024.103728","article-title":"Protein\u2013protein interactions in the core nucleotide excision repair pathway","volume":"141","author":"D'Souza","year":"2024","journal-title":"DNA Repair (Amst)"},{"key":"2026020505452439500_B26","doi-asserted-by":"publisher","first-page":"170","DOI":"10.1038\/s41586-023-05959-z","article-title":"Lesion recognition by XPC, TFIIH and XPA in DNA excision repair","volume":"617","author":"Kim","year":"2023","journal-title":"Nature"},{"key":"2026020505452439500_B27","doi-asserted-by":"publisher","first-page":"9870","DOI":"10.1074\/jbc.275.13.9870","article-title":"The xeroderma pigmentosum group C protein complex XPC\u2013HR23B plays an important role in the recruitment of transcription factor IIH to damaged DNA","volume":"275","author":"Yokoi","year":"2000","journal-title":"J Biol Chem"},{"key":"2026020505452439500_B28","doi-asserted-by":"publisher","first-page":"13043","DOI":"10.1093\/nar\/gkx970","article-title":"Common TFIIH recruitment mechanism in global genome and transcription-coupled repair subpathways","volume":"45","author":"Okuda","year":"2017","journal-title":"Nucleic Acids Res"},{"key":"2026020505452439500_B29","doi-asserted-by":"publisher","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":"2026020505452439500_B30","doi-asserted-by":"publisher","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":"2026020505452439500_B31","doi-asserted-by":"publisher","first-page":"2173","DOI":"10.1093\/nar\/gkz1231","article-title":"A key interaction with RPA orients XPA in NER complexes","volume":"48","author":"Topolska-Wos","year":"2020","journal-title":"Nucleic Acids Res"},{"key":"2026020505452439500_B32","doi-asserted-by":"publisher","first-page":"449","DOI":"10.1016\/S0092-8674(00)00136-7","article-title":"Structural basis for the recognition of DNA repair proteins UNG2, XPA, and RAD52 by replication factor RPA","volume":"103","author":"Mer","year":"2000","journal-title":"Cell"},{"key":"2026020505452439500_B33","doi-asserted-by":"publisher","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":"2026020505452439500_B34","doi-asserted-by":"publisher","first-page":"3705","DOI":"10.1074\/jbc.M109.067538","article-title":"The XPA-binding domain of ERCC1 is required for nucleotide excision repair but not other DNA repair pathways","volume":"285","author":"Orelli","year":"2010","journal-title":"J Biol Chem"},{"key":"2026020505452439500_B35","doi-asserted-by":"publisher","first-page":"4768","DOI":"10.1038\/sj.emboj.7601894","article-title":"Structural basis for the recruitment of ERCC1\u2013XPF to nucleotide excision repair complexes by XPA","volume":"26","author":"Tsodikov","year":"2007","journal-title":"EMBO J"},{"key":"2026020505452439500_B36","doi-asserted-by":"publisher","first-page":"5789","DOI":"10.1093\/nar\/gkm503","article-title":"Analysis of the XPA and ssDNA-binding surfaces on the central domain of human ERCC1 reveals evidence for subfunctionalization","volume":"35","author":"Tripsianes","year":"2007","journal-title":"Nucleic Acids Res"},{"key":"2026020505452439500_B37","doi-asserted-by":"publisher","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":"Araujo","year":"2001","journal-title":"Mol Cell Biol"},{"key":"2026020505452439500_B38","doi-asserted-by":"publisher","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":"2026020505452439500_B39","doi-asserted-by":"publisher","first-page":"8868","DOI":"10.1128\/MCB.00695-06","article-title":"Recruitment of the nucleotide excision repair endonuclease XPG to sites of UV-induced DNA damage depends on functional TFIIH","volume":"26","author":"Zotter","year":"2006","journal-title":"Mol Cell Biol"},{"key":"2026020505452439500_B40","doi-asserted-by":"publisher","first-page":"1019","DOI":"10.1038\/emboj.2009.230","article-title":"A scanning-to-incision switch in TFIIH\u2013XPG induced by DNA damage licenses nucleotide excision repair","volume":"51","author":"Brali\u0107","year":"2023","journal-title":"Nucleic Acids Res"},{"key":"2026020505452439500_B41","doi-asserted-by":"publisher","first-page":"182","DOI":"10.1038\/363182a0","article-title":"Complementation of the DNA repair defect in xeroderma pigmentosum group G cells by a human cDNA related to yeast RAD2","volume":"363","author":"Scherly","year":"1993","journal-title":"Nature"},{"key":"2026020505452439500_B42","doi-asserted-by":"publisher","first-page":"7030","DOI":"10.1074\/jbc.M412228200","article-title":"The spacer region of XPG mediates recruitment to nucleotide excision repair complexes and determines substrate specificity","volume":"280","author":"Dunand-Sauthier","year":"2005","journal-title":"J Biol Chem"},{"key":"2026020505452439500_B43","doi-asserted-by":"publisher","first-page":"10670","DOI":"10.1128\/MCB.24.24.10670-10680.2004","article-title":"Definition of a short region of XPG necessary for TFIIH interaction and stable recruitment to sites of UV damage","volume":"24","author":"Thorel","year":"2004","journal-title":"Mol Cell Biol"},{"key":"2026020505452439500_B44","doi-asserted-by":"publisher","first-page":"616","DOI":"10.1038\/nsmb782","article-title":"TFIIH contains a PH domain involved in DNA nucleotide excision repair","volume":"11","author":"Gervais","year":"2004","journal-title":"Nat Struct Mol Biol"},{"key":"2026020505452439500_B45","doi-asserted-by":"publisher","first-page":"2736","DOI":"10.1093\/nar\/gks1321","article-title":"Structural and functional evidence that Rad4 competes with Rad2 for binding to the Tfb1 subunit of TFIIH in NER","volume":"41","author":"Lafrance-Vanasse","year":"2013","journal-title":"Nucleic Acids Res"},{"key":"2026020505452439500_B46","doi-asserted-by":"publisher","first-page":"6333","DOI":"10.1093\/nar\/gkae286","article-title":"Interplay of the Tfb1 pleckstrin homology domain with Rad2 and Rad4 in transcription coupled and global genomic nucleotide excision repair","volume":"52","author":"Gong","year":"2024","journal-title":"Nucleic Acids Res"},{"key":"2026020505452439500_B47","doi-asserted-by":"publisher","first-page":"5739","DOI":"10.1093\/nar\/gks194","article-title":"Structural and functional characterization of interactions involving the Tfb1 subunit of TFIIH and the NER factor Rad2","volume":"40","author":"Lafrance-Vanasse","year":"2012","journal-title":"Nucleic Acids Res"},{"key":"2026020505452439500_B48","doi-asserted-by":"publisher","first-page":"1827","DOI":"10.1016\/j.str.2015.07.009","article-title":"Structural insight into the mechanism of TFIIH recognition by the acidic string of the nucleotide excision repair factor XPC","volume":"23","author":"Okuda","year":"2015","journal-title":"Structure"},{"key":"2026020505452439500_B49","doi-asserted-by":"publisher","first-page":"8511","DOI":"10.1038\/s41467-024-52860-y","article-title":"Molecular architecture and functional dynamics of the pre-incision complex in nucleotide excision repair","volume":"15","author":"Yu","year":"2024","journal-title":"Nat Commun"},{"key":"2026020505452439500_B50","doi-asserted-by":"publisher","first-page":"19500","DOI":"10.1074\/jbc.M213155200","article-title":"Structural determinants for substrate binding and catalysis by the structure-specific endonuclease XPG","volume":"278","author":"Hohl","year":"2003","journal-title":"J Biol Chem"},{"key":"2026020505452439500_B51","doi-asserted-by":"publisher","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly accurate protein structure prediction with AlphaFold","volume":"596","author":"Jumper","year":"2021","journal-title":"Nature"},{"key":"2026020505452439500_B52","doi-asserted-by":"publisher","first-page":"Unit 4.21","DOI":"10.1002\/0471142301.ns0421s37","article-title":"Production and titration of lentiviral vectors","volume":"Chapter 4","author":"Salmon","year":"2006","journal-title":"Curr Protoc Neurosci"},{"key":"2026020505452439500_B53","doi-asserted-by":"publisher","first-page":"1388","DOI":"10.1038\/s41467-024-45664-7","article-title":"Trabectedin derails transcription-coupled nucleotide excision repair to induce DNA breaks in highly transcribed genes","volume":"15","author":"Son","year":"2024","journal-title":"Nat Commun"},{"key":"2026020505452439500_B54","doi-asserted-by":"publisher","first-page":"8337","DOI":"10.1093\/nar\/gkz629","article-title":"Single-molecule visualization reveals the damage search mechanism for the human NER protein XPC\u2013RAD23B","volume":"47","author":"Cheon","year":"2019","journal-title":"Nucleic Acids Res"},{"key":"2026020505452439500_B55","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/bs.mie.2017.03.008.","article-title":"MacroBac: new technologies for robust and efficient large-scale production of recombinant multiprotein complexes","volume":"592","author":"Gradia","year":"2017","journal-title":"Methods Enzymol"},{"key":"2026020505452439500_B56","doi-asserted-by":"publisher","first-page":"6346","DOI":"10.1021\/ja9013634","article-title":"NMR analysis of the architecture and functional remodeling of a modular multidomain protein, RPA","volume":"131","author":"Brosey","year":"2009","journal-title":"J Am Chem Soc"},{"key":"2026020505452439500_B57","doi-asserted-by":"publisher","first-page":"2045","DOI":"10.1093\/emboj\/21.8.2045","article-title":"The active site of the DNA repair endonuclease XPF\u2013ERCC1 forms a highly conserved nuclease motif","volume":"21","author":"Enzlin","year":"2002","journal-title":"EMBO J"},{"key":"2026020505452439500_B58","doi-asserted-by":"publisher","first-page":"W122","DOI":"10.1093\/nar\/gkad472","article-title":"DDMut: predicting effects of mutations on protein stability using deep learning","volume":"51","author":"Zhou","year":"2023","journal-title":"Nucleic Acids Res"},{"key":"2026020505452439500_B59","doi-asserted-by":"publisher","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":"2026020505452439500_B60","doi-asserted-by":"publisher","first-page":"21846","DOI":"10.1074\/jbc.M111.337899","article-title":"Multiple DNA binding domains mediate the function of the ERCC1\u2013XPF protein in nucleotide excision repair","volume":"287","author":"Su","year":"2012","journal-title":"J Biol Chem"},{"key":"2026020505452439500_B61","doi-asserted-by":"publisher","first-page":"16030","DOI":"10.1074\/jbc.272.25.16030","article-title":"The non-catalytic function of XPG protein during dual incision in human nucleotide excision repair","volume":"272","author":"Wakasugi","year":"1997","journal-title":"J Biol Chem"},{"key":"2026020505452439500_B62","doi-asserted-by":"publisher","first-page":"5637","DOI":"10.1074\/jbc.274.9.5637","article-title":"Conserved residues of human XPG protein important for nuclease activity and function in nucleotide excision repair","volume":"274","author":"Constantinou","year":"1999","journal-title":"J Biol Chem"},{"key":"2026020505452439500_B63","doi-asserted-by":"publisher","first-page":"e13","DOI":"10.1093\/nar\/gkz1077","article-title":"Sensitive CometChip assay for screening potentially carcinogenic DNA adducts by trapping DNA repair intermediates","volume":"48","author":"Ngo","year":"2020","journal-title":"Nucleic Acids Res"},{"key":"2026020505452439500_B64","doi-asserted-by":"publisher","first-page":"2298","DOI":"10.1093\/carcin\/bgm157","article-title":"H2AX phosphorylation after UV irradiation is triggered by DNA repair intermediates and is mediated by the ATR kinase","volume":"28","author":"Hanasoge","year":"2007","journal-title":"Carcinogenesis"},{"key":"2026020505452439500_B65","doi-asserted-by":"publisher","first-page":"1104","DOI":"10.1242\/jcs.03391","article-title":"Perturbed gap-filling synthesis in nucleotide excision repair causes histone H2AX phosphorylation in human quiescent cells","volume":"120","author":"Matsumoto","year":"2007","journal-title":"J Cell Sci"},{"key":"2026020505452439500_B66","doi-asserted-by":"publisher","first-page":"198","DOI":"10.1016\/j.cell.2011.03.004","article-title":"Human flap endonuclease structures, DNA double-base flipping, and a unified understanding of the FEN1 superfamily","volume":"145","author":"Tsutakawa","year":"2011","journal-title":"Cell"},{"key":"2026020505452439500_B67","doi-asserted-by":"publisher","first-page":"30915","DOI":"10.1074\/jbc.R400015200","article-title":"Structural mechanisms of DNA replication, repair, and recombination","volume":"279","author":"Stauffer","year":"2004","journal-title":"J Biol Chem"}],"container-title":["Nucleic Acids Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/academic.oup.com\/nar\/article-pdf\/54\/4\/gkag078\/66773735\/gkag078.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/nar\/article-pdf\/54\/4\/gkag078\/66773735\/gkag078.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,2,5]],"date-time":"2026-02-05T10:45:36Z","timestamp":1770288336000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/nar\/article\/doi\/10.1093\/nar\/gkag078\/8462615"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,2,5]]},"references-count":67,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2026,2,5]]}},"URL":"https:\/\/doi.org\/10.1093\/nar\/gkag078","relation":{},"ISSN":["0305-1048","1362-4962"],"issn-type":[{"value":"0305-1048","type":"print"},{"value":"1362-4962","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2026,2,27]]},"published":{"date-parts":[[2026,2,5]]},"article-number":"gkag078"}}