{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T09:04:05Z","timestamp":1790672645696,"version":"4.1.0"},"reference-count":77,"publisher":"National Academy of Sciences","issue":"25","license":[{"start":{"date-parts":[[2020,6,10]],"date-time":"2020-06-10T00:00:00Z","timestamp":1591747200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000054","name":"HHS | NIH | National Cancer Institute","doi-asserted-by":"publisher","award":["CA092584"],"award-info":[{"award-number":["CA092584"]}],"id":[{"id":"10.13039\/100000054","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000054","name":"HHS | NIH | National Cancer Institute","doi-asserted-by":"publisher","award":["R35CA22043"],"award-info":[{"award-number":["R35CA22043"]}],"id":[{"id":"10.13039\/100000054","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"HHS | NIH | National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["RO1GM110387"],"award-info":[{"award-number":["RO1GM110387"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"HHS | NIH | National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["PO1AG017242"],"award-info":[{"award-number":["PO1AG017242"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000066","name":"HHS | NIH | National Institute of Environmental Health Sciences","doi-asserted-by":"publisher","award":["RO1ES019935"],"award-info":[{"award-number":["RO1ES019935"]}],"id":[{"id":"10.13039\/100000066","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000066","name":"HHS | NIH | National Institute of Environmental Health Sciences","doi-asserted-by":"publisher","award":["Ro1ES013773"],"award-info":[{"award-number":["Ro1ES013773"]}],"id":[{"id":"10.13039\/100000066","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"HHS | NIH | National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["GM31819"],"award-info":[{"award-number":["GM31819"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"HHS | NIH | National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["T32AG000266"],"award-info":[{"award-number":["T32AG000266"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"HHS | NIH | National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["P30 GM124169"],"award-info":[{"award-number":["P30 GM124169"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003422","name":"Global Collaborative Research, King Abdullah University of Science and Technology","doi-asserted-by":"publisher","award":["CRG3"],"award-info":[{"award-number":["CRG3"]}],"id":[{"id":"10.13039\/501100003422","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2020,6,23]]},"abstract":"<jats:p>\n                    Xeroderma pigmentosum group G (XPG) protein is both a functional partner in multiple DNA damage responses (DDR) and a pathway coordinator and structure-specific endonuclease in nucleotide excision repair (NER). Different mutations in the XPG gene\n                    <jats:italic>ERCC5<\/jats:italic>\n                    lead to either of two distinct human diseases: Cancer-prone xeroderma pigmentosum (XP-G) or the fatal neurodevelopmental disorder Cockayne syndrome (XP-G\/CS). To address the enigmatic structural mechanism for these differing disease phenotypes and for XPG\u2019s role in multiple DDRs, here we determined the crystal structure of human XPG catalytic domain (XPGcat), revealing XPG-specific features for its activities and regulation. Furthermore, XPG DNA binding elements conserved with FEN1 superfamily members enable insights on DNA interactions. Notably, all but one of the known pathogenic point mutations map to XPGcat, and both XP-G and XP-G\/CS mutations destabilize XPG and reduce its cellular protein levels. Mapping the distinct mutation classes provides structure-based predictions for disease phenotypes: Residues mutated in XP-G are positioned to reduce local stability and NER activity, whereas residues mutated in XP-G\/CS have implied long-range structural defects that would likely disrupt stability of the whole protein, and thus interfere with its functional interactions. Combined data from crystallography, biochemistry, small angle X-ray scattering, and electron microscopy unveil an XPG homodimer that binds, unstacks, and sculpts duplex DNA at internal unpaired regions (bubbles) into strongly bent structures, and suggest how XPG complexes may bind both NER bubble junctions and replication forks. Collective results support XPG scaffolding and DNA sculpting functions in multiple DDR processes to maintain genome stability.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1921311117","type":"journal-article","created":{"date-parts":[[2020,6,10]],"date-time":"2020-06-10T20:15:42Z","timestamp":1591820142000},"page":"14127-14138","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":61,"title":["Human XPG nuclease structure, assembly, and activities with insights for neurodegeneration and cancer from pathogenic mutations"],"prefix":"10.1073","volume":"117","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4918-4571","authenticated-orcid":false,"given":"Susan E.","family":"Tsutakawa","sequence":"first","affiliation":[{"name":"Molecular Biophysics and Integrated Bioimaging, Lawrence Berkeley National Laboratory, Berkeley, CA 94720;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6868-8460","authenticated-orcid":false,"given":"Altaf H.","family":"Sarker","sequence":"additional","affiliation":[{"name":"Biological Systems and Engineering, Lawrence Berkeley National Laboratory, Berkeley, CA 94720;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8581-7938","authenticated-orcid":false,"given":"Clifford","family":"Ng","sequence":"additional","affiliation":[{"name":"Biological Systems and Engineering, Lawrence Berkeley National Laboratory, Berkeley, CA 94720;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrew S.","family":"Arvai","sequence":"additional","affiliation":[{"name":"Integrative Structural &amp; Computational Biology, The Scripps Research Institute, La Jolla, CA 92037;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David S.","family":"Shin","sequence":"additional","affiliation":[{"name":"Molecular Biophysics and Integrated Bioimaging, Lawrence Berkeley National Laboratory, Berkeley, CA 94720;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brian","family":"Shih","sequence":"additional","affiliation":[{"name":"Biological Systems and Engineering, Lawrence Berkeley National Laboratory, Berkeley, CA 94720;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shuai","family":"Jiang","sequence":"additional","affiliation":[{"name":"Biological Systems and Engineering, Lawrence Berkeley National Laboratory, Berkeley, CA 94720;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aye C.","family":"Thwin","sequence":"additional","affiliation":[{"name":"Biological Systems and Engineering, Lawrence Berkeley National Laboratory, Berkeley, CA 94720;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Miaw-Sheue","family":"Tsai","sequence":"additional","affiliation":[{"name":"Biological Systems and Engineering, Lawrence Berkeley National Laboratory, Berkeley, CA 94720;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexandra","family":"Willcox","sequence":"additional","affiliation":[{"name":"Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, NC 27599"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mai Zong","family":"Her","sequence":"additional","affiliation":[{"name":"Molecular Biophysics and Integrated Bioimaging, Lawrence Berkeley National Laboratory, Berkeley, CA 94720;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kelly S.","family":"Trego","sequence":"additional","affiliation":[{"name":"Biological Systems and Engineering, Lawrence Berkeley National Laboratory, Berkeley, CA 94720;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alan G.","family":"Raetz","sequence":"additional","affiliation":[{"name":"Biological Systems and Engineering, Lawrence Berkeley National Laboratory, Berkeley, CA 94720;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8017-8156","authenticated-orcid":false,"given":"Daniel","family":"Rosenberg","sequence":"additional","affiliation":[{"name":"Molecular Biophysics and Integrated Bioimaging, Lawrence Berkeley National Laboratory, Berkeley, CA 94720;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0206-8423","authenticated-orcid":false,"given":"Albino","family":"Bacolla","sequence":"additional","affiliation":[{"name":"Department of Cancer Biology, University of Texas MD Anderson Cancer Center, Houston, TX 77030;"},{"name":"Department of Molecular and Cellular Oncology, University of Texas MD Anderson Cancer Center, Houston, TX 77030"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5610-9289","authenticated-orcid":false,"given":"Michal","family":"Hammel","sequence":"additional","affiliation":[{"name":"Molecular Biophysics and Integrated Bioimaging, Lawrence Berkeley National Laboratory, Berkeley, CA 94720;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jack D.","family":"Griffith","sequence":"additional","affiliation":[{"name":"Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, NC 27599"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3563-3647","authenticated-orcid":false,"given":"Priscilla K.","family":"Cooper","sequence":"additional","affiliation":[{"name":"Biological Systems and Engineering, Lawrence Berkeley National Laboratory, Berkeley, CA 94720;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1659-2429","authenticated-orcid":false,"given":"John A.","family":"Tainer","sequence":"additional","affiliation":[{"name":"Molecular Biophysics and Integrated Bioimaging, Lawrence Berkeley National Laboratory, Berkeley, CA 94720;"},{"name":"Department of Cancer Biology, University of Texas MD Anderson Cancer Center, Houston, TX 77030;"},{"name":"Department of Molecular and Cellular Oncology, University of Texas MD Anderson Cancer Center, Houston, TX 77030"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2020,6,10]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1038\/371432a0","article-title":"XPG endonuclease makes the 3\u2032 incision in human DNA nucleotide excision repair","volume":"371","author":"O\u2019Donovan A.","year":"1994","unstructured":"A. O\u2019Donovan, A. A. Davies, J. G. Moggs, S. C. West, R. D. Wood, XPG endonuclease makes the 3\u2032 incision in human DNA nucleotide excision repair. Nature 371, 432\u2013435 (1994).","journal-title":"Nature"},{"key":"e_1_3_4_2_2","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 G.","year":"2019","unstructured":"G. Kokic ., Structural basis of TFIIH activation for nucleotide excision repair. Nat. Commun. 10, 2885 (2019).","journal-title":"Nat. Commun."},{"key":"e_1_3_4_3_2","doi-asserted-by":"crossref","first-page":"2157","DOI":"10.1021\/bi9524124","article-title":"Interactions involving the human RNA polymerase II transcription\/nucleotide excision repair complex TFIIH, the nucleotide excision repair protein XPG, and Cockayne syndrome group B (CSB) protein","volume":"35","author":"Iyer N.","year":"1996","unstructured":"N. Iyer, M. S. Reagan, K. J. Wu, B. Canagarajah, E. C. Friedberg, Interactions involving the human RNA polymerase II transcription\/nucleotide excision repair complex TFIIH, the nucleotide excision repair protein XPG, and Cockayne syndrome group B (CSB) protein. Biochemistry 35, 2157\u20132167 (1996).","journal-title":"Biochemistry"},{"key":"e_1_3_4_4_2","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/j.molcel.2005.09.022","article-title":"Recognition of RNA polymerase II and transcription bubbles by XPG, CSB, and TFIIH: Insights for transcription-coupled repair and Cockayne syndrome","volume":"20","author":"Sarker A. H.","year":"2005","unstructured":"A. H. Sarker ., Recognition of RNA polymerase II and transcription bubbles by XPG, CSB, and TFIIH: Insights for transcription-coupled repair and Cockayne syndrome. Mol. Cell 20, 187\u2013198 (2005).","journal-title":"Mol. Cell"},{"key":"e_1_3_4_5_2","doi-asserted-by":"crossref","first-page":"24522","DOI":"10.1074\/jbc.272.39.24522","article-title":"The DNA repair endonuclease XPG binds to proliferating cell nuclear antigen (PCNA) and shares sequence elements with the PCNA-binding regions of FEN-1 and cyclin-dependent kinase inhibitor p21","volume":"272","author":"Gary R.","year":"1997","unstructured":"R. Gary, D. L. Ludwig, H. L. Cornelius, M. A. MacInnes, M. S. Park, The DNA repair endonuclease XPG binds to proliferating cell nuclear antigen (PCNA) and shares sequence elements with the PCNA-binding regions of FEN-1 and cyclin-dependent kinase inhibitor p21. J. Biol. Chem. 272, 24522\u201324529 (1997).","journal-title":"J. Biol. Chem."},{"key":"e_1_3_4_6_2","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 L.","year":"2009","unstructured":"L. Staresincic ., Coordination of dual incision and repair synthesis in human nucleotide excision repair. EMBO J. 28, 1111\u20131120 (2009).","journal-title":"EMBO J."},{"key":"e_1_3_4_7_2","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1038\/nrm3822","article-title":"Understanding nucleotide excision repair and its roles in cancer and ageing","volume":"15","author":"Marteijn J. A.","year":"2014","unstructured":"J. A. Marteijn, H. Lans, W. Vermeulen, J. H. Hoeijmakers, Understanding nucleotide excision repair and its roles in cancer and ageing. Nat. Rev. Mol. Cell Biol. 15, 465\u2013481 (2014).","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"e_1_3_4_8_2","doi-asserted-by":"crossref","first-page":"e1004686","DOI":"10.1371\/journal.pgen.1004686","article-title":"Cell-autonomous progeroid changes in conditional mouse models for repair endonuclease XPG deficiency","volume":"10","author":"Barnhoorn S.","year":"2014","unstructured":"S. Barnhoorn ., Cell-autonomous progeroid changes in conditional mouse models for repair endonuclease XPG deficiency. PLoS Genet. 10, e1004686 (2014).","journal-title":"PLoS Genet."},{"key":"e_1_3_4_9_2","doi-asserted-by":"crossref","first-page":"2757","DOI":"10.1016\/j.febslet.2007.05.014","article-title":"DNA photodamage recognition by RNA polymerase II","volume":"581","author":"Brueckner F.","year":"2007","unstructured":"F. Brueckner, P. Cramer, DNA photodamage recognition by RNA polymerase II. FEBS Lett. 581, 2757\u20132760 (2007).","journal-title":"FEBS Lett."},{"key":"e_1_3_4_10_2","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1016\/j.molcel.2015.12.026","article-title":"Non-catalytic roles for XPG with BRCA1 and BRCA2 in homologous recombination and genome stability","volume":"61","author":"Trego K. S.","year":"2016","unstructured":"K. S. Trego ., Non-catalytic roles for XPG with BRCA1 and BRCA2 in homologous recombination and genome stability. Mol. Cell 61, 535\u2013546 (2016).","journal-title":"Mol. Cell"},{"key":"e_1_3_4_11_2","doi-asserted-by":"crossref","first-page":"979","DOI":"10.1093\/nar\/27.4.979","article-title":"Nucleotide excision repair 3\u2032 endonuclease XPG stimulates the activity of base excision repairenzyme thymine glycol DNA glycosylase","volume":"27","author":"Bessho T.","year":"1999","unstructured":"T. Bessho, Nucleotide excision repair 3\u2032 endonuclease XPG stimulates the activity of base excision repairenzyme thymine glycol DNA glycosylase. Nucleic Acids Res. 27, 979\u2013983 (1999).","journal-title":"Nucleic Acids Res."},{"key":"e_1_3_4_12_2","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/S1097-2765(00)80172-0","article-title":"Base excision repair of oxidative DNA damage activated by XPG protein","volume":"3","author":"Klungland A.","year":"1999","unstructured":"A. Klungland ., Base excision repair of oxidative DNA damage activated by XPG protein. Mol. Cell 3, 33\u201342 (1999).","journal-title":"Mol. Cell"},{"key":"e_1_3_4_13_2","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/j.bbrc.2004.06.136","article-title":"Human NTH1 physically interacts with p53 and proliferating cell nuclear antigen","volume":"321","author":"Oyama M.","year":"2004","unstructured":"M. Oyama ., Human NTH1 physically interacts with p53 and proliferating cell nuclear antigen. Biochem. Biophys. Res. Commun. 321, 183\u2013191 (2004).","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"e_1_3_4_14_2","doi-asserted-by":"crossref","first-page":"1998","DOI":"10.4161\/cc.10.12.15878","article-title":"The DNA repair endonuclease XPG interacts directly and functionally with the WRN helicase defective in Werner syndrome","volume":"10","author":"Trego K. S.","year":"2011","unstructured":"K. S. Trego ., The DNA repair endonuclease XPG interacts directly and functionally with the WRN helicase defective in Werner syndrome. Cell Cycle 10, 1998\u20132007 (2011).","journal-title":"Cell Cycle"},{"key":"e_1_3_4_15_2","doi-asserted-by":"crossref","first-page":"3485","DOI":"10.1093\/nar\/gkz025","article-title":"ATM pathway activation limits R-loop-associated genomic instability in Werner syndrome cells","volume":"47","author":"Marabitti V.","year":"2019","unstructured":"V. Marabitti ., ATM pathway activation limits R-loop-associated genomic instability in Werner syndrome cells. Nucleic Acids Res. 47, 3485\u20133502 (2019).","journal-title":"Nucleic Acids Res."},{"key":"e_1_3_4_16_2","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1016\/j.molcel.2014.10.020","article-title":"Transcription-coupled nucleotide excision repair factors promote R-loop-induced genome instability","volume":"56","author":"Sollier J.","year":"2014","unstructured":"J. Sollier ., Transcription-coupled nucleotide excision repair factors promote R-loop-induced genome instability. Mol. Cell 56, 777\u2013785 (2014).","journal-title":"Mol. Cell"},{"key":"e_1_3_4_17_2","doi-asserted-by":"crossref","first-page":"558","DOI":"10.1016\/j.cell.2018.08.056","article-title":"Human Rad52 promotes XPG-mediated R-loop processing to initiate transcription-associated homologous recombination repair","volume":"175","author":"Yasuhara T.","year":"2018","unstructured":"T. Yasuhara ., Human Rad52 promotes XPG-mediated R-loop processing to initiate transcription-associated homologous recombination repair. Cell 175, 558\u2013570.e11 (2018).","journal-title":"Cell"},{"key":"e_1_3_4_18_2","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/0027-5107(79)90231-8","article-title":"A seventh complementation group in excision-deficient xeroderma pigmentosum","volume":"62","author":"Keijzer W.","year":"1979","unstructured":"W. Keijzer ., A seventh complementation group in excision-deficient xeroderma pigmentosum. Mutat. Res. 62, 183\u2013190 (1979).","journal-title":"Mutat. Res."},{"key":"e_1_3_4_19_2","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1111\/1523-1747.ep12584287","article-title":"DNA repair and ultraviolet mutagenesis in cells from a new patient with xeroderma pigmentosum group G and cockayne syndrome resemble xeroderma pigmentosum cells","volume":"107","author":"Moriwaki S.","year":"1996","unstructured":"S. Moriwaki ., DNA repair and ultraviolet mutagenesis in cells from a new patient with xeroderma pigmentosum group G and cockayne syndrome resemble xeroderma pigmentosum cells. J. Invest. Dermatol. 107, 647\u2013653 (1996).","journal-title":"J. Invest. Dermatol."},{"key":"e_1_3_4_20_2","doi-asserted-by":"crossref","first-page":"3116","DOI":"10.1073\/pnas.94.7.3116","article-title":"A common mutational pattern in Cockayne syndrome patients from xeroderma pigmentosum group G: Implications for a second XPG function","volume":"94","author":"Nouspikel T.","year":"1997","unstructured":"T. Nouspikel, P. Lalle, S. A. Leadon, P. K. Cooper, S. G. Clarkson, A common mutational pattern in Cockayne syndrome patients from xeroderma pigmentosum group G: Implications for a second XPG function. Proc. Natl. Acad. Sci. U.S.A. 94, 3116\u20133121 (1997).","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"e_1_3_4_21_2","doi-asserted-by":"crossref","first-page":"3712","DOI":"10.1128\/MCB.24.9.3712-3719.2004","article-title":"Identification of the XPG region that causes the onset of Cockayne syndrome by using Xpg mutant mice generated by the cDNA-mediated knock-in method","volume":"24","author":"Shiomi N.","year":"2004","unstructured":"N. Shiomi ., Identification of the XPG region that causes the onset of Cockayne syndrome by using Xpg mutant mice generated by the cDNA-mediated knock-in method. Mol. Cell. Biol. 24, 3712\u20133719 (2004).","journal-title":"Mol. Cell. Biol."},{"key":"e_1_3_4_22_2","doi-asserted-by":"crossref","first-page":"2237","DOI":"10.1128\/MCB.24.6.2237-2242.2004","article-title":"Deficiency in the nuclease activity of xeroderma pigmentosum G in mice leads to hypersensitivity to UV irradiation","volume":"24","author":"Tian M.","year":"2004","unstructured":"M. Tian, D. A. Jones, M. Smith, R. Shinkura, F. W. Alt, Deficiency in the nuclease activity of xeroderma pigmentosum G in mice leads to hypersensitivity to UV irradiation. Mol. Cell. Biol. 24, 2237\u20132242 (2004).","journal-title":"Mol. Cell. Biol."},{"key":"e_1_3_4_23_2","doi-asserted-by":"crossref","first-page":"2366","DOI":"10.1128\/MCB.19.3.2366","article-title":"Postnatal growth failure, short life span, and early onset of cellular senescence and subsequent immortalization in mice lacking the xeroderma pigmentosum group G gene","volume":"19","author":"Harada Y. N.","year":"1999","unstructured":"Y. N. Harada ., Postnatal growth failure, short life span, and early onset of cellular senescence and subsequent immortalization in mice lacking the xeroderma pigmentosum group G gene. Mol. Cell. Biol. 19, 2366\u20132372 (1999).","journal-title":"Mol. Cell. Biol."},{"key":"e_1_3_4_24_2","doi-asserted-by":"crossref","first-page":"1841","DOI":"10.1038\/jid.2013.54","article-title":"Characterization of three XPG-defective patients identifies three missense mutations that impair repair and transcription","volume":"133","author":"Sch\u00e4fer A.","year":"2013","unstructured":"A. Sch\u00e4fer ., Characterization of three XPG-defective patients identifies three missense mutations that impair repair and transcription. J. Invest. Dermatol. 133, 1841\u20131849 (2013).","journal-title":"J. Invest. Dermatol."},{"key":"e_1_3_4_25_2","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1203\/00006450-200103000-00016","article-title":"Xeroderma pigmentosum group G with severe neurological involvement and features of Cockayne syndrome in infancy","volume":"49","author":"Zafeiriou D. I.","year":"2001","unstructured":"D. I. Zafeiriou ., Xeroderma pigmentosum group G with severe neurological involvement and features of Cockayne syndrome in infancy. Pediatr. Res. 49, 407\u2013412 (2001).","journal-title":"Pediatr. Res."},{"key":"e_1_3_4_26_2","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1093\/emboj\/16.3.625","article-title":"Open complex formation around a lesion during nucleotide excision repair provides a structure for cleavage by human XPG protein","volume":"16","author":"Evans E.","year":"1997","unstructured":"E. Evans, J. Fellows, A. Coffer, R. D. Wood, Open complex formation around a lesion during nucleotide excision repair provides a structure for cleavage by human XPG protein. EMBO J. 16, 625\u2013638 (1997).","journal-title":"EMBO J."},{"key":"e_1_3_4_27_2","doi-asserted-by":"crossref","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 E.","year":"1997","unstructured":"E. Evans, J. G. Moggs, J. R. Hwang, J. M. Egly, R. D. 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