{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,2]],"date-time":"2026-01-02T12:50:38Z","timestamp":1767358238464,"version":"3.48.0"},"reference-count":38,"publisher":"The Royal Society","issue":"1319","license":[{"start":{"date-parts":[[1995,1,30]],"date-time":"1995-01-30T00:00:00Z","timestamp":791424000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/royalsociety.org\/journals\/ethics-policies\/data-sharing-mining\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[1995,1,30]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>The most versatile strategy for repair of damage to DNA, and the main process for repair of uv-induced damage, is nucleotide excision repair. In mammalian cells, the complete mechanism involves more than 20 polypeptides, and defects in many of these are associated with various forms of inherited disorders in humans. The syndrome xeroderma pigmentosum (XP) is associated with mutagen hypersensitivity and increased cancer frequency, and studies of the nucleotide excision repair defect in this disease have been particularly informative. Many of the XP proteins are now being characterized. XPA binds to DNA, with a preference for damaged base pairs. XPC activity is part of a protein complex with single-stranded DNA binding activity. The XPG protein is a nuclease.<\/jats:p>","DOI":"10.1098\/rstb.1995.0011","type":"journal-article","created":{"date-parts":[[2006,12,18]],"date-time":"2006-12-18T19:03:56Z","timestamp":1166468636000},"page":"69-74","source":"Crossref","is-referenced-by-count":11,"title":["Proteins that participate in nucleotide excision repair of DNA in mammalian cells"],"prefix":"10.1098","volume":"347","author":[{"given":"Richard Dean","family":"Wood","sequence":"first","affiliation":[{"name":"Imperial Cancer Research Fund, Clare Hall Laboratories, South Mimms, Herts. EN6 3LD, U. K."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"175","reference":[{"key":"p_1","first-page":"22493","article-title":"Purification of an ultraviolet-inducible, damage-specific DNA-binding protein from primate cells. 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J. biol","volume":"267","author":"Lin J.J.","year":"1992","journal-title":"Chem."},{"key":"p_23","doi-asserted-by":"crossref","first-page":"17688","DOI":"10.1016\/S0021-9258(19)37097-8","article-title":"Active site of (A)BC excinuclease 1. Evidence for 5' incision by UvrC through a catalytic site involving Asp 399","volume":"267","author":"Lin J.J.","year":"1992","journal-title":"J. biol. Chem."},{"key":"p_24","doi-asserted-by":"publisher","DOI":"10.1128\/MCB.13.10.6393"},{"key":"p_25","unstructured":"Mansbridge J. & Hanawalt P. 1983 Domain-limited repair of DNA in ultraviolet irradiated fibroblasts from xeroderma pigmentosum complementation group C. In Cellular responses to DNA damage (ed. E. Friedberg and B. Bridges) pp. 195-207. New York: Alan R. Liss."},{"key":"p_26","doi-asserted-by":"publisher","DOI":"10.1002\/j.1460-2075.1994.tb06452.x"},{"key":"p_27","first-page":"639","article-title":"Restoration of proliferating cell nuclear antigen (PCNA) complex-formation in xeroderma-pigmentosum group-A cells following cis-diam m ine-dichloroplatinum(II)-treatment by cell-fusion with normal-cells. J. cell","volume":"152","author":"Miura M.","year":"1992","journal-title":"Physiol."},{"key":"p_28","first-page":"12182","article-title":"Mutational analysis of the structure and function of the xeroderma-pigmentosum group-A complementing protein - identification of essential domains for nuclearlocalization and DNA excision repair. J. biol","volume":"267","author":"Miyamoto I.","year":"1992","journal-title":"Chem."},{"key":"p_29","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/20.13.3549-a"},{"key":"p_30","first-page":"501","article-title":"DNA repair synthesis in human fibroblasts requires DNA polymerase 8. 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J. biol","volume":"268","author":"Sung P.","year":"1993","journal-title":"Chem."},{"key":"p_34","first-page":"1931","article-title":"DNA repair by eukaryotic nucleotide excision nuclease: removal of thymine dimer and psoralen monoadduct by HeLa cell-free extract and of thymine dimer by Xenopus laevis oocytes. J. biol","volume":"268","author":"Svoboda D.L.","year":"1993","journal-title":"Chem."},{"key":"p_35","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.90.21.9823"},{"key":"p_36","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/21.17.4111"},{"key":"p_37","unstructured":"Tomkinson A.E. Bardwell A.J. Bardwell L. Tappe N.J."},{"key":"p_38","unstructured":"Nature Lond. 363 185-188. & Friedberg E.C. 1993 Yeast DNA repair and recombination proteins Rad 1 and Rad 10 constitute a single"}],"container-title":["Philosophical Transactions of the Royal Society of London. 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