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A defining feature of nucleotide excision repair is its dual incision mechanism, in which two nucleolytic incision events on the damaged strand of<jats:styled-content style=\"fixed-case\">DNA<\/jats:styled-content>at sites bracketing the lesion generate a damage\u2010containing<jats:styled-content style=\"fixed-case\">DNA<\/jats:styled-content>oligonucleotide and a single\u2010stranded<jats:styled-content style=\"fixed-case\">DNA<\/jats:styled-content>gap approximately 30 nucleotides in length. Although the early events of nucleotide excision repair, which include lesion recognition and the dual incisions, have been explored in detail and are reasonably well understood, the fate of the single\u2010stranded<jats:styled-content style=\"fixed-case\">DNA<\/jats:styled-content>gaps and excised oligonucleotide products of repair have not been as extensively examined. In this review, recent findings that address these less\u2010explored aspects of nucleotide excision repair are discussed and support the concept that postincision gap and excised oligonucleotide processing are critical steps in the cellular response to<jats:styled-content style=\"fixed-case\">DNA<\/jats:styled-content>damage induced by<jats:styled-content style=\"fixed-case\">UV<\/jats:styled-content>light and other environmental carcinogens. Defects in these latter stages of repair lead to cell death and other<jats:styled-content style=\"fixed-case\">DNA<\/jats:styled-content>damage signaling responses and may therefore contribute to a number of human disease states associated with exposure to<jats:styled-content style=\"fixed-case\">UV<\/jats:styled-content>wavelengths of sunlight, including skin cancer, aging and autoimmunity.<\/jats:p>","DOI":"10.1111\/php.12641","type":"journal-article","created":{"date-parts":[[2016,9,20]],"date-time":"2016-09-20T00:26:40Z","timestamp":1474331200000},"page":"178-191","source":"Crossref","is-referenced-by-count":28,"title":["PostExcision Events in Human Nucleotide Excision Repair"],"prefix":"10.1111","volume":"93","author":[{"given":"Michael G.","family":"Kemp","sequence":"first","affiliation":[{"name":"Department of Pharmacology and Toxicology Wright State University Boonshoft School of Medicine Dayton 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