{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T10:17:54Z","timestamp":1790849874632,"version":"4.1.0"},"reference-count":186,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"National Institutes of Health (NIH)","award":["ES-031086"],"award-info":[{"award-number":["ES-031086"]}]},{"name":"National Institutes of Health (NIH)","award":["CA-55678"],"award-info":[{"award-number":["CA-55678"]}]},{"name":"National Institutes of Health (NIH)","award":["ES-029357"],"award-info":[{"award-number":["ES-029357"]}]},{"name":"National Institutes of Health (NIH)","award":["CA-160032"],"award-info":[{"award-number":["CA-160032"]}]},{"name":"National Institutes of Health (NIH)","award":["656.630"],"award-info":[{"award-number":["656.630"]}]},{"name":"Oregon Institute of Occupational Health Sciences at Oregon Health &amp; Science University","award":["ES-031086"],"award-info":[{"award-number":["ES-031086"]}]},{"name":"Oregon Institute of Occupational Health Sciences at Oregon Health &amp; Science University","award":["CA-55678"],"award-info":[{"award-number":["CA-55678"]}]},{"name":"Oregon Institute of Occupational Health Sciences at Oregon Health &amp; Science University","award":["ES-029357"],"award-info":[{"award-number":["ES-029357"]}]},{"name":"Oregon Institute of Occupational Health Sciences at Oregon Health &amp; Science University","award":["CA-160032"],"award-info":[{"award-number":["CA-160032"]}]},{"name":"Oregon Institute of Occupational Health Sciences at Oregon Health &amp; Science University","award":["656.630"],"award-info":[{"award-number":["656.630"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["DNA"],"abstract":"<jats:p>DNA glycosylases promote genomic stability by initiating base excision repair (BER) in both the nuclear and mitochondrial genomes. Several of these enzymes have overlapping substrate recognition, through which a degree of redundancy in lesion recognition is achieved. For example, OGG1 and NEIL1 both recognize and release the imidazole-ring-fragmented guanine, FapyGua as part of a common overall pathway to cleanse the genome of damaged bases. However, these glycosylases have many differences, including their differential breadth of substrate specificity, the contrasting chemistries through which base release occurs, the subsequent steps required to complete the BER pathway, and the identity of specific protein-binding partners. Beyond these differences, the complexities and differences of their in vivo biological roles have been primarily elucidated in studies of murine models harboring a knockout of Neil1 or Ogg1, with the diversity of phenotypic manifestations exceeding what might have been anticipated for a DNA glycosylase deficiency. Pathologies associated with deficiencies in nuclear DNA repair include differential cancer susceptibilities, where Ogg1-deficient mice are generally refractory to carcinogenesis, while deficiencies in Neil1-deficient mice confer cancer susceptibility. In contrast to NEIL1, OGG1 functions as a key transcription factor in regulating inflammation and other complex gene cascades. With regard to phenotypes attributed to mitochondrial repair, knockout of either of these genes results in age- and diet-induced metabolic syndrome. The adverse health consequences associated with metabolic syndrome can be largely overcome by expression of a mitochondrial-targeted human OGG1 in both wild-type and Ogg1-deficient mice. The goal of this review is to compare the roles that NEIL1 and OGG1 play in maintaining genomic integrity, with emphasis on insights gained from not only the diverse phenotypes that are manifested in knockout and transgenic mice, but also human disease susceptibility associated with polymorphic variants.<\/jats:p>","DOI":"10.3390\/dna2040020","type":"journal-article","created":{"date-parts":[[2022,12,2]],"date-time":"2022-12-02T03:28:04Z","timestamp":1669951684000},"page":"279-301","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":18,"title":["Complex Roles of NEIL1 and OGG1: Insights Gained from Murine Knockouts and Human Polymorphic Variants"],"prefix":"10.3390","volume":"2","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7273-372X","authenticated-orcid":false,"given":"R. Stephen","family":"Lloyd","sequence":"first","affiliation":[{"name":"Oregon Institute of Occupational Health Sciences, Department of Molecular and Medical Genetics, Oregon Health & Science University, Portland, OR 97239, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,12,1]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1111\/j.1749-6632.1994.tb52812.x","article-title":"Base excision repair in E. coli\u2014An overview","volume":"726","author":"Kow","year":"1994","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"ref_2","first-page":"14","article-title":"Role of DNA repair enzymes in the cellular resistance to oxidative stress","volume":"44","author":"Laval","year":"1996","journal-title":"Pathol. 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