{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T00:29:31Z","timestamp":1792024171507,"version":"4.4.0"},"reference-count":80,"publisher":"Portland Press Ltd.","issue":"1","license":[{"start":{"date-parts":[[2022,2,22]],"date-time":"2022-02-22T00:00:00Z","timestamp":1645488000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2022,2,28]]},"abstract":"<jats:p>Inosine-5\u2032-monophosphate dehydrogenase (IMPDH) is a highly conserved enzyme in purine metabolism that is tightly regulated on multiple levels. IMPDH has a critical role in purine biosynthesis, where it regulates flux at the branch point between adenine and guanine nucleotide synthesis, but it also has a role in transcription regulation and other moonlighting functions have been described. Vertebrates have two isoforms, IMPDH1 and IMPDH2, and point mutations in each are linked to human disease. Mutations in IMPDH2 in humans are associated with neurodevelopmental disease, but the effects of mutations at the enzyme level have not yet been characterized. Mutations in IMPDH1 lead to retinal degeneration in humans, and recent studies have characterized how they cause functional defects in regulation. IMPDH1 is expressed as two unique splice variants in the retina, a tissue with very high and specific demands for purine nucleotides. Recent studies have revealed functional differences among splice variants, demonstrating that retinal variants up-regulate guanine nucleotide synthesis by reducing sensitivity to feedback inhibition by downstream products. A better understanding of the role of IMPDH1 in the retina and the characterization of an animal disease model will be critical for determining the molecular mechanism of IMPDH1-associated blindness.<\/jats:p>","DOI":"10.1042\/bst20210446","type":"journal-article","created":{"date-parts":[[2022,2,22]],"date-time":"2022-02-22T13:33:44Z","timestamp":1645536824000},"page":"71-82","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":54,"title":["IMPDH dysregulation in disease: a mini review"],"prefix":"10.1042","volume":"50","author":[{"given":"Anika L.","family":"Burrell","sequence":"first","affiliation":[{"name":"Department of Biochemistry, University of Washington, Seattle, WA, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6943-9570","authenticated-orcid":false,"given":"Justin M.","family":"Kollman","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Washington, Seattle, WA, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2022,2,22]]},"reference":[{"key":"2022030117191966400_BST-2021-0446CC1","doi-asserted-by":"publisher","first-page":"2903","DOI":"10.1021\/cr900021w","article-title":"IMP dehydrogenase: structure, mechanism, and inhibition","volume":"109","year":"2009","journal-title":"Chem. 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