{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,6]],"date-time":"2026-07-06T11:04:55Z","timestamp":1783335895467,"version":"3.54.6"},"reference-count":101,"publisher":"MDPI AG","issue":"8","license":[{"start":{"date-parts":[[2025,8,1]],"date-time":"2025-08-01T00:00:00Z","timestamp":1754006400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["JPM"],"abstract":"<jats:p>Type 10 17\u03b2-hydroxysteroid dehydrogenase (17\u03b2-HSD10) is the HSD17B10 gene product. It plays an appreciable part in the carcinogenesis and pathogenesis of neurodegeneration, such as Alzheimer\u2019s disease and infantile neurodegeneration. This mitochondrial, homo-tetrameric protein is a central hub in various metabolic pathways, e.g., branched-chain amino acid degradation and neurosteroid metabolism. It can bind to other proteins carrying out diverse physiological functions, e.g., tRNA maturation. It has also previously been proposed to be an A\u03b2-binding alcohol dehydrogenase (ABAD) or endoplasmic reticulum-associated A\u03b2-binding protein (ERAB), although those reports are controversial due to data analyses. For example, the reported km value of some substrate of ABAD\/ERAB was five times higher than its natural solubility in the assay employed to measure km. Regarding any reported \u201cone-site competitive inhibition\u201d of ABAD\/ERAB by A\u03b2, the ki value estimations were likely impacted by non-physiological concentrations of 2-octanol at high concentrations of vehicle DMSO and, therefore, are likely artefactual. Certain data associated with ABAD\/ERAB were found not reproducible, and multiple experimental approaches were undertaken under non-physiological conditions. In contrast, 17\u03b2-HSD10 studies prompted a conclusion that A\u03b2 inhibited 17\u03b2-HSD10 activity, thus harming brain cells, replacing a prior supposition that \u201cABAD\u201d mediates A\u03b2 neurotoxicity. Furthermore, it is critical to find answers to the question as to why elevated levels of 17\u03b2-HSD10, in addition to A\u03b2 and phosphorylated Tau, are present in the brains of AD patients and mouse AD models. Addressing this question will likely prompt better approaches to develop treatments for Alzheimer\u2019s disease.<\/jats:p>","DOI":"10.3390\/jpm15080346","type":"journal-article","created":{"date-parts":[[2025,8,4]],"date-time":"2025-08-04T13:11:11Z","timestamp":1754313071000},"page":"346","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Roles of Type 10 17\u03b2-Hydroxysteroid Dehydrogenase in Health and Disease"],"prefix":"10.3390","volume":"15","author":[{"given":"Xue-Ying","family":"He","sequence":"first","affiliation":[{"name":"Department of Molecular Biology, NYS Institute for Basic Research in Developmental Disabilities, Staten Island, NY 10314, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7428-5083","authenticated-orcid":false,"given":"Janusz","family":"Frackowiak","sequence":"additional","affiliation":[{"name":"Department of Developmental Neurobiology, NYS Institute for Basic Research in Developmental Disabilities, Staten Island, NY 10314, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Song-Yu","family":"Yang","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology, NYS Institute for Basic Research in Developmental Disabilities, Staten Island, NY 10314, USA"},{"name":"Ph.D. Program in Biology-Neuroscience, Graduate Center, The City University of New York, New York, NY 10016, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,8,1]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"He, X.Y., Frackowiak, J., Dobkin, C., Brown, W.T., and Yang, S.Y. 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