{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,28]],"date-time":"2026-08-28T07:18:21Z","timestamp":1787901501354,"version":"build-2784847793"},"reference-count":27,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2006,1,12]],"date-time":"2006-01-12T00:00:00Z","timestamp":1137024000000},"content-version":"vor","delay-in-days":682,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Annals of the New York Academy of Sciences"],"published-print":{"date-parts":[[2004,3]]},"abstract":"<jats:p><jats:bold>A<jats:sc>bstract<\/jats:sc>: <\/jats:bold> Many lines of evidence indicate that oxidative stress is one of the earliest events in the genesis of Alzheimer's disease (AD). Iron is a transition metal capable of generating hydroxyl radicals, the most potent reactive oxygen species. Consequently, a disruption in the metabolism of iron has been postulated to have a role in the pathogenesis of AD. Indeed, both senile plaques and neurofibrillary tangles, the major pathological landmarks of AD, as well as neurons in the earliest stages of the disease, show elevated iron deposition. However, it is clear that the iron bound to lesion\u2010associated proteins such as amyloid\u2010\u03b2 and tau plays only a minor, late role in the disease, with the RNA\u2010associated iron found in the neuronal cytoplasm occurring early and being of paramount importance. In this regard, it is probably not surprising that there is significant oxidation of cytoplasmic RNA among the populations of neurons vulnerable to AD. In this review, we consider the role of iron\u2010induced oxidative stress as a key event in AD pathophysiology.<\/jats:p>","DOI":"10.1196\/annals.1306.015","type":"journal-article","created":{"date-parts":[[2004,4,23]],"date-time":"2004-04-23T03:27:51Z","timestamp":1082690871000},"page":"179-182","source":"Crossref","is-referenced-by-count":160,"title":["Oxidative Stress and Redox\u2010Active Iron in Alzheimer's Disease"],"prefix":"10.1111","volume":"1012","author":[{"given":"KAZUHIRO","family":"HONDA","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"GEMMA","family":"CASADESUS","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"ROBERT B.","family":"PETERSEN","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"GEORGE","family":"PERRY","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"MARK A.","family":"SMITH","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2006,1,12]]},"reference":[{"key":"e_1_2_8_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-510X(98)00092-6"},{"key":"e_1_2_8_3_2","doi-asserted-by":"publisher","DOI":"10.1002\/jnr.490310111"},{"key":"e_1_2_8_4_2","first-page":"191","article-title":"Most amyloid plaques contain ferritin\u2010rich cells","volume":"1","author":"Robinson S.R.","year":"1995","journal-title":"Alzheimer's Res."},{"key":"e_1_2_8_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0006-8993(98)00002-X"},{"key":"e_1_2_8_6_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.94.18.9866"},{"key":"e_1_2_8_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0006-8993(01)02303-4"},{"key":"e_1_2_8_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0960-894X(99)00357-1"},{"key":"e_1_2_8_9_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1471-4159.1993.tb03639.x"},{"key":"e_1_2_8_10_2","doi-asserted-by":"publisher","DOI":"10.1620\/tjem.174.263"},{"key":"e_1_2_8_11_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0891-5849(00)00494-9"},{"key":"e_1_2_8_12_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0197-4580(00)83347-3"},{"key":"e_1_2_8_13_2","doi-asserted-by":"publisher","DOI":"10.1093\/jnen\/60.8.759"},{"key":"e_1_2_8_14_2","first-page":"783","article-title":"Increasing amyloid A\u03b2 42 deposition is associated with decreasing neuronal RNA oxidation in Down's syndrome and familial Alzheimer's disease","volume":"10","author":"Nunomura A.","year":"2000","journal-title":"Brain Pathol."},{"key":"e_1_2_8_15_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.C000165200"},{"key":"e_1_2_8_16_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1471-4159.2000.0740270.x"},{"key":"e_1_2_8_17_2","doi-asserted-by":"publisher","DOI":"10.1038\/ng0996-55"},{"key":"e_1_2_8_18_2","doi-asserted-by":"crossref","first-page":"1959","DOI":"10.1523\/JNEUROSCI.19-06-01959.1999","article-title":"RNA oxidation is a prominent feature of vulnerable neurons in Alzheimer disease","volume":"19","author":"Nunomura A.","year":"1999","journal-title":"J. Neurosci."},{"key":"e_1_2_8_19_2","doi-asserted-by":"publisher","DOI":"10.1523\/JNEUROSCI.23-12-04913.2003"},{"key":"e_1_2_8_20_2","first-page":"42","article-title":"Heme oxygenase\u20101 is associated with the neurofibrillary pathology of Alzheimer's disease","volume":"145","author":"Smith M.A.","year":"1994","journal-title":"Am. J. Pathol."},{"key":"e_1_2_8_21_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1471-4159.1995.65031399.x"},{"key":"e_1_2_8_22_2","doi-asserted-by":"publisher","DOI":"10.1002\/ana.410370609"},{"key":"e_1_2_8_23_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.86.1.99"},{"key":"e_1_2_8_24_2","doi-asserted-by":"publisher","DOI":"10.1523\/JNEUROSCI.21-09-03017.2001"},{"key":"e_1_2_8_25_2","doi-asserted-by":"publisher","DOI":"10.1016\/0140-6736(91)92978-B"},{"key":"e_1_2_8_26_2","doi-asserted-by":"publisher","DOI":"10.1097\/00007691-199312000-00027"},{"key":"e_1_2_8_27_2","doi-asserted-by":"publisher","DOI":"10.3233\/JAD-1998-1103"},{"key":"e_1_2_8_28_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0140-6736(05)72173-5"}],"container-title":["Annals of the New York Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1196%2Fannals.1306.015","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/nyaspubs.onlinelibrary.wiley.com\/doi\/pdf\/10.1196\/annals.1306.015","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,9,25]],"date-time":"2023-09-25T09:11:03Z","timestamp":1695633063000},"score":1,"resource":{"primary":{"URL":"https:\/\/nyaspubs.onlinelibrary.wiley.com\/doi\/10.1196\/annals.1306.015"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2004,3]]},"references-count":27,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2004,3]]}},"alternative-id":["10.1196\/annals.1306.015"],"URL":"https:\/\/doi.org\/10.1196\/annals.1306.015","archive":["Portico"],"relation":{},"ISSN":["0077-8923","1749-6632"],"issn-type":[{"value":"0077-8923","type":"print"},{"value":"1749-6632","type":"electronic"}],"subject":[],"published":{"date-parts":[[2004,3]]}}}