{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T03:30:06Z","timestamp":1791343806467,"version":"4.3.1"},"reference-count":16,"publisher":"SAGE Publications","issue":"7","license":[{"start":{"date-parts":[[2010,4,1]],"date-time":"2010-04-01T00:00:00Z","timestamp":1270080000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.sagepub.com\/page\/policies\/text-and-data-mining-license"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Antioxidants &amp; Redox Signaling"],"published-print":{"date-parts":[[2010,4]]},"abstract":"<jats:p>\n                    The beneficial role of the trace element selenium (Se) in human health has been known for several decades and is attributed both to low-molecular-weight Se compounds and to its presence within 25 selenoproteins in the form of the amino acid selenocysteine (Sec). Incorporation of Sec into selenoproteins involves decoding of the UGA codon. This process requires multiple features, such as the Sec-insertion sequence (SECIS) element and protein factors, including a specific elongation factor EFSec and the SECIS-binding protein 2, SBP2. Although many selenoproteins remain functionally uncharacterized, some of their known functions include redox regulation of intracellular signaling, redox homeostasis, and thyroid hormone metabolism. Pathologically, reduced expression of selenoproteins has been directly linked with the congenital muscle disease referred to as selenoprotein N (SEPN)-related myopathy and with thyroid-hormone metabolism defects (deficiency of deiodinases due to genetic defects in SBP2). From a broader, less well defined aspect, selenium compounds and selenoproteins have been linked to prevention of some forms of cancer, Alzheimer's disease, cardiovascular disease, and life span. This forum summarizes recent advances in our understanding of important roles of selenium, selenoproteins, and factors involved in selenoprotein synthesis in health and disease and discusses potential targets for therapy.\n                    <jats:italic toggle=\"yes\">Antioxid. Redox Signal.<\/jats:italic>\n                    12, 793\u2013795.\n                  <\/jats:p>","DOI":"10.1089\/ars.2009.2973","type":"journal-article","created":{"date-parts":[[2009,11,11]],"date-time":"2009-11-11T13:06:49Z","timestamp":1257944809000},"page":"793-795","source":"Crossref","is-referenced-by-count":228,"title":["Selenium and Selenoproteins in Health and Disease"],"prefix":"10.1177","volume":"12","author":[{"given":"Laura V.","family":"Papp","sequence":"first","affiliation":[{"name":"Queensland Institute of Medical Research","place":["Australia"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arne","family":"Holmgren","sequence":"additional","affiliation":[{"name":"Karolinska Institute","place":["Sweden"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kum Kum","family":"Khanna","sequence":"additional","affiliation":[{"name":"Queensland Institute of Medical Research","place":["Australia"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"179","published-online":{"date-parts":[[2010,4]]},"reference":[{"key":"e_1_3_1_2_2","doi-asserted-by":"crossref","unstructured":"Conrad M Schweizer U. Unveiling the molecular mechanisms behind selenium-related diseases through knockout mouse studies. Antioxid Redox Signal 12:851\u2013865. 2010.","DOI":"10.1089\/ars.2009.2912"},{"key":"e_1_3_1_3_2","doi-asserted-by":"publisher","DOI":"10.1210\/jc.2009-0686"},{"key":"e_1_3_1_4_2","doi-asserted-by":"crossref","unstructured":"Donovan J Copeland PR. Threading the needle: getting selenocysteine into proteins. Antioxid Redox Signal 12:881\u2013892. 2010.","DOI":"10.1089\/ars.2009.2878"},{"key":"e_1_3_1_5_2","doi-asserted-by":"crossref","unstructured":"Dumitrescu AM Di Cosmo C Liao XH Weiss RE Refetoff S. The syndrome of inherited partial SBP2 deficiency in humans. Antioxid Redox Signal 12:905\u2013920. 2010.","DOI":"10.1089\/ars.2009.2892"},{"key":"e_1_3_1_6_2","doi-asserted-by":"publisher","DOI":"10.1038\/ng1654"},{"key":"e_1_3_1_7_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1083516"},{"key":"e_1_3_1_8_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.1332607100"},{"key":"e_1_3_1_9_2","doi-asserted-by":"crossref","unstructured":"Novoselov SV Kim HY Hua D Lee BC Astle CM Harrison DE Friguet B Moustafa ME Carlson BA Hatfield DL Gladyshev VN. Regulation of selenoproteins and methionine sulfoxide reductases A and B1 by age calorie restriction and dietary selenium in mice. Antioxid Redox Signal 12:829\u2013838. 2010.","DOI":"10.1089\/ars.2009.2895"},{"key":"e_1_3_1_10_2","doi-asserted-by":"crossref","unstructured":"Papp LV Lu J Bolderson E Boucher D Singh R Holmgren A Khanna KK. SECIS-binding protein 2 promotes cell survival by protecting against oxidative stress. Antioxid Redox Signal 12:797\u2013808. 2010.","DOI":"10.1089\/ars.2009.2913"},{"key":"e_1_3_1_11_2","doi-asserted-by":"publisher","DOI":"10.1089\/ars.2007.1528"},{"key":"e_1_3_1_12_2","doi-asserted-by":"crossref","unstructured":"Reeves MA Bellinger FP Berry MJ. The neuroprotective functions of selenoprotein M and its role in cytosolic calcium regulation. Antioxid Redox Signal 12:809\u2013818. 2010.","DOI":"10.1089\/ars.2009.2883"},{"key":"e_1_3_1_13_2","doi-asserted-by":"crossref","unstructured":"Arbogast S Ferreiro A. Selenoproteins and protection against oxidative stress: selenoprotein N as a novel player at the crossroads of redox signaling and calcium homeostasis. Antioxid Redox Signal 12:893\u2013904. 2010.","DOI":"10.1089\/ars.2009.2890"},{"key":"e_1_3_1_14_2","doi-asserted-by":"crossref","unstructured":"Selenius M Rundl\u00f6f AK Olm E Fernandes AP Bj\u00f6rnstedt M. Selenium and the selenoprotein thioredoxin reductase in the prevention treatment and diagnostics of cancer. Antioxid Redox Signal 12:867\u2013880. 2010.","DOI":"10.1089\/ars.2009.2884"},{"key":"e_1_3_1_15_2","doi-asserted-by":"crossref","unstructured":"Shchedrina VA Zhang Y Labunskyy VM Hatfield DL Gladyshev VN. Structure\u2013function relations physiological roles and evolution of mammalian ER-resident selenoproteins. Antioxid Redox Signal 12:839\u2013849. 2010.","DOI":"10.1089\/ars.2009.2865"},{"key":"e_1_3_1_16_2","doi-asserted-by":"publisher","DOI":"10.1089\/ars.2006.8.2021"},{"key":"e_1_3_1_17_2","doi-asserted-by":"crossref","unstructured":"Yoo MH Gu X Xu XM Kim JY Carlson BA Patterson AD Cai H Gladyshev VN Hatfield DL. Delineating the role of glutathione peroxidase 4 in protecting cells against lipid hydroperoxide damage and in Alzheimer's disease. 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