{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,26]],"date-time":"2026-06-26T16:21:57Z","timestamp":1782490917796,"version":"3.54.5"},"reference-count":75,"publisher":"SAGE Publications","issue":"1","license":[{"start":{"date-parts":[[2015,1,1]],"date-time":"2015-01-01T00:00:00Z","timestamp":1420070400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.sagepub.com\/page\/policies\/text-and-data-mining-license"}],"content-domain":{"domain":["journals.sagepub.com"],"crossmark-restriction":true},"short-container-title":["Antioxidants &amp; Redox Signaling"],"published-print":{"date-parts":[[2015,1]]},"abstract":"<jats:p>\n                    <jats:bold>\n                      <jats:italic toggle=\"yes\">Aims:<\/jats:italic>\n                    <\/jats:bold>\n                    To examine the role of the enzyme methionine sulfoxide reductase A-1 (MSRA-1) in amyloid-\u03b2 peptide (A\u03b2)-peptide aggregation and toxicity\n                    <jats:italic toggle=\"yes\">in vivo,<\/jats:italic>\n                    using a\n                    <jats:italic toggle=\"yes\">Caenorhabditis elegans<\/jats:italic>\n                    model of the human amyloidogenic disease inclusion body myositis.\n                    <jats:bold>\n                      <jats:italic toggle=\"yes\">Results:<\/jats:italic>\n                    <\/jats:bold>\n                    MSRA-1 specifically reduces oxidized methionines in proteins. Therefore, a deletion of the\n                    <jats:italic toggle=\"yes\">msra-1<\/jats:italic>\n                    gene was introduced into transgenic\n                    <jats:italic toggle=\"yes\">C. elegans<\/jats:italic>\n                    worms that express the A\u03b2-peptide in muscle cells to prevent the reduction of oxidized methionines in proteins. In a constitutive transgenic A\u03b2 strain that lacks MSRA-1, the number of amyloid aggregates decreases while the number of oligomeric A\u03b2 species increases. These results correlate with enhanced synaptic dysfunction and mislocalization of the nicotinic acetylcholine receptor ACR-16 at the neuromuscular junction (NMJ).\n                    <jats:bold>\n                      <jats:italic toggle=\"yes\">Innovation:<\/jats:italic>\n                    <\/jats:bold>\n                    This approach aims at modulating the oxidation of A\u03b2\n                    <jats:italic toggle=\"yes\">in vivo<\/jats:italic>\n                    indirectly by dismantling the methionine sulfoxide repair system. The evidence presented here shows that the absence of MSRA-1 influences A\u03b2 aggregation and aggravates locomotor behavior and NMJ dysfunction. The results suggest that therapies which boost the activity of the Msr system could have a beneficial effect in managing amyloidogenic pathologies.\n                    <jats:bold>\n                      <jats:italic toggle=\"yes\">Conclusion:<\/jats:italic>\n                    <\/jats:bold>\n                    The absence of MSRA-1 modulates A\u03b2-peptide aggregation and increments its deleterious effects\n                    <jats:italic toggle=\"yes\">in vivo<\/jats:italic>\n                    .\n                    <jats:italic toggle=\"yes\">Antioxid. Redox Signal<\/jats:italic>\n                    . 22, 48\u201362.\n                  <\/jats:p>","DOI":"10.1089\/ars.2013.5803","type":"journal-article","created":{"date-parts":[[2014,7,2]],"date-time":"2014-07-02T09:02:21Z","timestamp":1404291741000},"page":"48-62","update-policy":"https:\/\/doi.org\/10.1177\/sage-journals-update-policy","source":"Crossref","is-referenced-by-count":25,"title":["The Protein Oxidation Repair Enzyme Methionine Sulfoxide Reductase A Modulates A\u03b2 Aggregation and Toxicity\n                    <i>In Vivo<\/i>"],"prefix":"10.1177","volume":"22","author":[{"given":"Alicia N.","family":"Minniti","sequence":"first","affiliation":[{"name":"Pontificia Universidad Cat\u00f3lica de Chile","place":["Chile"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Macarena S.","family":"Arrazola","sequence":"additional","affiliation":[{"name":"Pontificia Universidad Cat\u00f3lica de Chile","place":["Chile"]},{"name":"Center for Aging and Regeneration 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