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Nakamura\n                    <jats:italic>et al.<\/jats:italic>\n                    found that this S-nitrosylation occurs in an unusual way. They detected a series of transnitrosylation events in which an NO group is passed between at least three proteins. The deubiquinating enzyme Uch-L1 was S-nitrosylated in brains from human AD patients or in mouse models of AD. Uch-L1 could lead to S-nitrosylation of Drp1 after transferring the NO group to another enzyme, Cdk5 (cyclin-dependent kinase 5). The results implicate a mechanism in which unrelated enzymes might aberrantly function together to disrupt brain function.\n                  <\/jats:p>\n                  <jats:p>\n                    <jats:italic>Science<\/jats:italic>\n                    , this issue p.\n                    <jats:related-article xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"doi\" related-article-type=\"in-this-issue\" xlink:href=\"10.1126\/science.aaw0843\">eaaw0843<\/jats:related-article>\n                  <\/jats:p>","DOI":"10.1126\/science.aaw0843","type":"journal-article","created":{"date-parts":[[2020,12,3]],"date-time":"2020-12-03T19:11:29Z","timestamp":1607022689000},"source":"Crossref","is-referenced-by-count":88,"title":["Noncanonical transnitrosylation network contributes to synapse loss in Alzheimer\u2019s 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