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We then discuss the consequences when this activity is partially inhibited in sickle cell disease and the possibility that the same attenuation is occurring in multiple organ dysfunction syndrome. We finish by discussing the reasons for believing that nonerythroid \u03b1 spectrin isoforms (I and II) also have this activity and the importance of testing this hypothesis. If correct, this would suggest that the nonerythroid spectrin isoforms play a major role in protein ubiquitination in all cell types. This would open new fields in experimental biology focused on uncovering the impact that this enzymatic activity has upon protein\u2013protein interactions, protein turnover, cellular signaling, and many other functions impacted by spectrin, including DNA repair.<\/jats:p>","DOI":"10.1177\/1535370215596084","type":"journal-article","created":{"date-parts":[[2015,8,17]],"date-time":"2015-08-17T08:53:00Z","timestamp":1439801580000},"page":"1039-1049","update-policy":"https:\/\/doi.org\/10.1177\/sage-journals-update-policy","source":"Crossref","is-referenced-by-count":18,"title":["Spectrin\u2019s chimeric E2\/E3 enzymatic activity"],"prefix":"10.3389","volume":"240","author":[{"given":"Steven R","family":"Goodman","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, Department of Pediatrics, SUNY Upstate Medical University, Syracuse, NY 13210, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rachel","family":"Petrofes 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