{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T23:07:41Z","timestamp":1791414461965,"version":"4.3.3"},"reference-count":73,"publisher":"Wiley","issue":"12","license":[{"start":{"date-parts":[[2010,4,11]],"date-time":"2010-04-11T00:00:00Z","timestamp":1270944000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"name":"Dutch Cancer Foundation","award":["KWF KUN 2009-4527"],"award-info":[{"award-number":["KWF KUN 2009-4527"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["FEBS Letters"],"published-print":{"date-parts":[[2010,6,18]]},"abstract":"<jats:p>Acute myeloid leukemia (AML) associated translocations often cause gene fusions that encode oncofusion proteins. Although many of the breakpoints involved in chromosomal translocations have been cloned, in most cases the role of the chimeric proteins in tumorigenesis is not elucidated. Here we will discuss the fusion proteins of the 4 most common translocations associated with AML as well as the common molecular mechanisms that these four and other fusion proteins utilize to transform progenitor cells. Intriguingly, although the individual partners within the fusion proteins represent a wide variety of cellular functions, at the molecular level many commodities can be found.<\/jats:p>","DOI":"10.1016\/j.febslet.2010.04.002","type":"journal-article","created":{"date-parts":[[2010,4,13]],"date-time":"2010-04-13T09:19:45Z","timestamp":1271150385000},"page":"2662-2669","source":"Crossref","is-referenced-by-count":90,"title":["The molecular signature of oncofusion proteins in acute myeloid leukemia"],"prefix":"10.1002","volume":"584","author":[{"given":"Joost H.A.","family":"Martens","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Henk G.","family":"Stunnenberg","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2010,4,11]]},"reference":[{"key":"e_1_2_13_2_1","doi-asserted-by":"publisher","DOI":"10.1002\/cncr.22233"},{"key":"e_1_2_13_3_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.278.5340.1059"},{"key":"e_1_2_13_4_1","doi-asserted-by":"publisher","DOI":"10.1038\/nrc2091"},{"key":"e_1_2_13_5_1","doi-asserted-by":"publisher","DOI":"10.1182\/blood.V94.2.417"},{"key":"e_1_2_13_6_1","doi-asserted-by":"publisher","DOI":"10.1182\/blood.V93.10.3167.410k44_3167_3215"},{"key":"e_1_2_13_7_1","unstructured":"Mitelman F. 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