{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,10,31]],"date-time":"2023-10-31T05:04:57Z","timestamp":1698728697407},"reference-count":21,"publisher":"Wiley","issue":"1-2","license":[{"start":{"date-parts":[[1999,5,21]],"date-time":"1999-05-21T00:00:00Z","timestamp":927244800000},"content-version":"vor","delay-in-days":21,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["FEBS Letters"],"published-print":{"date-parts":[[1999,4,30]]},"abstract":"<jats:p>The 26S proteasome subunit 5a binds polyubiquitin chains and has previously been shown to inhibit the degradation of mitotic cyclins. Presumably inhibition results from S5a binding and preventing recognition of Ub\u2010cyclin conjugates by the 26S proteasome. Here we show that S5a does not inhibit the degradation of full\u2010length ornithine decarboxylase (ODC) consistent with previous reports that the enzyme is degraded in an antizyme\u2010dependent, but ubiquitin\u2010independent reaction. S5a does, however, inhibit degradation of short ODC translation products generated by internal initiation events. Because in vitro translation often produces some shortened products, the existence of ubiquitin conjugated to a <jats:sup>35<\/jats:sup>S\u2010labeled protein is not necessarily evidence that the full\u2010length protein is a substrate of the Ub\u2010dependent proteolytic pathway.<\/jats:p>","DOI":"10.1016\/s0014-5793(99)00456-1","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T17:52:28Z","timestamp":1027619548000},"page":"123-125","source":"Crossref","is-referenced-by-count":8,"title":["Discrimination between ubiquitin\u2010dependent and ubiquitin\u2010independent proteolytic pathways by the 26S proteasome subunit 5a"],"prefix":"10.1002","volume":"450","author":[{"given":"David","family":"Mahaffey","sequence":"first","affiliation":[]},{"given":"Martin","family":"Rechsteiner","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[1999,5,21]]},"reference":[{"key":"e_1_2_5_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0955-0674(97)80079-8"},{"key":"e_1_2_5_3_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.biochem.67.1.425"},{"key":"e_1_2_5_4_1","doi-asserted-by":"publisher","DOI":"10.1093\/emboj\/17.20.5964"},{"key":"e_1_2_5_5_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.2538923"},{"key":"e_1_2_5_6_1","unstructured":"Pickart C.M. (1998) in: J.-M Peters J.R. Harris and D. Finley (Eds.) Ubiquitin and the Biology of the Cell Plenum New York pp. 411&#x2013;428."},{"key":"e_1_2_5_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(17)35950-1"},{"key":"e_1_2_5_8_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(17)37244-7"},{"key":"e_1_2_5_9_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.93.2.856"},{"key":"e_1_2_5_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(96)00101-9"},{"key":"e_1_2_5_11_1","doi-asserted-by":"publisher","DOI":"10.1128\/MCB.16.11.6020"},{"key":"e_1_2_5_12_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.270.40.23726"},{"key":"e_1_2_5_13_1","doi-asserted-by":"publisher","DOI":"10.1042\/bj3060001"},{"key":"e_1_2_5_14_1","doi-asserted-by":"crossref","unstructured":"Coffino P. (1998) in: J.-M. Peters J.R. Harris and D. Finley (Eds.) 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