{"title":"Myc的泛素化:蛋白酶体降解及其他。","authors":"J Müller, M Eilers","doi":"10.1007/2789_2008_103","DOIUrl":null,"url":null,"abstract":"<p><p>The level of Myc proteins is a critical determinant of cellular proliferation and apoptosis. Ubiquitination of Myc plays a key role in controlling protein levels by stimulating proteasomal degradation of the protein. Some experiments suggest that ubiquitination may also regulate Myc function in addition to turnover. This review attempts to summarize current knowledge about this field.</p>","PeriodicalId":87471,"journal":{"name":"Ernst Schering Foundation symposium proceedings","volume":" 1","pages":"99-113"},"PeriodicalIF":0.0000,"publicationDate":"2008-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/2789_2008_103","citationCount":"22","resultStr":"{\"title\":\"Ubiquitination of Myc: proteasomal degradation and beyond.\",\"authors\":\"J Müller, M Eilers\",\"doi\":\"10.1007/2789_2008_103\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The level of Myc proteins is a critical determinant of cellular proliferation and apoptosis. Ubiquitination of Myc plays a key role in controlling protein levels by stimulating proteasomal degradation of the protein. Some experiments suggest that ubiquitination may also regulate Myc function in addition to turnover. This review attempts to summarize current knowledge about this field.</p>\",\"PeriodicalId\":87471,\"journal\":{\"name\":\"Ernst Schering Foundation symposium proceedings\",\"volume\":\" 1\",\"pages\":\"99-113\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2008-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1007/2789_2008_103\",\"citationCount\":\"22\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Ernst Schering Foundation symposium proceedings\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1007/2789_2008_103\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Ernst Schering Foundation symposium proceedings","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1007/2789_2008_103","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Ubiquitination of Myc: proteasomal degradation and beyond.
The level of Myc proteins is a critical determinant of cellular proliferation and apoptosis. Ubiquitination of Myc plays a key role in controlling protein levels by stimulating proteasomal degradation of the protein. Some experiments suggest that ubiquitination may also regulate Myc function in addition to turnover. This review attempts to summarize current knowledge about this field.
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