{"title":"利用伊马替尼的滥交性。","authors":"Shun J Lee, Jean Y J Wang","doi":"10.1186/jbiol134","DOIUrl":null,"url":null,"abstract":"<p><p>The protein kinase inhibitor imatinib, also known as Gleevec, has been a notable success in treating chronic myelogenous leukemia. A recent paper in BMC Structural Biology reports a 1.75 A crystal structure of imatinib bound to the oxidoreductase NQO2 and reveals insights into the binding specificity and the off-target effects of the inhibitor.</p>","PeriodicalId":15075,"journal":{"name":"Journal of Biology","volume":"8 3","pages":"30"},"PeriodicalIF":0.0000,"publicationDate":"2009-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1186/jbiol134","citationCount":"38","resultStr":"{\"title\":\"Exploiting the promiscuity of imatinib.\",\"authors\":\"Shun J Lee, Jean Y J Wang\",\"doi\":\"10.1186/jbiol134\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The protein kinase inhibitor imatinib, also known as Gleevec, has been a notable success in treating chronic myelogenous leukemia. A recent paper in BMC Structural Biology reports a 1.75 A crystal structure of imatinib bound to the oxidoreductase NQO2 and reveals insights into the binding specificity and the off-target effects of the inhibitor.</p>\",\"PeriodicalId\":15075,\"journal\":{\"name\":\"Journal of Biology\",\"volume\":\"8 3\",\"pages\":\"30\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2009-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1186/jbiol134\",\"citationCount\":\"38\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Biology\",\"FirstCategoryId\":\"1089\",\"ListUrlMain\":\"https://doi.org/10.1186/jbiol134\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2009/4/15 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Biology","FirstCategoryId":"1089","ListUrlMain":"https://doi.org/10.1186/jbiol134","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2009/4/15 0:00:00","PubModel":"Epub","JCR":"","JCRName":"","Score":null,"Total":0}
The protein kinase inhibitor imatinib, also known as Gleevec, has been a notable success in treating chronic myelogenous leukemia. A recent paper in BMC Structural Biology reports a 1.75 A crystal structure of imatinib bound to the oxidoreductase NQO2 and reveals insights into the binding specificity and the off-target effects of the inhibitor.
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