{"title":"溴域AAA+ atp酶形成形状。","authors":"Magdalena Murawska, Andreas G Ladurner","doi":"10.1080/19491034.2020.1741304","DOIUrl":null,"url":null,"abstract":"<p><p>Bromodomain AAA+ ATPases (<u>A</u>TPases <u>a</u>ssociated with diverse cellular <u>a</u>ctivities) are emerging as oncogenic proteins and compelling targets for anticancer therapies. However, structural and biochemical insight into these machines is missing. A recent study by Cho <i>et al</i>. reports the first cryo-EM structure of a bromodomain AAA+ ATPase and provides first insights into the functions of this putative histone chaperone.</p>","PeriodicalId":74323,"journal":{"name":"Nucleus (Austin, Tex.)","volume":"11 1","pages":"32-34"},"PeriodicalIF":0.0000,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19491034.2020.1741304","citationCount":"2","resultStr":"{\"title\":\"Bromodomain AAA+ ATPases get into shape.\",\"authors\":\"Magdalena Murawska, Andreas G Ladurner\",\"doi\":\"10.1080/19491034.2020.1741304\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Bromodomain AAA+ ATPases (<u>A</u>TPases <u>a</u>ssociated with diverse cellular <u>a</u>ctivities) are emerging as oncogenic proteins and compelling targets for anticancer therapies. However, structural and biochemical insight into these machines is missing. A recent study by Cho <i>et al</i>. reports the first cryo-EM structure of a bromodomain AAA+ ATPase and provides first insights into the functions of this putative histone chaperone.</p>\",\"PeriodicalId\":74323,\"journal\":{\"name\":\"Nucleus (Austin, Tex.)\",\"volume\":\"11 1\",\"pages\":\"32-34\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2020-12-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1080/19491034.2020.1741304\",\"citationCount\":\"2\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nucleus (Austin, Tex.)\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1080/19491034.2020.1741304\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nucleus (Austin, Tex.)","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1080/19491034.2020.1741304","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Bromodomain AAA+ ATPases (ATPases associated with diverse cellular activities) are emerging as oncogenic proteins and compelling targets for anticancer therapies. However, structural and biochemical insight into these machines is missing. A recent study by Cho et al. reports the first cryo-EM structure of a bromodomain AAA+ ATPase and provides first insights into the functions of this putative histone chaperone.