Charles C. Query, Jadwiga Meissner, Maria M. Konarska
{"title":"寻找和回收停滞的剪接体","authors":"Charles C. Query, Jadwiga Meissner, Maria M. Konarska","doi":"10.1038/s41594-025-01536-2","DOIUrl":null,"url":null,"abstract":"Splicing of pre-mRNA requires both high fidelity and enormous sequence flexibility, inevitably resulting in aberrant, stalled complexes that must be discarded. A study now describes cryo-EM structures of stalled complexes poised for disassembly, determining aspects of aberrant complex recognition and splicing quality control.","PeriodicalId":18822,"journal":{"name":"Nature structural & molecular biology","volume":"25 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2025-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Finding and recycling stalled spliceosomes\",\"authors\":\"Charles C. Query, Jadwiga Meissner, Maria M. Konarska\",\"doi\":\"10.1038/s41594-025-01536-2\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Splicing of pre-mRNA requires both high fidelity and enormous sequence flexibility, inevitably resulting in aberrant, stalled complexes that must be discarded. A study now describes cryo-EM structures of stalled complexes poised for disassembly, determining aspects of aberrant complex recognition and splicing quality control.\",\"PeriodicalId\":18822,\"journal\":{\"name\":\"Nature structural & molecular biology\",\"volume\":\"25 1\",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2025-04-08\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nature structural & molecular biology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1038/s41594-025-01536-2\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nature structural & molecular biology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1038/s41594-025-01536-2","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Splicing of pre-mRNA requires both high fidelity and enormous sequence flexibility, inevitably resulting in aberrant, stalled complexes that must be discarded. A study now describes cryo-EM structures of stalled complexes poised for disassembly, determining aspects of aberrant complex recognition and splicing quality control.
求助内容：
应助结果提醒方式：
京公网安备 11010802042870号
