{"title":"结构转变调节了 Grp94 的伴侣活性。","authors":"","doi":"10.1016/j.tibs.2024.06.007","DOIUrl":null,"url":null,"abstract":"<div><p>A recent study by <span><span>Amankwah <em>et al.</em></span><svg><path></path></svg></span><span> reports how co-chaperone proteins and ATP hydrolysis<span><span> fine-tune the function of endoplasmic reticulum (ER)-resident Hsp90 </span>paralog Grp94.</span></span></p></div>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":"49 9","pages":"Pages 752-753"},"PeriodicalIF":11.6000,"publicationDate":"2024-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Structural transitions modulate the chaperone activities of Grp94\",\"authors\":\"\",\"doi\":\"10.1016/j.tibs.2024.06.007\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>A recent study by <span><span>Amankwah <em>et al.</em></span><svg><path></path></svg></span><span> reports how co-chaperone proteins and ATP hydrolysis<span><span> fine-tune the function of endoplasmic reticulum (ER)-resident Hsp90 </span>paralog Grp94.</span></span></p></div>\",\"PeriodicalId\":440,\"journal\":{\"name\":\"Trends in Biochemical Sciences\",\"volume\":\"49 9\",\"pages\":\"Pages 752-753\"},\"PeriodicalIF\":11.6000,\"publicationDate\":\"2024-09-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Trends in Biochemical Sciences\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0968000424001506\",\"RegionNum\":1,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Trends in Biochemical Sciences","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0968000424001506","RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
摘要
Amankwah 等人最近的一项研究报告了共伴侣蛋白和 ATP 水解如何微调内质网（ER）驻留 Hsp90 旁系亲属 Grp94 的功能。
Structural transitions modulate the chaperone activities of Grp94
A recent study by Amankwah et al. reports how co-chaperone proteins and ATP hydrolysis fine-tune the function of endoplasmic reticulum (ER)-resident Hsp90 paralog Grp94.
期刊介绍：
For over 40 years, Trends in Biochemical Sciences (TIBS) has been a leading publication keeping readers informed about recent advances in all areas of biochemistry and molecular biology. Through monthly, peer-reviewed issues, TIBS covers a wide range of topics, from traditional subjects like protein structure and function to emerging areas in signaling and metabolism. Articles are curated by the Editor and authored by top researchers in their fields, with a focus on moving beyond simple literature summaries to providing novel insights and perspectives. Each issue primarily features concise and timely Reviews and Opinions, supplemented by shorter articles including Spotlights, Forums, and Technology of the Month, as well as impactful pieces like Science & Society and Scientific Life articles.
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