你能做的任何事情,聚糖都能做得更好:脱糖基化和非经典泛素化争夺蛋白酶体的统治权。

IF 11.6 1区 生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY Trends in Biochemical Sciences Pub Date : 2024-10-16 DOI:10.1016/j.tibs.2024.10.001
Nicolas Lehrbach
{"title":"你能做的任何事情,聚糖都能做得更好:脱糖基化和非经典泛素化争夺蛋白酶体的统治权。","authors":"Nicolas Lehrbach","doi":"10.1016/j.tibs.2024.10.001","DOIUrl":null,"url":null,"abstract":"<p><p>The Nrf1/Nfe2L1 transcription factor is a master regulator of proteasome biogenesis. New work by Yoshida and colleagues reveals a surprising mechanism by which ubiquitination of N-glycosylated Nrf1 controls its function.</p>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":" ","pages":""},"PeriodicalIF":11.6000,"publicationDate":"2024-10-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Anything you can do, glycans do better: deglycosylation and noncanonical ubiquitination vie to rule the proteasome.\",\"authors\":\"Nicolas Lehrbach\",\"doi\":\"10.1016/j.tibs.2024.10.001\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The Nrf1/Nfe2L1 transcription factor is a master regulator of proteasome biogenesis. New work by Yoshida and colleagues reveals a surprising mechanism by which ubiquitination of N-glycosylated Nrf1 controls its function.</p>\",\"PeriodicalId\":440,\"journal\":{\"name\":\"Trends in Biochemical Sciences\",\"volume\":\" \",\"pages\":\"\"},\"PeriodicalIF\":11.6000,\"publicationDate\":\"2024-10-16\",\"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://doi.org/10.1016/j.tibs.2024.10.001\",\"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://doi.org/10.1016/j.tibs.2024.10.001","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

Nrf1/Nfe2L1 转录因子是蛋白酶体生物生成的主调节因子。Yoshida 及其同事的新研究揭示了 N-糖基化 Nrf1 泛素化控制其功能的惊人机制。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
Anything you can do, glycans do better: deglycosylation and noncanonical ubiquitination vie to rule the proteasome.

The Nrf1/Nfe2L1 transcription factor is a master regulator of proteasome biogenesis. New work by Yoshida and colleagues reveals a surprising mechanism by which ubiquitination of N-glycosylated Nrf1 controls its function.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
Trends in Biochemical Sciences
Trends in Biochemical Sciences 生物-生化与分子生物学
CiteScore
22.90
自引率
0.70%
发文量
148
审稿时长
6-12 weeks
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.
期刊最新文献
How does p53 work? Regulation by the intrinsically disordered domains. Textbook oxidative phosphorylation needs to be rewritten. ERK-dependent protein phosphorylation in KRAS-mutant cancer: a mix of the expected and surprising. TEX264-mediated selective autophagy directs DNA damage repair. Eph receptor signaling complexes in the plasma membrane.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1