RGS4 and RGS5 are in vivo substrates of the N-end rule pathway
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference24 articles.
1. In Vivo Half-Life of a Protein Is a Function of Its Amino-Terminal Residue
2. Alternative Splicing Results in Differential Expression, Activity, and Localization of the Two Forms of Arginyl-tRNA-Protein Transferase, a Component of the N-End Rule Pathway
3. An Essential Role of N-Terminal Arginylation in Cardiovascular Development
4. G Protein Pathways
5. RGS4 Is Arginylated and Degraded by the N-end Rule Pathway in Vitro
Cited by 223 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. N-degron pathways;Proceedings of the National Academy of Sciences;2024-09-12
2. The enzymatic oxygen sensor cysteamine dioxygenase binds its protein substrates through their N-termini;Journal of Biological Chemistry;2024-09
3. Arginyltransferase 1 (ATE1)-mediated proteasomal degradation of viral haemagglutinin protein: a unique host defence mechanism;Journal of General Virology;2024-08-29
4. Top-down Proteomics for the Characterization and Quantification of Calreticulin Arginylation;2024-08-08
5. Oligomerization and a distinct tRNA-binding loop are important regulators of human arginyl-transferase function;Nature Communications;2024-07-28
1.学者识别学者识别
2.学术分析学术分析
3.人才评估人才评估
"同舟云学术"是以全球学者为主线，采集、加工和组织学术论文而形成的新型学术文献查询和分析系统，可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容，当前同舟云学术共收录了国内外主流学术期刊6万余种，收集的期刊论文及会议论文总量共计约1.5亿篇，并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询！咨询电话：010-8811{复制后删除}0370
www.globalauthorid.com
TOP
Copyright © 2019-2024 北京同舟云网络信息技术有限公司 京公网安备11010802033243号 京ICP备18003416号-3