Ligand-induced Conformational Shift in the N-terminal Domain of GRP94, an Hsp90 Chaperone
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference47 articles.
1. Structure, function, and mechanism of the Hsp90 molecular chaperone
2. The 90-kDa Molecular Chaperone Family
3. Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability
4. The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains.
5. Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum
Cited by 97 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. Structural transitions modulate the chaperone activities of Grp94;Proceedings of the National Academy of Sciences;2024-03-14
2. Exploring Endoplasmic Reticulum Stress Pathways in Apostichopus Japonicus Under Heat Stress Based on Transcriptome Analysis;2024
3. Exploring Endoplasmic Reticulum Stress Pathways in Apostichopus japonicus Under Heat Stress Based on Transcriptome Analysis;2023-12-29
4. Visualization of conformational transition of GRP94 in solution;Life Science Alliance;2023-11-10
5. Insight into the Nucleotide Based Modulation of the Grp94 Molecular Chaperone Using Multiscale Dynamics;The Journal of Physical Chemistry B;2023-06-09
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