Plasmodium falciparum heat shock protein 70 is able to suppress the thermosensitivity of an Escherichia coli DnaK mutant strain
Author:
Publisher
Springer Science and Business Media LLC
Subject
Genetics,Molecular Biology,General Medicine
Link
http://link.springer.com/content/pdf/10.1007/s00438-005-1150-9.pdf
Reference47 articles.
1. Banecki B, Zylicz M, Bertoli E, Tanfani F (1992) Structural and functional relationships in DnaK and DnaK756 heat-shock proteins from Escherichia coli. J Biol Chem 267:25051–25058
2. Banumathy G, Singh V, Pavithra SR, Tatu U (2003) Heat shock protein 90 is essential for Plasmodium falciparum growth in human erythrocytes. J Biol Chem 278:18336–18345
3. Biswas S, Sharma YD (1994) Enhanced expression of Plasmodium falciparum heat shock protein PFHSP70-1 at higher temperatures and parasite survival. FEMS Microbiol Lett 124:425–430
4. Buchberger A, Gassler CS, Buttner M, McMacken R, Bukau B (1999) Functional defects of the DnaK756 mutant chaperone of Escherichia coli indicate distinct roles for amino- and carboxyl-terminal residues in substrate and co-chaperone interaction and interdomain communication. J Biol Chem 274:38017–38026
5. Bukau B, Horwich AL (1998) The Hsp70 and Hsp60 chaperone machines. Cell 92:351–366
Cited by 62 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. Proteostasis is a key driver of the pathogenesis in Apicomplexa;Biochimica et Biophysica Acta (BBA) - Molecular Cell Research;2024-12
2. Swapping the linkers of canonical Hsp70 and Hsp110 chaperones compromises both self-association and client selection;Heliyon;2024-05
3. <em>Escherichia coli</em>-based Complementation Assay to Study the Chaperone Function of Heat Shock Protein 70;Journal of Visualized Experiments;2024-03-08
4. Insertion of GGMP repeat residues of Plasmodium falciparum Hsp70-1 in the lid of DnaK adversely impacts client recognition;International Journal of Biological Macromolecules;2024-01
5. Swapping the Linkers of Canonical Hsp70 and Hsp110 Chaperones Compromises Both Self-Association and Client Selection;2024
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