Multitude of binding modes attainable by intrinsically disordered proteins: a portrait gallery of disorder-based complexes
Author:
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2011/CS/C0CS00057D
Reference119 articles.
1. Dynamic equilibrium engagement of a polyvalent ligand with a single-site receptor
2. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
3. Why are ?natively unfolded? proteins unstructured under physiologic conditions?
4. What does it mean to be natively unfolded?
Cited by 230 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. The Disorderly Nature of Caliciviruses;Viruses;2024-08-19
2. Exploring Intrinsic Disorder in Human Synucleins and Associated Proteins;International Journal of Molecular Sciences;2024-08-01
3. Intrinsic Disorder in the Host Proteins Entrapped in Rabies Virus Particles;Viruses;2024-06-04
4. Structural insights into the disulfide isomerase and chaperone activity of TrbB of the F plasmid type IV secretion system;Current Research in Structural Biology;2024
5. Probing excited state 1Hα chemical shifts in intrinsically disordered proteins with a triple resonance-based CEST experiment: Application to a disorder-to-order switch;Methods;2023-10
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