Interaction between the C-terminal domains of measles virus nucleoprotein and phosphoprotein: A tight complex implying one binding site-Reference-Cited by-同舟云学术

登录注册会员服务联系我们

Interaction between the C-terminal domains of measles virus nucleoprotein and phosphoprotein: A tight complex implying one binding site

Published:2012-09-17 Issue:10 Volume:21 Page:1577-1585
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Blocquel David,Habchi Johnny,Costanzo Stéphanie,Doizy Anthony,Oglesbee Michael,Longhi Sonia

Funder

Agence Nationale de la Recherche (Physico-Chimie du Vivant)

Direction Générale de l'Armement (DGA) and the CNRS

French-Italian University and the Direction Générale de l'Enseignement Supérieur et l'Insertion Professionnelle (DGESIP)

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.2138/fullpdf

Reference45 articles.

1. Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein;Johansson;J Biol Chem,2003

2. The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded;Bourhis;Protein Sci,2005

3. Assessing induced folding of an intrinsically disordered protein by site-directed spin-labeling EPR spectroscopy;Morin;J Phys Chem B,2006

4. Mapping alpha-helical induced folding within the intrinsically disordered C-terminal domain of the measles virus nucleoprotein by site-directed spin-labeling EPR spectroscopy;Belle;Proteins,2008

5. Interaction between the C-terminal domains of N and P proteins of measles virus investigated by NMR;Bernard;FEBS Lett,2009

Cited by 15 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. Distance-Based Metrics for Comparing Conformational Ensembles of Intrinsically Disordered Proteins;Biophysical Journal;2020-06

2. Distance-based metrics for comparing conformational ensembles of intrinsically disordered proteins;2020-04-07

3. Dissecting the Energetics of Intrinsically Disordered Proteins via a Hybrid Experimental and Computational Approach;The Journal of Physical Chemistry B;2019-11-08

4. Probing the dynamic properties of two sites simultaneously in a protein–protein interaction process: a SDSL-EPR study;Physical Chemistry Chemical Physics;2019

5. Partner-Mediated Polymorphism of an Intrinsically Disordered Protein;Journal of Molecular Biology;2018-08

同舟云学术

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