Structural dynamics of the N‐terminal <scp>SH2</scp> domain of <scp>PI3K</scp> in its free and <scp>CD28</scp> ‐bound states-Reference-Cited by-同舟云学术

登录注册会员服务联系我们

Structural dynamics of the N‐terminal SH2 domain of PI3K in its free and CD28 ‐bound states

Published:2022-11-04 Issue:9 Volume:290 Page:2366-2378
ISSN:1742-464X
Container-title:The FEBS Journal
language:en
Short-container-title:The FEBS Journal

Author:

Hosoe Yuhi¹,Miyanoiri Yohei²,Re Suyong³,Ochi Saki¹,Asahina Yuya²,Kawakami Toru²,Kuroda Masataka³⁴,Mizuguchi Kenji²³,Oda Masayuki¹^ORCID

Affiliation:

1. Graduate School of Life and Environmental Sciences Kyoto Prefectural University Japan

2. Institute for Protein Research Osaka University Japan

3. Artificial Intelligence Center for Health and Biomedical Research National Institutes of Biomedical Innovation, Health, and Nutrition Osaka Japan

4. Discovery Technology Laboratories Mitsubishi Tanabe Pharma Corporation Yokohama Japan

Funder

Japan Society for the Promotion of Science

Institute for Protein Research, Osaka University

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1111/febs.16666

Reference54 articles.

1. Src homology-2 domains: Structure, mechanisms, and drug discovery

2. Molecular recognition by SH2 domains

3. Crystal Structures and Thermodynamic Analysis Reveal Distinct Mechanisms of CD28 Phosphopeptide Binding to the Src Homology 2 (SH2) Domains of Three Adaptor Proteins

4. Molecular interactions of the CTLA-4 cytoplasmic region with the phosphoinositide 3-kinase SH2 domains

5. Targeted inhibition of STATs and IRFs as a potential treatment strategy in cardiovascular disease

Cited by 2 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. Structure and Dynamics of Drk-SH2 Domain and Its Site-Specific Interaction with Sev Receptor Tyrosine Kinase;International Journal of Molecular Sciences;2024-06-09

2. Unravelling the complexity of enzyme catalysis;The FEBS Journal;2023-05

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