Thermal unfolding pathway for the thermostable P22 tailspike endorhamnosidase
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00239a026
Reference50 articles.
1. MUTATIONAL EFFECTS ON PROTEIN STABILITY
2. Tryptophan repressor of Escherichia coli shows unusual thermal stability.
3. Structure and Functions of the Bacteriophage P22 Tail Protein
4. Fine structure genetic and physical map of the phage P22 tail protein gene.
5. Mechanism of head assembly and DNA encapsulation in Salmonella phage P22
Cited by 65 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. Extraction and Characterizations of Viral Protein Particles: A Methodological Study;BioNanoScience;2024-01-09
2. Structural Insights into the Chaperone-Assisted Assembly of a Simplified Tail Fiber of the Myocyanophage Pam3;Viruses;2022-10-14
3. Single Amino Acid Change Mutation in the Hydrophobic Core of the N-terminal Domain of P22 TSP affects the Proteins Stability;2021-12-20
4. The E34 Phage Tailspike Protein: An in vitro characterization, Structure Prediction, Potential Interaction with S. newington LPS and Cytotoxicity Assessment to Animal Cell Line;2021-09-20
5. A genetic analysis of an important hydrophobic interaction at the P22 tailspike protein N-terminal domain;Archives of Virology;2018-03-02
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