Substrate specificity determinants for casein kinase II as deduced from studies with synthetic peptides.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference37 articles.
1. Role of multiple basic residues in determining the substrate specificity of cyclic AMP-dependent protein kinase.
2. Optimal spatial requirements for the location of basic residues in peptide substrates for the cyclic AMP-dependent protein kinase.
3. Comparison of the substrate specificity of adenosine 3':5'-monophosphate- and guanosine 3':5'-monophosphate-dependent protein kinases. Kinetic studies using synthetic peptides corresponding to phosphorylation sites in histone H2B.
4. Phosphorylation by guanosine 3‘:5‘-monophosphate-dependent protein kinase of synthetic peptide analogs of a site phosphorylated in histone H2B.
5. Studies on the specificity of phosphorylase kinase using peptide substrates.
Cited by 311 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. Discovery of a CK2α′-Biased ATP-Competitive Inhibitor from a High-Throughput Screen of an Allosteric-Inhibitor-Like Compound Library;ACS Chemical Neuroscience;2024-06-22
2. Casein kinase 2 phosphorylates and induces the SALL2 tumor suppressor degradation in colon cancer cells;Cell Death & Disease;2024-03-16
3. Identification of CK2α’ selective inhibitors by the screening of an allosteric-kinase-inhibitor-like compound library;2024-01-22
4. Minor Kinases with Major Roles in Cytokinesis Regulation;Cells;2022-11-17
5. Protein kinase CK2 modulates the activity of Maf-family bZIP transcription factor NRL in rod photoreceptors of mammalian retina;Human Molecular Genetics;2022-10-13
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