Examining the role of phosphorylation of p19INK4d in its stability and ubiquitination using chemical protein synthesis
Author:
Affiliation:
1. Schulich Faculty of Chemistry
2. Technion-Israel Institute of Technology
3. Hailfa 32000
4. Israel
Abstract
This study describes the chemical synthesis of unmodified and phosphorylated p19INK4d that were characterized by circular dichroism and biochemical methods to examine the effect of phosphorylation on the thermal stability and ubiquitination.
Funder
Horizon 2020 Framework Programme
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2020/SC/C9SC06300E
Reference29 articles.
1. Identification of human and mouse p19, a novel CDK4 and CDK6 inhibitor with homology to p16ink4
2. Structure of human cyclin-dependent kinase inhibitor p19INK4d: comparison to known ankyrin-repeat-containing structures and implications for the dysfunction of tumor suppressor p16INK4a
3. INK4 proteins, a family of mammalian CDK inhibitors with novel biological functions
4. The INK4 family of cell cycle inhibitors in cancer
5. Structure of the cyclin-dependent kinase inhibitor p19Ink4d
Cited by 7 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. Multiphosphorylation-Dependent Recognition of Anti-pS2 Antibodies against RNA Polymerase II C-Terminal Domain Revealed by Chemical Synthesis;Journal of the American Chemical Society;2024-04-19
2. CIP/KIP and INK4 families as hostages of oncogenic signaling;Cell Division;2024-04-01
3. Deciphering the Role of the Ser‐Phosphorylation Pattern on the DNA‐Binding Activity of Max Transcription Factor Using Chemical Protein Synthesis;Angewandte Chemie International Edition;2023-09-12
4. Deciphering the Role of the Ser‐Phosphorylation Pattern on the DNA‐Binding Activity of Max Transcription Factor Using Chemical Protein Synthesis;Angewandte Chemie;2023-09-12
5. D‐Peptide and D‐Protein Technology: Recent Advances, Challenges, and Opportunities**;ChemBioChem;2022-11-16
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