Charles Brobbey
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Charles Brobbey has a total of 3 co-authors. Here are the top co-authors by number of shared publications:
- Liu Liu
Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC 29425, USA
1 shared publication - Shasha Yin
Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC 29425, USA
1 shared publication - Wenjian Gan
Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, USA
1 shared publication
Latest Publications
- Open Access
- 29 August 2022
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 23 (17) , 9780
The Role of Protein Arginine Methyltransferases in DNA Damage Response
In response to DNA damage, cells have developed a sophisticated signaling pathway, consisting of DNA damage sensors, transducers, and effectors, to ensure efficient and proper repair of damaged DNA. During this process, posttranslational modifications (PTMs) are central events that modulate the recruitment, dissociation, and activation of DNA repair proteins at damage sites. Emerging evidence reveals that protein arginine methylation is one of the common PTMs and plays critical roles in DNA damage response. Protein arginine methyltransferases (PRMTs) either directly methylate DNA repair proteins or deposit methylation marks on histones to regulate their transcription, RNA splicing, protein stability, interaction with partners, enzymatic activities, and localization. In this review, we summarize the substrates and roles of each PRMTs in DNA damage response and discuss the synergistic anticancer effects of PRMTs and DNA damage pathway inhibitors, providing insight into the significance of arginine methylation in the maintenance of genome integrity and cancer therapies.
- 29 August 2022
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 23 (17) , 9780
Open AccessThe Role of Protein Arginine Methyltransferases in DNA Damage Response
In response to DNA damage, cells have developed a sophisticated signaling pathway, consisting of DNA damage sensors, transducers, and effectors, to ensure efficient and proper repair of damaged DNA. During this process, posttranslational modifications (PTMs) are central events that modulate the recruitment, dissociation, and activation of DNA repair proteins at damage sites. Emerging evidence reveals that protein arginine methylation is one of the common PTMs and plays critical roles in DNA damage response. Protein arginine methyltransferases (PRMTs) either directly methylate DNA repair proteins or deposit methylation marks on histones to regulate their transcription, RNA splicing, protein stability, interaction with partners, enzymatic activities, and localization. In this review, we summarize the substrates and roles of each PRMTs in DNA damage response and discuss the synergistic anticancer effects of PRMTs and DNA damage pathway inhibitors, providing insight into the significance of arginine methylation in the maintenance of genome integrity and cancer therapies.