Nucleoside protein arginine methyltransferase 5 (PRMT5) inhibitors
Author:
Publisher
Elsevier BV
Subject
Organic Chemistry,Clinical Biochemistry,Drug Discovery,Pharmaceutical Science,Molecular Biology,Molecular Medicine,Biochemistry
Reference48 articles.
1. Crystal structure of the human PRMT5:MEP50 complex;Antonysamy;Proc Natl Acad Sci USA,2012
2. Human SWI/SNFassociated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes;Pal;Mol Cell Biol,2004
3. Role of pICLn in methylation of Sm proteins by PRMT5;Pesiridis;J Biol Chem,2009
4. Application of machine learning methods to histone methylation ChIP-Seq data reveals H4R3me2 globally represses gene expression;Xu;BMC Bioinf,2010
5. Arginine methylation: the coming of age;Blanc;Mol Cell,2017
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1. Overview of the development of protein arginine methyltransferase modulators: Achievements and future directions;European Journal of Medicinal Chemistry;2024-03
2. Structure-based discovery of a new series of nucleoside-derived ring-opening PRMT5 inhibitors;European Journal of Medicinal Chemistry;2024-03
3. PRMT5 inhibition drives therapeutic vulnerability to combination treatment with BCL-2 inhibition in mantle cell lymphoma;Blood Advances;2023-10-13
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5. Targeting Arginine Methyltransferase PRMT5 for Cancer Therapy: Updated Progress and Novel Strategies;Journal of Medicinal Chemistry;2023-06-27
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