Global ETD Search

Kinetic Characterization, Inhibition, and Activity-Based Protein Profiling of Protein Arginine Methyltransferase 1

Obianyo, Obiamaka

<p>Protein arginine methyltransferases (PRMTs) are SAM-dependent enzymes that catalyze the mono- and di-methylation of peptidyl arginine residues. Although all PRMTs produce mono-methyl arginine (MMA), type I PRMTs go on to form asymmetrically dimethylated arginine (ADMA), while type II enzymes …

south-carolina Repository record for Kinetic Characterization, Inhibition, and Activity-Based Protein Profiling of Protein Arginine Methyltransferase 1 (opens in a new tab)

TARGETING TYPE-I PRMTS RESTORES PLATINUM SENSITIVITY IN OVARIAN CARCINOMA THROUGH MITOCHONDRIAL METABOLISM

MONDAL, AYUSIUniversità degli Studi di Milano2025

… platinum-induced genotoxic stress, type-I protein arginine methyltransferases–mediated post-translational modifications, and mitochondrial metabolic plasticity underpinning chemoresistance in EOC. We present an integrative multi-omics analysis of carboplatin-resistant A2780 ovarian cancer …

milano Repository record for TARGETING TYPE-I PRMTS RESTORES PLATINUM SENSITIVITY IN OVARIAN CARCINOMA THROUGH MITOCHONDRIAL METABOLISM (opens in a new tab)

Development of Novel Methods and Their Utilization in the Analysis of the Effect of the N-Terminus of Human Protein Arginine Methyltransferase 1 Variant 1 on Enzymatic Activity, Protein-Protein Interactions, and Substrate Specificity

Suh-Lailam, Brenda Bienka

utahstate Repository record for Development of Novel Methods and Their Utilization in the Analysis of the Effect of the N-Terminus of Human Protein Arginine Methyltransferase 1 Variant 1 on Enzymatic Activity, Protein-Protein Interactions, and Substrate Specificity (opens in a new tab)