Protein methylation in mitochondria

JM Małecki, E Davydova, PØ Falnes - Journal of Biological Chemistry, 2022 - ASBMB
Many proteins are modified by posttranslational methylation, introduced by a number of
methyltransferases (MTases). Protein methylation plays important roles in modulating …

The biological axis of protein arginine methylation and asymmetric dimethylarginine

MD Fulton, T Brown, YG Zheng - International journal of molecular …, 2019 - mdpi.com
Protein post-translational modifications (PTMs) in eukaryotic cells play important roles in the
regulation of functionalities of the proteome and in the tempo-spatial control of cellular …

Chemical probes and methods for the study of protein arginine methylation

T Brown, T Nguyen, B Zhou, YG Zheng - RSC Chemical Biology, 2023 - pubs.rsc.org
Protein arginine methylation is a widespread post-translational modification (PTM) in
eukaryotic cells. This chemical modification in proteins functionally modulates diverse …

[PDF][PDF] The Dictyostelium model for mitochondrial biology and disease

XG Pearce, SJ Annesley… - The International Journal of …, 2019 - scholar.archive.org
The unicellular slime mould Dictyostelium discoideum is a valuable eukaryotic model
organism in the study of mitochondrial biology and disease. As a member of the …

Exceptionally versatile–arginine in bacterial post-translational protein modifications

J Lassak, F Koller, R Krafczyk, W Volkwein - Biological Chemistry, 2019 - degruyter.com
Post-translational modifications (PTM) are the evolutionary solution to challenge and extend
the boundaries of genetically predetermined proteomic diversity. As PTMs are highly …

A conserved arginine residue is critical for stabilizing the N2 FeS cluster in mitochondrial complex I

MA Hameedi, DN Grba, KH Richardson… - Journal of Biological …, 2021 - ASBMB
Respiratory complex I (NADH: ubiquinone oxidoreductase), the first enzyme of the electron-
transport chain, captures the free energy released by NADH oxidation and ubiquinone …

Effects of methylation of arginine residue 83 on the enzymatic activity of human arsenic (+ 3 oxidation state) methyltransferase

D Sumi, Y Nakamura, H Taguchi, Y Okamoto… - Toxicology in Vitro, 2023 - Elsevier
Abstract Arsenic (+ 3 oxidation state) methyltransferase is an enzyme responsible for arsenic
methylation, and it requires S-adenosyl-methionine (SAM) as a coenzyme. We here …

In Silico Identification and Characterization of a Hypothetical Protein From Rhodobacter capsulatus Revealing S-Adenosylmethionine-Dependent Methyltransferase …

SM Mondol, D Das, DM Priom… - … and Biology Insights, 2022 - journals.sagepub.com
Rhodobacter capsulatus is a purple non-sulfur bacteria widely used as a model organism to
study bacterial photosynthesis. It exhibits extensive metabolic activities and demonstrates …

Comprehensive transcriptomic analysis and machine learning reveal unique gene expression profiles in patients with immune‐mediated necrotizing myopathy

H Liu, L Deng, Y Guo, H Liu, B Chen… - The Journal of Gene …, 2024 - Wiley Online Library
Background Immune‐mediated necrotizing myopathy (IMNM) is an autoimmune myopathy
characterized by severe proximal weakness and muscle fiber necrosis, yet its pathogenesis …

[PDF][PDF] Mechanistic investigations of protein arginine N-methyltransferases and elucidation of their implications in the yeast stress response

J Brown - 2021 - open.library.ubc.ca
Protein arginine N-methyltransferases (PRMTs) catalyze the transfer of methyl groups from
the methyl donor S-adenosyl-L-methionine (SAM) to polypeptide substrates. PRMTs are …