One Citation
Ablation of FUNDC1-dependent mitophagy renders myocardium resistant to paraquat-induced ferroptosis and contractile dysfunction.
- BiologyBiochimica et biophysica acta. Molecular basis of disease
- 2022
References
SHOWING 1-10 OF 142 REFERENCES
Protein histidine methylation.
- Biology, ChemistryCurrent protein & peptide science
- 2020
This review aims to summarize the recent advances in the understanding of the chemical, enzymological and physiological aspects of protein histidine methylation.
Nonhistone Lysine Methylation in the Regulation of Cancer Pathways.
- Biology, ChemistryCold Spring Harbor perspectives in medicine
- 2016
The history and molecular functions of lysine methylation are reviewed, and the large number of candidate methyltransferase and demethylation enzymes whose enzymatic activity is not yet defined and which are potentially associated with cancer through genetic studies are understood.
Protein arginine methyltransferases: promising targets for cancer therapy
- BiologyExperimental & molecular medicine
- 2021
The biological functions of protein arginine methyltransferases in cancer and the current development status of PRMT inhibitors in cancer therapy are discussed.
Protein lysine methylation by seven-β-strand methyltransferases.
- Biology, ChemistryThe Biochemical journal
- 2016
A number of novel 7BS KMTs have now been discovered, and, in particular, several recently characterized human and yeast members of MTase family 16 (MTF16) have been found to methylate lysines in non-histone proteins.
Human METTL20 Is a Mitochondrial Lysine Methyltransferase That Targets the β Subunit of Electron Transfer Flavoprotein (ETFβ) and Modulates Its Activity*
- BiologyThe Journal of Biological Chemistry
- 2014
The present study establishes METTL20 as the first human KMT localized to mitochondria and suggests that it may regulate cellular metabolism through modulating the interaction between its substrate ETFβ and dehydrogenases.
The methyltransferase METTL9 mediates pervasive 1-methylhistidine modification in mammalian proteomes
- Biology, ChemistryNature communications
- 2021
It is reported that METTL9 is a broad-specificity methyltransferase that mediates the formation of the majority of 1MH present in mouse and human proteomes, and the results establishMETTL9-mediated 1MH as a pervasive protein modification, thus setting the stage for further functional studies on protein histidine methylation.
Lysine methylation by the mitochondrial methyltransferase FAM173B optimizes the function of mitochondrial ATP synthase
- Biology, ChemistryThe Journal of Biological Chemistry
- 2018
FAM173B is identified as the long-sought KMT responsible for methylation of ATPSc, a key protein in cellular ATP production, and functional significance of ATP Sc methylation is demonstrated.
Uncovering human METTL12 as a mitochondrial methyltransferase that modulates citrate synthase activity through metabolite-sensitive lysine methylation
- BiologyThe Journal of Biological Chemistry
- 2017
A novel human mitochondrial KMT is uncovered that introduces a methyl modification into a metabolic enzyme and whose activity can be modulated by metabolic cues and should be renamed CS-KMT (gene name CSKMT).
Proteomic Analysis Reveals Diverse Classes of Arginine Methylproteins in Mitochondria of Trypanosomes*
- BiologyMolecular & Cellular Proteomics
- 2012
This study is the first comprehensive analysis of mitochondrial arg methylation in any organism, and represents a significant advance in knowledge of the range of arg methylproteins and their sites of modification.
Human METTL12 is a mitochondrial methyltransferase that modifies citrate synthase
- BiologyFEBS letters
- 2017
It is described that lysine‐368 of human citrate synthase is methylated and that the modifying enzyme, localized in the mitochondrial matrix, is methyltransferase‐like protein 12 (METTL12), a member of the family of 7β‐strand methyltransferases.