SIRT4 is the last puzzle of mitochondrial sirtuins
- 19 July 2018
- journal article
- review article
- Published by Elsevier BV in Bioorganic & Medicinal Chemistry
- Vol. 26 (14), 3861-3865
- https://doi.org/10.1016/j.bmc.2018.07.031
Abstract
No abstract availableKeywords
Funding Information
- National Natural Science Foundation of China (21662010)
- Innovation Team of Natural Science Foundation of Department of Education of Guizhou Province ([2015]57)
- Natural Science Foundation of Department of Education of Guizhou Province ([2015]371)
This publication has 40 references indexed in Scilit:
- Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathwaysProceedings of the National Academy of Sciences of the United States of America, 2013
- Lysine Succinylation and Lysine Malonylation in HistonesMolecular & Cellular Proteomics, 2012
- The First Identification of Lysine Malonylation Substrates and Its Regulatory EnzymeMolecular & Cellular Proteomics, 2011
- Sirt5 Is a NAD-Dependent Protein Lysine Demalonylase and DesuccinylaseScience, 2011
- Plasmodium falciparum Sir2A Preferentially Hydrolyzes Medium and Long Chain Fatty Acyl LysineACS Chemical Biology, 2011
- Identification of lysine succinylation as a new post-translational modificationNature Chemical Biology, 2010
- SIRT5 Deacetylates Carbamoyl Phosphate Synthetase 1 and Regulates the Urea CycleCell, 2009
- Mammalian Sir2 Homolog SIRT3 Regulates Global Mitochondrial Lysine AcetylationMolecular and Cellular Biology, 2007
- A Mitochondrial Paradigm of Metabolic and Degenerative Diseases, Aging, and Cancer: A Dawn for Evolutionary MedicineAnnual Review of Genetics, 2005
- Phylogenetic Classification of Prokaryotic and Eukaryotic Sir2-like ProteinsBiochemical and Biophysical Research Communications, 2000