References
- Verdin E, Ott M. 50 years of protein acetylation: from gene regulation to epigenetics, metabolism and beyond. Nat Rev Mol Cell Biol. 2015;16:258–264.
- Wagner GR, Payne RM. Widespread and enzyme-independent Nε - acetylation and Nε-succinylation of proteins in the chemical conditions of the mitochondrial matrix. J Biol Chem. 2013;288:29036–29045.
- Gil J, Ramírez-Torres A, Encarnación-Guevara S. Lysine acetylation and cancer: a proteomics perspective. J Proteomics. 2017;150:297–309.
- Gil, J Chiappe D, Luna-Peñaloza J, et al. Lysine acetylation stoichiometry and proteomics analyses reveal pathways regulated by sirtuin 1 in human cells. J Biol Chem. 2017;292:18129–18144.
- Irwin, DJ, Cohen TJ, Grossman M, et al. Acetylated tau, a novel pathological signature in Alzheimer’s disease and other tauopathies. Brain. 2012;135:807–818.
- Li L, Yang XJ. Tubulin acetylation: responsible enzymes, biological functions and human diseases. Cell Mol Life Sci. 2015;72:4237–4255.
- Gilks, WP, Abou-Sleiman PM, Gandhi S, et al. A common LRRK2 mutation in idiopathic Parkinson’s disease. Lancet. 2005;365:415–416.
- Law, BMH. A direct interaction between Leucine-rich repeat Kinase 2 and specific beta-tubulin isoforms regulates tubulin acetylation. J Biol Chem. 2014;289:895–908.
- Dompierre JP, Rettinger J, Bhargava Y, et al. Histone deacetylase 6 inhibition compensates for the transport deficit in huntington’s disease by increasing tubulin acetylation. J Neurosci. 2007;27:3571–3583.
- Husain M, Cheung C-Y, Deacetylase H. 6 inhibits influenza A virus release by downregulating the trafficking of viral components to the plasma membrane via its substrate, acetylated microtubules. J Virol. 2014;88:11229–11239.
- Farria A, Li W, Dent SYR. KATs in cancer: functions and therapies. Oncogene. 2015;34:4901–4913.
- Gallo, P, Latronico MV, Gallo P, et al. Inhibition of class I histone deacetylase with an apicidin derivative prevents cardiac hypertrophy and failure. Cardiovasc Res. 2008;80:416–424.
- Kong, Y, Tannous P, Lu G, et al. Suppression of class I and II histone deacetylases blunts pressure-overload cardiac hypertrophy. Circulation. 2006;113:2579–2588.
- Yang Q, Vijayakumar A, Kahn BB. Metabolites as regulators of insulin sensitivity and metabolism. Nat Rev Mol Cell Biol. 2018. DOI:10.1038/s41580-018-0044-8
- Kim HJ, Bae SC. Histone deacetylase inhibitors: molecular mechanisms of action and clinical trials as anti-cancer drugs. Am J Transl Res. 2011;3:166–179.
- Eckschlager, T, Plch J, Stiborova M, et al. Histone deacetylase inhibitors as anticancer drugs. Int J Mol Sci. 2017;18:1–25.
- Narita T, Weinert BT, Choudhary C. Functions and mechanisms of non-histone protein acetylation. Mol Cell Biol. DOI:10.1038/s41580-018-0081-3