Acetylation and deacetylation of non-histone proteins.

By M. Glozak, N. Sengupta, Xiaohong Zhang, E. Seto. Gene, 2005

1,580 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/0f0c8f312b3324ec4e634b7bcd3e499d07da6b19

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. E. Seto
2. PA Marks
3. Xiang-Jiao Yang
4. W. Gu
5. E. Verdin
6. Ricky W. Johnstone
7. John C. Newman
8. Minoru Yoshida

Citations in the corpus

• SIRT5 regulates the mitochondrial lysine succinylome and metabolic networks (2013, positive): “Lysine acetylation is regulated by the competing activities of acetyltransferases, such as p300, and deacetylases, such as the nicotinamide adenine dinucleotide (NAD+)-dependent class III protein deacetylase sirtuins (Glozak et al., 2005).”
• How corticosteroids control inflammation: Quintiles Prize Lecture 2005 (2006, background): “However, therapeutic doses of inhaled corticosteroids have not been shown to increase annexin-1 concentrations in bronchoalveolar lavage fluid (Hall et al., 1999) and an increase in IkB-a has not been shown in most cell types, including epithelial cells (Heck et al., 1997; Newton et al., 1998a).”
• T cell metabolism drives immunity (2015, background): “Protein acetylation is a reversible PTM that influences epigenetic changes mediated by HATs and HDACs and also controls the actions of transcription factors and molecular chaperones (Glozak et al., 2005).”
• Tip60-dependent acetylation of p53 modulates the decision between cell-cycle arrest and apoptosis. (2006, background): “Acetylation of p53 is also reversible in the presence of deacetylases such as HDAC1 and SIRT1 (Luo et al., 2000, 2001), and the dynamic regulation of nonhistone proteins by acetylation and deacetylation is now verified in the studies of many cellular factors (Brooks and Gu, 2003; Glozak et al., 200”
• Lysine acetylation: codified crosstalk with other posttranslational modifications (2008, background): “Acetylation patterns and the mechanistic impact vary from one protein to another (Glozak et al., 2005).”
• β-Hydroxybutyrate (2017, positive): “Many nonhistone proteins, including NF-κB, TP53, MYC, and MYOD1, among others (34), are also subject to HDAC-mediated deacetylation and regulation.”
• Regulation of Inflammation by Short Chain Fatty Acids (2011, background): “By inhibiting the HDAC activity, SCFAs increase the acetylation of histone and non histone proteins including NFκB, MyoD, p53 and N-FAT [57] and, consequently, modulate gene”
• Histone deacetylase inhibitors: molecular mechanisms of action (2007, background): “At least 50 non-histone proteins of known biological function have been identified, which may be acetylated and substrates of HDACs (Table 1) (Glozak et al., 2005; Marks and Dokmanovic, 2005; Rosato and Grant, 2005; Bolden et al., 2006; Minucci and Pelicci, 2006; Zhao et al., 2006).”
• Erasers of histone acetylation: the histone deacetylase enzymes. (2014, background): “Some of the contributions that HDACs play in the development and progression of cancer may also be mediated through deacetylation of nonhistone proteins, including many oncogenes, tumor suppressors, and proteins that regulate tumor cell invasion and metastasis (reviewed by Glozak et al. 2005).”
• Deacetylase inhibition promotes the generation and function of regulatory T cells (2007, background): “HATs and HDACs also regulate the functions of nonhistone protein”