Acetylation: a regulatory modification to rival phosphorylation?
By Tony Kouzarides. EMBO Journal, 2000
1,209 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/a9088eb3ae6cde76290ed0992ffa88022c17f034
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Citations in the corpus
- HDAC6 is a microtubule-associated deacetylase (2002, background): “Furthermore, there are also cytoplasmic proteins that are subject to modification by acetylation (reviewed in ref”
- p300/CBP and cancer (2004, background): “This has led to the suggestion that acetylation of nonhistone proteins is an important post-translation modification, analogous to phosphorylation (Kouzarides, 2000).”
- Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation. (2003, background): “Acetylation Nearly 40 years ago, acetylation was shown to be an important modification of histones that correlated with increased transcriptional activity [55].”
- The many roles of histone deacetylases in development and physiology: implications for disease and therapy (2009, background): “Direct acetylation and deacetylation of transcription factors has also been shown to have positive and negative consequences on gene transcription, respectivel”
- Histone acetylation: a switch between repressive and permissive chromatin (2002, background): “Following the ‘classical’ route of signal transduction, histone acetyltransferase activity may be activated or repressed by phosphorylation or acetylation (Cheung et al., 2000a; Kouzarides, 2000).”
- Overview of Nomenclature of Nuclear Receptors (2006, background): “…types of modification, such as acetylation, SUMOylation, ubiquitinylation and methylation, have been reported to modulate the functions of NRs, potentially constituting an important cellular integration mechanism (Kouzarides, 2000; Wang et al., 2001a; Fu et al., 2002; Perissi and Rosenfeld, 2005).”
- Histone deacetylases and cancer: causes and therapies (2001, background): “The modification of the structure of these N-terminal tails of histones — by acetylation/deacetylation — is crucial in modulating gene expression, as it affects the interaction of DNA with transcription-regulatory non-nucleosomal protein complexe”
- Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis. (2004, background): “Indeed, it has been suggested that regulatory acetylation/deacetylation is considerably more widespread than presently appreciated, acting in a manner similar to phosphorylation and dephosphorylation.(16) HDACs have recently enjoyed increased attention because HDAC inhibitors (e.”
- Post-translational modifications in signal integration (2010, background): “Furthermore, acetylation of transcription factors such as p53 and E2F1 increases binding to DN”
- Acetylation of the C terminus of Ku70 by CBP and PCAF controls Bax-mediated apoptosis. (2004, background): “Molecular Cell, Vol. 13, 627–638, March 12, 2004, Copyright 2004 by Cell Press Acetylation of the C Terminus of Ku70 by CBP and PCAF Controls Bax-Mediated Apoptosis Kouzarides, 2000; Liu et al., 1999).”
- Histone Recognition and Large-Scale Structural Analysis of the Human Bromodomain Family (2012, background): “Acetylation has a profound 214 Cell 149, 214–231, March 30, 2012 ª2012 Elsevier Inc. effect on the physiochemical properties of modified lysine residues neutralizing the positive charge of the ε-amino group (Kouzarides, 2000).”