Histone acetyltransferases.

By S. Roth, J. Denu, C. D. Allis. Annual Review of Biochemistry, 2001

1,469 citations recorded by the source corpus.

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Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation. (2002, background): “In general, acetylation of core histone tails correlates with the opening of the chromatin structure to allow transcription to occur (for review, see Roth et al. 2001).”
Histone acetylation: a switch between repressive and permissive chromatin (2002, background): “These principles are not only at the heart of transcriptional regulation but are also likely to govern other processes involving chromatin substrates, including replication, site-specific recombination and DNA repair (Wolffe and Hayes, 1999; Roth et al., 2001).”
How corticosteroids control inflammation: Quintiles Prize Lecture 2005 (2006, background): “This results in acetylation of core histones, thereby reducing their charge which allows the chromatin structure to transform from the resting closed conformation to an activated open form (Roth et al., 2001) (Figure 1).”
Nuclear retinoid receptors and the transcription of retinoid-target genes. (2004, methodology): “Then the opening of the chromatin environment is achieved by the recruitment through pCIP and CBP, of larger complexes with histone acetyltransferase (PCAF) or histone methyltransferase activities (Kouzarides, 2000; Roth et al., 2001; Zhang and Reinberg, 2001).”
HATs and HDACs: from structure, function and regulation to novel strategies for therapy and prevention (2007, background): “There are three major families of HATs: general control non-derepressible 5 (Gcn5)-related N-acetyltransferases (GNATs), p300/CBP and MYST proteins (reviewed by Sterner and Berger, 2000; Roth et al., 2001; Lee and Workman, 2007).”
Histone Deacetylases 5 and 9 Govern Responsiveness of the Heart to a Subset of Stress Signals and Play Redundant Roles in Heart Development (2004, neutral): “structure and consequent transcriptional activation (13, 37).”
Genome-wide mapping of HATs and HDACs reveals distinct functions in active and inactive genes (2009, background): “HATs Are Enriched in Active Genes and Correlated with Gene Expression CBP and p300 are structurally highly homologous and functionally redundant (Roth et al., 2001).”
Histone deacetylases 1 and 2 redundantly regulate cardiac morphogenesis, growth, and contractility. (2007, background): “Acetylation results in a loss of positive charge, relaxing chromatin structure and allowing access of transcription factors to their target genes (Roth et al. 2001).”
Distinct roles of GCN5/PCAF‐mediated H3K9ac and CBP/p300‐mediated H3K18/27ac in nuclear receptor transactivation (2011, methodology): “However, it remains to be established whether the increased histone acetylations are a cause or a consequence of the increased transcription in mammalian cells (Roth et al, 2001).”
Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. (2004, background): “While acetylation is generally early studies suggested the possibility that histone decorrelated with active transcription (Roth et al., 2001), methylases may exist, but the molecular identities of histone methylation is linked to both transcriptional acti- these putative histone demethylases have…”
Mechanisms of diabetic complications. (2013, background): “Conversely, histone deacetylases (HDACs) remove lysine acetylation and in general oppose the actions of HATs as components of repressor complexes (310, 502).”
Circadian regulator CLOCK is a histone acetyltransferase. (2006, positive): “In support of this notion, a wide variety of nuclear proteins involved in transcriptional control have been demonstrated to possess intrinsic histone acetyltransferase (HAT) activity (Kouzarides, 1999; Roth et al., 2001; Sterner and Berger, 2000).”
An epigenetic road map for histone lysine methylation (2003, background): “Acetylation (Roth et al., 2001) and arginine methylation (Stallcup, 2001) have been linked mainly with transcriptional stimulation.”
Sirtuins in aging and age-related disease. (2006, background): “It has been known for four decades that histones can be acetylated (Roth et al., 2001), although the enzymes that acetylate and deacetylate lysine residues on histones and other proteins have only been discovered more recently.”