Histone acetylation and deacetylation

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a central metabolic intermediate that is also the acetyl donor in histone acetylation. Glucose is converted to acetyl-CoA by the pyruvate dehydrogenase complex (PDC), which produces acetyl-CoA from glucose-derived pyruvate; and by adenosine triphosphate-citrate lyase (ACLY), which generates acetyl-CoA from glucose-derived citrate. PDC and ACLY activity depend on glucose availability, which thereby influences histone acetylation and consequently modulates gene expression and cell cycle progression. Dysregulation of ACLY and PDC contributes to metabolic reprogramming and promotes the development of multiple cancers. At the same time, glucose metabolism maintains the NAD+/NADH ratio, and NAD+ participates in SIRT-mediated histone deacetylation. SIRT enzyme activity is altered in various malignancies, and inhibiting SIRT6, a histone deacetylase that acts on acetylated H3K9 and H3K56, promotes tumorigenesis. SIRT7, which deacetylates H3K18 and thereby represses transcription of target genes, is activated in cancer to stabilize cells in the transformed state. Nutrients appear to modulate SIRT activity. For example, long-chain fatty acids activate the deacetylase function of SIRT6, and this may affect histone acetylation.

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structural changes at their specific points, but can cause many structural changes in distant locations which inevitably affects function. As the chromosome is replicated, the modifications that exist on the parental chromosomes are handed down to daughter chromosomes. The modifications, as part of their function, can recruit enzymes for their particular function and can contribute to the continuation of modifications and their effects after replication has taken place. It has been shown that, even past one replication, expression of genes may still be affected many cell generations later. A study showed that, upon inhibition of HDAC enzymes by Trichostatin A, genes inserted next to centric heterochromatin showed increased expression. Many cell generations later, in the absence of the inhibitor, the increased gene expression was still expressed, showing modifications can be carried through many replication processes such as mitosis and meiosis.

145: 263:. Major features of the GNAT family include HAT domains approximately 160 residues in length and a conserved bromodomain that has been found to be an acetyl-lysine targeting motif. Gcn5 has been shown to acetylate substrates when it is part of a complex. Recombinant Gcn5 has been found to be involved in the acetylation of the H3 histones of the nucleosome. To a lesser extent, it has been found to also acetylate H2B and H4 histones when involved with other complexes. PCAF has the ability to act as a HAT protein and acetylate histones, it can acetylate non-histone proteins related to transcription, as well as act as a coactivator in many processes including 212:

association, leading to weaker binding of the nucleosomal components. By doing this, the DNA is more accessible and leads to more transcription factors being able to reach the DNA. Thus, acetylation of histones is known to increase the expression of genes through transcription activation. Deacetylation performed by HDAC molecules has the opposite effect. By deacetylating the histone tails, the DNA becomes more tightly wrapped around the histone cores, making it harder for transcription factors to bind to the DNA. This leads to decreased levels of gene expression and is known as gene silencing.

804:, the acetylation of histones can attract proteins to elongated chromatin that has been marked by acetyl groups. It has been hypothesized that the histone tails offer recognition sites that attract proteins responsible for transcriptional activation. Unlike histone core proteins, histone tails are not part of the nucleosome core and are exposed to protein interaction. A model proposed that the acetylation of H3 histones activates gene transcription by attracting other transcription related complexes. Therefore, the acetyl mark provides a site for protein recognition where 825:

cores can be interpreted by transcription factors and complexes which leads to functional implications. This process is facilitated by enzymes such as HATs and HDACs that add or remove modifications on histones, and transcription factors that process and "read" the modification codes. The outcome can be activation of transcription or repression of a gene. For example, the combination of acetylation and phosphorylation have synergistic effects on the chromosomes overall structural condensation level and, hence, induces transcription activation of

641:. HDACs 4 and 5 have been found to most closely resemble each other while HDAC7 maintains a resemblance to both of them. There have been three discovered variants of HDAC9 including HDAC9a, HDAC9b and HDAC9c/HDRP, while more have been suspected. The variants of HDAC9 have been found to have similarities to the rest of the Class IIA HDACs. For HDAC9, the splicing variants can be seen as a way of creating a "fine-tuned mechanism" for differentiation expression levels in the cell. Different cell types may take advantage and utilize different 315:. HAT domains for this family are approximately 250 residues which include cysteine-rich, zinc binding domains as well as N-terminal chromodomains. The MYST proteins Esa1, Sas2 and Sas3 are found in yeast, MOF is found in Drosophila and mice while Tip60, MOZ, MORF, and HBO1 are found in humans. Tip60 has roles in the regulation of gene transcription, HBO has been found to impact the DNA replication process, MORF is able to acetylate free histones (especially H3 and H4) as well as nucleosomal histones. 20: 723:, meaning this HDAC is prone to degradation. HDAC10 has two catalytic domains as well. One active domain is located in the N-terminus and a putative catalytic domain is located in the C-terminus along with an NES domain. Two putative Rb-binding domains have also been found on HDAC10 which shows it may have roles in the regulation of the cell cycle. Two variants of HDAC10 have been found, both having slight differences in length. HDAC6 is the only HDAC to be shown to act on 731:. It is mostly found in the cytoplasm but has been known to be found in the nucleus, complexed together with HDAC11. HDAC10 has been seen to act on HDACs 1, 2, 3 (or SMRT), 4, 5 and 7. Some evidence has been shown that it may have small interactions with HDAC6 as well. This leads researchers to believe that HDAC10 may function more as a recruiter rather than a factor for deacetylation. However, experiments conducted with HDAC10 did indeed show deacetylation activity. 777:. Histone modification is now considered a major regulatory mechanism that is involved in many different stages of genetic functions. Our current understanding is that acetylated lysine residues on histone tails is associated with transcriptional activation. In turn, deacetylated histones are associated with transcriptional repression. In addition, negative correlations have been found between several histone acetylation marks. 511:) leads to increased deacetylase activity, but degrades complex formation between HDACs 1 and 2 and between HDAC1 and mSin3A/YY1. A lower than normal amount of phosphorylation (hypophosphorylation) leads to a decrease in the amount of deacetylase activity, but increases the amount of complex formation. Mutation studies found that major phosphorylation happens at residues 225: 793:. Repression of gene transcription is achieved by the reverse of this mechanism. The acetyl group is removed by one of the HDAC enzymes during deacetylation, allowing histones to interact with DNA more tightly to form compacted nucleosome assembly. This increase in the rigid structure prevents the incorporation of transcriptional machinery, effectively 1163:. Current studies indicate that inhibitors of the HDAC family have therapeutic benefits in a wide range of neurological and psychiatric disorders. Many neurological disorders only affect specific brain regions; therefore, understanding of the specificity of HDACs is still required for further investigations for improved treatments. 515:

and Ser. Indeed, when these residues were mutated, a drastic reduction was seen in the amount of deacetylation activity. This difference in the state of phosphorylation is a way of keeping an optimal level of phosphorylation to ensure there is no over or under expression of deacetylation. HDACs 1 and

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Carbon source availability is reflected in histone acetylation in cancer. Glucose and glutamine are the major carbon sources of most mammalian cells, and glucose metabolism is closely related to histone acetylation and deacetylation. Glucose availability affects the intracellular pool of acetyl-CoA,

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in order to modify long-term gene expression. The acetylation pattern is regulated by HAT and HADC enzymes and, in turn, sets the local chromatin structure. In this way, acetylation patterns are transmitted and interconnected with protein binding ability and functions in subsequent cell generation.

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has been shown to be related to HDACs 3 and 8, but its overall sequence is quite different from the other HDACs, leading it to be in its own category. HDAC11 has a catalytic domain located in its N-terminus. It has not been found incorporated in any HDAC complexes such as Nurd or SMRT which means it

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factors must be utilized by HDAC3 in order to activate it. Upon doing so, it gains the ability to co-precipitate with HDACs 4, 5, and 7. HDAC3 can also be found complexed together with HDAC-related protein (HDRP). HDACs 1 and 3 have been found to mediate Rb-RbAp48 interactions which suggests that it

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Histone Acetyltransferases, also known as HATs, are a family of enzymes that acetylate the histone tails of the nucleosome. This, and other modifications, are expressed based on the varying states of the cellular environment. Many proteins with acetylating abilities have been documented and, after a

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of the DNA and extend through the double helix, which leaves them open for modifications involved in transcriptional activation. Acetylation has been closely associated with increases in transcriptional activation while deacetylation has been linked with transcriptional deactivation. These reactions

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and have a significance in regulating gene expression. Structural analysis of transcription factors has shown that highly conserved bromodomains are essential for protein to bind to acetylated lysine. This suggests that specific histone site acetylation has a regulatory role in gene transcriptional

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in muscle control differentiation as well as cellular hypertrophy in muscle and cartilage tissues. HDACs 5 and 7 have been shown to work in opposition to HDAC4 during muscle differentiation regulation so as to keep a proper level of expression. There has been evidence that these HDACs also interact

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has been found to be most similar to HDAC3. Its major feature is its catalytic domain which contains an NLS region in the center. Two transcripts of this HDAC have been found which include a 2.0kb transcript and a 2.4kb transcript. Unlike the other HDAC molecules, when purified, this HDAC showed to

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MOZ (Monocytic Leukemia Zinc Finger Protein), Ybf2/Sas3, Sas2 and Tip60 (Tat Interacting Protein) all make up MYST, another well known family that exhibits acetylating capabilities. This family includes Sas3, essential SAS-related acetyltransferase (Esa1), Sas2, Tip60, MOF, MOZ, MORF, and HBO1. The

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histones. This protein complex forms a cylindrical shape that dsDNA wraps around with approximately 147 base pairs. Nucleosomes are formed as a beginning step for DNA compaction that also contributes to structural support as well as serves functional roles. These functional roles are contributed by

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In rodent models, many agents causing addiction, including tobacco smoke products, alcohol, cocaine, heroin and methamphetamine, cause DNA damage in the brain. During repair of DNA damages some individual repair events may alter the acetylations of histones at the sites of damage, or cause other

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factors in the nucleus. Absence of the HDAC3 enzyme has shown to lead to inactivity which makes researchers believe that HDACs 4, 5 and 7 help the incorporation of DNA-binding recruiters for the HDAC3-containing HDAC complexes located in the nucleus. When HDAC4 is knocked out in mice, they suffer

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of the HDAC9 enzyme allowing for different forms of regulation. HDACs 4, 5 and 7 have their catalytic domains located in the C-terminus along with an NLS region while HDAC9 has its catalytic domain located in the N-terminus. However, the HDAC9 variant HDAC9c/HDRP lacks a catalytic domain but has a

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hypothesis suggests the idea that patterns of post-translational modifications on histones, collectively, can direct specific cellular functions. Chemical modifications of histone proteins often occur on particular amino acids. This specific addition of single or multiple modifications on histone

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Acetylation has the effect of changing the overall charge of the histone tail from positive to neutral. Nucleosome formation is dependent on the positive charges of the H4 histones and the negative charge on the surface of H2A histone fold domains. Acetylation of the histone tails disrupts this

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make up the next family of HATs. This family of HATs contain HAT domains that are approximately 500 residues long and contain bromodomains as well as three cysteine-histidine rich domains that help with protein interactions. These HATs are known to acetylate all of the histone subunits in the

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Shown in this illustration, the dynamic state of histone acetylation/deacetylation regulated by HAT and HDAC enzymes. Acetylation of histones alters accessibility of chromatin and allows DNA binding proteins to interact with exposed sites to activate gene transcription and downstream cellular

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Acetylated histones, the octomeric protein cores of nucleosomes, represent a type of epigenetic marker within chromatin. Studies have shown that one modification has the tendency to influence whether another modification will take place. Modifications of histones can not only cause secondary

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are in the first class of HDACs are most closely related to one another. By analyzing the overall sequences of both HDACs, their similarity was found to be approximately 82% homologous. These enzymes have been found to be inactive when isolated which led to the conclusion that they must be

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Substance Abuse and Mental Health Services Administration, Results from the 2013 National Survey on Drug Use and Health: Summary of National Findings, NSDUH Series H-48, HHS Publication No. (SMA) 14-4863. Rockville, MD: Substance Abuse and Mental Health Services Administration,

711:. These two HDACs are most closely related to each other in overall sequence. However, HDAC6's catalytic domain is most similar to HDAC9. A unique feature of HDAC6 is that it contains two catalytic domains in tandem of one another. Another unique feature of HDAC6 is the HDAC6-, 250:

General Control Non-Derepressible 5 (Gcn5) –related N-Acetyltransferases (GNATs) is one of the many studied families with acetylation abilities. This superfamily includes the factors Gcn5 which is included in the SAGA, SLIK, STAGA, ADA, and A2 complexes, Gcn5L,

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showed there is an overall decrease in HDAC activity with unchanged levels of HAT activity. Results have shown that there is an important role for HAT/HDAC activity balance in inflammatory lung diseases and provided insights on possible therapeutic targets.

661:. All three HDACs work to repress the myogenic transcription factor MEF2 which an essential role in muscle differentiation as a DNA binding transcription factor. Binding of HDACs to MEF2 inhibits muscle differentiation, which can be reversed by action of 242:

time, were categorized based on sequence similarities between them. These similarities are high among members of a family, but members from different families show very little resemblance. Some of the major families identified so far are as follows.

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tails of histones have a tendency to weaken the chromatin's overall structure. Addition of an acetyl group, which carries a negative charge, effectively removes the positive charge and hence, reduces the interaction between the histone tail and the

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Epigenetic modifications also play a role in neurological disorders. Deregulation of histones modification are found to be responsible for deregulated gene expression and hence associated with neurological and psychological disorders, such as

948:, suggesting an important regulatory role of histone deacetylation on the expression of tumor suppressor genes. One of the examples is the regulation role of histone acetylation/deacetylation in P300 and CBP, both of which contribute to 963:

represents a new category for anticancer drugs that are in development. Vorinostat targets histone acetylation mechanisms and can effectively inhibit abnormal chromatin remodeling in cancerous cells. Targets of Vorinostat includes

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Gene expression is regulated by histone acetylation and deacetylation, and this regulation is also applicable to inflammatory genes. Inflammatory lung diseases are characterized by expression of specific inflammatory genes such as

441:. Classes of HDAC proteins are divided and grouped together based on the comparison to the sequence homologies of Rpd3, Hos1 and Hos2 for Class I HDACs, HDA1 and Hos3 for the Class II HDACs and the sirtuins for Class III HDACs. 3223:

D'Addario C, Caputi FF, Ekström TJ, Di Benedetto M, Maccarrone M, Romualdi P, Candeletti S (February 2013). "Ethanol induces epigenetic modulation of prodynorphin and pronociceptin gene expression in the rat amygdala complex".

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members of this family have multiple functions, not only with activating and silencing genes, but also affect development and have implications in human diseases. Sas2 and Sas3 are involved in transcription silencing, MOZ and

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models, it has been demonstrated that cardiac stress can result in gene expression changes and alter cardiac function. These changes are mediated through HATs/HDACs posttranslational modification signaling. HDAC inhibitor

1003:, and much of the work on addiction has focused on histone acetylation. Once particular epigenetic alterations occur, they appear to be long lasting "molecular scars" that may account for the persistence of addictions. 487:

which make up the core of each complex. Other complexes may be needed though in order to initiate the maximum amount of available activity possible. HDACs 1 and 2 can also bind directly to DNA binding proteins such as

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of mice after chronic cocaine exposure, were found to be associated with hyperacetylation of H3 or H4. Many of these individual genes are directly related to aspects of addiction associated with cocaine exposure.

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of the other Class I HDACs could compensate for the loss of HDAC1. This inability to recover from HDAC1 KO leads researchers to believe that there are both functional uniqueness to each HDAC as well as regulatory

571:. The NLS functions as a signal for nuclear action while an NES functions with HDACs that perform work outside of the nucleus. A presence of both signals for HDAC3 suggests it travels between the nucleus and the 466:

in order to activate their deacetylase abilities. There are three major protein complexes that HDAC 1 & 2 may incorporate themselves into. These complexes include Sin3 (named after its characteristic protein

1112:, regulatory functions of histone acetylation and deacetylation can have implications with genes that cause other diseases. Studies on histone modifications may reveal many novel therapeutic targets. 3483:

de Souza MF, Gonçales TA, Steinmetz A, Moura DJ, Saffi J, Gomez R, Barros HM (April 2014). "Cocaine induces DNA damage in distinct brain areas of female rats under different hormonal conditions".

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Renthal W, Kumar A, Xiao G, Wilkinson M, Covington HE, Maze I, Sikder D, Robison AJ, LaPlant Q, Dietz DM, Russo SJ, Vialou V, Chakravarty S, Kodadek TJ, Stack A, Kabbaj M, Nestler EJ (May 2009).

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groups of lysine amino acid residues. These residues are located on the tails of histones that make up the nucleosome of packaged dsDNA. The process is aided by factors known as

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Gallinari P, Di Marco S, Jones P, Pallaoro M, Steinkühler C (March 2007). "HDACs, histone deacetylation and gene transcription: from molecular biology to cancer therapeutics".

4173: 120:. Acetylation removes the positive charge on the histones, thereby decreasing the interaction of the N termini of histones with the negatively charged phosphate groups of 612:

have revealed that different tissue types show varying degrees of HDAC8 expression but has been observed in smooth muscles and is thought to contribute to contractility.

3403:"Biomarkers of disease can be detected in mice as early as 4 weeks after initiation of exposure to third-hand smoke levels equivalent to those found in homes of smokers" 2522:

Mroz RM, Noparlik J, Chyczewska E, Braszko JJ, Holownia A (November 2007). "Molecular basis of chronic inflammation in lung diseases: new therapeutic approach".

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Qiusheng Z, Yuntao Z, Rongliang Z, Dean G, Changling L (July 2005). "Effects of verbascoside and luteolin on oxidative damage in brain of heroin treated mice".

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Grayson DR, Kundakovic M, Sharma RP (February 2010). "Is there a future for histone deacetylase inhibitors in the pharmacotherapy of psychiatric disorders?".

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of N- and C-terminal histone tails attracts various transcription initiation factors that contain bromodomains, including human transcriptional coactivator

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In 2013, 22.7 million persons aged 12 or older needed treatment for an illicit drug or alcohol use problem (8.6 percent of persons aged 12 or older).

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region that was found to be required for transcriptional repression as well as its deacetylase activity. It also contains two regions, one called a

1050:. In rats exposed to alcohol for up to 5 days, there was an increase in histone 3 lysine 9 acetylation in the pronociceptin promoter in the brain 3553:

Johnson Z, Venters J, Guarraci FA, Zewail-Foote M (June 2015). "Methamphetamine induces DNA damage in specific regions of the female rat brain".

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Spange S, Wagner T, Heinzel T, Krämer OH (January 2009). "Acetylation of non-histone proteins modulates cellular signalling at multiple levels".

789:. This opens up the usually tightly packed nucleosome and allows transcription machinery to come into contact with the DNA template, leading to 608:

be enzymatically active. At this point, due to its recent discovery, it is not yet known if it is regulated by co-repressor protein complexes.

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nucleosome. They also have the ability to acetylate and mediate non-histone proteins involved in transcription and are also involved in the

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activity can be traced back to the work of Vicent Allfrey and colleagues in 1964. The group hypothesized that histone proteins modified by

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There are other proteins that have acetylating abilities but differ in structure to the previously mentioned families. One HAT is called

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Experiments investigating acetylation patterns of H4 histones suggested that these modification patterns are collectively maintained in

124:. As a consequence, the condensed chromatin is transformed into a more relaxed structure that is associated with greater levels of gene 128:. This relaxation can be reversed by deacetylation catalyzed by HDAC activity. Relaxed, transcriptionally active DNA is referred to as 1328: 4121: 662: 529: 665:

which works to dissociate the HDAC/MEF2 complex by phosphorylating the HDAC portion. They have been seen to be involved in cellular

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Jiang H, Gao Q, Zheng W, Yin S, Wang L, Zhong L, Ali A, Khan T, Hao Q, Fang H, Sun X, Xu P, Pandita TK, Jiang X, Shi Q (May 2018).

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The regulatory mechanism is thought to be twofold. Lysine is an amino acid with a positive charge when unmodified. Lysines on the

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Specifically, gene expression data demonstrated increased activity of HAT and decreased level of HDAC activity in patients with

695:. HDAC9 KO mice are shown to suffer from cardiac hypertrophy which is exacerbated in mice that are double KO for HDACs 9 and 5. 3444:"Alcohol induces DNA damage and the Fanconi anemia D2 protein implicating FANCD2 in the DNA damage response pathways in brain" 2678:

Duvic M, Talpur R, Ni X, Zhang C, Hazarika P, Kelly C, Chiao JH, Reilly JF, Ricker JL, Richon VM, Frankel SR (January 2007).

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Torok MS, Grant PA (2004). "Histone acetyltransferase proteins contribute to transcriptional processes at multiple levels".

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that are wrapped around protein complexes called histone cores. These histone cores are composed of 8 subunits, two each of

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Due to the regulatory role during transcription of epigenetic modifications in genes, it is not surprising that changes in

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Levine A, Huang Y, Drisaldi B, Griffin EA, Pollak DD, Xu S, Yin D, Schaffran C, Kandel DB, Kandel ER (November 2011).

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are involved with the formation of leukemic transclocation products while MOF is involved in dosage compensation in

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Shikama N, Lutz W, Kretzschmar R, Sauter N, Roth JF, Marino S, Wittwer J, Scheidweiler A, Eckner R (October 2003).

3074:"Molecular mechanism for a gateway drug: epigenetic changes initiated by nicotine prime gene expression by cocaine" 1013:. After 7 days of nicotine treatment of mice, acetylation of both histone H3 and histone H4 was increased at the 4858: 4415: 4359: 671: 584: 580: 540: 1359: 4911: 4354: 858: 801: 358: 289: 275:-signaled activation. Elp3 has the ability to acetylate all histone subunits and also shows involvement in the 4853: 3694:

Cao DJ, Wang ZV, Battiprolu PK, Jiang N, Morales CR, Kong Y, Rothermel BA, Gillette TG, Hill JA (March 2011).

4906: 4442: 4373: 4114: 2291:"Mitogen-stimulated phosphorylation of histone H3 is targeted to a small hyperacetylation-sensitive fraction" 1081: 564: 101:) to another. Deacetylation is simply the reverse reaction where an acetyl group is removed from a molecule. 74: 4874: 4848: 4178: 2389:

Filippakopoulos P, Knapp S (May 2014). "Targeting bromodomains: epigenetic readers of lysine acetylation".

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Kuo MH, Allis CD (August 1998). "Roles of histone acetyltransferases and deacetylases in gene regulation".

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may have a special function unique to itself. It has been found that HDAC11 remains mainly in the nucleus.

112:, the basic structural unit of the chromosomes and ultimately higher order structures, represent a type of 144: 4501: 324: 1730:"HATs and HDACs: from structure, function and regulation to novel strategies for therapy and prevention" 4951: 4534: 4393: 1882:

Marmorstein R, Roth SY (April 2001). "Histone acetyltransferases: function, structure, and catalysis".

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There are a total of four classes that categorize Histone Deacetylases (HDACs). Class I includes HDACs

4731: 4667: 4637: 4615: 1172: 1097:. Such epigenetic scars likely contribute to the persistent epigenetic changes found in addictions. 932:

markers, such as acetylation, can contribute to cancer development. HDACs expression and activity in

897: 366: 189: 177: 82: 3953:"Disease- and age-related changes in histone acetylation at gene promoters in psychiatric disorders" 3904:"Essential function of p300 acetyltransferase activity in heart, lung and small intestine formation" 3324: 2930: 1919:"Acetylation and Methylation of Histones and Their Possible Role in the Regulation of RNA Synthesis" 4525: 4517: 4437: 4225: 4138: 4107: 2019:

Zentner GE, Henikoff S (March 2013). "Regulation of nucleosome dynamics by histone modifications".

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of the brain, causing 61% increase in FosB expression. This would also increase expression of the

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functions as a "sustained molecular switch" and "master control protein" in the development of an

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Ruffle JK (November 2014). "Molecular neurobiology of addiction: what's all the (Δ)FosB about?".

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Suggested by the idea that the structure of chromatin can be modified to allow or deny access of

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groups added negative charges to the positive lysines, and thus, reduced the interaction between

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has been found to be most closely related to HDAC8. HDAC3 contains a non-conserved region in the

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for inflammatory lung diseases interfere with HAT/HDAC activity to turn off inflammatory genes.

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complex. This acetylation is an activating mark for pronociceptin. The nociceptin/nociceptin

684: 362: 3696:"Histone deacetylase (HDAC) inhibitors attenuate cardiac hypertrophy by suppressing autophagy" 800:

Another implication of histone acetylation is to provide a platform for protein binding. As a

496:. HDACs 1 and 2 have been found to express regulatory roles in key cell cycle genes including 4925: 4920: 4788: 4690: 4318: 4303: 4183: 2064:"Uncovering correlated variability in epigenomic datasets using the Karhunen-Loeve transform" 1144: 805: 568: 458: 2242:"Covalent histone modifications--miswritten, misinterpreted and mis-erased in human cancers" 1080:

region and deacetylation at 206 genes. At least 45 genes, shown in previous studies to be

409:. Class II is divided into two subgroups, Class IIA and Class IIB. Class IIA includes HDACs 4822: 4736: 4702: 4596: 4425: 4323: 4241: 3707: 3650: 3177: 2302: 1930: 1374: 1135:

with cellular HAT activity suggesting an essential role of histone acetylation status with

1025: 870: 826: 508: 333: 3755:"Class II histone deacetylases act as signal-responsive repressors of cardiac hypertrophy" 3389: 2877:. Progress in Molecular Biology and Translational Science. Vol. 128. pp. 51–87. 136:. Condensation can be brought about by processes including deacetylation and methylation. 8: 4805: 4773: 4659: 4633: 4251: 3853:"Dysregulation of histone acetyltransferases and deacetylases in cardiovascular diseases" 1182: 1177: 1132: 1125: 1116: 1017: 874: 727:, acting as a tubulin deacetylase which helps in the regulation of microtubule-dependent 545: 201: 86: 4486: 3711: 3654: 3181: 2306: 1934: 1378: 224: 4574: 4386: 4269: 4074: 4026: 4001: 3977: 3952: 3879: 3852: 3828: 3803: 3779: 3754: 3730: 3695: 3671: 3638: 3578: 3508: 3367: 3342: 3312: 3295: 3276: 3249: 3146: 3098: 3073: 3022: 2997: 2970: 2945: 2918: 2901: 2882: 2850: 2825: 2798: 2771: 2752: 2704: 2679: 2655: 2630: 2611: 2499: 2474: 2414: 2366: 2349: 2266: 2241: 2222: 2179: 2090: 2063: 2044: 2004: 1977: 1859: 1832: 1759: 1582: 1493: 1468: 1398: 1340: 1160: 1061: 790: 3928: 3903: 3770: 2166: 2149: 1953: 1918: 1895: 1833:"MOF influences meiotic expansion of H2AX phosphorylation and spermatogenesis in mice" 1799: 4956: 4893: 4066: 4031: 3982: 3933: 3884: 3833: 3784: 3735: 3676: 3619: 3570: 3535: 3500: 3465: 3460: 3443: 3424: 3372: 3343:"Genome-wide analysis of chromatin regulation by cocaine reveals a role for sirtuins" 3300: 3280: 3241: 3205: 3200: 3165: 3138: 3103: 3027: 2975: 2906: 2886: 2855: 2803: 2756: 2744: 2709: 2660: 2603: 2568: 2527: 2504: 2455: 2406: 2371: 2330: 2325: 2290: 2271: 2214: 2171: 2130: 2095: 2036: 1958: 1899: 1864: 1813: 1803: 1751: 1705: 1663: 1623: 1574: 1498: 1390: 1332: 1290: 1230: 1085: 1032: 1021: 472: 276: 193: 98: 4470: 3582: 3512: 3253: 3150: 2418: 2226: 2183: 2048: 1763: 1586: 1344: 192:(HATs). HAT molecules facilitate the transfer of an acetyl group from a molecule of 4815: 4798: 4078: 4058: 4021: 4013: 3972: 3964: 3923: 3915: 3874: 3864: 3823: 3815: 3774: 3766: 3725: 3715: 3666: 3658: 3609: 3562: 3492: 3455: 3414: 3362: 3354: 3290: 3272: 3233: 3195: 3185: 3130: 3093: 3085: 3017: 3009: 2965: 2957: 2896: 2878: 2845: 2837: 2793: 2783: 2736: 2699: 2691: 2650: 2642: 2615: 2595: 2558: 2494: 2486: 2445: 2398: 2361: 2320: 2310: 2261: 2253: 2206: 2197:

Winston F, Allis CD (July 1999). "The bromodomain: a chromatin-targeting module?".

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For HDACs 4, 5 and 7, conserved binding domains have been discovered that bind for

361:, which has a HAT domain located at the C-terminus end of the protein along with a 268: 2490: 4679: 4447: 4284: 4130: 3358: 3134: 3089: 3013: 2695: 2563: 2547:"Histone acetylation and deacetylation: importance in inflammatory lung diseases" 2546: 2450: 2434:"Histone acetylation and deacetylation: importance in inflammatory lung diseases" 2433: 2126: 1849: 1192: 1055: 1006: 901: 642: 504: 304: 297: 133: 67: 3598:"The peroxidative DNA damage and apoptosis in methamphetamine-treated rat brain" 1467:

de Ruijter AJ, van Gennip AH, Caron HN, Kemp S, van Kuilenburg AB (March 2003).

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Proceedings of the National Academy of Sciences of the United States of America

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Proceedings of the National Academy of Sciences of the United States of America

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Proceedings of the National Academy of Sciences of the United States of America

1923:

Proceedings of the National Academy of Sciences of the United States of America

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core histones, and DNA. The view is from the top through the superhelical axis.

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the tails of the histone subunits. The histone tails insert themselves in the

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Hitchcock LN, Lattal KM (2014). "Histone-mediated epigenetics in addiction".

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and showed a drastic reduction in the production but increased expression of

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Zhang CL, McKinsey TA, Chang S, Antos CL, Hill JA, Olson EN (August 2002).

3739: 3680: 3623: 3574: 3539: 3504: 3469: 3428: 3376: 3304: 3245: 3209: 3190: 3142: 3107: 3031: 2979: 2910: 2859: 2807: 2748: 2713: 2664: 2607: 2599: 2572: 2531: 2508: 2459: 2410: 2375: 2275: 2218: 2175: 2134: 2099: 2040: 1962: 1903: 1868: 1817: 1755: 1746: 1729: 1709: 1701: 1667: 1578: 1502: 1294: 905: 821: 680: 517: 3869: 2334: 1943: 1646:

Turner BM (September 2000). "Histone acetylation and an epigenetic code".

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system is involved in the reinforcing or conditioning effects of alcohol.

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10.1002/(sici)1521-1878(199808)20:8<615::aid-bies4>3.0.co;2-h

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Marmorstein R (August 2001). "Structure of histone acetyltransferases".

479:. The Sin3 complex and the NuRD complex both contain HDACs 1 and 2, the 4930: 4624: 4579: 4569: 4564: 4559: 4554: 4410: 3968: 3614: 3597: 3419: 3402: 1484: 1197: 1073: 1069: 1047: 960: 945: 940:

and increased activity of HDACs has been shown to be characteristic of

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group on lysine. When a lysine is to be deacetylated, factors known as

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located at the C-terminus region and a HAT domain located in-between.

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Tokunaga I, Ishigami A, Kubo S, Gotohda T, Kitamura O (August 2008).

1128: 1094: 1040: 1000: 720: 719:(HUB) domain in the C-terminus which shows some functions related to 688: 589: 588:

functions in cell cycle progression. HDAC3 also shows involvement in

572: 346: 308: 204:(HDACs) catalyze the removal of the acetyl group with a molecule of H 184:

The mechanism for acetylation and deacetylation takes place on the NH

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Glozak MA, Seto E (August 2007). "Histone deacetylases and cancer".

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Kuo CH, Hsieh CC, Lee MS, Chang KT, Kuo HF, Hung CH (January 2014).

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tails in specific regions of the brain are of central importance in

23:

The crystal structure of the nucleosome core particle consisting of

4793: 4783: 4430: 4420: 4344: 3639:"Epigenetic abnormalities in cardiac hypertrophy and heart failure" 3442:

Rulten SL, Hodder E, Ripley TL, Stephens DN, Mayne LV (July 2008).

3271:. Handbook of Clinical Neurology. Vol. 148. pp. 747–765. 1660:

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smokers (about 21% of the US population) are usually addicted to

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functional group is transferred from one molecule (in this case,

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Walker DM, Nestler EJ (2018). "Neuroepigenetics and addiction".

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Grant S, Easley C, Kirkpatrick P (January 2007). "Vorinostat".

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Verdone L, Agricola E, Caserta M, Di Mauro E (September 2006).

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Silencing Mediator for Retinoic Acid and Thyroid Hormone (SMRT)

536: 512: 438: 430: 94: 78: 47: 3482: 2628: 1556: 1360:"Histone acetylation in chromatin structure and transcription" 1266: 4810: 4662: 4188: 2521: 1466: 1140: 1093:

epigenetic alterations, and thus leave an epigenetic scar on

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Histone acetylation and deacetylation are essential parts of

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The International Journal of Biochemistry & Cell Biology

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recognition on histones by nucleosome remodelling proteins.

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Lee J, Hwang YJ, Kim KY, Kowall NW, Ryu H (October 2013).

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Cohen I, Poręba E, Kamieniarz K, Schneider R (June 2011).

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Barratt MJ, Hazzalin CA, Cano E, Mahadevan LC (May 1994).

691:. This interaction leads to a role in clonal expansion of 4516: 4158: 4094:

Animation of histone tail acetylation and deacetylation:

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Wang Y, Miao X, Liu Y, Li F, Liu Q, Sun J, Cai L (2014).

3801: 3340: 2112: 770: 532: 497: 489: 156: 121: 2826:"Transcriptional and epigenetic mechanisms of addiction" 2147: 761:

The discovery of histone acetylation causing changes in

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which has a Kinase domain at the N-terminus region, two

132:. More condensed (tightly packed) DNA is referred to as 4048: 3802:

Lehmann LH, Worst BC, Stanmore DA, Backs J (May 2014).

3752: 3555:

Clinical and Experimental Pharmacology & Physiology

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Clinical and Experimental Pharmacology & Physiology

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https://www.drugsandalcohol.ie/12728/1/NIDA_Cocaine.pdf

3166:"DeltaFosB: a sustained molecular switch for addiction" 1225:

Watson JD, Baker TA, Gann A, Levine M, Losik R (2014).

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Nucleosome Remodelling and Deacetylating complex (NuRD)

148:

Histone tails and their function in chromatin formation

3693: 2726: 2150:"Signaling to chromatin through histone modifications" 1916: 1224: 1064:

occurs in about 0.5% of the US population. Repeated

808:

interact with the acetylated histone tails via their

2388: 2148:

Cheung P, Allis CD, Sassone-Corsi P (October 2000).

1875: 3804:"Histone deacetylase signaling in cardioprotection" 2875:

Epigenetics and Neuroplasticity—Evidence and Debate

2354:

Current Opinion in Drug Discovery & Development

1068:administration in mice induces hyperacetylation of 646:50% similarity to the N-terminus of HDACs 4 and 5. 236: 3401:Adhami N, Chen Y, Martins-Green M (October 2017). 2946:"Epigenetic regulation in substance use disorders" 2677: 1131:. Studies on p300 and CREB-binding protein linked 670:with HDAC3 as a co-recruitment factor to the SMRT/ 330:Adenoviral E1A-associated protein of 300kDa (p300) 253:p300/CREB-binding protein associated factor (PCAF) 108:, octameric proteins that organize chromatin into 3999: 3163: 2998:"Epigenome Maintenance in Response to DNA Damage" 2819: 2817: 2061: 1273:Briefings in Functional Genomics & Proteomics 575:. HDAC3 has even been found to interact with the 369:in the middle. Another is ATF-2 which contains a 4943: 3164:Nestler EJ, Barrot M, Self DW (September 2001). 2995: 2472: 1830: 2872: 2631:"Histone modifiers in cancer: friends or foes?" 2544: 2431: 2018: 1978:"Vincent Allfrey's Work on Histone Acetylation" 1881: 1229:(Seventh ed.). Boston: Pearson/CSH Press. 936:cells is very different from normal cells. The 229:Histone acetylation alters chromatin structure. 3950: 3448:Alcoholism: Clinical and Experimental Research 3123:The American Journal of Drug and Alcohol Abuse 2823: 2814: 1917:Allfrey VG, Faulkner R, Mirsky AE (May 1964). 853:is a motif that is responsible for acetylated 388: 300:in mice as it is involved in the expansion of 4502: 4115: 3850: 3266: 2772:"Metabolic recoding of epigenetics in cancer" 1884:Current Opinion in Genetics & Development 1683: 1681: 1679: 1677: 1046:About 7% of the US population is addicted to 77:. These reactions are typically catalysed by 3944: 3643:Environmental Health and Preventive Medicine 3589: 3546: 3519: 3476: 3435: 3394: 3260: 3216: 3157: 3114: 3065: 2937: 2866: 2239: 2196: 1975: 1910: 1824: 1552: 1550: 1548: 1546: 1544: 1542: 1540: 1538: 1536: 1534: 1532: 1462: 1460: 1458: 1456: 1454: 1452: 1450: 1448: 1446: 1444: 1442: 1440: 1438: 1436: 1434: 1432: 16:Biological processes used in gene regulation 3951:Tang B, Dean B, Thomas EA (December 2011). 2943: 2347: 1687: 1530: 1528: 1526: 1524: 1522: 1520: 1518: 1516: 1514: 1512: 1430: 1428: 1426: 1424: 1422: 1420: 1418: 1416: 1414: 1412: 756: 503:Activity of these HDACs can be affected by 181:occur post-translation and are reversible. 4509: 4495: 4270:Precursor mRNA (pre-mRNA / hnRNA) 4122: 4108: 3336: 3334: 2585: 2545:Barnes PJ, Adcock IM, Ito K (March 2005). 2432:Barnes PJ, Adcock IM, Ito K (March 2005). 1785: 1674: 815: 530:Cyclin-Dependent Kinase Inhibitors (CDKIs) 516:2 have been found only exclusively in the 507:. An increased amount of phosphorylation ( 377:with a HAT domain in-between. The last is 4025: 3976: 3927: 3878: 3868: 3857:Oxidative Medicine and Cellular Longevity 3827: 3778: 3729: 3719: 3670: 3613: 3459: 3418: 3366: 3294: 3199: 3189: 3097: 3021: 2996:Dabin J, Fortuny A, Polo SE (June 2016). 2969: 2900: 2849: 2797: 2787: 2703: 2654: 2562: 2498: 2449: 2365: 2324: 2314: 2265: 2165: 2089: 2079: 2021:Nature Structural & Molecular Biology 2003: 1993: 1952: 1942: 1858: 1848: 1745: 1617: 1492: 1357: 1284: 1262: 1260: 1258: 1256: 1254: 1252: 1250: 1248: 1246: 220:Histone acetylation/deacetylation enzymes 3043: 3041: 2991: 2989: 1781: 1779: 1777: 1775: 1773: 1727: 1641: 1639: 1637: 1509: 1409: 1314: 1269:"Histone acetylation in gene regulation" 886: 592:and a transcription independent role in 223: 143: 18: 3331: 2824:Robison AJ, Nestler EJ (October 2011). 2769: 1723: 1721: 1719: 1593: 751: 371:transcriptional activation (ACT) domain 4944: 3120: 2524:Journal of Physiology and Pharmacology 2240:Chi P, Allis CD, Wang GG (July 2010). 1645: 1599: 1243: 1124:was reported to reduce stress induced 375:basic zipper DNA-binding (bZip) domain 139: 4655:Histone acetylation and deacetylation 4490: 4290:Histone acetylation and deacetylation 4103: 3038: 2986: 2348:Sanchez R, Zhou MM (September 2009). 2062:Madrigal P, Krajewski P (July 2015). 1770: 1634: 1351: 1310: 1308: 1306: 1304: 917:chronic obstructive pulmonary disease 663:Ca/calmodulin-dependent kinase (CaMK) 585:Nuclear Receptor Co-Repressor (N-CoR) 359:steroid receptor coactivator 1 (SRC1) 44:Histone acetylation and deacetylation 4355:Ribosome-nascent chain complex (RNC) 3808:Cellular and Molecular Life Sciences 3636: 3602:The Journal of Medical Investigation 1716: 449: 4129: 683:. HDAC7 has been shown to suppress 679:hypertrophy and die due to extreme 365:and PAS A and PAS B domains with a 13: 3277:10.1016/B978-0-444-64076-5.00048-X 2944:McQuown SC, Wood MA (April 2010). 2883:10.1016/B978-0-12-800977-2.00003-6 1301: 1103: 318: 14: 4973: 4088: 3226:Journal of Molecular Neuroscience 881: 734: 651:C-terminal binding protein (CtBP) 615: 565:Nuclear Localization Signal (NLS) 481:Rb-associated protein 48 (RbAp48) 3461:10.1111/j.1530-0277.2008.00673.x 2551:The European Respiratory Journal 2438:The European Respiratory Journal 655:myocyte enhancer factor 2 (MEF2) 524:, mice were found to die during 444: 367:LXXLL receptor interacting motif 237:Histone acetyltransferase (HATs) 4962:Post-translational modification 4859:Archaeal transcription factor B 4360:Post-translational modification 4042: 3993: 3895: 3844: 3795: 3746: 3687: 3630: 3383: 3051: 2763: 2720: 2671: 2622: 2579: 2538: 2515: 2466: 2425: 2382: 2341: 2282: 2233: 2190: 2141: 2106: 2055: 2012: 1982:Journal of Biological Chemistry 1969: 1728:Yang XJ, Seto E (August 2007). 859:Posttranslational modifications 425:while Class IIB includes HDACs 46:are the processes by which the 3078:Science Translational Medicine 2729:Nature Reviews. Drug Discovery 2391:Nature Reviews. Drug Discovery 1358:Grunstein M (September 1997). 844: 802:posttranslational modification 282: 245: 1: 3771:10.1016/S0092-8674(02)00861-9 2526:. 58 Suppl 5 (Pt 2): 453–60. 2491:10.5415/apallergy.2014.4.1.14 2167:10.1016/s0092-8674(00)00118-5 1896:10.1016/S0959-437X(00)00173-8 1800:10.1016/S0065-3233(04)67007-0 1788:Advances in Protein Chemistry 1227:Molecular biology of the gene 1203: 955:Approved in 2006 by the U.S. 625:The Class IIA HDACs includes 352: 3359:10.1016/j.neuron.2009.03.026 3135:10.3109/00952990.2014.933840 3090:10.1126/scitranslmed.3003062 3014:10.1016/j.molcel.2016.04.006 2830:Nature Reviews. Neuroscience 2770:Wang YP, Lei QY (May 2018). 2696:10.1182/blood-2006-06-025999 2564:10.1183/09031936.05.00117504 2451:10.1183/09031936.05.00117504 2127:10.1016/j.biocel.2008.08.027 1850:10.1371/journal.pgen.1007300 1690:Journal of Molecular Biology 1076:at 1,696 genes in one brain 987: 957:Food and Drug Administration 703:The Class IIB HDACs include 698: 620: 66:and deacetylated as part of 7: 1166: 569:Nuclear Export Signal (NES) 492:, Rb binding protein 1 and 437:and Class IV contains only 389:Histone deacetylase (HDACs) 325:p300-CBP coactivator family 157:double-stranded DNA (dsDNA) 10: 4978: 4535:Transcriptional regulation 2950:Current Psychiatry Reports 334:CREB-binding protein (CBP) 322: 190:histone acetyltransferases 4902: 4867: 4841: 4766: 4732:Transcription coregulator 4724: 4701: 4678: 4668:Histone acetyltransferase 4638:Histone methyltransferase 4616:Histone-modifying enzymes 4614: 4607: 4542: 4533: 4463: 4372: 4337: 4311: 4302: 4260: 4234: 4208: 4199: 4137: 4018:10.1007/s13311-013-0206-5 3820:10.1007/s00018-013-1516-9 3663:10.1007/s12199-007-0007-8 3238:10.1007/s12031-012-9829-y 2962:10.1007/s11920-010-0099-5 2789:10.1186/s40880-018-0302-3 2199:Nature Structural Biology 2081:10.1186/s13040-015-0051-7 1173:Histone acetyltransferase 1139:responsive genes such as 923: 898:AP-1 transcription factor 739: 433:. Class III contains the 271:-mediated activation and 83:histone acetyltransferase 54:tail protruding from the 4421:sequestration (P-bodies) 3957:Translational Psychiatry 3059:"Is nicotine addictive?" 2647:10.1177/1947601911417176 1110:transcription activators 757:Transcription regulation 599: 551: 93:is the process where an 4833:Internal control region 4399:Gene regulatory network 3721:10.1073/pnas.1015081108 3637:Mano H (January 2008). 3567:10.1111/1440-1681.12404 3497:10.1111/1440-1681.12218 2316:10.1073/pnas.91.11.4781 1995:10.1074/jbc.O112.000248 1976:Mukhopadhyay R (2012). 1606:Genes & Development 1600:Struhl K (March 1998). 1473:The Biochemical Journal 816:Histone code hypothesis 311:to pachytene stages of 296:. MOF also influences 4404:cis-regulatory element 4063:10.1124/mol.109.061333 4051:Molecular Pharmacology 3269:Neurogenetics, Part II 3191:10.1073/pnas.191352698 2600:10.1038/sj.onc.1210610 2246:Nature Reviews. Cancer 1747:10.1038/sj.onc.1210599 1702:10.1006/jmbi.2001.4859 590:stem cell self-renewal 363:basic helix-loop-helix 233: 196:(Acetyl-CoA) to the NH 149: 40: 4926:Intrinsic termination 4691:DNA methyltransferase 2776:Cancer Communications 1944:10.1073/pnas.51.5.786 1571:10.1038/sj.cr.7310149 887:Inflammatory diseases 806:transcription factors 227: 147: 22: 4703:Chromatin remodeling 4426:alternative splicing 4416:Post-transcriptional 4242:Transcription factor 3920:10.1093/emboj/cdg502 2479:Asia Pacific Allergy 1619:10.1101/gad.12.5.599 871:CREB-binding protein 827:immediate early gene 797:gene transcription. 752:Biological functions 715:, and Brap2-related 509:hyperphosphorylation 490:Yin and Yang 1 (YY1) 202:histone deacetylases 50:residues within the 4660:Histone deacetylase 4650:Histone demethylase 4634:Histone methylation 4350:Transfer RNA (tRNA) 3870:10.1155/2014/641979 3712:2011PNAS..108.4123C 3655:2008EHPM...13...25M 3182:2001PNAS...9811042N 2307:1994PNAS...91.4781B 1935:1964PNAS...51..786A 1379:1997Natur.389..349G 1286:10.1093/bfgp/ell028 1183:Histone methylation 1178:Histone deacetylase 1133:cardiac hypertrophy 1117:cardiac hypertrophy 1115:Based on different 140:Mechanism of action 89:" (HDAC) activity. 87:histone deacetylase 4464:Influential people 4443:Post-translational 4262:Post-transcription 3969:10.1038/tp.2011.61 3615:10.2152/jmi.55.241 3420:10.1042/CS20171053 2635:Genes & Cancer 1485:10.1042/BJ20021321 1161:Huntington disease 900:. Treatments with 791:gene transcription 675:from a pronounced 522:knockout (KO) mice 462:incorporated with 234: 150: 41: 4952:Organic reactions 4939: 4938: 4894:RNA polymerase II 4762: 4761: 4720: 4719: 4484: 4483: 4368: 4367: 4298: 4297: 4174:Special transfers 4006:Neurotherapeutics 3413:(19): 2409–2426. 3084:(107): 107ra109. 2033:10.1038/nsmb.2470 1236:978-0-321-76243-6 1062:Cocaine addiction 1033:nucleus accumbens 1022:nucleus accumbens 995:modifications of 915:. Patients with 717:zinc finger motif 548:between factors. 450:HDAC1 & HDAC2 277:RNA polymerase II 194:acetyl-coenzyme A 99:acetyl coenzyme A 4969: 4816:Response element 4799:Response element 4612: 4611: 4540: 4539: 4511: 4504: 4497: 4488: 4487: 4309: 4308: 4206: 4205: 4124: 4117: 4110: 4101: 4100: 4083: 4082: 4046: 4040: 4039: 4029: 3997: 3991: 3990: 3980: 3948: 3942: 3941: 3931: 3908:The EMBO Journal 3899: 3893: 3892: 3882: 3872: 3848: 3842: 3841: 3831: 3799: 3793: 3792: 3782: 3750: 3744: 3743: 3733: 3723: 3691: 3685: 3684: 3674: 3634: 3628: 3627: 3617: 3593: 3587: 3586: 3550: 3544: 3543: 3523: 3517: 3516: 3480: 3474: 3473: 3463: 3439: 3433: 3432: 3422: 3407:Clinical Science 3398: 3392: 3387: 3381: 3380: 3370: 3338: 3329: 3328: 3322: 3318: 3316: 3308: 3298: 3264: 3258: 3257: 3220: 3214: 3213: 3203: 3193: 3161: 3155: 3154: 3118: 3112: 3111: 3101: 3069: 3063: 3062: 3055: 3049: 3045: 3036: 3035: 3025: 2993: 2984: 2983: 2973: 2941: 2935: 2934: 2928: 2924: 2922: 2914: 2904: 2870: 2864: 2863: 2853: 2821: 2812: 2811: 2801: 2791: 2767: 2761: 2760: 2724: 2718: 2717: 2707: 2675: 2669: 2668: 2658: 2626: 2620: 2619: 2583: 2577: 2576: 2566: 2542: 2536: 2535: 2519: 2513: 2512: 2502: 2470: 2464: 2463: 2453: 2429: 2423: 2422: 2386: 2380: 2379: 2369: 2345: 2339: 2338: 2328: 2318: 2286: 2280: 2279: 2269: 2237: 2231: 2230: 2194: 2188: 2187: 2169: 2145: 2139: 2138: 2110: 2104: 2103: 2093: 2083: 2059: 2053: 2052: 2016: 2010: 2009: 2007: 1997: 1988:(3): 2270–2271. 1973: 1967: 1966: 1956: 1946: 1914: 1908: 1907: 1879: 1873: 1872: 1862: 1852: 1828: 1822: 1821: 1783: 1768: 1767: 1749: 1725: 1714: 1713: 1685: 1672: 1671: 1643: 1632: 1631: 1621: 1597: 1591: 1590: 1554: 1507: 1506: 1496: 1479:(Pt 3): 737–49. 1464: 1407: 1406: 1373:(6649): 349–52. 1364: 1355: 1349: 1348: 1312: 1299: 1298: 1288: 1264: 1241: 1240: 1222: 269:nuclear-receptor 155:are portions of 38: 34: 30: 26: 4977: 4976: 4972: 4971: 4970: 4968: 4967: 4966: 4942: 4941: 4940: 4935: 4910: 4904: 4898: 4863: 4837: 4758: 4716: 4697: 4680:DNA methylation 4674: 4618: 4603: 4529: 4515: 4485: 4480: 4459: 4394:Transcriptional 4364: 4333: 4294: 4285:Polyadenylation 4256: 4230: 4195: 4189:Protein→Protein 4140: 4133: 4131:Gene expression 4128: 4091: 4086: 4047: 4043: 3998: 3994: 3949: 3945: 3914:(19): 5175–85. 3900: 3896: 3849: 3845: 3800: 3796: 3751: 3747: 3692: 3688: 3635: 3631: 3594: 3590: 3551: 3547: 3524: 3520: 3481: 3477: 3440: 3436: 3399: 3395: 3388: 3384: 3339: 3332: 3320: 3319: 3310: 3309: 3287: 3265: 3261: 3221: 3217: 3176:(20): 11042–6. 3162: 3158: 3119: 3115: 3070: 3066: 3057: 3056: 3052: 3046: 3039: 2994: 2987: 2942: 2938: 2926: 2925: 2916: 2915: 2893: 2871: 2867: 2842:10.1038/nrn3111 2822: 2815: 2768: 2764: 2741:10.1038/nrd2227 2725: 2721: 2676: 2672: 2627: 2623: 2594:(37): 5420–32. 2584: 2580: 2543: 2539: 2520: 2516: 2471: 2467: 2430: 2426: 2403:10.1038/nrd4286 2387: 2383: 2346: 2342: 2287: 2283: 2258:10.1038/nrc2876 2238: 2234: 2195: 2191: 2146: 2142: 2111: 2107: 2060: 2056: 2017: 2013: 1974: 1970: 1915: 1911: 1880: 1876: 1843:(5): e1007300. 1829: 1825: 1810: 1784: 1771: 1726: 1717: 1686: 1675: 1644: 1635: 1598: 1594: 1555: 1510: 1465: 1410: 1362: 1356: 1352: 1313: 1302: 1265: 1244: 1237: 1223: 1210: 1206: 1193:Phosphorylation 1169: 1106: 1104:Other disorders 1056:opioid receptor 990: 926: 902:corticosteroids 889: 884: 847: 818: 759: 754: 742: 737: 701: 623: 618: 602: 577:plasma membrane 554: 505:phosphorylation 452: 447: 391: 355: 343:differentiation 327: 321: 319:p300/CBP family 305:phosphorylation 298:spermatogenesis 285: 248: 239: 222: 207: 199: 187: 142: 134:heterochromatin 75:gene regulation 68:gene regulation 36: 32: 28: 24: 17: 12: 11: 5: 4975: 4965: 4964: 4959: 4954: 4937: 4936: 4934: 4933: 4928: 4923: 4917: 4915: 4900: 4899: 4897: 4896: 4890:RNA polymerase 4884: 4878:RNA polymerase 4871: 4869: 4865: 4864: 4862: 4861: 4856: 4851: 4845: 4843: 4839: 4838: 4836: 4835: 4830: 4825: 4820: 4819: 4818: 4813: 4803: 4802: 4801: 4796: 4791: 4786: 4781: 4770: 4768: 4764: 4763: 4760: 4759: 4757: 4756: 4751: 4750: 4749: 4744: 4739: 4728: 4726: 4722: 4721: 4718: 4717: 4715: 4714: 4708: 4706: 4699: 4698: 4696: 4695: 4694: 4693: 4685: 4683: 4676: 4675: 4673: 4672: 4671: 4670: 4665: 4652: 4647: 4646: 4645: 4630: 4628: 4609: 4605: 4604: 4602: 4601: 4600: 4599: 4594: 4584: 4583: 4582: 4577: 4572: 4567: 4562: 4557: 4546: 4544: 4537: 4531: 4530: 4514: 4513: 4506: 4499: 4491: 4482: 4481: 4479: 4478: 4473: 4471:François Jacob 4467: 4465: 4461: 4460: 4458: 4457: 4456: 4455: 4450: 4440: 4435: 4434: 4433: 4428: 4423: 4413: 4408: 4407: 4406: 4401: 4391: 4390: 4389: 4378: 4376: 4370: 4369: 4366: 4365: 4363: 4362: 4357: 4352: 4347: 4341: 4339: 4335: 4334: 4332: 4331: 4326: 4321: 4315: 4313: 4306: 4300: 4299: 4296: 4295: 4293: 4292: 4287: 4282: 4277: 4272: 4266: 4264: 4258: 4257: 4255: 4254: 4249: 4247:RNA polymerase 4244: 4238: 4236: 4232: 4231: 4229: 4228: 4223: 4218: 4212: 4210: 4203: 4197: 4196: 4194: 4193: 4192: 4191: 4186: 4181: 4171: 4170: 4169: 4151: 4145: 4143: 4135: 4134: 4127: 4126: 4119: 4112: 4104: 4098: 4097: 4090: 4089:External links 4087: 4085: 4084: 4041: 3992: 3943: 3894: 3843: 3814:(9): 1673–90. 3794: 3745: 3706:(10): 4123–8. 3686: 3629: 3608:(3–4): 241–5. 3588: 3545: 3518: 3475: 3454:(7): 1186–96. 3434: 3393: 3382: 3330: 3321:|journal= 3285: 3259: 3215: 3156: 3113: 3064: 3050: 3037: 3002:Molecular Cell 2985: 2936: 2927:|journal= 2891: 2865: 2836:(11): 623–37. 2813: 2762: 2719: 2670: 2621: 2578: 2537: 2514: 2465: 2424: 2381: 2340: 2301:(11): 4781–5. 2281: 2232: 2189: 2140: 2105: 2068:BioData Mining 2054: 2011: 1968: 1909: 1874: 1823: 1808: 1769: 1740:(37): 5310–8. 1715: 1673: 1633: 1612:(5): 599–606. 1592: 1565:(3): 195–211. 1508: 1408: 1350: 1300: 1242: 1235: 1207: 1205: 1202: 1201: 1200: 1195: 1190: 1185: 1180: 1175: 1168: 1165: 1122:trichostatin A 1105: 1102: 1074:histone 4 (H4) 1070:histone 3 (H3) 1035:of the brain, 1026:splice variant 989: 986: 938:overexpression 925: 922: 888: 885: 883: 882:Human diseases 880: 873:(CBP), to the 846: 843: 817: 814: 782:amino terminal 758: 755: 753: 750: 741: 738: 736: 735:Class IV HDACs 733: 721:ubiquitination 700: 697: 622: 619: 617: 616:Class II HDACs 614: 610:Northern blots 601: 598: 583:receptors and 553: 550: 451: 448: 446: 443: 390: 387: 354: 351: 323:Main article: 320: 317: 284: 281: 247: 244: 238: 235: 221: 218: 205: 197: 185: 141: 138: 116:marker within 15: 9: 6: 4: 3: 2: 4974: 4963: 4960: 4958: 4955: 4953: 4950: 4949: 4947: 4932: 4929: 4927: 4924: 4922: 4919: 4918: 4916: 4913: 4908: 4901: 4895: 4891: 4888: 4885: 4883: 4879: 4876: 4873: 4872: 4870: 4866: 4860: 4857: 4855: 4852: 4850: 4847: 4846: 4844: 4840: 4834: 4831: 4829: 4826: 4824: 4821: 4817: 4814: 4812: 4809: 4808: 4807: 4804: 4800: 4797: 4795: 4792: 4790: 4787: 4785: 4782: 4780: 4777: 4776: 4775: 4772: 4771: 4769: 4765: 4755: 4752: 4748: 4745: 4743: 4740: 4738: 4735: 4734: 4733: 4730: 4729: 4727: 4723: 4713: 4710: 4709: 4707: 4704: 4700: 4692: 4689: 4688: 4687: 4686: 4684: 4681: 4677: 4669: 4666: 4664: 4661: 4658: 4657: 4656: 4653: 4651: 4648: 4644: 4641: 4640: 4639: 4635: 4632: 4631: 4629: 4626: 4622: 4617: 4613: 4610: 4606: 4598: 4597:trp repressor 4595: 4593: 4592:lac repressor 4590: 4589: 4588: 4585: 4581: 4578: 4576: 4573: 4571: 4568: 4566: 4563: 4561: 4558: 4556: 4553: 4552: 4551: 4548: 4547: 4545: 4541: 4538: 4536: 4532: 4527: 4523: 4519: 4518:Transcription 4512: 4507: 4505: 4500: 4498: 4493: 4492: 4489: 4477: 4476:Jacques Monod 4474: 4472: 4469: 4468: 4466: 4462: 4454: 4451: 4449: 4446: 4445: 4444: 4441: 4439: 4438:Translational 4436: 4432: 4429: 4427: 4424: 4422: 4419: 4418: 4417: 4414: 4412: 4409: 4405: 4402: 4400: 4397: 4396: 4395: 4392: 4388: 4385: 4384: 4383: 4380: 4379: 4377: 4375: 4371: 4361: 4358: 4356: 4353: 4351: 4348: 4346: 4343: 4342: 4340: 4336: 4330: 4327: 4325: 4322: 4320: 4317: 4316: 4314: 4310: 4307: 4305: 4301: 4291: 4288: 4286: 4283: 4281: 4278: 4276: 4273: 4271: 4268: 4267: 4265: 4263: 4259: 4253: 4250: 4248: 4245: 4243: 4240: 4239: 4237: 4233: 4227: 4224: 4222: 4219: 4217: 4214: 4213: 4211: 4207: 4204: 4202: 4201:Transcription 4198: 4190: 4187: 4185: 4182: 4180: 4177: 4176: 4175: 4172: 4168: 4164: 4160: 4157: 4156: 4155: 4154:Central dogma 4152: 4150: 4147: 4146: 4144: 4142: 4136: 4132: 4125: 4120: 4118: 4113: 4111: 4106: 4105: 4102: 4096: 4093: 4092: 4080: 4076: 4072: 4068: 4064: 4060: 4057:(2): 126–35. 4056: 4052: 4045: 4037: 4033: 4028: 4023: 4019: 4015: 4012:(4): 664–76. 4011: 4007: 4003: 3996: 3988: 3984: 3979: 3974: 3970: 3966: 3962: 3958: 3954: 3947: 3939: 3935: 3930: 3925: 3921: 3917: 3913: 3909: 3905: 3898: 3890: 3886: 3881: 3876: 3871: 3866: 3862: 3858: 3854: 3847: 3839: 3835: 3830: 3825: 3821: 3817: 3813: 3809: 3805: 3798: 3790: 3786: 3781: 3776: 3772: 3768: 3765:(4): 479–88. 3764: 3760: 3756: 3749: 3741: 3737: 3732: 3727: 3722: 3717: 3713: 3709: 3705: 3701: 3697: 3690: 3682: 3678: 3673: 3668: 3664: 3660: 3656: 3652: 3648: 3644: 3640: 3633: 3625: 3621: 3616: 3611: 3607: 3603: 3599: 3592: 3584: 3580: 3576: 3572: 3568: 3564: 3560: 3556: 3549: 3541: 3537: 3534:(7): 539–43. 3533: 3529: 3528:Die Pharmazie 3522: 3514: 3510: 3506: 3502: 3498: 3494: 3490: 3486: 3479: 3471: 3467: 3462: 3457: 3453: 3449: 3445: 3438: 3430: 3426: 3421: 3416: 3412: 3408: 3404: 3397: 3391: 3386: 3378: 3374: 3369: 3364: 3360: 3356: 3353:(3): 335–48. 3352: 3348: 3344: 3337: 3335: 3326: 3314: 3306: 3302: 3297: 3292: 3288: 3286:9780444640765 3282: 3278: 3274: 3270: 3263: 3255: 3251: 3247: 3243: 3239: 3235: 3231: 3227: 3219: 3211: 3207: 3202: 3197: 3192: 3187: 3183: 3179: 3175: 3171: 3167: 3160: 3152: 3148: 3144: 3140: 3136: 3132: 3129:(6): 428–37. 3128: 3124: 3117: 3109: 3105: 3100: 3095: 3091: 3087: 3083: 3079: 3075: 3068: 3060: 3054: 3044: 3042: 3033: 3029: 3024: 3019: 3015: 3011: 3008:(5): 712–27. 3007: 3003: 2999: 2992: 2990: 2981: 2977: 2972: 2967: 2963: 2959: 2956:(2): 145–53. 2955: 2951: 2947: 2940: 2932: 2920: 2912: 2908: 2903: 2898: 2894: 2892:9780128009772 2888: 2884: 2880: 2876: 2869: 2861: 2857: 2852: 2847: 2843: 2839: 2835: 2831: 2827: 2820: 2818: 2809: 2805: 2800: 2795: 2790: 2785: 2781: 2777: 2773: 2766: 2758: 2754: 2750: 2746: 2742: 2738: 2734: 2730: 2723: 2715: 2711: 2706: 2701: 2697: 2693: 2689: 2685: 2681: 2674: 2666: 2662: 2657: 2652: 2648: 2644: 2641:(6): 631–47. 2640: 2636: 2632: 2625: 2617: 2613: 2609: 2605: 2601: 2597: 2593: 2589: 2582: 2574: 2570: 2565: 2560: 2557:(3): 552–63. 2556: 2552: 2548: 2541: 2533: 2529: 2525: 2518: 2510: 2506: 2501: 2496: 2492: 2488: 2484: 2480: 2476: 2469: 2461: 2457: 2452: 2447: 2444:(3): 552–63. 2443: 2439: 2435: 2428: 2420: 2416: 2412: 2408: 2404: 2400: 2397:(5): 337–56. 2396: 2392: 2385: 2377: 2373: 2368: 2363: 2360:(5): 659–65. 2359: 2355: 2351: 2344: 2336: 2332: 2327: 2322: 2317: 2312: 2308: 2304: 2300: 2296: 2292: 2285: 2277: 2273: 2268: 2263: 2259: 2255: 2252:(7): 457–69. 2251: 2247: 2243: 2236: 2228: 2224: 2220: 2216: 2212: 2211:10.1038/10640 2208: 2204: 2200: 2193: 2185: 2181: 2177: 2173: 2168: 2163: 2160:(2): 263–71. 2159: 2155: 2151: 2144: 2136: 2132: 2128: 2124: 2121:(1): 185–98. 2120: 2116: 2109: 2101: 2097: 2092: 2087: 2082: 2077: 2073: 2069: 2065: 2058: 2050: 2046: 2042: 2038: 2034: 2030: 2027:(3): 259–66. 2026: 2022: 2015: 2006: 2001: 1996: 1991: 1987: 1983: 1979: 1972: 1964: 1960: 1955: 1950: 1945: 1940: 1936: 1932: 1929:(5): 786–94. 1928: 1924: 1920: 1913: 1905: 1901: 1897: 1893: 1890:(2): 155–61. 1889: 1885: 1878: 1870: 1866: 1861: 1856: 1851: 1846: 1842: 1838: 1837:PLOS Genetics 1834: 1827: 1819: 1815: 1811: 1809:9780120342679 1805: 1801: 1797: 1793: 1789: 1782: 1780: 1778: 1776: 1774: 1765: 1761: 1757: 1753: 1748: 1743: 1739: 1735: 1731: 1724: 1722: 1720: 1711: 1707: 1703: 1699: 1696:(3): 433–44. 1695: 1691: 1684: 1682: 1680: 1678: 1669: 1665: 1661: 1657: 1654:(9): 836–45. 1653: 1649: 1642: 1640: 1638: 1629: 1625: 1620: 1615: 1611: 1607: 1603: 1596: 1588: 1584: 1580: 1576: 1572: 1568: 1564: 1560: 1559:Cell Research 1553: 1551: 1549: 1547: 1545: 1543: 1541: 1539: 1537: 1535: 1533: 1531: 1529: 1527: 1525: 1523: 1521: 1519: 1517: 1515: 1513: 1504: 1500: 1495: 1490: 1486: 1482: 1478: 1474: 1470: 1463: 1461: 1459: 1457: 1455: 1453: 1451: 1449: 1447: 1445: 1443: 1441: 1439: 1437: 1435: 1433: 1431: 1429: 1427: 1425: 1423: 1421: 1419: 1417: 1415: 1413: 1404: 1400: 1396: 1392: 1388: 1387:10.1038/38664 1384: 1380: 1376: 1372: 1368: 1361: 1354: 1346: 1342: 1338: 1334: 1330: 1326: 1323:(8): 615–26. 1322: 1318: 1311: 1309: 1307: 1305: 1296: 1292: 1287: 1282: 1279:(3): 209–21. 1278: 1274: 1270: 1263: 1261: 1259: 1257: 1255: 1253: 1251: 1249: 1247: 1238: 1232: 1228: 1221: 1219: 1217: 1215: 1213: 1208: 1199: 1196: 1194: 1191: 1189: 1186: 1184: 1181: 1179: 1176: 1174: 1171: 1170: 1164: 1162: 1158: 1157:Schizophrenia 1152: 1150: 1146: 1142: 1138: 1134: 1130: 1127: 1126:cardiomyocyte 1123: 1118: 1113: 1111: 1101: 1098: 1096: 1090: 1087: 1083: 1079: 1075: 1071: 1067: 1063: 1059: 1057: 1053: 1049: 1044: 1042: 1038: 1034: 1030: 1027: 1023: 1019: 1016: 1012: 1008: 1004: 1002: 998: 994: 985: 981: 979: 975: 971: 967: 962: 958: 953: 951: 947: 943: 942:tumorigenesis 939: 935: 931: 921: 918: 914: 909: 907: 903: 899: 895: 879: 876: 872: 868: 864: 860: 856: 852: 842: 839: 835: 830: 828: 823: 813: 811: 807: 803: 798: 796: 792: 788: 783: 778: 776: 772: 768: 764: 763:transcription 749: 746: 732: 730: 729:cell motility 726: 722: 718: 714: 710: 706: 696: 694: 690: 686: 682: 678: 673: 668: 664: 660: 656: 652: 647: 644: 640: 636: 632: 628: 613: 611: 606: 597: 595: 591: 586: 582: 578: 574: 570: 567:as well as a 566: 562: 558: 549: 547: 542: 538: 534: 531: 527: 526:embryogenesis 523: 519: 514: 510: 506: 501: 499: 495: 491: 486: 482: 478: 474: 470: 465: 460: 456: 445:Class I HDACs 442: 440: 436: 432: 428: 424: 420: 416: 412: 408: 404: 400: 396: 386: 384: 380: 376: 372: 368: 364: 360: 350: 348: 344: 340: 335: 331: 326: 316: 314: 310: 306: 303: 299: 295: 291: 280: 278: 274: 273:growth-factor 270: 266: 262: 258: 254: 243: 230: 226: 217: 213: 209: 203: 195: 191: 182: 179: 178:minor grooves 174: 170: 166: 162: 158: 154: 146: 137: 135: 131: 127: 126:transcription 123: 119: 115: 111: 107: 102: 100: 96: 92: 88: 84: 80: 76: 71: 69: 65: 61: 57: 53: 49: 45: 21: 4654: 4453:irreversible 4338:Key elements 4289: 4235:Key elements 4149:Genetic code 4139:Introduction 4054: 4050: 4044: 4009: 4005: 3995: 3960: 3956: 3946: 3911: 3907: 3897: 3860: 3856: 3846: 3811: 3807: 3797: 3762: 3758: 3748: 3703: 3699: 3689: 3646: 3642: 3632: 3605: 3601: 3591: 3561:(6): 570–5. 3558: 3554: 3548: 3531: 3527: 3521: 3491:(4): 265–9. 3488: 3484: 3478: 3451: 3447: 3437: 3410: 3406: 3396: 3385: 3350: 3346: 3268: 3262: 3232:(2): 312–9. 3229: 3225: 3218: 3173: 3169: 3159: 3126: 3122: 3116: 3081: 3077: 3067: 3053: 3005: 3001: 2953: 2949: 2939: 2874: 2868: 2833: 2829: 2779: 2775: 2765: 2732: 2728: 2722: 2687: 2683: 2673: 2638: 2634: 2624: 2591: 2587: 2581: 2554: 2550: 2540: 2523: 2517: 2482: 2478: 2468: 2441: 2437: 2427: 2394: 2390: 2384: 2357: 2353: 2343: 2298: 2294: 2284: 2249: 2245: 2235: 2205:(7): 601–4. 2202: 2198: 2192: 2157: 2153: 2143: 2118: 2114: 2108: 2071: 2067: 2057: 2024: 2020: 2014: 1985: 1981: 1971: 1926: 1922: 1912: 1887: 1883: 1877: 1840: 1836: 1826: 1791: 1787: 1737: 1733: 1693: 1689: 1651: 1647: 1609: 1605: 1595: 1562: 1558: 1476: 1472: 1370: 1366: 1353: 1320: 1316: 1276: 1272: 1226: 1153: 1114: 1107: 1099: 1091: 1060: 1045: 1005: 991: 982: 954: 927: 910: 906:theophylline 890: 878:activation. 848: 831: 822:Histone code 819: 799: 779: 760: 743: 702: 681:ossification 648: 624: 603: 555: 541:upregulation 502: 453: 392: 383:bromodomains 356: 328: 286: 279:holoenzyme. 249: 240: 228: 214: 210: 183: 151: 103: 85:" (HAT) or " 72: 58:core of the 43: 42: 4903:Termination 4779:Pribnow box 4747:Corepressor 4742:Coactivator 4543:prokaryotic 4304:Translation 4141:to genetics 3963:(12): e64. 3649:(1): 25–9. 2735:(1): 21–2. 2690:(1): 31–9. 2485:(1): 14–8. 1188:Acetylation 1137:hypertrophy 1082:upregulated 950:oncogenesis 869:, GCN5 and 851:bromodomain 845:Bromodomain 810:bromodomain 687:-dependent 677:chondrocyte 667:hypertrophy 539:. Not even 520:. In HDAC1 307:during the 283:MYST family 259:, HPA2 and 246:GNAT family 153:Nucleosomes 130:euchromatin 110:nucleosomes 104:Acetylated 91:Acetylation 4946:Categories 4931:Rho factor 4921:Terminator 4912:eukaryotic 4887:eukaryotic 4868:Elongation 4854:Eukaryotic 4842:Initiation 4625:nucleosome 4608:eukaryotic 4580:gal operon 4575:ara operon 4570:Gua Operon 4565:gab operon 4560:trp operon 4555:lac operon 4526:Eukaryotic 4448:reversible 4411:lac operon 4387:imprinting 4382:Epigenetic 4374:Regulation 4329:Eukaryotic 4275:5' capping 4226:Eukaryotic 3863:: 641979. 1794:: 181–99. 1204:References 1198:Nucleosome 1037:Delta FosB 1031:. In the 1029:Delta FosB 1001:addictions 993:Epigenetic 961:Vorinostat 946:metastasis 930:epigenetic 787:nucleosome 561:C-terminal 546:cross-talk 353:Other HATs 339:cell-cycle 294:Drosophila 265:myogenesis 232:functions. 114:epigenetic 64:acetylated 60:nucleosome 52:N-terminal 4907:bacterial 4875:bacterial 4849:Bacterial 4823:Insulator 4767:Promotion 4737:Activator 4587:Repressor 4522:Bacterial 4319:Bacterial 4216:Bacterial 3323:ignored ( 3313:cite book 2929:ignored ( 2919:cite book 2782:(1): 25. 2757:262487540 1648:BioEssays 1317:BioEssays 1129:autophagy 1095:chromatin 1041:addiction 1007:Cigarette 988:Addiction 795:silencing 699:Class IIB 689:apoptosis 621:Class IIA 573:cytoplasm 464:cofactors 347:apoptosis 309:leptotene 118:chromatin 4957:Proteins 4828:Silencer 4806:Enhancer 4794:CAAT box 4784:TATA box 4774:Promoter 4431:microRNA 4345:Ribosome 4324:Archaeal 4280:Splicing 4252:Promoter 4221:Archaeal 4165: → 4161: → 4071:19917878 4036:24006238 3987:22832356 3938:14517255 3889:24693336 3838:24310814 3789:12202037 3740:21367693 3681:19568876 3624:18797138 3583:24182756 3575:25867833 3540:16076083 3513:20849951 3505:24552452 3470:18482162 3429:28912356 3377:19447090 3305:29478612 3254:14013417 3246:22684622 3210:11572966 3151:19157711 3143:25083822 3108:22049069 3032:27259203 2980:20425300 2911:25410541 2860:21989194 2808:29784032 2749:17269160 2714:16960145 2665:21941619 2608:17694083 2588:Oncogene 2573:15738302 2532:18204158 2509:24527405 2460:15738302 2419:12172346 2411:24751816 2376:19736624 2276:20574448 2227:22196542 2219:10404206 2184:16237908 2176:11057899 2135:18804549 2100:26140054 2049:23873925 2041:23463310 1963:14172992 1904:11250138 1869:29795555 1818:14969728 1764:10662910 1756:17694074 1734:Oncogene 1710:11492997 1668:10944586 1587:30268983 1579:17325692 1503:12429021 1345:35433573 1295:16877467 1167:See also 1078:"reward" 1052:amygdala 1018:promoter 1011:nicotine 875:promoter 775:histones 643:isoforms 435:Sirtuins 379:TAFII250 332:and the 106:histones 4754:Inducer 4621:histone 4184:RNA→DNA 4179:RNA→RNA 4167:Protein 4079:3112549 4027:3805871 3978:3305989 3880:3945289 3829:3983897 3780:4459650 3731:3053983 3708:Bibcode 3672:2698246 3651:Bibcode 3368:2779727 3296:5868351 3178:Bibcode 3099:4042673 3023:5476208 2971:2847696 2902:5914502 2851:3272277 2799:5993135 2705:1785068 2656:3174261 2616:2976852 2500:3921865 2367:2921942 2335:8197135 2303:Bibcode 2267:3262678 2091:4488123 2005:3265906 1931:Bibcode 1860:6019819 1628:9499396 1494:1223209 1403:4419816 1395:9311776 1375:Bibcode 1337:9780836 1084:in the 1066:cocaine 1048:alcohol 1020:in the 997:histone 959:(FDA), 838:meiosis 834:mitosis 725:tubulin 693:T cells 594:mitosis 518:nucleus 477:Co-REST 313:meiosis 79:enzymes 56:histone 4550:Operon 4077: 4069: 4034: 4024: 3985: 3975: 3936: 3929:204485 3926: 3887: 3877: 3836: 3826: 3787: 3777: 3738: 3728: 3679: 3669: 3622: 3581: 3573: 3538: 3511: 3503: 3468: 3427: 3375: 3365: 3347:Neuron 3303: 3293: 3283: 3252: 3244: 3208: 3198: 3149: 3141: 3106: 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Histone acetylation and deacetylation

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