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.

274:. 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 156: 223:

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.

815:, 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 836:

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

652:. 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 326:. 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. 734:, 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 742:. 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. 31: 788:. 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. 522:) 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 804:. 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 1174:. 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. 236: 526:

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,

722:. 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-, 261:

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.

672:. 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 253:

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

959:, 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 974:

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

452:. 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. 3234:

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

1014:, 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. 498:

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

582:. 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 477:

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

1123:, 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. 3494:

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".

131:. 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 623:

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.

3414:"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" 2533:

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

1061:. 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 4519: 3564:

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".

800:. This opens up the usually tightly packed nucleosome and allows transcription machinery to come into contact with the DNA template, leading to 619:

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

135:. As a consequence, the condensed chromatin is transformed into a more relaxed structure that is associated with greater levels of gene 139:. This relaxation can be reversed by deacetylation catalyzed by HDAC activity. Relaxed, transcriptionally active DNA is referred to as 4184: 4164: 1339: 4272: 3295: 2901: 1818: 676:

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

706:. HDAC9 KO mice are shown to suffer from cardiac hypertrophy which is exacerbated in mice that are double KO for HDACs 9 and 5. 4869: 4426: 4370: 682: 595: 591: 551: 3455:"Alcohol induces DNA damage and the Fanconi anemia D2 protein implicating FANCD2 in the DNA damage response pathways in brain" 4365: 2689:

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).

3085:"Molecular mechanism for a gateway drug: epigenetic changes initiated by nicotine prime gene expression by cocaine" 1024:. After 7 days of nicotine treatment of mice, acetylation of both histone H3 and histone H4 was increased at the 4742: 4678: 4648: 4626: 1183: 908: 377: 200: 188: 93: 1370: 4922: 4897: 4864: 4536: 4528: 4448: 4236: 4149: 4118: 1120: 773: 723: 504: 353: 286:-signaled activation. Elp3 has the ability to acetylate all histone subunits and also shows involvement in the 136: 3705:

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

2302:"Mitogen-stimulated phosphorylation of histone H3 is targeted to a small hyperacetylation-sensitive fraction" 112:) to another. Deacetylation is simply the reverse reaction where an acetyl group is removed from a molecule. 4917: 4885: 4859: 4843: 4532: 4409: 4226: 4211: 474: 304: 2400:

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.

235: 123:, the basic structural unit of the chromosomes and ultimately higher order structures, represent a type of 4752: 4505: 4414: 4339: 4231: 695: 373: 4936: 4931: 4799: 4701: 4329: 4314: 4194: 1741:"HATs and HDACs: from structure, function and regulation to novel strategies for therapy and prevention" 1155: 816: 579: 469: 1893:

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

4833: 4747: 4713: 4607: 4436: 4334: 4252: 3718: 3661: 3188: 2313: 1941: 1385: 1108:. Such epigenetic scars likely contribute to the persistent epigenetic changes found in addictions. 1036: 943:

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

881: 837: 519: 344: 3964:"Disease- and age-related changes in histone acetylation at gene promoters in psychiatric disorders" 3915:"Essential function of p300 acetyltransferase activity in heart, lung and small intestine formation" 1930:"Acetylation and Methylation of Histones and Their Possible Role in the Regulation of RNA Synthesis" 4816: 4784: 4670: 4644: 4262: 2030:

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

30: 4967: 4904: 4481: 4077: 4042: 3993: 3944: 3895: 3844: 3795: 3746: 3707:"Histone deacetylase (HDAC) inhibitors attenuate cardiac hypertrophy by suppressing autophagy" 3687: 3630: 3581: 3546: 3511: 3476: 3435: 3383: 3311: 3291: 3252: 3216: 3149: 3114: 3038: 2986: 2917: 2897: 2866: 2814: 2755: 2720: 2671: 2614: 2579: 2538: 2515: 2466: 2417: 2382: 2341: 2282: 2225: 2182: 2141: 2106: 2047: 1969: 1910: 1875: 1824: 1814: 1762: 1716: 1674: 1634: 1585: 1509: 1401: 1343: 1301: 1241: 1096: 1043: 1032: 811:

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

507:. HDACs 1 and 2 have been found to express regulatory roles in key cell cycle genes including 483: 287: 204: 109: 2075:"Uncovering correlated variability in epigenomic datasets using the Karhunen-Loeve transform" 4826: 4809: 4069: 4032: 4024: 3983: 3975: 3934: 3926: 3885: 3875: 3834: 3826: 3785: 3777: 3736: 3726: 3677: 3669: 3620: 3573: 3503: 3466: 3425: 3373: 3365: 3301: 3283: 3244: 3206: 3196: 3141: 3104: 3096: 3028: 3020: 2976: 2968: 2907: 2889: 2856: 2848: 2804: 2794: 2747: 2710: 2702: 2661: 2653: 2606: 2569: 2505: 2497: 2456: 2409: 2372: 2331: 2321: 2272: 2264: 2253:"Covalent histone modifications--miswritten, misinterpreted and mis-erased in human cancers" 2217: 2172: 2133: 2096: 2086: 2039: 2010: 2000: 1959: 1949: 1902: 1865: 1855: 1806: 1752: 1708: 1666: 1624: 1577: 1499: 1491: 1393: 1335: 1291: 1091:

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

420:. Class II is divided into two subgroups, Class IIA and Class IIB. Class IIA includes HDACs 279: 1146:

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

4690: 4458: 4295: 4141: 3766:"Class II histone deacetylases act as signal-responsive repressors of cardiac hypertrophy" 3400: 3335: 2941: 2888:. Progress in Molecular Biology and Translational Science. Vol. 128. pp. 51–87. 1203: 1066: 912: 653: 515: 315: 308: 147:. Condensation can be brought about by processes including deacetylation and methylation. 144: 78: 3864:"Dysregulation of histone acetyltransferases and deacetylases in cardiovascular diseases" 738:, acting as a tubulin deacetylase which helps in the regulation of microtubule-dependent 4497: 3722: 3665: 3192: 2317: 1945: 1389: 4900: 4888: 4838: 4285: 4257: 4037: 4012: 3988: 3963: 3890: 3863: 3839: 3814: 3790: 3765: 3741: 3706: 3682: 3649: 3378: 3353: 3306: 3287: 3109: 3084: 3033: 3008: 2981: 2956: 2912: 2893: 2861: 2836: 2809: 2782: 2715: 2690: 2666: 2641: 2510: 2485: 2377: 2360: 2277: 2252: 2101: 2074: 2015: 1988: 1870: 1843: 1504: 1479: 1132: 960: 952: 948: 805: 792: 739: 669: 532: 17: 3939: 3914: 3781: 2177: 2160: 1964: 1929: 1906: 1844:"MOF influences meiotic expansion of H2AX phosphorylation and spermatogenesis in mice" 1810: 4956: 4602: 4486: 4173: 3471: 3454: 3354:"Genome-wide analysis of chromatin regulation by cocaine reveals a role for sirtuins" 3211: 3176: 2767: 2336: 2301: 1167: 1088: 620: 587: 536: 283: 3593: 3523: 3264: 3161: 2429: 2237: 2194: 2059: 1774: 1597: 1355: 203:(HATs). HAT molecules facilitate the transfer of an acetyl group from a molecule of 4360: 4290: 4159: 4089: 2626: 2208:

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

1413: 916: 832: 691: 660:

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

528: 372:, which has a HAT domain located at the C-terminus end of the protein along with a 2501: 3369: 3145: 3100: 3024: 2706: 2574: 2558:"Histone acetylation and deacetylation: importance in inflammatory lung diseases" 2557: 2461: 2445:"Histone acetylation and deacetylation: importance in inflammatory lung diseases" 2444: 2137: 1860: 4789: 4757: 4660: 4463: 4392: 3609:"The peroxidative DNA damage and apoptosis in methamphetamine-treated rat brain" 1478:

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

1198: 1147: 1003: 861: 820: 727: 687: 677: 393: 385: 175: 171: 140: 101: 3711:

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

3181:

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

2306:

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

1934:

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

50:

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

4941: 4635: 4590: 4580: 4575: 4570: 4565: 4421: 4028: 3830: 3673: 3248: 2972: 2799: 2091: 1208: 1084: 1080: 1058: 971: 956: 940: 797: 571: 381: 349: 275: 187:

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".

2657: 1480:"Histone deacetylases (HDACs): characterization of the classical HDAC family" 539:

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

4597: 3731: 3577: 3507: 2361:"The role of human bromodomains in chromatin biology and gene transcription" 2326: 2005: 1139: 1105: 1051: 1017: 1011: 731: 699: 600: 583: 357: 319: 128: 74: 4081: 4073: 4046: 3997: 3948: 3930: 3899: 3848: 3799: 3764:

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

3750: 3691: 3634: 3585: 3550: 3515: 3480: 3439: 3387: 3315: 3256: 3220: 3201: 3153: 3118: 3042: 2990: 2921: 2870: 2818: 2759: 2724: 2675: 2618: 2610: 2583: 2542: 2519: 2470: 2421: 2386: 2286: 2229: 2186: 2145: 2110: 2051: 1973: 1914: 1879: 1828: 1766: 1757: 1740: 1720: 1712: 1678: 1589: 1513: 1305: 3880: 2345: 1954: 1657:

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

1638: 1581: 1405: 1347: 1296: 1279: 1069:

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

4804: 4794: 4441: 4431: 4355: 1629: 1612: 1340:

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

1062: 1021: 904: 785: 1699:

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

490:. The Sin3 complex and the NuRD complex both contain HDACs 1 and 2, the 4764: 4631: 4177: 3979: 3625: 3608: 3430: 3413: 1495: 1076: 1007: 951:

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

848: 844: 735: 604: 445: 323: 211:

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

116: 66: 2043: 396:

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

4560: 3607:

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

923: 865: 777: 755: 730:(HUB) domain in the C-terminus which shows some functions related to 719: 703: 599:

functions in cell cycle progression. HDAC3 also shows involvement in

547: 523: 449: 441: 215:(HDACs) catalyze the removal of the acetyl group with a molecule of H 195:

The mechanism for acetylation and deacetylation takes place on the NH

105: 89: 58: 4013:"Epigenetic mechanisms of neurodegeneration in Huntington's disease" 2852: 2751: 2597:

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

2484:

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

2413: 2268: 1010:

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

34:

The crystal structure of the nucleosome core particle consisting of

3650:"Epigenetic abnormalities in cardiac hypertrophy and heart failure" 3453:

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

3282:. Handbook of Clinical Neurology. Vol. 148. pp. 747–765. 1671:

10.1002/1521-1878(200009)22:9<836::AID-BIES9>3.0.CO;2-X

4821: 4673: 4199: 4110: 2221: 1397: 1151: 988: 984: 980: 976: 944: 715: 661: 649: 645: 641: 637: 615: 567: 495: 491: 487: 479: 465: 437: 433: 429: 425: 421: 417: 413: 409: 405: 340: 312: 234: 154: 29: 1020:

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

108:

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

4892: 4722: 4653: 3278:

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

2486:"Epigenetic regulation in allergic diseases and related studies" 1159: 1047: 1039: 1025: 877: 873: 665: 389: 271: 267: 263: 4501: 4114: 2738:

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

1613:"Histone acetylation and transcriptional regulatory mechanisms" 1278:

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

1231: 1229: 1227: 1225: 1223: 592:

Silencing Mediator for Retinoic Acid and Thyroid Hormone (SMRT)

4169: 1371:"Histone acetylation in chromatin structure and transcription" 781: 543: 508: 500: 167: 132: 1104:

epigenetic alterations, and thus leave an epigenetic scar on

84:

Histone acetylation and deacetylation are essential parts of

2126:

The International Journal of Biochemistry & Cell Biology

868:

recognition on histones by nucleosome remodelling proteins.

4011:

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

2640:

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

2300:

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

702:. This interaction leads to a role in clonal expansion of 4105:

Animation of histone tail acetylation and deacetylation:

3862:

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

2837:"Transcriptional and epigenetic mechanisms of addiction" 772:

The discovery of histone acetylation causing changes in

392:

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

143:. More condensed (tightly packed) DNA is referred to as 3813:

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

3566:

Clinical and Experimental Pharmacology & Physiology

3496:

Clinical and Experimental Pharmacology & Physiology

3401:

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

3177:"DeltaFosB: a sustained molecular switch for addiction" 1236:

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

484:

Nucleosome Remodelling and Deacetylating complex (NuRD)

159:

Histone tails and their function in chromatin formation

2161:"Signaling to chromatin through histone modifications" 1075:

occurs in about 0.5% of the US population. Repeated

819:

interact with the acetylated histone tails via their

2159:

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

4913: 4878: 4852: 4777: 4735: 4712: 4689: 4625: 4618: 4553: 4544: 4474: 4383: 4348: 4322: 4313: 4271: 4245: 4219: 4210: 4148: 3815:"Histone deacetylase signaling in cardioprotection" 2886:

Epigenetics and Neuroplasticity—Evidence and Debate

2365:

Current Opinion in Drug Discovery & Development

1079:administration in mice induces hyperacetylation of 657:50% similarity to the N-terminus of HDACs 4 and 5. 3412:Adhami N, Chen Y, Martins-Green M (October 2017). 2957:"Epigenetic regulation in substance use disorders" 1142:. Studies on p300 and CREB-binding protein linked 681:with HDAC3 as a co-recruitment factor to the SMRT/ 341:Adenoviral E1A-associated protein of 300kDa (p300) 264:p300/CREB-binding protein associated factor (PCAF) 119:, octameric proteins that organize chromatin into 3009:"Epigenome Maintenance in Response to DNA Damage" 2830: 2828: 1284:Briefings in Functional Genomics & Proteomics 586:. HDAC3 has even been found to interact with the 380:in the middle. Another is ATF-2 which contains a 3175:Nestler EJ, Barrot M, Self DW (September 2001). 2642:"Histone modifiers in cancer: friends or foes?" 1989:"Vincent Allfrey's Work on Histone Acetylation" 1240:(Seventh ed.). Boston: Pearson/CSH Press. 947:cells is very different from normal cells. The 240:Histone acetylation alters chromatin structure. 3459:Alcoholism: Clinical and Experimental Research 3134:The American Journal of Drug and Alcohol Abuse 1928:Allfrey VG, Faulkner R, Mirsky AE (May 1964). 864:is a motif that is responsible for acetylated 311:in mice as it is involved in the expansion of 4513: 4126: 2783:"Metabolic recoding of epigenetics in cancer" 1895:Current Opinion in Genetics & Development 1694: 1692: 1690: 1688: 1057:About 7% of the US population is addicted to 88:. These reactions are typically catalysed by 8: 3654:Environmental Health and Preventive Medicine 1563: 1561: 1559: 1557: 1555: 1553: 1551: 1549: 1547: 1545: 1543: 1473: 1471: 1469: 1467: 1465: 1463: 1461: 1459: 1457: 1455: 1453: 1451: 1449: 1447: 1445: 1443: 27:Biological processes used in gene regulation 3962:Tang B, Dean B, Thomas EA (December 2011). 1541: 1539: 1537: 1535: 1533: 1531: 1529: 1527: 1525: 1523: 1441: 1439: 1437: 1435: 1433: 1431: 1429: 1427: 1425: 1423: 514:Activity of these HDACs can be affected by 192:occur post-translation and are reversible. 4622: 4550: 4520: 4506: 4498: 4319: 4281:Precursor mRNA (pre-mRNA / hnRNA) 4216: 4133: 4119: 4111: 3347: 3345: 2556:Barnes PJ, Adcock IM, Ito K (March 2005). 2443:Barnes PJ, Adcock IM, Ito K (March 2005). 541:Cyclin-Dependent Kinase Inhibitors (CDKIs) 527:2 have been found only exclusively in the 518:. An increased amount of phosphorylation ( 388:with a HAT domain in-between. The last is 4036: 3987: 3938: 3889: 3879: 3868:Oxidative Medicine and Cellular Longevity 3838: 3789: 3740: 3730: 3681: 3624: 3470: 3429: 3377: 3305: 3210: 3200: 3108: 3032: 3007:Dabin J, Fortuny A, Polo SE (June 2016). 2980: 2911: 2860: 2808: 2798: 2714: 2665: 2573: 2509: 2460: 2376: 2335: 2325: 2276: 2176: 2100: 2090: 2032:Nature Structural & Molecular Biology 2014: 2004: 1963: 1953: 1869: 1859: 1756: 1628: 1503: 1295: 1273: 1271: 1269: 1267: 1265: 1263: 1261: 1259: 1257: 231:Histone acetylation/deacetylation enzymes 3054: 3052: 3002: 3000: 1792: 1790: 1788: 1786: 1784: 1652: 1650: 1648: 1280:"Histone acetylation in gene regulation" 603:and a transcription independent role in 2835:Robison AJ, Nestler EJ (October 2011). 1734: 1732: 1730: 1219: 382:transcriptional activation (ACT) domain 3331: 3321: 2937: 2927: 2535:Journal of Physiology and Pharmacology 2251:Chi P, Allis CD, Wang GG (July 2010). 1135:was reported to reduce stress induced 386:basic zipper DNA-binding (bZip) domain 4666:Histone acetylation and deacetylation 4301:Histone acetylation and deacetylation 2359:Sanchez R, Zhou MM (September 2009). 2073:Madrigal P, Krajewski P (July 2015). 1321: 1319: 1317: 1315: 928:chronic obstructive pulmonary disease 674:Ca/calmodulin-dependent kinase (CaMK) 596:Nuclear Receptor Co-Repressor (N-CoR) 370:steroid receptor coactivator 1 (SRC1) 55:Histone acetylation and deacetylation 7: 4366:Ribosome-nascent chain complex (RNC) 3819:Cellular and Molecular Life Sciences 3613:The Journal of Medical Investigation 694:. HDAC7 has been shown to suppress 690:hypertrophy and die due to extreme 376:and PAS A and PAS B domains with a 3288:10.1016/B978-0-444-64076-5.00048-X 2955:McQuown SC, Wood MA (April 2010). 2894:10.1016/B978-0-12-800977-2.00003-6 25: 3237:Journal of Molecular Neuroscience 662:C-terminal binding protein (CtBP) 576:Nuclear Localization Signal (NLS) 492:Rb-associated protein 48 (RbAp48) 3472:10.1111/j.1530-0277.2008.00673.x 2562:The European Respiratory Journal 2449:The European Respiratory Journal 666:myocyte enhancer factor 2 (MEF2) 535:, mice were found to die during 378:LXXLL receptor interacting motif 248:Histone acetyltransferase (HATs) 4973:Post-translational modification 4870:Archaeal transcription factor B 4371:Post-translational modification 1993:Journal of Biological Chemistry 1739:Yang XJ, Seto E (August 2007). 870:Posttranslational modifications 436:while Class IIB includes HDACs 57:are the processes by which the 3089:Science Translational Medicine 2740:Nature Reviews. Drug Discovery 2402:Nature Reviews. Drug Discovery 1369:Grunstein M (September 1997). 813:posttranslational modification 1: 3782:10.1016/S0092-8674(02)00861-9 2537:. 58 Suppl 5 (Pt 2): 453–60. 2502:10.5415/apallergy.2014.4.1.14 2178:10.1016/s0092-8674(00)00118-5 1907:10.1016/S0959-437X(00)00173-8 1811:10.1016/S0065-3233(04)67007-0 1799:Advances in Protein Chemistry 1238:Molecular biology of the gene 966:Approved in 2006 by the U.S. 636:The Class IIA HDACs includes 3370:10.1016/j.neuron.2009.03.026 3146:10.3109/00952990.2014.933840 3101:10.1126/scitranslmed.3003062 3025:10.1016/j.molcel.2016.04.006 2841:Nature Reviews. Neuroscience 2781:Wang YP, Lei QY (May 2018). 2707:10.1182/blood-2006-06-025999 2575:10.1183/09031936.05.00117504 2462:10.1183/09031936.05.00117504 2138:10.1016/j.biocel.2008.08.027 1861:10.1371/journal.pgen.1007300 1701:Journal of Molecular Biology 1087:at 1,696 genes in one brain 968:Food and Drug Administration 714:The Class IIB HDACs include 77:and deacetylated as part of 580:Nuclear Export Signal (NES) 503:, Rb binding protein 1 and 448:and Class IV contains only 400:Histone deacetylase (HDACs) 336:p300-CBP coactivator family 168:double-stranded DNA (dsDNA) 4989: 4546:Transcriptional regulation 2961:Current Psychiatry Reports 345:CREB-binding protein (CBP) 333: 201:histone acetyltransferases 4743:Transcription coregulator 4679:Histone acetyltransferase 4649:Histone methyltransferase 4627:Histone-modifying enzymes 4029:10.1007/s13311-013-0206-5 3831:10.1007/s00018-013-1516-9 3674:10.1007/s12199-007-0007-8 3249:10.1007/s12031-012-9829-y 2973:10.1007/s11920-010-0099-5 2800:10.1186/s40880-018-0302-3 2210:Nature Structural Biology 2092:10.1186/s13040-015-0051-7 1184:Histone acetyltransferase 1150:responsive genes such as 909:AP-1 transcription factor 444:. Class III contains the 282:-mediated activation and 94:histone acetyltransferase 65:tail protruding from the 4432:sequestration (P-bodies) 3968:Translational Psychiatry 3070:"Is nicotine addictive?" 2658:10.1177/1947601911417176 1121:transcription activators 768:Transcription regulation 104:is the process where an 4844:Internal control region 4410:Gene regulatory network 3732:10.1073/pnas.1015081108 3648:Mano H (January 2008). 3578:10.1111/1440-1681.12404 3508:10.1111/1440-1681.12218 2327:10.1073/pnas.91.11.4781 2006:10.1074/jbc.O112.000248 1987:Mukhopadhyay R (2012). 1617:Genes & Development 1611:Struhl K (March 1998). 1484:The Biochemical Journal 827:Histone code hypothesis 322:to pachytene stages of 307:. MOF also influences 18:Acetylation of histones 4415:cis-regulatory element 4074:10.1124/mol.109.061333 4062:Molecular Pharmacology 3280:Neurogenetics, Part II 3202:10.1073/pnas.191352698 2611:10.1038/sj.onc.1210610 2257:Nature Reviews. Cancer 1758:10.1038/sj.onc.1210599 1713:10.1006/jmbi.2001.4859 601:stem cell self-renewal 374:basic helix-loop-helix 244: 207:(Acetyl-CoA) to the NH 160: 51: 4937:Intrinsic termination 4702:DNA methyltransferase 2787:Cancer Communications 1955:10.1073/pnas.51.5.786 1582:10.1038/sj.cr.7310149 898:Inflammatory diseases 817:transcription factors 238: 158: 33: 4714:Chromatin remodeling 4437:alternative splicing 4427:Post-transcriptional 4253:Transcription factor 3931:10.1093/emboj/cdg502 2490:Asia Pacific Allergy 1630:10.1101/gad.12.5.599 882:CREB-binding protein 838:immediate early gene 808:gene transcription. 763:Biological functions 726:, and Brap2-related 520:hyperphosphorylation 501:Yin and Yang 1 (YY1) 213:histone deacetylases 61:residues within the 4671:Histone deacetylase 4661:Histone demethylase 4645:Histone methylation 4361:Transfer RNA (tRNA) 3881:10.1155/2014/641979 3723:2011PNAS..108.4123C 3666:2008EHPM...13...25M 3193:2001PNAS...9811042N 2318:1994PNAS...91.4781B 1946:1964PNAS...51..786A 1390:1997Natur.389..349G 1297:10.1093/bfgp/ell028 1194:Histone methylation 1189:Histone deacetylase 1144:cardiac hypertrophy 1128:cardiac hypertrophy 1126:Based on different 151:Mechanism of action 100:" (HDAC) activity. 98:histone deacetylase 4475:Influential people 4454:Post-translational 4273:Post-transcription 3980:10.1038/tp.2011.61 3626:10.2152/jmi.55.241 3431:10.1042/CS20171053 2646:Genes & Cancer 1496:10.1042/BJ20021321 1172:Huntington disease 911:. Treatments with 802:gene transcription 686:from a pronounced 533:knockout (KO) mice 473:incorporated with 245: 161: 52: 4963:Organic reactions 4950: 4949: 4905:RNA polymerase II 4773: 4772: 4731: 4730: 4495: 4494: 4379: 4378: 4309: 4308: 4185:Special transfers 4017:Neurotherapeutics 3424:(19): 2409–2426. 3095:(107): 107ra109. 2044:10.1038/nsmb.2470 1247:978-0-321-76243-6 1073:Cocaine addiction 1044:nucleus accumbens 1033:nucleus accumbens 1006:modifications of 926:. Patients with 728:zinc finger motif 559:between factors. 461:HDAC1 & HDAC2 288:RNA polymerase II 205:acetyl-coenzyme A 110:acetyl coenzyme A 16:(Redirected from 4980: 4827:Response element 4810:Response element 4623: 4551: 4522: 4515: 4508: 4499: 4320: 4217: 4135: 4128: 4121: 4112: 4094: 4093: 4057: 4051: 4050: 4040: 4008: 4002: 4001: 3991: 3959: 3953: 3952: 3942: 3919:The EMBO Journal 3910: 3904: 3903: 3893: 3883: 3859: 3853: 3852: 3842: 3810: 3804: 3803: 3793: 3761: 3755: 3754: 3744: 3734: 3702: 3696: 3695: 3685: 3645: 3639: 3638: 3628: 3604: 3598: 3597: 3561: 3555: 3554: 3534: 3528: 3527: 3491: 3485: 3484: 3474: 3450: 3444: 3443: 3433: 3418:Clinical Science 3409: 3403: 3398: 3392: 3391: 3381: 3349: 3340: 3339: 3333: 3329: 3327: 3319: 3309: 3275: 3269: 3268: 3231: 3225: 3224: 3214: 3204: 3172: 3166: 3165: 3129: 3123: 3122: 3112: 3080: 3074: 3073: 3066: 3060: 3056: 3047: 3046: 3036: 3004: 2995: 2994: 2984: 2952: 2946: 2945: 2939: 2935: 2933: 2925: 2915: 2881: 2875: 2874: 2864: 2832: 2823: 2822: 2812: 2802: 2778: 2772: 2771: 2735: 2729: 2728: 2718: 2686: 2680: 2679: 2669: 2637: 2631: 2630: 2594: 2588: 2587: 2577: 2553: 2547: 2546: 2530: 2524: 2523: 2513: 2481: 2475: 2474: 2464: 2440: 2434: 2433: 2397: 2391: 2390: 2380: 2356: 2350: 2349: 2339: 2329: 2297: 2291: 2290: 2280: 2248: 2242: 2241: 2205: 2199: 2198: 2180: 2156: 2150: 2149: 2121: 2115: 2114: 2104: 2094: 2070: 2064: 2063: 2027: 2021: 2020: 2018: 2008: 1999:(3): 2270–2271. 1984: 1978: 1977: 1967: 1957: 1925: 1919: 1918: 1890: 1884: 1883: 1873: 1863: 1839: 1833: 1832: 1794: 1779: 1778: 1760: 1736: 1725: 1724: 1696: 1683: 1682: 1654: 1643: 1642: 1632: 1608: 1602: 1601: 1565: 1518: 1517: 1507: 1490:(Pt 3): 737–49. 1475: 1418: 1417: 1384:(6649): 349–52. 1375: 1366: 1360: 1359: 1323: 1310: 1309: 1299: 1275: 1252: 1251: 1233: 280:nuclear-receptor 166:are portions of 49: 45: 41: 37: 21: 4988: 4987: 4983: 4982: 4981: 4979: 4978: 4977: 4953: 4952: 4951: 4946: 4921: 4915: 4909: 4874: 4848: 4769: 4727: 4708: 4691:DNA methylation 4685: 4629: 4614: 4540: 4526: 4496: 4491: 4470: 4405:Transcriptional 4375: 4344: 4305: 4296:Polyadenylation 4267: 4241: 4206: 4200:Protein→Protein 4151: 4144: 4142:Gene expression 4139: 4102: 4097: 4059: 4058: 4054: 4010: 4009: 4005: 3961: 3960: 3956: 3925:(19): 5175–85. 3912: 3911: 3907: 3861: 3860: 3856: 3812: 3811: 3807: 3763: 3762: 3758: 3704: 3703: 3699: 3647: 3646: 3642: 3606: 3605: 3601: 3563: 3562: 3558: 3536: 3535: 3531: 3493: 3492: 3488: 3452: 3451: 3447: 3411: 3410: 3406: 3399: 3395: 3351: 3350: 3343: 3330: 3320: 3298: 3277: 3276: 3272: 3233: 3232: 3228: 3187:(20): 11042–6. 3174: 3173: 3169: 3131: 3130: 3126: 3082: 3081: 3077: 3068: 3067: 3063: 3057: 3050: 3006: 3005: 2998: 2954: 2953: 2949: 2936: 2926: 2904: 2883: 2882: 2878: 2853:10.1038/nrn3111 2834: 2833: 2826: 2780: 2779: 2775: 2752:10.1038/nrd2227 2737: 2736: 2732: 2688: 2687: 2683: 2639: 2638: 2634: 2605:(37): 5420–32. 2596: 2595: 2591: 2555: 2554: 2550: 2532: 2531: 2527: 2483: 2482: 2478: 2442: 2441: 2437: 2414:10.1038/nrd4286 2399: 2398: 2394: 2358: 2357: 2353: 2299: 2298: 2294: 2269:10.1038/nrc2876 2250: 2249: 2245: 2207: 2206: 2202: 2158: 2157: 2153: 2123: 2122: 2118: 2072: 2071: 2067: 2029: 2028: 2024: 1986: 1985: 1981: 1927: 1926: 1922: 1892: 1891: 1887: 1854:(5): e1007300. 1841: 1840: 1836: 1821: 1796: 1795: 1782: 1738: 1737: 1728: 1698: 1697: 1686: 1656: 1655: 1646: 1610: 1609: 1605: 1567: 1566: 1521: 1477: 1476: 1421: 1373: 1368: 1367: 1363: 1325: 1324: 1313: 1277: 1276: 1255: 1248: 1235: 1234: 1221: 1217: 1204:Phosphorylation 1180: 1117: 1115:Other disorders 1067:opioid receptor 1001: 937: 913:corticosteroids 900: 895: 858: 829: 770: 765: 753: 748: 712: 634: 629: 613: 588:plasma membrane 565: 516:phosphorylation 463: 458: 402: 366: 354:differentiation 338: 332: 330:p300/CBP family 316:phosphorylation 309:spermatogenesis 296: 259: 250: 233: 218: 210: 198: 153: 145:heterochromatin 86:gene regulation 79:gene regulation 47: 43: 39: 35: 28: 23: 22: 15: 12: 11: 5: 4986: 4984: 4976: 4975: 4970: 4965: 4955: 4954: 4948: 4947: 4945: 4944: 4939: 4934: 4928: 4926: 4911: 4910: 4908: 4907: 4901:RNA polymerase 4895: 4889:RNA polymerase 4882: 4880: 4876: 4875: 4873: 4872: 4867: 4862: 4856: 4854: 4850: 4849: 4847: 4846: 4841: 4836: 4831: 4830: 4829: 4824: 4814: 4813: 4812: 4807: 4802: 4797: 4792: 4781: 4779: 4775: 4774: 4771: 4770: 4768: 4767: 4762: 4761: 4760: 4755: 4750: 4739: 4737: 4733: 4732: 4729: 4728: 4726: 4725: 4719: 4717: 4710: 4709: 4707: 4706: 4705: 4704: 4696: 4694: 4687: 4686: 4684: 4683: 4682: 4681: 4676: 4663: 4658: 4657: 4656: 4641: 4639: 4620: 4616: 4615: 4613: 4612: 4611: 4610: 4605: 4595: 4594: 4593: 4588: 4583: 4578: 4573: 4568: 4557: 4555: 4548: 4542: 4541: 4527: 4525: 4524: 4517: 4510: 4502: 4493: 4492: 4490: 4489: 4484: 4482:François Jacob 4478: 4476: 4472: 4471: 4469: 4468: 4467: 4466: 4461: 4451: 4446: 4445: 4444: 4439: 4434: 4424: 4419: 4418: 4417: 4412: 4402: 4401: 4400: 4389: 4387: 4381: 4380: 4377: 4376: 4374: 4373: 4368: 4363: 4358: 4352: 4350: 4346: 4345: 4343: 4342: 4337: 4332: 4326: 4324: 4317: 4311: 4310: 4307: 4306: 4304: 4303: 4298: 4293: 4288: 4283: 4277: 4275: 4269: 4268: 4266: 4265: 4260: 4258:RNA polymerase 4255: 4249: 4247: 4243: 4242: 4240: 4239: 4234: 4229: 4223: 4221: 4214: 4208: 4207: 4205: 4204: 4203: 4202: 4197: 4192: 4182: 4181: 4180: 4162: 4156: 4154: 4146: 4145: 4140: 4138: 4137: 4130: 4123: 4115: 4109: 4108: 4101: 4100:External links 4098: 4096: 4095: 4052: 4003: 3954: 3905: 3854: 3825:(9): 1673–90. 3805: 3756: 3717:(10): 4123–8. 3697: 3640: 3619:(3–4): 241–5. 3599: 3556: 3529: 3486: 3465:(7): 1186–96. 3445: 3404: 3393: 3341: 3332:|journal= 3296: 3270: 3226: 3167: 3124: 3075: 3061: 3048: 3013:Molecular Cell 2996: 2947: 2938:|journal= 2902: 2876: 2847:(11): 623–37. 2824: 2773: 2730: 2681: 2632: 2589: 2548: 2525: 2476: 2435: 2392: 2351: 2312:(11): 4781–5. 2292: 2243: 2200: 2151: 2116: 2079:BioData Mining 2065: 2022: 1979: 1920: 1885: 1834: 1819: 1780: 1751:(37): 5310–8. 1726: 1684: 1644: 1623:(5): 599–606. 1603: 1576:(3): 195–211. 1519: 1419: 1361: 1311: 1253: 1246: 1218: 1216: 1213: 1212: 1211: 1206: 1201: 1196: 1191: 1186: 1179: 1176: 1133:trichostatin A 1116: 1113: 1085:histone 4 (H4) 1081:histone 3 (H3) 1046:of the brain, 1037:splice variant 1000: 997: 949:overexpression 936: 933: 899: 896: 894: 893:Human diseases 891: 884:(CBP), to the 857: 854: 828: 825: 793:amino terminal 769: 766: 764: 761: 752: 749: 747: 746:Class IV HDACs 744: 732:ubiquitination 711: 708: 633: 630: 628: 627:Class II HDACs 625: 621:Northern blots 612: 609: 594:receptors and 564: 561: 462: 459: 457: 454: 401: 398: 365: 362: 334:Main article: 331: 328: 295: 292: 258: 255: 249: 246: 232: 229: 216: 208: 196: 152: 149: 127:marker within 26: 24: 14: 13: 10: 9: 6: 4: 3: 2: 4985: 4974: 4971: 4969: 4966: 4964: 4961: 4960: 4958: 4943: 4940: 4938: 4935: 4933: 4930: 4929: 4927: 4924: 4919: 4912: 4906: 4902: 4899: 4896: 4894: 4890: 4887: 4884: 4883: 4881: 4877: 4871: 4868: 4866: 4863: 4861: 4858: 4857: 4855: 4851: 4845: 4842: 4840: 4837: 4835: 4832: 4828: 4825: 4823: 4820: 4819: 4818: 4815: 4811: 4808: 4806: 4803: 4801: 4798: 4796: 4793: 4791: 4788: 4787: 4786: 4783: 4782: 4780: 4776: 4766: 4763: 4759: 4756: 4754: 4751: 4749: 4746: 4745: 4744: 4741: 4740: 4738: 4734: 4724: 4721: 4720: 4718: 4715: 4711: 4703: 4700: 4699: 4698: 4697: 4695: 4692: 4688: 4680: 4677: 4675: 4672: 4669: 4668: 4667: 4664: 4662: 4659: 4655: 4652: 4651: 4650: 4646: 4643: 4642: 4640: 4637: 4633: 4628: 4624: 4621: 4617: 4609: 4608:trp repressor 4606: 4604: 4603:lac repressor 4601: 4600: 4599: 4596: 4592: 4589: 4587: 4584: 4582: 4579: 4577: 4574: 4572: 4569: 4567: 4564: 4563: 4562: 4559: 4558: 4556: 4552: 4549: 4547: 4543: 4538: 4534: 4530: 4529:Transcription 4523: 4518: 4516: 4511: 4509: 4504: 4503: 4500: 4488: 4487:Jacques Monod 4485: 4483: 4480: 4479: 4477: 4473: 4465: 4462: 4460: 4457: 4456: 4455: 4452: 4450: 4449:Translational 4447: 4443: 4440: 4438: 4435: 4433: 4430: 4429: 4428: 4425: 4423: 4420: 4416: 4413: 4411: 4408: 4407: 4406: 4403: 4399: 4396: 4395: 4394: 4391: 4390: 4388: 4386: 4382: 4372: 4369: 4367: 4364: 4362: 4359: 4357: 4354: 4353: 4351: 4347: 4341: 4338: 4336: 4333: 4331: 4328: 4327: 4325: 4321: 4318: 4316: 4312: 4302: 4299: 4297: 4294: 4292: 4289: 4287: 4284: 4282: 4279: 4278: 4276: 4274: 4270: 4264: 4261: 4259: 4256: 4254: 4251: 4250: 4248: 4244: 4238: 4235: 4233: 4230: 4228: 4225: 4224: 4222: 4218: 4215: 4213: 4212:Transcription 4209: 4201: 4198: 4196: 4193: 4191: 4188: 4187: 4186: 4183: 4179: 4175: 4171: 4168: 4167: 4166: 4165:Central dogma 4163: 4161: 4158: 4157: 4155: 4153: 4147: 4143: 4136: 4131: 4129: 4124: 4122: 4117: 4116: 4113: 4107: 4104: 4103: 4099: 4091: 4087: 4083: 4079: 4075: 4071: 4068:(2): 126–35. 4067: 4063: 4056: 4053: 4048: 4044: 4039: 4034: 4030: 4026: 4023:(4): 664–76. 4022: 4018: 4014: 4007: 4004: 3999: 3995: 3990: 3985: 3981: 3977: 3973: 3969: 3965: 3958: 3955: 3950: 3946: 3941: 3936: 3932: 3928: 3924: 3920: 3916: 3909: 3906: 3901: 3897: 3892: 3887: 3882: 3877: 3873: 3869: 3865: 3858: 3855: 3850: 3846: 3841: 3836: 3832: 3828: 3824: 3820: 3816: 3809: 3806: 3801: 3797: 3792: 3787: 3783: 3779: 3776:(4): 479–88. 3775: 3771: 3767: 3760: 3757: 3752: 3748: 3743: 3738: 3733: 3728: 3724: 3720: 3716: 3712: 3708: 3701: 3698: 3693: 3689: 3684: 3679: 3675: 3671: 3667: 3663: 3659: 3655: 3651: 3644: 3641: 3636: 3632: 3627: 3622: 3618: 3614: 3610: 3603: 3600: 3595: 3591: 3587: 3583: 3579: 3575: 3571: 3567: 3560: 3557: 3552: 3548: 3545:(7): 539–43. 3544: 3540: 3539:Die Pharmazie 3533: 3530: 3525: 3521: 3517: 3513: 3509: 3505: 3501: 3497: 3490: 3487: 3482: 3478: 3473: 3468: 3464: 3460: 3456: 3449: 3446: 3441: 3437: 3432: 3427: 3423: 3419: 3415: 3408: 3405: 3402: 3397: 3394: 3389: 3385: 3380: 3375: 3371: 3367: 3364:(3): 335–48. 3363: 3359: 3355: 3348: 3346: 3342: 3337: 3325: 3317: 3313: 3308: 3303: 3299: 3297:9780444640765 3293: 3289: 3285: 3281: 3274: 3271: 3266: 3262: 3258: 3254: 3250: 3246: 3242: 3238: 3230: 3227: 3222: 3218: 3213: 3208: 3203: 3198: 3194: 3190: 3186: 3182: 3178: 3171: 3168: 3163: 3159: 3155: 3151: 3147: 3143: 3140:(6): 428–37. 3139: 3135: 3128: 3125: 3120: 3116: 3111: 3106: 3102: 3098: 3094: 3090: 3086: 3079: 3076: 3071: 3065: 3062: 3055: 3053: 3049: 3044: 3040: 3035: 3030: 3026: 3022: 3019:(5): 712–27. 3018: 3014: 3010: 3003: 3001: 2997: 2992: 2988: 2983: 2978: 2974: 2970: 2967:(2): 145–53. 2966: 2962: 2958: 2951: 2948: 2943: 2931: 2923: 2919: 2914: 2909: 2905: 2903:9780128009772 2899: 2895: 2891: 2887: 2880: 2877: 2872: 2868: 2863: 2858: 2854: 2850: 2846: 2842: 2838: 2831: 2829: 2825: 2820: 2816: 2811: 2806: 2801: 2796: 2792: 2788: 2784: 2777: 2774: 2769: 2765: 2761: 2757: 2753: 2749: 2745: 2741: 2734: 2731: 2726: 2722: 2717: 2712: 2708: 2704: 2700: 2696: 2692: 2685: 2682: 2677: 2673: 2668: 2663: 2659: 2655: 2652:(6): 631–47. 2651: 2647: 2643: 2636: 2633: 2628: 2624: 2620: 2616: 2612: 2608: 2604: 2600: 2593: 2590: 2585: 2581: 2576: 2571: 2568:(3): 552–63. 2567: 2563: 2559: 2552: 2549: 2544: 2540: 2536: 2529: 2526: 2521: 2517: 2512: 2507: 2503: 2499: 2495: 2491: 2487: 2480: 2477: 2472: 2468: 2463: 2458: 2455:(3): 552–63. 2454: 2450: 2446: 2439: 2436: 2431: 2427: 2423: 2419: 2415: 2411: 2408:(5): 337–56. 2407: 2403: 2396: 2393: 2388: 2384: 2379: 2374: 2371:(5): 659–65. 2370: 2366: 2362: 2355: 2352: 2347: 2343: 2338: 2333: 2328: 2323: 2319: 2315: 2311: 2307: 2303: 2296: 2293: 2288: 2284: 2279: 2274: 2270: 2266: 2263:(7): 457–69. 2262: 2258: 2254: 2247: 2244: 2239: 2235: 2231: 2227: 2223: 2222:10.1038/10640 2219: 2215: 2211: 2204: 2201: 2196: 2192: 2188: 2184: 2179: 2174: 2171:(2): 263–71. 2170: 2166: 2162: 2155: 2152: 2147: 2143: 2139: 2135: 2132:(1): 185–98. 2131: 2127: 2120: 2117: 2112: 2108: 2103: 2098: 2093: 2088: 2084: 2080: 2076: 2069: 2066: 2061: 2057: 2053: 2049: 2045: 2041: 2038:(3): 259–66. 2037: 2033: 2026: 2023: 2017: 2012: 2007: 2002: 1998: 1994: 1990: 1983: 1980: 1975: 1971: 1966: 1961: 1956: 1951: 1947: 1943: 1940:(5): 786–94. 1939: 1935: 1931: 1924: 1921: 1916: 1912: 1908: 1904: 1901:(2): 155–61. 1900: 1896: 1889: 1886: 1881: 1877: 1872: 1867: 1862: 1857: 1853: 1849: 1848:PLOS Genetics 1845: 1838: 1835: 1830: 1826: 1822: 1820:9780120342679 1816: 1812: 1808: 1804: 1800: 1793: 1791: 1789: 1787: 1785: 1781: 1776: 1772: 1768: 1764: 1759: 1754: 1750: 1746: 1742: 1735: 1733: 1731: 1727: 1722: 1718: 1714: 1710: 1707:(3): 433–44. 1706: 1702: 1695: 1693: 1691: 1689: 1685: 1680: 1676: 1672: 1668: 1665:(9): 836–45. 1664: 1660: 1653: 1651: 1649: 1645: 1640: 1636: 1631: 1626: 1622: 1618: 1614: 1607: 1604: 1599: 1595: 1591: 1587: 1583: 1579: 1575: 1571: 1570:Cell Research 1564: 1562: 1560: 1558: 1556: 1554: 1552: 1550: 1548: 1546: 1544: 1542: 1540: 1538: 1536: 1534: 1532: 1530: 1528: 1526: 1524: 1520: 1515: 1511: 1506: 1501: 1497: 1493: 1489: 1485: 1481: 1474: 1472: 1470: 1468: 1466: 1464: 1462: 1460: 1458: 1456: 1454: 1452: 1450: 1448: 1446: 1444: 1442: 1440: 1438: 1436: 1434: 1432: 1430: 1428: 1426: 1424: 1420: 1415: 1411: 1407: 1403: 1399: 1398:10.1038/38664 1395: 1391: 1387: 1383: 1379: 1372: 1365: 1362: 1357: 1353: 1349: 1345: 1341: 1337: 1334:(8): 615–26. 1333: 1329: 1322: 1320: 1318: 1316: 1312: 1307: 1303: 1298: 1293: 1290:(3): 209–21. 1289: 1285: 1281: 1274: 1272: 1270: 1268: 1266: 1264: 1262: 1260: 1258: 1254: 1249: 1243: 1239: 1232: 1230: 1228: 1226: 1224: 1220: 1214: 1210: 1207: 1205: 1202: 1200: 1197: 1195: 1192: 1190: 1187: 1185: 1182: 1181: 1177: 1175: 1173: 1169: 1168:Schizophrenia 1163: 1161: 1157: 1153: 1149: 1145: 1141: 1138: 1137:cardiomyocyte 1134: 1129: 1124: 1122: 1114: 1112: 1109: 1107: 1101: 1098: 1094: 1090: 1086: 1082: 1078: 1074: 1070: 1068: 1064: 1060: 1055: 1053: 1049: 1045: 1041: 1038: 1034: 1030: 1027: 1023: 1019: 1015: 1013: 1009: 1005: 998: 996: 992: 990: 986: 982: 978: 973: 969: 964: 962: 958: 954: 953:tumorigenesis 950: 946: 942: 934: 932: 929: 925: 920: 918: 914: 910: 906: 897: 892: 890: 887: 883: 879: 875: 871: 867: 863: 855: 853: 850: 846: 841: 839: 834: 826: 824: 822: 818: 814: 809: 807: 803: 799: 794: 789: 787: 783: 779: 775: 774:transcription 767: 762: 760: 757: 750: 745: 743: 741: 740:cell motility 737: 733: 729: 725: 721: 717: 709: 707: 705: 701: 697: 693: 689: 684: 679: 675: 671: 667: 663: 658: 655: 651: 647: 643: 639: 631: 626: 624: 622: 617: 610: 608: 606: 602: 597: 593: 589: 585: 581: 578:as well as a 577: 573: 569: 562: 560: 558: 553: 549: 545: 542: 538: 537:embryogenesis 534: 530: 525: 521: 517: 512: 510: 506: 502: 497: 493: 489: 485: 481: 476: 471: 467: 460: 456:Class I HDACs 455: 453: 451: 447: 443: 439: 435: 431: 427: 423: 419: 415: 411: 407: 399: 397: 395: 391: 387: 383: 379: 375: 371: 363: 361: 359: 355: 351: 346: 342: 337: 329: 327: 325: 321: 317: 314: 310: 306: 302: 293: 291: 289: 285: 284:growth-factor 281: 277: 273: 269: 265: 256: 254: 247: 241: 237: 230: 228: 224: 220: 214: 206: 202: 193: 190: 189:minor grooves 185: 181: 177: 173: 169: 165: 157: 150: 148: 146: 142: 138: 137:transcription 134: 130: 126: 122: 118: 113: 111: 107: 103: 99: 95: 91: 87: 82: 80: 76: 72: 68: 64: 60: 56: 32: 19: 4665: 4464:irreversible 4349:Key elements 4300: 4246:Key elements 4160:Genetic code 4150:Introduction 4065: 4061: 4055: 4020: 4016: 4006: 3971: 3967: 3957: 3922: 3918: 3908: 3871: 3867: 3857: 3822: 3818: 3808: 3773: 3769: 3759: 3714: 3710: 3700: 3657: 3653: 3643: 3616: 3612: 3602: 3572:(6): 570–5. 3569: 3565: 3559: 3542: 3538: 3532: 3502:(4): 265–9. 3499: 3495: 3489: 3462: 3458: 3448: 3421: 3417: 3407: 3396: 3361: 3357: 3279: 3273: 3243:(2): 312–9. 3240: 3236: 3229: 3184: 3180: 3170: 3137: 3133: 3127: 3092: 3088: 3078: 3064: 3016: 3012: 2964: 2960: 2950: 2885: 2879: 2844: 2840: 2790: 2786: 2776: 2743: 2739: 2733: 2698: 2694: 2684: 2649: 2645: 2635: 2602: 2598: 2592: 2565: 2561: 2551: 2534: 2528: 2493: 2489: 2479: 2452: 2448: 2438: 2405: 2401: 2395: 2368: 2364: 2354: 2309: 2305: 2295: 2260: 2256: 2246: 2216:(7): 601–4. 2213: 2209: 2203: 2168: 2164: 2154: 2129: 2125: 2119: 2082: 2078: 2068: 2035: 2031: 2025: 1996: 1992: 1982: 1937: 1933: 1923: 1898: 1894: 1888: 1851: 1847: 1837: 1802: 1798: 1748: 1744: 1704: 1700: 1662: 1658: 1620: 1616: 1606: 1573: 1569: 1487: 1483: 1381: 1377: 1364: 1331: 1327: 1287: 1283: 1237: 1164: 1125: 1118: 1110: 1102: 1071: 1056: 1016: 1002: 993: 965: 938: 921: 917:theophylline 901: 889:activation. 859: 842: 833:Histone code 830: 810: 790: 771: 754: 713: 692:ossification 659: 635: 614: 566: 552:upregulation 513: 464: 403: 394:bromodomains 367: 339: 297: 290:holoenzyme. 260: 251: 239: 225: 221: 194: 162: 114: 96:" (HAT) or " 83: 69:core of the 54: 53: 4914:Termination 4790:Pribnow box 4758:Corepressor 4753:Coactivator 4554:prokaryotic 4315:Translation 4152:to genetics 3974:(12): e64. 3660:(1): 25–9. 2746:(1): 21–2. 2701:(1): 31–9. 2496:(1): 14–8. 1199:Acetylation 1148:hypertrophy 1093:upregulated 961:oncogenesis 880:, GCN5 and 862:bromodomain 856:Bromodomain 821:bromodomain 698:-dependent 688:chondrocyte 678:hypertrophy 550:. Not even 531:. In HDAC1 318:during the 294:MYST family 270:, HPA2 and 257:GNAT family 164:Nucleosomes 141:euchromatin 121:nucleosomes 115:Acetylated 102:Acetylation 4957:Categories 4942:Rho factor 4932:Terminator 4923:eukaryotic 4898:eukaryotic 4879:Elongation 4865:Eukaryotic 4853:Initiation 4636:nucleosome 4619:eukaryotic 4591:gal operon 4586:ara operon 4581:Gua Operon 4576:gab operon 4571:trp operon 4566:lac operon 4537:Eukaryotic 4459:reversible 4422:lac operon 4398:imprinting 4393:Epigenetic 4385:Regulation 4340:Eukaryotic 4286:5' capping 4237:Eukaryotic 3874:: 641979. 1805:: 181–99. 1215:References 1209:Nucleosome 1048:Delta FosB 1042:. In the 1040:Delta FosB 1012:addictions 1004:Epigenetic 972:Vorinostat 957:metastasis 941:epigenetic 798:nucleosome 572:C-terminal 557:cross-talk 364:Other HATs 350:cell-cycle 305:Drosophila 276:myogenesis 243:functions. 125:epigenetic 75:acetylated 71:nucleosome 63:N-terminal 4918:bacterial 4886:bacterial 4860:Bacterial 4834:Insulator 4778:Promotion 4748:Activator 4598:Repressor 4533:Bacterial 4330:Bacterial 4227:Bacterial 3334:ignored ( 3324:cite book 2940:ignored ( 2930:cite book 2793:(1): 25. 2768:262487540 1659:BioEssays 1328:BioEssays 1140:autophagy 1106:chromatin 1052:addiction 1018:Cigarette 999:Addiction 806:silencing 710:Class IIB 700:apoptosis 632:Class IIA 584:cytoplasm 475:cofactors 358:apoptosis 320:leptotene 129:chromatin 4968:Proteins 4839:Silencer 4817:Enhancer 4805:CAAT box 4795:TATA box 4785:Promoter 4442:microRNA 4356:Ribosome 4335:Archaeal 4291:Splicing 4263:Promoter 4232:Archaeal 4176: → 4172: → 4082:19917878 4047:24006238 3998:22832356 3949:14517255 3900:24693336 3849:24310814 3800:12202037 3751:21367693 3692:19568876 3635:18797138 3594:24182756 3586:25867833 3551:16076083 3524:20849951 3516:24552452 3481:18482162 3440:28912356 3388:19447090 3316:29478612 3265:14013417 3257:22684622 3221:11572966 3162:19157711 3154:25083822 3119:22049069 3043:27259203 2991:20425300 2922:25410541 2871:21989194 2819:29784032 2760:17269160 2725:16960145 2676:21941619 2619:17694083 2599:Oncogene 2584:15738302 2543:18204158 2520:24527405 2471:15738302 2430:12172346 2422:24751816 2387:19736624 2287:20574448 2238:22196542 2230:10404206 2195:16237908 2187:11057899 2146:18804549 2111:26140054 2060:23873925 2052:23463310 1974:14172992 1915:11250138 1880:29795555 1829:14969728 1775:10662910 1767:17694074 1745:Oncogene 1721:11492997 1679:10944586 1598:30268983 1590:17325692 1514:12429021 1356:35433573 1306:16877467 1178:See also 1089:"reward" 1063:amygdala 1029:promoter 1022:nicotine 886:promoter 786:histones 654:isoforms 446:Sirtuins 390:TAFII250 343:and the 117:histones 4765:Inducer 4632:histone 4195:RNA→DNA 4190:RNA→RNA 4178:Protein 4090:3112549 4038:3805871 3989:3305989 3891:3945289 3840:3983897 3791:4459650 3742:3053983 3719:Bibcode 3683:2698246 3662:Bibcode 3379:2779727 3307:5868351 3189:Bibcode 3110:4042673 3034:5476208 2982:2847696 2913:5914502 2862:3272277 2810:5993135 2716:1785068 2667:3174261 2627:2976852 2511:3921865 2378:2921942 2346:8197135 2314:Bibcode 2278:3262678 2102:4488123 2016:3265906 1942:Bibcode 1871:6019819 1639:9499396 1505:1223209 1414:4419816 1406:9311776 1386:Bibcode 1348:9780836 1095:in the 1077:cocaine 1059:alcohol 1031:in the 1008:histone 970:(FDA), 849:meiosis 845:mitosis 736:tubulin 704:T cells 605:mitosis 529:nucleus 488:Co-REST 324:meiosis 90:enzymes 67:histone 4561:Operon 4088: 4080: 4045: 4035: 3996: 3986: 3947: 3940:204485 3937: 3898: 3888: 3847: 3837: 3798: 3788: 3749: 3739: 3690: 3680: 3633: 3592: 3584: 3549: 3522: 3514: 3479: 3438: 3386: 3376: 3358:Neuron 3314: 3304: 3294: 3263: 3255: 3219: 3209: 3160: 3152: 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Knowledge (XXG)

Histone acetylation and deacetylation

Index