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	Histone acetylase coactivators increase the rate of a
	Histone acetylation as well as other modifications (m
Allis was the first to mechanistically link	histone acetylation to transcription activation.
In general,	histone acetylation is linked to transcriptional acti
essential vehicle for determining the role of	histone acetylation in chromatin structure and functi
	Histone acetylation and deacetylation, catalyzed by m
ssibility of the TCR gamma locus by STAT5 and	histone acetylation.
f transcription factors (TF) and supported by	histone acetylation.
	Histone acetylation/deacetylation alters chromosome s
at the gene promoter through their intrinsic	histone acetyltransferase (HAT) activity.
1996, Allis and colleagues discovered that a	histone acetyltransferase from Tetrahymena was the ho
tein-protein interaction for example with the	histone acetyltransferase TIP60 (HIV-1 Tat interactin
receptor interacting domains and an intrinsic	histone acetyltransferase activity.
Some coactivators possess intrinsic	histone acetyltransferase (HAT) activity, which acety
dition p300 and CBP each contain a protein or	histone acetyltransferase (PAT/HAT) domain and a brom
	Histone acetyltransferases including CBP histone acet
The opposing enzymatic activities of	histone acetyltransferases and histone deacetylases,
	Histone acetyltransferases (HATs) and histone deacety
teract with some basal transcription factors,	histone acetyltransferases, and methyltransferases.
See nucleosome,	histone and chromatin.
makrishnan is also known for his past work on	histone and chromatin structure.
mally present, thus reducing affinity between	histone and (negatively charged) DNA, which renders D
cell, neutralizes the positive charges on the	histone by changing amines into amides and decreases
on of nucleosomes from free histones and DNA (	histone chaperone activity).
-terminus of Spt16 (a common feature of known	histone chaperones) does not prevent Spt16 from formi
The critical concept of the	Histone Code Hypothesis is that the histone modificat
The	Histone Code is a hypothesis that the transcription o
udies provided inspiration for the eukaryotic	histone code and underlie the modern study of epigene
e for the sequence of RNA's and proteins, the	Histone Code may ultimately be responsible for the ep
Acetylation of	histone core particles modulates chromatin structure
	Histone deacetylase 2 has been shown to interact with
	Histone deacetylase
The MITR protein lacks the	histone deacetylase catalytic domain.
Many corepressors can recruit	histone deacetylase (HDAC) enzymes to promoters.
This gene product belongs to the	histone deacetylase family.
	Histone deacetylase 11 is an enzyme that in humans is
	Histone deacetylase inhibitors (HDI) have a broad spe
	Histone deacetylase 3 is an enzyme that in humans is
It has	histone deacetylase activity and represses transcript
	Histone deacetylase 9 is an enzyme that in humans is
gene has sequence homology to members of the	histone deacetylase family.
	Histone deacetylase 10 is an enzyme that in humans is
HDAC10 has been shown to interact with	Histone deacetylase 2 and Nuclear receptor co-repress
It possesses	histone deacetylase activity and represses transcript
It works by inhibiting mainly	histone deacetylase 1 (HDAC1), but also HDAC2, HDAC3,
	Histone deacetylase 1 is an enzyme that in humans is
	Histone deacetylase 2 is an enzyme that in humans is
	Histone deacetylase 7 is an enzyme that in humans is
Panobinostat inhibits multiple	histone deacetylase enzymes, a mechanism leading to a
gh the C-terminal domain, also interacts with	histone deacetylase complexes.
	Histone deacetylase 4, also known as HDAC4, is a prot
(INN) or gavinostat (originally ITF2357) is a	histone deacetylase inhibitor with potential anti-inf
Zolinza was the first	histone deacetylase inhibitor approved by the U.S. Fo
re typically silenced or downregulated due to	histone deacetylase activity.
an HDAC inhibitor, inhibiting the function of	histone deacetylase enzymes, thereby favoring an acet
Various proteins, such as the	histone deacetylase 6 (HDAC6), are thought to act as
ptional repressor and may be part of the NuRD	histone deacetylase (HDAC) complex.
known as SNDX-275 and MS-275, is a benzamide	histone deacetylase inhibitor undergoing clinical tri
found that N-terminal regions of Gli1 recruit	histone deacetylase complexes via SuFu, which are inv
has been shown to interact with HDAC1, STUB1,	Histone deacetylase 2, TTC1, NAD(P)H dehydrogenase (q
9, Ku70, MIS12, Lamin B receptor, MBD1, TAF4,	Histone deacetylase 5, TRIM28, HDAC4, CBX3, SMARCA4,
een shown to interact with USF1 (human gene),	Histone deacetylase 2, PRKG1, Myc, MAPK3, HDAC3, Seru
Mocetinostat (MGCD0103) is a benzamide	histone deacetylase inhibitor undergoing clinical tri
nc atom in the binding pocket of Zn-dependent	histone deacetylase to block its activity.
	Histone deacetylase 8 is an enzyme that in humans is
BCL6 has been shown to interact with	Histone deacetylase 5, HDAC1, HDAC7A, ZBTB7A, Zinc fi
repression and to interact with components of	histone deacetylase co-repressor complexes including
and the University of Tokyo found it to be a	histone deacetylase inhibitor with effects similar to
proliferator-activated receptor delta, GTF2I,	Histone deacetylase 5, RELA, MAPK11, TBL1X, Nuclear r
, Methyl-CpG-binding domain protein 2, HDAC1,	Histone deacetylase 2, Zinc finger and BTB domain-con
ylline in vitro can restore the reduced HDAC (	histone deacetylase) activity that is induced by oxid
etylation of histones, an effect mediated via	histone deacetylase-2 (HDAC2).
nscriptional corepressor and interacts with a	histone deacetylase.
e protein encoded by this gene belongs to the	histone deacetylase/acuc/apha family and is a compone
e protein encoded by this gene belongs to the	histone deacetylase/acuc/apha family.
coded by this gene belongs to class II of the	histone deacetylase/acuc/apha family.
ncoded by this gene belongs to class I of the	histone deacetylase/acuc/apha family.
ses and the acetoin utilization proteins, the	histone deacetylases form an ancient protein superfam
	Histone deacetylases remove those acetyl groups, incr
Givinostat inhibits class I and class II	histone deacetylases (HDACs) and several pro-inflamma
r of a larger class of compounds that inhibit	histone deacetylases (HDAC).
	Histone deacetylases act via the formation of large m
	Histone deacetylases, such as HDAC11, control DNA exp
I) contain zinc and are known as Zn-dependent	histone deacetylases.
ressor for thyroid hormone and interacts with	histone deacetylases.
Two specific JmjC	histone demethylases are PHF8 and KIAA1718.
ate 2005 the Jumonji domain-containing (JmjC)	histone demethylases were discovered which are able t
dicted to function as protein hydroxylases or	histone demethylases.
Very recently two families of	histone demethylating enzymes were discovered.
UTX has been linked with	histone demethylation, a potential means of regulatin
A	histone gene is a gene that codes for histone protein
This gene is found in the small	histone gene cluster on chromosome 6p22-p21.3.
with Hir1p and Hir2p, the two corepressors of	histone gene transcription characterized in the yeast
The mRNAs of metazoan	histone genes lack polyadenylation and a poly-A tail,
ene is intronless and encodes a member of the	histone H1 family.
CDK3 can phosphorylate	histone H1 and interacts with an unknown type of cycl
The linker	histone, H1, interacts with linker DNA between nucleo
rminal kinase domain is able to phosphorylate	histone H1.
	Histone H1.5 is a protein that in humans is encoded b
binds specifically to mononulceosomes and the	histone H2A/H2B dimer, but not to the H3/H4 tetramer
	Histone H2B is one of the 5 main histone proteins inv
am was based on DNA sequences of both nuclear	histone H3 and mitochondrial cytochrome-c oxidase I (
ay of the Non-coding RNA ANRIL and Methylated	Histone H3 Lysine 27 by Polycomb CBX7 in Transcriptio
it replaces 1 or both copies of conventional	histone H3 in the (H3-H4)2 tetrameric core of the nuc
methylation of lysine 9 of	histone H3) which target the genomic region for heter
	Histone H4, Hsp70, melanocortin-4-receptor).
-loop binding protein (SLBP - also termed the	histone hairpin binding protein, or HBP).
cally, butyrate treatment of cells results in	histone hyperacetylation, and butyrate itself inhibit
	Histone methylation is generally associated with tran
	Histone methylation is the modification of certain am
For many years	histone methylation was thought to be a permanent mod
hromatin by binding to coactivators increases	histone methylation and enhances the accessibility of
ed into heterochromatin and possessing unique	histone methylation patterns.
al silencing of the KCNQ1 locus by regulating	histone methylation.
It interacts with chromatin, the	histone methyltransferase G9a (responsible for the mo
MT1), but does not affect the interactions of	histone methyltransferases with KCNQ1OT1.
equences are enriched for the heterochromatic	histone modification H3K9me3.
Other	histone modifications have similar or opposite effect
For details of gene expression regulation by	histone modifications see table below.
Allis lab focuses on chromatin signaling via	histone modifications - acetylation, methylation and
genetic process that involves methylation and	histone modifications in order to achieve monoallelic
Polyuridylation of a	histone mRNA promotes its degradation, involving the
group of RNAs that can be polyuridylated are	histone mRNAs that lack a poly(A) tail.
These histones of the	histone octamer all contain N-terminal tails that ema
ould then propagate across the surface of the	histone octamer in a wave-like manner, resulting in t
A	histone octamer is an octamer of the histones found a
er element downstream of the cleavage site in	histone pre-mRNA.
molecule involved in the splicing of metazoan	histone pre-mRNAs, which are spliced by a different m
Other	histone proteins involved: H1 H2A H3 H4
ine residues restoring the positive charge to	histone proteins and hence the tie between histone an
consists of 2 copies of each of the four core	histone proteins (H2A, H2B, H3 and H4).
Structural determinants of	histone recognition by readers, writers and erasers o
emethylase, converting specific trimethylated	histone residues to the dimethylated form.
emethylase, converting specific trimethylated	histone residues to the dimethylated form, and as a t
Many of the	histone tail modifications correlate very well to chr
mplished by posttranslational modification of	histone tails (e.g.
	Histone tails are normally positively charged due to
These positive charges help the	histone tails to interact with and bind to the negati
hich recognises methylated lysine residues in	histone tails.

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