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1 n each structure is roughly 18 basepairs per histone protein.
2 so increases acetylation of histones and non-histone proteins.
3 f acetyl groups from histones as well as non-histone proteins.
4 ally recognize methylated lysine residues on histone proteins.
5 versible epigenetic modifications of DNA and histone proteins.
6 ulated by chemical modifications of the core histone proteins.
7  binding partner of Bcl6 which ubiquitinates histone proteins.
8 n and increasingly through regulation of non-histone proteins.
9 ove active marks and add repressive marks to histone proteins.
10 of DNA wrapped around a symmetric octamer of histone proteins.
11  DNA into nucleosomes that contain a core of histone proteins.
12 cation that is found on both histone and non-histone proteins.
13 is wrapped around largely positively charged histone proteins.
14 nucleosomes, where the DNA is wrapped around histone proteins.
15 irect the post-translational modification of histone proteins.
16 ugh changes in the local environment and the histone proteins.
17 e future study of acetylated histone and non-histone proteins.
18  DNA is packaged into chromatin by canonical histone proteins.
19 at this Rtt106:HIR complex included Asf1 and histone proteins.
20 cription factors (NRF2, C/EBP, and E2F1) and histone proteins.
21 ssing, resulting in severe depletion of core histone proteins.
22 binding events and chemical modifications of histone proteins.
23 cently been found to also associate with non-histone proteins.
24 moval of post-translational modifications on histone proteins.
25  of acetyl groups from both histones and non-histone proteins.
26 zymes, and chromatin, the complex of DNA and histone proteins.
27 ylation of lysyl residues in histone and non-histone proteins.
28 ression by deacetylation of histones and non-histone proteins.
29 matin must be unwound and the DNA cleared of histone proteins.
30 ription, through methylating histone and non-histone proteins.
31 d intermediates that associate with cellular histone proteins.
32 verse tumour types and in crucial regions of histone proteins.
33 al macro domain that is not present in other histone proteins.
34 cell death acting through acetylation of non-histone proteins.
35  configuration imposed by the binding of the histone proteins.
36 s have been developed to purify and separate histone proteins.
37 ed in part by lysine methylation of the core histone proteins.
38  and post-translational modifications of the histone proteins.
39 s, such as posttranslational modification of histone proteins.
40 tone proteins and 5 mutations with increased histone proteins.
41  checkpoint and the resulting degradation of histone proteins.
42 ysine methylation events decorating the core histone proteins.
43 inked to epigenetic modifications on DNA and histone proteins.
44 , and/or post-translational modifications of histone proteins.
45 nslational modifications on core and variant histone proteins.
46 consists of DNA wound around a core of eight histone proteins.
47 cally by post-translational modifications of histone proteins.
48 me: 147bp of DNA wrapped about an octamer of histone proteins.
49 er lysine acylations in both histone and non-histone proteins.
50 s a dynamic PTM occurring on histone and non-histone proteins.
51 tion of the binding properties of individual histone proteins.
52 yl group from lysine residues of several non-histone proteins.
53 elements by supporting an adequate supply of histone proteins.
54 -aging proteome response by upregulating H2B histone proteins 1 week after 4-week intermittent fastin
55 ved in interactions between histones and non-histone proteins, 80-90% of residues in histones H3 and
56 nano-liquid chromatography (nanoLC) and, for histone proteins, a 2-d sample preparation that includes
57 model organism, we found that reducing yeast histone proteins accelerates chronological aging and inc
58 o known as TP53) was an early example of non-histone protein acetylation and its precise role remains
59 g cellular reprogramming and to quantify non-histone protein acetylation dynamics.
60                                            A histone/protein acetyltransferase (HAT), p300, was recen
61                                              Histone/protein acetyltransferases (HATs) promote chroma
62 on, a process catalyzed by distinct types of histone/protein acetyltransferases (HATs) that regulate
63                 The reaction is catalyzed by histone/protein acetyltransferases (HATs), and is revers
64 ctivity is regulated post-translationally by histone/protein acetyltransferases and histone/protein d
65 table for the preparation of fully synthetic histone proteins, allowing for site-specific incorporati
66   Furthermore, an comparism of Khib sites in histone proteins among human, mouse and P. patens found
67 vered 15 substitution mutations with reduced histone proteins and 5 mutations with increased histone
68 The extensive interactions between the basic histone proteins and acidic DNA make the nucleosomal uni
69 m enhancer, enabling acetylation of multiple histone proteins and activating Erm expression.
70 tes the acetylation state of histone and non-histone proteins and could be a powerful regulator of th
71 ovides similar regulatory complexity for non-histone proteins and for histones.
72 , with differing preferences for the various histone proteins and for specific sites on individual hi
73 ty increased, including deacetylation of non-histone proteins and functional diversification in mamma
74 , such as post-translational modification of histone proteins and incorporation of histone variants,
75 s mRNA abnormalities through modification of histone proteins and may prove to be of therapeutic valu
76 one chaperone Rtt106 binds newly synthesized histone proteins and mediates their delivery into chroma
77 atens found conserved sites in the H3 and H4 histone proteins and novel sites in H1, H2A and H2B hist
78 stone deacetylases remove acetyl groups from histone proteins and play important roles in many genomi
79 al processes by acetylating histones and non-histone proteins and regulating chromatin and gene-speci
80 romatin, which consists of the histones, non-histone proteins and RNA molecules that package DNA.
81 ns decrease the attractive force between the histone proteins and the DNA but also stabilize H2A/H2B
82 tone gene transcription and depletion of the histone proteins, and (4) repression of E2F1-dependent g
83 ple peptides from various known prohormones, histone proteins, and DNA- and RNA-binding proteins as b
84  modification of histones, on individual non-histone proteins, and globally across the proteome.
85 ts of purified NET components including DNA, histone proteins, and neutrophil enzymes on coagulation
86 romatin self-assembly, starting from DNA and histone proteins, and use these to understand the constr
87 of this, post-translational modifications of histone proteins are central to the regulation of chroma
88 to DNA replication, focusing on how parental histone proteins are chaperoned around the replication f
89 anslational modifications in histone and non-histone proteins are crucial to DNA replication, DNA rep
90 genomes, and which variant forms of the core histone proteins are deposited is incompletely understoo
91                                The canonical histone proteins are encoded by replication-dependent ge
92 INGS: Chemical modifications of DNA and core histone proteins are epigenetic marks that constitute th
93                                              Histone proteins are especially prone to this, as they a
94                                         Core histone proteins are essential for packaging the genomic
95                                              Histone proteins are essential for the organization, exp
96            Chemical modifications to DNA and histone proteins are involved in epigenetic programs und
97                                              Histone proteins are key components of chromatin.
98                       The genes for the five histone proteins are linked.
99     Epigenetic modifications of both DNA and histone proteins are now emerging as fundamental mechani
100                                              Histone proteins are particularly susceptible to NECMs d
101                                              Histone proteins are subject to a host of posttranslatio
102                                              Histone proteins are subject to dynamic post-translation
103 rsible; however, it is not known whether non-histone proteins are substrates for demethylation.
104                                              Histone proteins are synthesized in large amounts during
105                                              Histone proteins are the major protein components of chr
106 intrinsically disordered terminal regions of histone proteins, are key modulators of the structure an
107 ails, which are the terminal segments of the histone proteins, are prominent IDPs that are implicated
108  that epigenetic methylation modification on histone protein arginine residues is a regulatory mechan
109 g an acetylome analysis revealed several non-histone proteins as candidates.
110                             Deacetylation of histone proteins at the HIV type 1 (HIV-1) long terminal
111 (immediate early, early, and late) bind with histone proteins at the start of viral gene expression.
112  methylarginine residues to citrulline, with histone proteins being among its best-described substrat
113 by posttranslational modifications (PTMs) of histone proteins bound to cccDNA through analysis of de
114 ow that LPS treatment reduces acetylation of histone proteins bound to the NAPE-PLD promoter, an effe
115 a naked heteroduplex or a heterology free of histone proteins but between two nucleosomes.
116 e reversible acetylation of histones and non-histone proteins by histone acetyltransferases and deace
117                              Modification of histone proteins by lysine methylation is a principal ch
118                               Acetylation of histone proteins by the yeast Spt-Ada-Gcn5-acetyltansfer
119 kaged into basic units of DNA wrapped around histone proteins called nucleosomes.
120   Ubiquitin and ubiquitin-like (UBL) PTMs on histone proteins can function as signaling molecules by
121                                              Histone proteins carry information contained in post-tra
122 ositions within nucleosomes reveals that the histone proteins catalyze strand scission and increase t
123  episomes and recruit the diatom centromeric histone protein CENH3, suggesting nonnative sequences ca
124 the elaborate combination of histone and non-histone protein complexes defines chromatin organization
125                   Nucleosomes are stable DNA-histone protein complexes that must be unwrapped and dis
126 ast promoters are predominantly bound by non-histone protein complexes, with little evidence for frag
127 abeled methyl groups in both DNA and the H2B histone protein component of the 200-kDa nucleosome core
128 ed by acetylation including histones and non-histone proteins component of transcription factors cont
129 ay of posttranslational modifications of the histone protein constituents of chromatin and regulatory
130 e covalent methylation of lysine residues on histone proteins constitutes a principal molecular mecha
131                                              Histone proteins contain epigenetic information that is
132 ation and posttranslational modifications of histone proteins, contribute to gene regulation.
133           Eukaryotic DNA is wrapped around a histone protein core to constitute the fundamental repea
134 me is typically centered around an octameric histone protein core: one central tetramer plus two sepa
135                       Sequence variations in histone proteins, core components of chromatin, provide
136 rmacologic modulation of Treg function using histone/protein deacetylase inhibitors (HDACi) may allow
137 myces pombe (Sp) Hst4 is an NAD(+)-dependent histone/protein deacetylase involved in gene silencing a
138 duced by the Sir2-catalyzed NAD(+)-dependent histone/protein deacetylase reaction, regulates diverse
139                                     SIRT1, a histone/protein deacetylase, and AMP-activated protein k
140               Sirtuin 1 (Sirt1), a class III histone/protein deacetylase, is central to cellular meta
141                         Mef2 is inhibited by histone/protein deacetylase-9 (Hdac9), and Hdac9 deletio
142 herefore, understanding the roles of various histone/protein deacetylases (HDAC) are key to promoting
143 experimental studies show that inhibition of histone/protein deacetylases (HDAC) can have important a
144                                              Histone/protein deacetylases (HDACs) regulate chromatin
145              Foxp3(+) Tregs express multiple histone/protein deacetylases (HDACs) that regulate chrom
146       Like other cells, Foxp3+ Tregs express histone/protein deacetylases (HDACs), which regulate chr
147 ly by histone/protein acetyltransferases and histone/protein deacetylases (HDACs).
148 cetyltransferases (HATs), and is reversed by histone/protein deacetylases (HDACs).
149 we discuss possible mechanisms whereby these histone/protein deacetylases facilitate the switch betwe
150                                              Histone/protein deacetylases play multiple roles in regu
151               Results demonstrating that the histone/protein deacetylation inhibitor trichostatin A c
152                                      DNA and histone proteins define the structure and composition of
153 pression is mildly compromised, the maternal histone protein deposits are essential for proper early
154 yotic DNA and are composed of four different histone proteins, designated H3, H4, H2A, and H2B.
155 leosome unfolding in which DNA unwinding and histone protein disassembly are coupled.
156 phase of eukaryotic cells are unprotected by histone proteins during entire cell cycles and because t
157              NETs carried the characteristic histone proteins, elastase, lysozyme, myeloperoxidase, a
158 to systematically dissect their roles on non-histone proteins, especially for their relationships wit
159 , 2 and 3 are members of the SMH (single Myb histone) protein family, which comprises double-stranded
160            Chemical modifications to DNA and histone proteins form a complex regulatory network that
161                                 We find that histone proteins from the archaeon Methanothermus fervid
162 l aging is accompanied by a profound loss of histone proteins from the genome.
163 ct "code," it is becoming clear that PTMs on histone proteins function in elaborate combinations to r
164 mmunoprecipitated proteins included cellular histone proteins H2A, H3, and H4; the intermediate filam
165 e, in vivo, we show that in murine cells the histone protein H2AX prevents nucleases other than Artem
166                       Phosphorylation of the histone protein H2AX, as well as nuclear localization, w
167 eptide (MitoFlag) enables the trafficking of histone protein H2B, a nuclear protein, to the mitochond
168 differences in basal levels of trimethylated histone protein H3 at lysine 9 (H3K9me3) in hippocampus
169 ly conserved signature N-terminal peptide of histone protein H3 plays crucial roles in gene expressio
170      Ischemia promotes deacetylation of core histone proteins H3 and H4 and dimethylation of histone
171                     The N-terminal region of histone protein H4 contributes significantly to DNA-prot
172 regulatory factors (CRF)] and genes encoding histone proteins harbor recurrent mutations in most huma
173                        Lysine methylation of histone proteins has been extensively studied, but it ha
174                    Lysine methylation of non-histone proteins has emerged as a key regulator of many
175 in sterile inflammation, the role of nuclear histone proteins has not yet been investigated.
176                             Modifications of histone proteins have essential roles in normal developm
177                    Covalent modifications of histone proteins have profound consequences on chromatin
178    We conclude that unlike DNA or individual histone proteins, human intact NETs do not directly init
179 al mechanism whereby citrullination of a non-histone protein impacts gene regulation.
180 Finally, AspAlk was shown to modify the core histone proteins, implicating aspirin as a potential che
181  the lysine-rich tail region of the proximal histone protein in the form of a lactam.
182 ms are the posttranslational modification of histone proteins in chromatin and the methylation of DNA
183       Post-translational modification of the histone proteins in chromatin plays a central role in th
184 es encoding chromatin regulatory factors and histone proteins in human cancer, implicating them as ma
185 nthesis of dual posttranslationally modified histone proteins in live cells.
186 s have focused on the role of acetylation of histone proteins in modulating transcription, whereas de
187 ine residues in the N-terminal tails of core histone proteins in nucleosome is of fundamental importa
188 he DNA is often inaccessible, wrapped around histone proteins in nucleosomes forming the chromatin.
189  proteins and novel sites in H1, H2A and H2B histone proteins in P. patens.
190                                              Histone proteins in particular are extensively post-tran
191 ive profile of Khib sites in histone and non-histone proteins in Physcomitrella patens.
192 s accomplished by the wrapping of DNA around histone proteins in repeating units of nucleosomes to fo
193   Their ability to stabilize highly abundant histone proteins in the cellular environment prevents no
194 enrichment of permissive epigenetic marks on histone proteins in the hippocampus of male cocaine-sire
195 e of the highest binding affinities for core histone proteins in the mouse genome were not altered by
196 s post-translational modifications (PTMs) on histone proteins in the nucleosome and by nucleobase mod
197                                              Histone proteins in Thermococcus kodakarensis are suffic
198     Here we show that Acr forms adducts with histone proteins in vitro and in vivo and preferentially
199 tors, independently of FOXP3, as well as non-histone proteins, in addition to their effects on chroma
200  shown also to play a role in regulating non-histone proteins, including the tumor suppressor protein
201 n nucleosome core particles reveals that the histone proteins increase strand scission between 130- a
202            cccDNA is assembled with cellular histone proteins into chromatin, but little is known abo
203 in the context of large genomes condensed by histone proteins into chromatin.
204  which regulates the function of several non-histone proteins involved in tumorigenesis.
205                        Lysine acetylation of histone proteins is a fundamental post-translational mod
206 thylation of lysine residues on the tails of histone proteins is a major determinant of the transcrip
207 ently become evident that methylation of non-histone proteins is also abundant and important.
208 addition to DNA methylation, modification of histone proteins is also an important regulator of impri
209            Methylation of lysine residues in histone proteins is catalyzed by S-adenosylmethionine (S
210 reversible methylation of lysine residues on histone proteins is central to chromatin biology.
211        Schiff-base formation between DOB and histone proteins is detected in nucleosomes and NCPs, re
212 ene expression through citrullination of non-histone proteins is less well defined.
213                              Accumulation of histone proteins is necessary for packaging of replicate
214 tylation, the number of known methylated non-histone proteins is rapidly expanding.
215 mmetric dimethylarginine mark on histone/non-histone proteins, is reportedly overexpressed in various
216  may be regulating initiation by controlling histone protein levels and/or by affecting origin chroma
217 ucidated the posttranslational regulation of histone protein levels by the ubiquitin-proteasome pathw
218 ap1 contributes to their repression and that histone protein levels decline at senescence.
219                    We concomitantly observed histone protein levels to reduce by up to 40%, which in
220     Different mechanisms operate to regulate histone protein levels, and induction of human histone g
221 ative aging is accompanied by a reduction in histone protein levels, and this is a cause of aging in
222 vate concentrations inversely correlate with histone protein levels.
223  form reversible DNA-protein conjugates with histone proteins, likely contributing to regulation of n
224                                 However, non-histone protein lysine 2-hydroxyisobutyrylation remains
225 ated p300, which comprise the KAT3 family of histone/protein lysine acetyltransferases, interact with
226 s on how acetylation of both histone and non-histone proteins may drive cancer, and we will discuss t
227 ulatory roles of lysine methylation, the non-histone protein methylation may create binding sites for
228                                              Histone protein modifications control fate determination
229 in chromatin structure--hypersensitivity and histone protein modifications--between human embryonic s
230                  Here, we review the role of histone/protein modifications and HDACs in RNA splicing
231  are involved in binding epigenetic marks on histone proteins, more specifically acetylated lysine re
232 ion and association kinetics under different histone protein (NCP) and NaCl concentrations using sing
233 approximately 146 bp of DNA wrapped around a histone protein octamer that controls DNA accessibility
234 rged DNA wrapped around a positively charged histone protein octamer.
235 chemical modifications that are found on the histone proteins of eukaryotic cells form multiple compl
236   Post-translational modifications (PTMs) of histones, proteins onto which DNA is packaged, are invol
237 atin is a supramolecular assembly of DNA and histone proteins, organized into nucleosome repeat units
238 optosis by demethylating histone and the non-histone protein p53, respectively.
239 , however, as HATs and HDACs also target non-histone proteins particularly transcription factors to a
240                    Covalent modifications to histone proteins play a critical role in regulating gene
241 lational modifications of the DNA-associated histone proteins play fundamental roles in eukaryotic tr
242           Posttranslational modifications of histone proteins play important roles in the modulation
243 ones, and that interaction between MeCP2 and histone proteins plays a key role in gene expression reg
244                   Sirtuin 3 (SIRT3) mediates histone protein post-translational modification related
245 e through post-translational modification of histone proteins, primarily histone H3 phosphorylation a
246          Post-translational modifications of histone proteins produce dynamic signals that regulate t
247  apply MAS NMR to directly probe the dynamic histone protein regions in (13)C,(15)N-enriched recombin
248           Posttranslational modifications of histone proteins regulate gene expression via complex pr
249          Post-translational modifications of histone proteins regulate numerous cellular processes.
250 methyl groups to the amino terminal tails of histone proteins regulates cellular gene expression at v
251                        Lysine methylation of histone proteins regulates chromatin dynamics and plays
252 encoded in covalent modifications of DNA and histone proteins regulates fundamental biological proces
253      Posttranslational modification (PTM) of histone proteins regulates nucleosome function.
254 tanding of the fundamental mechanisms of non-histone protein regulation through this dynamic and mult
255           Posttranslational modifications of histone proteins represent a fundamental means to define
256                                              Histone proteins represent crucial epigenetic components
257       In Eukarya and most Archaea, DNA-bound histone proteins represent the most common and troubleso
258 ged molecules such as DNA, and any excess of histone proteins results in deleterious effects on genom
259 are responsible for binding the highly basic histone proteins, shielding them from non-specific inter
260 engineered transcription factors, to remodel histone proteins specifically at the Cdk5 gene.
261 and additionally control the activity of non-histone protein substrates.
262               Recently, modifications to non-histone proteins such as methylation, acetylation, phosp
263 ucho interacts with histone deacetylases and histone proteins, suggesting that it may effect repressi
264                                              Histone protein synthesis is activated as cells enter S
265 ociated with nucleosomes containing modified histone proteins that are generally found associated wit
266 ircular, gene dense, and organized either by histone proteins that are homologous to their eukaryotic
267 f select archaea have identified homologs of histone proteins that assemble into tetrameric nucleosom
268 in the form of covalent modifications to the histone proteins that comprise the nucleosome.
269 important post-translational modification of histone proteins that defines epigenetic status and cont
270 Yeast Scm3 and human HJURP are conserved non-histone proteins that interact physically with the (CenH
271         In eukaryotes, multiple genes encode histone proteins that package genomic deoxyribonucleic a
272       These fractions were also enriched for histone proteins that physically associate with TERRA in
273   Accelerated upregulation of genes encoding histone proteins that support DNA replication is the mos
274 otein modification for both histones and non-histone proteins, the mechanisms of acetylation-mediated
275                              However, beyond histone proteins, the proteome-wide extent of lysine met
276                          To date, other than histone proteins, there are very few identified substrat
277            Since multiple genes encode these histone proteins, there is potential for generating more
278 es negative feedback on the histone genes by histone proteins through the level of saturation of hist
279 lls, the genome is packaged and rolled up by histone proteins to create a series of DNA/histone core
280 A intermediates that associate with cellular histone proteins to form minichromosomes.
281                    Meters of DNA wrap around histone proteins to form nucleosomes and fit inside the
282 into chromatin through association with core histone proteins to form nucleosomes.
283              This CM strategy was applied to histone proteins to install a mimic of acetylated lysine
284 echanism in which Rtt106 sensed the level of histone proteins to maintain the proper level of histone
285 icroviscosity in live cells experienced by a histone protein using the photoswitching kinetics of Dro
286                                      DNA and histone proteins were also separately purified from norm
287                                              Histone proteins were depleted in both the chromatin fra
288    We determined that the levels of multiple histone proteins were markedly decreased in cohorts of i
289 hly flexible N- or C-terminal protrusions of histone proteins which facilitate the compaction of DNA
290 A and a variety of modified histones and non-histone proteins, which have an impact on cell different
291 n requires posttranslational modification of histone proteins, which, in concert with chromatin-remod
292 ctrophoresis; and immunoblotting of isolated histone proteins with modification-specific antibodies.
293 tant post-translational modifications on non-histone proteins, with emphasis on their roles in diseas
294 nts, the DNA unwinds asymmetrically from the histone proteins, with only one of its two ends preferen
295 llustrated through the chemical tailoring of histone proteins within a native chromatin setting.
296 sstalk between two modifications on separate histone proteins within a nucleosome.
297 NA sequence and its position with respect to histone proteins within NCPs.
298 st-translational modifications (PTMs) of the histone proteins within nucleosomes regulate these DNA p
299                                              Histone proteins wrap around DNA to form nucleosomes, wh
300                                An octamer of histone proteins wraps about 200bp of DNA into two super

 
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