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1 relative affinity of every site for the core histone octamer.
2 ith the DNA significantly unraveled from the histone octamer.
3  binding to the same extended surface of the histone octamer.
4 e rotational orientation with respect to the histone octamer.
5 nslational and rotational positioning of the histone octamer.
6  completely blocked by interactions with the histone octamer.
7 B dimers or induce a novel alteration in the histone octamer.
8 vation energy for short-range sliding of the histone octamer.
9  individuals having the highest affinity for histone octamer.
10 NA repeat and one molecule of histone H5 per histone octamer.
11 main of residual contact between the DNA and histone octamer.
12 uence of its left-handed wrapping around the histone octamer.
13     Unassisted, the junction is blocked by a histone octamer.
14  the extent that binding is inhibited by the histone octamer.
15 interact with DNA on both sides flanking the histone octamer.
16 fine a discrete domain on the surface of the histone octamer.
17  NN3']n motif might resist wrapping around a histone octamer.
18 the chromatin remodeler, SNF2h, distorts the histone octamer.
19 ular histone substrate in the context of the histone octamer.
20 e DNA double-stranded fiber wrapped around a histone octamer.
21 pproximately 1.7 times around a central core histone octamer.
22 le inward facing lesions are occluded by the histone octamer.
23 by engaging both the nucleosomal DNA and the histone octamer.
24 on between RAD51AP1 and both the NCP and the histone octamer.
25 detachment of upstream terminal DNA from the histone octamer.
26 e material made up from DNA wrapped around a histone octamer.
27 ly two coils of DNA wrapped around a central histone octamer.
28 m DSB formation remained associated with the histone octamer.
29 sotropy dictates how DNA is wrapped around a histone octamer.
30 ed acetylation on the lateral surface of the histone octamer.
31 mers, facilitating uncoiling of DNA from the histone octamer.
32 maged DNA is hindered by the presence of the histone octamer.
33 ased the affinity of these sequences for the histone octamer.
34 ere the DNA minor groove faces away from the histone octamer.
35 ears to intercalate between the DNA gyre and histone octamer.
36 th the side of nucleosomal DNA away from the histone octamer.
37 ces nucleosomal DNA to provide access to the histone octamer.
38  not freely diffuse about the surface of the histone octamer.
39 p DNA wrapped around an H2A, H2B, H3, and H4 histone octamer.
40 roximately 147 bases of DNA wrapped around a histone octamer.
41 d found that it is nearly as abundant as the histone octamer.
42 s by altering the position of DNA around the histone octamer.
43 e relative affinity of DNA sequences for the histone octamer.
44 inity of the underlying DNA sequence for the histone octamer.
45 es H2A-H2B from preassembled Cse4-containing histone octamers.
46 nd may involve the transient displacement of histone octamers.
47 o nucleosomes and via TREs on the surface of histone octamers.
48  is complexed with H3/H4 tetramers than with histone octamers.
49 er but can branch migrate in regions free of histone octamers.
50 ukaryotic cells package their genomes around histone octamers.
51  DNA wound in a continuous superhelix around histone octamers.
52 tails and the core domain/lateral surface of histone octamers.
53 to sequences predicted to better accommodate histone octamers.
54 contains one DNA molecule wrapped around two histone octamers.
55 ing dimethylation at R17 in CARM1-methylated histone octamers.
56 mics of force-induced unwrapping of DNA from histone octamers.
57 enetic histone marks, and a region devoid of histone octamers.
58 y external potential and arrays of DNA-bound histone octamers.
59  histones and these have been assembled into histone octamers.
60  chromatin structure by sliding and evicting histone octamers(3-8), creating DNA regions that become
61 NA by approximately two base pairs along the histone octamer accommodates the necessary DNA lifting f
62          In the case of mononucleosomes, the histone octamers accumulate at the DNA ends even in the
63 the translational position of the DNA on the histone octamer, accurate nucleosome positioning over re
64  a linear relationship between the extent of histone octamer acetylation and the extent of disruption
65 e sequence-dependent positions that the core histone octamer adopts when reconstituted onto DNA conta
66 ces, which were experimentally found to have histone octamer affinities comparable to the highest-aff
67 rtial, reversible unwrapping of DNA from the histone octamer, allowing hNTH1 to capture its DNA subst
68 e HSE, had unwrapped from the 3' edge of the histone octamer, allowing HSF to bind; approximately 100
69    Uniquely, SWI/SNF CRCs can both slide the histone octamer along the DNA or eject it from the DNA.
70  of whether they face inward or outward from histone octamers along the DNA helix axis.
71 aryotic cells, genomic DNA is wrapped around histone octamers (an H3-H4 tetramer and two H2A-H2B dime
72 lizes nucleosomes by displacing DNA from the histone octamer and creating DNA "bulges" that transloca
73 and H4, mediate key interactions between the histone octamer and DNA in forming the nucleosomal parti
74 sted a model in which Isw2 complex binds the histone octamer and DNA separately to generate the force
75                   While the structure of the histone octamer and its interaction with the DNA remain
76 titutions to control the loading of both the histone octamer and linker histone onto the 601 DNA arra
77 y conserved Snf5 subunit associates with the histone octamer and not with nucleosomal DNA.
78 ave obtained nucleosome arrays that have one histone octamer and one H5 bound per 200 bp repeat, and
79 ome, detaching two turns of the DNA from the histone octamer and placing the NAD(+) binding pocket cl
80 cule required for its tight curvature on the histone octamer and the neutralization of the DNA phosph
81  insertion of the catalytic core between the histone octamer and the unwrapped segment of DNA.
82  hotspots on both nucleosomal/linker DNA and histone octamer and unraveled diverse binding modes betw
83 es, termed "altosomes," each composed of two histone octamers and bearing an asymmetrically located r
84 gonucleosome fragments composed of only core histone octamers and DNA possess all of the structural f
85 n average free energy of interaction between histone octamers and DNA, and an average wrapping length
86 effects of PRMT2 towards PRMT1 on unmodified histone octamers and mononucleosomes and found marginal
87 nucleosomes assembled with human recombinant histone octamers and nucleosome-positioning DNA containi
88 resulting constructs tested for affinity for histone octamers and translational positioning in in vit
89 d nucleosomal arrays reconstituted from core histone octamers and twelve 208 bp tandem repeats of Lyt
90 dimethyl- and trimethyllysine on H2B, H3 and histone octamers and, most remarkably, the formation of
91 ations (neutralizing the acidic patch of the histone octamer), and the removal of histone tails were
92 oxidative lesions relative to the underlying histone octamer, and (iv) the distance between the lesio
93 the Xenopus borealis 5 S rRNA gene, a single histone octamer, and 1 or 2 molecules of histone H1.
94 elix, improves positioning of the DNA on the histone octamer, and stabilizes the nucleosome against d
95 ex with two DNA molecules wrapped around two histone octamers, and an altosome complex that contains
96 ere assembled from wild type and mutant core histone octamers, and Mg(2+)-dependent oligomerization w
97           On some sequences the repositioned histone octamer appears to be moved approximately 45 bp
98 the preferred translational positions of the histone octamer are not affected by this level of UV dam
99                            We also find that histone octamers are easily transferred in trans from ss
100              Transcription factors (TFs) and histone octamers are two abundant classes of DNA binding
101 istone octamer, or even partially facing the histone octamer, are fully accessible and that nucleosom
102 istone octamer, or even partially facing the histone octamer, are fully accessible for molecular reco
103 eosomes, which consist of DNA wrapped around histone octamers, are dynamic, and their structure, incl
104 sidues within the N-terminal segments of the histone octamer around which DNA is wrapped in the nucle
105 ble DNA sequence, promoting the formation of histone octamers as well as ordered nucleosome arrays.
106                             It consists of a histone octamer associated with approximately 80 base pa
107 n the kinetics and thermodynamics of the DNA-histone octamer association that are required to remodel
108 f the DNA dissociate from the surface of the histone octamer at relatively low ionic strength, under
109  phosphodiester bonds by lifting DNA off the histone octamer at the site of integration.
110 yze DNA sequences that are known to position histone octamers at single translational sites.
111  capable of de novo nucleosome assembly from histone octamer because of its ability to simultaneously
112  but ARID1A is required for cBAF to transfer histone octamers between DNA templates.
113 2B dimers between nucleosomes, and transfers histone octamers between pieces of DNA.
114 the edge of the nucleosome, translocates the histone octamer beyond the DNA ends via a DNA bulge prop
115 sh the relationship between DNA sequence and histone octamer binding affinity.
116 ied the strength of both the chicken or frog histone octamer binding sites on each DNA, the results o
117 have compared the relative free energies for histone octamer binding to various DNA sequences; howeve
118 -K115 and H3-K122 reduces the free energy of histone octamer binding.
119 eosome remodeling factors, not only the core histone octamer but also the H3/H4 tetramer provide an n
120  positioning sequences on the surface of the histone octamer but does cause minor perturbation of nuc
121 ound marginal PRMT1 activity improvements in histone octamers but significantly greater methylation o
122  that display low intrinsic affinity for the histone octamer, but its contribution to antagonizing RN
123 AP30 complex is active in deacetylating core histone octamers, but inactive in deacetylating nucleoso
124 hese polyamides prevent repositioning of the histone octamer by RNA polymerase, and thereby inhibit p
125 been rotationally phased with respect to the histone octamer by TG motifs.
126 rvation that supports the idea that the core histone octamer can exploit different patterns of sequen
127 h consists of 147 bp of DNA wrapped around a histone octamer composed of two copies each of the histo
128 ay disrupt histone-DNA contacts by affecting histone octamer conformation and through extensive inter
129                                              Histone octamers consisting of H2A, H2B, H3, and H4 are
130                           Purified HeLa core histone octamers containing an average of 2, 6, or 12 ac
131  a specific rotational setting of DNA on the histone octamer core in each of two reconstituted nucleo
132 ers the rotational setting of the DNA on the histone octamer core such that the lesion faces inward,
133  unraveling of the first DNA wrap around the histone octamer, could be mechanically induced in a reve
134 adjacent GAGA factor binding sitesaround the histone octamer creates a unique local DNA conformation.
135                   Furthermore, SNF2h couples histone octamer deformation to nucleosome sliding, but t
136 sient DNA unwrapping from the nucleosome and histone octamer deformations.
137 cupancy maps are a sensitive function of the histone octamer density (nucleosome repeat length) and f
138 nt-Sim (PAS) dimerization domains engage the histone octamer disc.
139 ink, significantly inhibited ATP-independent histone octamer-DNA sliding.
140 that orienting the flap substrate toward the histone octamer does not significantly alter the rotatio
141  interactions between methylated DNA and the histone octamer, doubling the number of contacts at some
142 s, however, how DNA is propagated around the histone octamer during this process is unclear.
143                              Within the core histone octamer each histone H4 interacts with each H2A-
144                   The CBS interacts with the histone octamer, engaging the H2A-H2B acidic patch in a
145            Nucleosomes were reconstituted by histone octamer exchange from chicken erythocyte core pa
146               5S nucleosomes were formed via histone octamer exchange from chicken erythrocyte core p
147 ucleosome core particles (Ub-NCP) as well as histone octamers, exhibiting sigmoidal kinetics, and sug
148 ors, competition of regulatory proteins with histone octamer for access to regulatory target sites re
149 e relative free energy of association of the histone octamer for differing DNA sequences has been ava
150 t allow absolute equilibrium affinity of the histone octamer for DNA to be measured.
151 that SWI-SNF action causes a mobilization of histone octamers for both the mononucleosome and nucleos
152 SWI/SNF complex, catalyzes the transfer of a histone octamer from a nucleosome core particle to naked
153    We find that DNA methylation prevents the histone octamer from interacting with an otherwise high
154 , we show that SMARCAD1 transfers the entire histone octamer from one DNA segment to another in an AT
155 otes histone acetylation and eviction of the histone octamer from the chromatin-assembled HTLV-1 prom
156 n substrate required for dissociation of the histone octamer from the promoter DNA.
157 and its ATPases have the ability to transfer histone octamers from donor nucleosomes to acceptor DNA.
158 n, the DNA contacts at specific sites in the histone octamer had not been changed.
159  consistent with models in which a canonical histone octamer has been 'pushed' off of the end of the
160 ich segments on the surface of reconstituted histone octamers, HMG-I(Y) binding site selection on ind
161 e of unwrapping the nucleosomal DNA from the histone octamer (HO).
162                 Tight wrapping of DNA around histone octamers, however, impedes access of repair prot
163  other through their distal face, encage the histone octamer in a nucleosome-like conformation and pr
164 xes can cause translocation (sliding) of the histone octamer in cis along DNA.
165 uenced, their affinities (free energies) for histone octamer in nucleosome reconstitution measured, a
166 % of bulk DNA sequences have an affinity for histone octamer in nucleosomes that is similar to that o
167 of H2A did not affect the positioning of the histone octamer in the nucleosome in either the absence
168  The path of DNA and the conformation of the histone octamer in the nucleosome remodeled or slid by I
169 DNA completes approximately 1.7 turns on the histone octamer in the presence and absence of linker hi
170 tational settings in its wrapping around the histone octamer in the two nucleosomes.
171 h region that we establish can chaperone the histone octamer in vitro.
172            The binding of DEK3 and DEK4 to a histone octamer in vivo affects histone modifications at
173  DNA to curve gently around proteins such as histone octamers in the nucleosome particle.
174           Here we report that Mit1 mobilizes histone octamers in vitro and requires ATP hydrolysis an
175 ver, upon methylation their affinity for the histone octamer increases and a highly positioned nucleo
176  including those containing novel asymmetric histone octamers, indicate that this cooperativity occur
177 rticle, we demonstrated that histones (H1 or histone octamers) interact with negatively charged bilay
178 ow that SWI/SNF-mediated displacement of the histone octamer is effectively blocked by a barrier intr
179 d, and then, in a slower reaction, an entire histone octamer is lost.
180 indicating that the general integrity of the histone octamer is maintained.
181  These data suggest that perturbation of the histone octamer is not a requirement or a consequence of
182                                          The histone octamer is predicted to be driven off chromatin
183 gher and lower ionic strengths, the complete histone octamer is transferred over the same distance by
184 Surprisingly, transfer of H2A/H2B dimers and histone octamers is initiated on a time scale of seconds
185 "intact" core histone octamers or "tailless" histone octamers lacking their N-terminal domains.
186  In addition, this mutation destabilizes the histone octamer, leading to defects in chromatin structu
187 sts of subunits Taf5, Sgf73 and Spt20, and a histone octamer-like fold.
188 her genetic evidence supports the model of a histone octamer-like structure within TFIID.
189 ne octamer, suggesting that TFIID contains a histone octamer-like substructure.
190 studies, the results suggest that there is a histone octamer-like TAF complex within TFIID.
191  nucleosomal barrier and displace the entire histone octamer, matching the observations in vivo.
192 f these substrates does not require dramatic histone octamer movements or displacement.
193 logical relevance for processes in which the histone octamer must be rapidly removed from or deposite
194  the relative contribution of the individual histone octamer N-terminal tails as well as the effect o
195 nucleosome formation with different types of histone octamers, namely acetylated or unacetylated, and
196                       Applied to recombinant histone octamers, NF1, and TBP in complex with DNA, our
197 ling, evidenced by its interactions with the histone octamer, nucleosomal and extranucleosomal DNA, a
198                              We reconstitute histone octamers, nucleosomes, and nucleosomal arrays be
199 karyotic polymerase can transcribe through a histone octamer on a simple chromatin template.
200 ientation with respect to the surface of the histone octamer on nucleosome structure and FEN1 activit
201 e of the free energy difference between core histone octamers on and off DNA.
202 odelers utilize ATP hydrolysis to reposition histone octamers on DNA, facilitating transcription by p
203 -2-phenylindole) inhibited the assembly of a histone octamer onto a 192-base pair circular DNA fragme
204 cularly favored in terms of affinity for the histone octamer or for positioning of the reconstituted
205  histone H5, and either native "intact" core histone octamers or "tailless" histone octamers lacking
206 articles (NCPs) dissociate into free DNA and histone octamers (or free histones) on dilution without
207 ne, within the same nucleosome (containing a histone octamer), or between nucleosomes in higher-order
208 ites on nucleosomal DNA facing away from the histone octamer, or even partially facing the histone oc
209 ites on nucleosomal DNA facing away from the histone octamer, or even partially facing the histone oc
210 nt histones in the context of free histones, histone octamers, or nucleosomal arrays.
211  a majority of the sample contained both one histone octamer per 5S rDNA repeat and one molecule of h
212       Posttranslational modifications of the histone octamer play important roles in regulating respo
213 t sequence is efficiently wrapped around the histone octamer, preferring to associate with histones a
214 ucleosomes, composed of DNA wrapped around a histone octamer, present a natural barrier to end resect
215                                          The histone octamer presents different levels of constraints
216 to facilitate both translational movement of histone octamers relative to DNA and the efficient deace
217 ely unperturbed and that the position of the histone octamers relative to the DNA is not altered duri
218                                    While the histone octamer remains intact, the DNA is lifted from t
219  modifications in the lateral surface of the histone octamer remains unclear.
220 despite the steric constraints placed by the histone octamer remains unknown.
221 cetylation of lateral surface lysines in the histone octamer serves as a crucial regulator of nucleos
222 focus here on the interaction of NP with the histone octamer, showing that NP could bind sequentially
223 unchanged upon GAL4 binding, suggesting that histone octamer sliding did not occur.
224 uires a significantly higher temperature for histone octamer sliding in vitro compared to comparable
225 ng the (H3/H4)2 heterotetrameric core of the histone octamer, suggesting that TFIID contains a histon
226 and translational settings of 5S rDNA on the histone octamer surface after induction of up to 0.8 CPD
227 ange in which a stretch of DNA peels off the histone octamer surface as a result of thermal fluctuati
228  holding DNA to the superhelical ramp on the histone octamer surface is obtained from a relatively sm
229 owever, uracils at sites oriented toward the histone octamer surface were excised at much slower rate
230  peels as much as 50 bp of DNA away from the histone octamer surface.
231 ansient dynamic exposure of the DNA from the histone octamer surface.
232 artial dissociation of the DNA ends from the histone octamer surface; however, no dissociation or sub
233                                              Histone octamer survives moderate transcription, but is
234 ify contacts between the nucleosomal DNA and histone octamer that prevent efficient processing of the
235 ontaneous partial unwrapping of DNA from the histone octamer; that the scaffolding protein XRCC1 enha
236 thymine glycol lesion faced outward from the histone octamer, the human DNA glycosylase NTH1 (hNTH1)
237  in terms of their relative affinity for the histone octamer, their locations with respect to the gen
238 SWI ATPase to pump a DNA distortion over the histone octamer, thereby changing the translational posi
239 m the nucleosome and promote transfer of the histone octamer to an acceptor protein.
240 dent reaction that favours attachment of the histone octamer to an acceptor site on the same molecule
241 NA-translocase domain to pump DNA around the histone octamer to enable sliding.
242 omatin through its association with the core histone octamer to form the nucleosome core particle (NC
243                   However, cross-linking the histone octamer to nucleosomal DNA does not inhibit remo
244 directly with an increased propensity of the histone octamer to reposition with respect to the DNA, a
245 DNA sequence that directed the deposition of histone octamers to a single site, and it was proposed t
246  Finally, NP was capable of transferring the histone octamers to DNA in vitro, assembling nucleosomes
247 level of organization, DNA is wrapped around histone octamers to form nucleosomal particles that are
248 and photoaffinity labeling using recombinant histone octamers to require the histone H4 N-terminal ta
249 suggesting a model in which dysregulation of histone octamer transfer activity of BAF complexes may b
250 ription factor Gal4-VP16 can enhance SWI/SNF histone octamer transfer activity, resulting in targeted
251 f SWI/SNF action, whereas few have described histone octamer transfer as the principal outcome.
252 e dimer or lead to alternative fates such as histone octamer transfer to another DNA or sliding along
253 chromatin remodeling complexes, the rates of histone octamer translocation and nucleosome reformation
254 re is composed of nucleosomes, or repetitive histone octamer units typically enfolded by 147 base pai
255 aining an average of two or six acetates per histone octamer was indistinguishable, while a level of
256  lesions whose minor groove faced toward the histone octamer was poor at low hNTH1 concentrations but
257 leosome array reconstituted from recombinant histone octamers, we have defined the relative contribut
258 ons between the nucleosomal DNA ends and the histone octamer were destabilized in A16 NCP.
259 ggest that these complexes each contain five histone octamers which dock to a central Np decamer.
260 achment of terminal nucleosomal DNA from the histone octamer, which increases DNA accessibility.
261 matic detachment of nucleosomal DNA from the histone octamer, which is a non-catalytic activity.
262 atic interactions with hydrogen bonds in the histone octamer with a dissociation constant of 250 nM.
263            Since this DNA sequence binds the histone octamer with much higher affinity than mixed seq
264 p double-stranded DNA are wrapped around one histone octamer with no free DNA ends remaining.
265 pendent on an increased mobility of the core histone octamer with respect to DNA sequence.
266 rs used in this study were derived from pure histone octamers with their native marks.
267  of the recombination signal sequence on the histone octamer, with cleavage of the 12 bp spacer RSS s
268 he increased salt-dependent stability of the histone octamer, with implications for the nucleosome as
269  base pairs remained in association with the histone octamer, with the same translational and rotatio
270 one is oriented away from the surface of the histone octamer, without significant disruption of histo

 
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