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1 spacing, are bent by EBNA1, and recruit the origin recognition complex.
2 nature and the characteristics of the human origin recognition complex.
3 in multiple, redundant binding sites for the origin recognition complex.
4 t with it being a part of the putative human origin recognition complex.
5 chromatin requires Xorc2, a component of the origin recognition complex.
6 the genome with the highest affinity for the origin recognition complex.
7 ied histone acetyltransferase binding to the origin recognition complex 1 (Hbo1) as a potential Plk1
8 information regulator 1 protein (Sir1p) and origin recognition complex 1 protein (Orc1p), the larges
9 rocesses including genome replication (ORC1 [origin recognition complex 1], ORC4, ORC6, CDT1, and CDC
10 munoprecipitation assay performed using anti-origin recognition complex 2 (alpha-ORC2) and alpha-LANA
11 cribe the mechanistic roles of two proteins--origin recognition complex 2 (Orc2) and heterochromatin
13 iP replication activity and increases EBNA1, origin recognition complex 2 (ORC2), and minichromosome
14 odomain-containing protein 2 (BRD2), and the origin recognition complex 2 protein (ORC2) and was enri
16 mutations in other pre-RC proteins (such as Origin Recognition Complex and Cdc6), but not to mutatio
17 ing minichromosome maintenance proteins, the origin recognition complex and DNA polymerase alpha.
18 ractions between MUM2 and a component of the origin recognition complex and polymerase alpha-primase
19 in to become functionally licensed: ORC (the origin recognition complex) and Cdc6, plus the two compo
20 pull-down assays demonstrate that ORCA-ORC (Origin Recognition Complex) and multiple H3K9 KMTs exist
21 CE3 and Ori-beta, are directly bound by Orc (origin recognition complex), and two-dimensional gel ana
23 l connection between wild-type Sum1p and the origin recognition complex, and this relationship also c
24 Human cells that lack a subunit in their origin recognition complex are viable, which suggests th
27 ing by PCNA and CDC45 mutations required the origin recognition complex binding site of the HMR-E sil
30 yeast, the eukaryotic initiator protein ORC (origin recognition complex) binds to a bipartite sequenc
31 mutations in ORC1, encoding a subunit of the origin recognition complex, cause microcephalic primordi
35 A replication, the Orc1 subunit of the human origin recognition complex controls centriole and centro
37 SWI/SNF-related complexes co-localizes with origin recognition complexes, GINS complexes, and prolif
38 the six subunits of Saccharomyces cerevisiae origin recognition complex have been reported so far.
40 and B1 elements, which are known to bind the origin recognition complex; however, the ARS1 A element
42 n of an initial complex containing the human origin recognition complex (HsORC), HsCdt1, HsCdc6, and
46 eins we identified is identical to the human origin recognition complex-interacting protein termed HB
47 tional silencing, and ORC is the six-subunit origin recognition complex involved in the initiation of
49 S1 association of Mcm2p, but not that of the origin recognition complex, is diminished by disruption
50 an evolutionarily conserved component of the origin recognition complex, is essential for deoxyribonu
51 hromatin-bound B-subunit in association with origin recognition complex mediates recruiting Polalpha-
52 o early G1 phase through an interaction with Origin Recognition Complex or another origin-associated
56 in transcriptional silencing mediated by the origin recognition complex (ORC) and a heterochromatin s
57 eucine enabled Sum1-1p to associate with the origin recognition complex (ORC) and accumulate near ORC
58 the association of the Cdc6 protein with the Origin Recognition Complex (ORC) and appears concomitant
59 y reveal a functional connection between the origin recognition complex (ORC) and Cdc45p but also ext
60 expected to recruit initiation proteins like origin recognition complex (ORC) and Cdc6 in eukaryotes
64 t1 onto origins bound by the heterohexameric origin recognition complex (ORC) and functions as a repl
66 ts DUE sequence, despite the presence of the origin recognition complex (ORC) and MCM proteins at the
68 f DNA replication in eukaryotes requires the origin recognition complex (ORC) and other proteins that
69 inhibits MCM loading by phosphorylating the origin recognition complex (ORC) and promotes CMG format
70 were reduced in their ability to recruit the origin recognition complex (ORC) and stimulate OriP repl
72 alyzed the developmental localization of the origin recognition complex (ORC) and the minichromosome
73 tiate DNA replication and interacts with the origin recognition complex (ORC) and the p34cdc2 CDK.
74 ental stage-specific binding regions for the Origin Recognition Complex (ORC) and the replicative hel
76 ion assay, we have measured the stability of origin recognition complex (ORC) associated with sperm c
77 itory sequence positioned 3' to the sites of origin recognition complex (ORC) binding and pre-RC asse
79 , which flank the silenced loci, includes an origin recognition complex (ORC) binding site (ACS).
85 architecture of the Saccharomyces cerevisiae origin recognition complex (ORC) bound to yeast origins
91 In a Xenopus egg replication system, the origin recognition complex (ORC) does not bind to CpG me
92 cle-dependent changes in the affinity of the origin recognition complex (ORC) for chromatin are invol
97 ARS consensus sequence (ACS) that binds the origin recognition complex (ORC) has been experimentally
98 plicative helicase and between one and three origin recognition complex (ORC) homologues involved in
99 first genome-wide analysis of binding of the origin recognition complex (ORC) in a differentiated met
100 tificial locus results in recruitment of the origin recognition complex (ORC) in a manner dependent o
119 le of Saccharomyces cerevisiae, the level of origin recognition complex (ORC) is constant and ORCs ar
123 e location analysis, we demonstrate that the origin recognition complex (ORC) is localized to specifi
125 visiae, sequence-specific DNA binding by the origin recognition complex (ORC) is responsible for sele
132 cetylation of nucleosomes and binding of the origin recognition complex (ORC) occur in a broad domain
135 of a pre-replication complex facilitated by Origin Recognition Complex (ORC) onto the chromatin duri
140 c7p kinase activity, or interaction with the origin recognition complex (ORC) postulated to recruit C
141 aintenance (MCM) proteins, together with the origin recognition complex (ORC) proteins and Cdc6, play
144 Budding yeast (Saccharomyces cerevisiae) origin recognition complex (ORC) requires ATP to bind sp
147 ins by chromatin immunoprecipitation against origin recognition complex (ORC) subunits 2 and 3 showed
148 protein complex of HP1 containing Drosophila origin recognition complex (ORC) subunits in the early D
149 e cyclin-dependent kinases (CDKs) target two origin recognition complex (ORC) subunits, Orc2 and Orc6
150 ure-sensitive mutation in a component of the origin recognition complex (ORC) that also causes a defe
151 role for the Orc1 protein, a subunit of the origin recognition complex (ORC) that is a key component
152 s of binding sites for Abf1p, Rap1p, and the origin recognition complex (ORC) that serve to recruit t
153 emonstrated that EBNA1 recruits the cellular origin recognition complex (ORC) through an RNA-dependen
154 myces cerevisiae requires the binding of the origin recognition complex (ORC) to autonomously replica
155 CM loading is orchestrated by binding of the origin recognition complex (ORC) to DNA, but how ORC coo
161 s solely responsible for in vitro binding of origin recognition complex (ORC) to specific AT-rich sit
162 otein complex (Mcm), topoisomerases, and the origin recognition complex (ORC) using an in vitro assay
169 s the silencer through interactions with the origin recognition complex (ORC), a protein complex that
170 In eukaryotes, DNA replication requires the origin recognition complex (ORC), a six-subunit assembly
172 sequence (ACS) element, presumed to bind the origin recognition complex (ORC), and a broad 3'-flankin
173 meters of transcription, localization of the origin recognition complex (ORC), and histone acetylatio
174 These loci are identified and bound by the origin recognition complex (ORC), and subsequently activ
175 g the role of the prereplication complex and origin recognition complex (ORC), and uncovering regulat
176 he ACS is the binding site for the initiator origin recognition complex (ORC), but the selected seque
177 he prereplicative complex (pre-RC) proteins: origin recognition complex (ORC), CDC-6, and CDT-1.
179 tions of a variety of proteins including the origin recognition complex (ORC), Cdc6 and the Mcm2-7 he
181 The loading of Mcm2-7 onto DNA requires the origin recognition complex (ORC), Cdc6, and Cdt1, and de
185 lex (pre-RC), and its formation requires the origin recognition complex (ORC), Cdc6, Cdt1, and ATP.
186 ins of replication through the action of the origin recognition complex (ORC), Cdc6, Cdt1, and the Mc
187 ential binding to replication origins of the origin recognition complex (ORC), Cdc6/Cdc18, Cdt1, and
190 re-RCs) as an inactive double hexamer by the origin recognition complex (ORC), Cdt1 and Cdc6; the hel
191 CM)2-7 recruitment to origins in G1 requires origin recognition complex (ORC), Cdt1, and Cdc6, and ac
192 la Orc6 protein, the smallest subunit of the origin recognition complex (ORC), directly binds to sept
193 mechanisms, including phosphorylation of the origin recognition complex (ORC), downregulation of Cdc6
195 ctors 1 (TRF1) and 2 (TRF2), subunits of the origin recognition complex (ORC), heterochromatin protei
197 ction with Orc1p, the largest subunit of the origin recognition complex (ORC), is critical for Sir1p'
198 we demonstrate that the yeast initiator, the origin recognition complex (ORC), is required to maintai
199 to DNA replication, including a role for the origin recognition complex (ORC), the DNA replication in
200 t sites of DNA replication are marked by the origin recognition complex (ORC), which coordinates Mcm2
201 esemble those generated in vitro by purified origin recognition complex (ORC), which is essential for
202 interaction between origin sequences and the origin recognition complex (ORC), which is highly conser
203 teraction between an origin sequence and the origin recognition complex (ORC), which is highly conser
204 origins of DNA replication are bound by the origin recognition complex (ORC), which scaffolds assemb
205 eported that a WD repeat-containing protein, origin recognition complex (ORC)-associated (ORCA/LRWD1)
206 ne response element directly adjacent to the origin recognition complex (ORC)-binding site in the II/
207 MCM) double hexamer, its precursors, and the origin recognition complex (ORC)-Cdc6-Cdt1-Mcm2-7 (OCCM)
208 o chromatin states during the cell cycle: an origin recognition complex (ORC)-dependent post-replicat
209 in S phase requires the prior assembly of an origin recognition complex (ORC)-dependent pre-replicati
230 the two pre-replicative complex components (origin recognition complex [ORC] and minichromosome main
231 in components of the prereplicative complex (origin recognition complex [ORC], Cdc6, and minichromoso
233 the gene encoding the second subunit of the origin recognition complex, ORC, and MCM3, another membe
235 cerevisiae Orc2 protein is a subunit of the origin recognition complex, ORC, which binds in a sequen
236 gest subunit of the Saccharomyces cerevisiae origin recognition complex (Orc1p) functions in transcri
237 of subunit 5 of the Drosophila melanogaster origin recognition complex (Orc5) and have characterized
238 ition correlate with the activity of hamster origin recognition complexes (ORCs) and the appearance o
239 mammalian chromosomes, the time when hamster origin recognition complexes (ORCs) became functional wa
243 Here we report that LANA associates with origin recognition complexes (ORCs) when bound to its 17
244 protein (Orc1p), the largest subunit of the origin recognition complex, plays an important role in t
245 In Drosophila, the largest subunit of the origin recognition complex protein 1 (ORC1) is degraded
246 binding patterns of EBNA1 with those of the origin recognition complex protein ORC2, the chromatin b
248 ised the interaction of the Aeropyrum pernix origin recognition complex proteins (ORC1 and ORC2) with
249 rget sites that in tissue-culture cells bind origin recognition complex proteins and function as repl
250 enetically interacts and coprecipitates with origin recognition complex proteins Orp1/Orc1 and Orp2/O
252 , and restriction (including subunits of the origin recognition complex, replication factor C protein
253 n turn, suggest the existence of a mammalian origin recognition complex, similar to that found in yea
254 o OriP in vivo as well as for assembling the origin recognition complex subunit 2 (ORC2) and trimethy
256 encodes the Drosophila homolog of the yeast origin recognition complex subunit 2 (Orc2p), a protein
258 We report that the smallest of Drosophila origin recognition complex subunits, Orc6, was found in
259 n an orderly association, beginning with the origin recognition complex, that culminates in the initi
260 ard B2, adjacent to the binding site for the origin recognition complex, the putative initiator prote
261 consisting of a single binding site for the origin recognition complex, the replication initiator pr
262 Strikingly, DUP protein colocalizes with the origin recognition complex to specific sites in the ovar
265 atin before licensing can occur: the Xenopus origin recognition complex (XORC) [8] [9] and Xenopus Cd
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