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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
9 information regulator 1 protein (Sir1p) and origin recognition complex 1 protein (Orc1p), the larges
10 rocesses including genome replication (ORC1 [origin recognition complex 1], ORC4, ORC6, CDT1, and CDC
11 munoprecipitation assay performed using anti-origin recognition complex 2 (alpha-ORC2) and alpha-LANA
12 cribe the mechanistic roles of two proteins--origin recognition complex 2 (Orc2) and heterochromatin
14 iP replication activity and increases EBNA1, origin recognition complex 2 (ORC2), and minichromosome
15 odomain-containing protein 2 (BRD2), and the origin recognition complex 2 protein (ORC2) and was enri
16 is also exploited by the RIF2 paralog ORC4 (Origin Recognition Complex 4) in Kluyveromyces lactis an
18 mutations in other pre-RC proteins (such as Origin Recognition Complex and Cdc6), but not to mutatio
19 ing minichromosome maintenance proteins, the origin recognition complex and DNA polymerase alpha.
20 ractions between MUM2 and a component of the origin recognition complex and polymerase alpha-primase
21 in to become functionally licensed: ORC (the origin recognition complex) and Cdc6, plus the two compo
22 pull-down assays demonstrate that ORCA-ORC (Origin Recognition Complex) and multiple H3K9 KMTs exist
23 CE3 and Ori-beta, are directly bound by Orc (origin recognition complex), and two-dimensional gel ana
25 l connection between wild-type Sum1p and the origin recognition complex, and this relationship also c
26 Human cells that lack a subunit in their origin recognition complex are viable, which suggests th
29 ing by PCNA and CDC45 mutations required the origin recognition complex binding site of the HMR-E sil
32 yeast, the eukaryotic initiator protein ORC (origin recognition complex) binds to a bipartite sequenc
33 hat one molecule of the helicase loader ORC (origin recognition complex) can sequentially load two Mc
34 mutations in ORC1, encoding a subunit of the origin recognition complex, cause microcephalic primordi
38 A replication, the Orc1 subunit of the human origin recognition complex controls centriole and centro
41 SWI/SNF-related complexes co-localizes with origin recognition complexes, GINS complexes, and prolif
42 the six subunits of Saccharomyces cerevisiae origin recognition complex have been reported so far.
44 and B1 elements, which are known to bind the origin recognition complex; however, the ARS1 A element
46 n of an initial complex containing the human origin recognition complex (HsORC), HsCdt1, HsCdc6, and
50 eins we identified is identical to the human origin recognition complex-interacting protein termed HB
51 tional silencing, and ORC is the six-subunit origin recognition complex involved in the initiation of
53 S1 association of Mcm2p, but not that of the origin recognition complex, is diminished by disruption
54 an evolutionarily conserved component of the origin recognition complex, is essential for deoxyribonu
55 hromatin-bound B-subunit in association with origin recognition complex mediates recruiting Polalpha-
56 o early G1 phase through an interaction with Origin Recognition Complex or another origin-associated
60 in transcriptional silencing mediated by the origin recognition complex (ORC) and a heterochromatin s
61 eucine enabled Sum1-1p to associate with the origin recognition complex (ORC) and accumulate near ORC
62 the association of the Cdc6 protein with the Origin Recognition Complex (ORC) and appears concomitant
63 y reveal a functional connection between the origin recognition complex (ORC) and Cdc45p but also ext
64 assembly of protein complexes, including the origin recognition complex (ORC) and CDC6 AAA(+) ATPases
65 expected to recruit initiation proteins like origin recognition complex (ORC) and Cdc6 in eukaryotes
69 helicase motor is deposited onto DNA by the origin recognition complex (ORC) and co-loader proteins
70 t1 onto origins bound by the heterohexameric origin recognition complex (ORC) and functions as a repl
72 ts DUE sequence, despite the presence of the origin recognition complex (ORC) and MCM proteins at the
74 f DNA replication in eukaryotes requires the origin recognition complex (ORC) and other proteins that
75 inhibits MCM loading by phosphorylating the origin recognition complex (ORC) and promotes CMG format
76 were reduced in their ability to recruit the origin recognition complex (ORC) and stimulate OriP repl
79 alyzed the developmental localization of the origin recognition complex (ORC) and the minichromosome
80 tiate DNA replication and interacts with the origin recognition complex (ORC) and the p34cdc2 CDK.
81 ental stage-specific binding regions for the Origin Recognition Complex (ORC) and the replicative hel
83 or is loaded onto replication origins by the origin recognition complex (ORC) as a head-to-head doubl
84 ion assay, we have measured the stability of origin recognition complex (ORC) associated with sperm c
85 itory sequence positioned 3' to the sites of origin recognition complex (ORC) binding and pre-RC asse
87 , which flank the silenced loci, includes an origin recognition complex (ORC) binding site (ACS).
94 architecture of the Saccharomyces cerevisiae origin recognition complex (ORC) bound to yeast origins
95 tion that are specifically recognized by the origin recognition complex (ORC) containing multiple ATP
101 In a Xenopus egg replication system, the origin recognition complex (ORC) does not bind to CpG me
102 0me1-reading BAHCC1 and the H4K20me2-reading Origin Recognition Complex (ORC) ensure genomic loading
103 cle-dependent changes in the affinity of the origin recognition complex (ORC) for chromatin are invol
108 ARS consensus sequence (ACS) that binds the origin recognition complex (ORC) has been experimentally
109 plicative helicase and between one and three origin recognition complex (ORC) homologues involved in
110 first genome-wide analysis of binding of the origin recognition complex (ORC) in a differentiated met
111 tificial locus results in recruitment of the origin recognition complex (ORC) in a manner dependent o
131 le of Saccharomyces cerevisiae, the level of origin recognition complex (ORC) is constant and ORCs ar
136 e location analysis, we demonstrate that the origin recognition complex (ORC) is localized to specifi
140 visiae, sequence-specific DNA binding by the origin recognition complex (ORC) is responsible for sele
144 ation for bidirectional DNA replication, the origin recognition complex (ORC) loads two hexameric MCM
149 cetylation of nucleosomes and binding of the origin recognition complex (ORC) occur in a broad domain
152 of a pre-replication complex facilitated by Origin Recognition Complex (ORC) onto the chromatin duri
157 c7p kinase activity, or interaction with the origin recognition complex (ORC) postulated to recruit C
158 aintenance (MCM) proteins, together with the origin recognition complex (ORC) proteins and Cdc6, play
161 Budding yeast (Saccharomyces cerevisiae) origin recognition complex (ORC) requires ATP to bind sp
164 lecule visualization, we show here that S.c. origin recognition complex (ORC) stably binds nucleosome
165 ins by chromatin immunoprecipitation against origin recognition complex (ORC) subunits 2 and 3 showed
166 protein complex of HP1 containing Drosophila origin recognition complex (ORC) subunits in the early D
167 e cyclin-dependent kinases (CDKs) target two origin recognition complex (ORC) subunits, Orc2 and Orc6
168 ure-sensitive mutation in a component of the origin recognition complex (ORC) that also causes a defe
169 role for the Orc1 protein, a subunit of the origin recognition complex (ORC) that is a key component
170 s of binding sites for Abf1p, Rap1p, and the origin recognition complex (ORC) that serve to recruit t
171 emonstrated that EBNA1 recruits the cellular origin recognition complex (ORC) through an RNA-dependen
172 myces cerevisiae requires the binding of the origin recognition complex (ORC) to autonomously replica
174 CM loading is orchestrated by binding of the origin recognition complex (ORC) to DNA, but how ORC coo
180 s solely responsible for in vitro binding of origin recognition complex (ORC) to specific AT-rich sit
181 otein complex (Mcm), topoisomerases, and the origin recognition complex (ORC) using an in vitro assay
189 tic DNA replication initiation relies on the origin recognition complex (ORC), a DNA-binding ATPase t
190 s the silencer through interactions with the origin recognition complex (ORC), a protein complex that
191 In eukaryotes, DNA replication requires the origin recognition complex (ORC), a six-subunit assembly
193 sequence (ACS) element, presumed to bind the origin recognition complex (ORC), and a broad 3'-flankin
194 meters of transcription, localization of the origin recognition complex (ORC), and histone acetylatio
195 These loci are identified and bound by the origin recognition complex (ORC), and subsequently activ
196 two factors: the sequence preferences of the origin recognition complex (ORC), and the interference o
197 g the role of the prereplication complex and origin recognition complex (ORC), and uncovering regulat
198 he ACS is the binding site for the initiator origin recognition complex (ORC), but the selected seque
199 he prereplicative complex (pre-RC) proteins: origin recognition complex (ORC), CDC-6, and CDT-1.
200 f how the double hexamer is assembled by the origin recognition complex (ORC), CDC6 and CDT1 comes mo
202 tions of a variety of proteins including the origin recognition complex (ORC), Cdc6 and the Mcm2-7 he
205 sing of replication origins-during which the origin recognition complex (ORC), CDC6, and CDT1 coopera
206 The loading of Mcm2-7 onto DNA requires the origin recognition complex (ORC), Cdc6, and Cdt1, and de
211 lex (pre-RC), and its formation requires the origin recognition complex (ORC), Cdc6, Cdt1, and ATP.
212 ins of replication through the action of the origin recognition complex (ORC), Cdc6, Cdt1, and the Mc
213 ential binding to replication origins of the origin recognition complex (ORC), Cdc6/Cdc18, Cdt1, and
216 re-RCs) as an inactive double hexamer by the origin recognition complex (ORC), Cdt1 and Cdc6; the hel
217 CM)2-7 recruitment to origins in G1 requires origin recognition complex (ORC), Cdt1, and Cdc6, and ac
219 la Orc6 protein, the smallest subunit of the origin recognition complex (ORC), directly binds to sept
220 mechanisms, including phosphorylation of the origin recognition complex (ORC), downregulation of Cdc6
222 ctors 1 (TRF1) and 2 (TRF2), subunits of the origin recognition complex (ORC), heterochromatin protei
224 ction with Orc1p, the largest subunit of the origin recognition complex (ORC), is critical for Sir1p'
225 we demonstrate that the yeast initiator, the origin recognition complex (ORC), is required to maintai
226 to DNA replication, including a role for the origin recognition complex (ORC), the DNA replication in
227 t sites of DNA replication are marked by the origin recognition complex (ORC), which coordinates Mcm2
228 esemble those generated in vitro by purified origin recognition complex (ORC), which is essential for
229 interaction between origin sequences and the origin recognition complex (ORC), which is highly conser
230 teraction between an origin sequence and the origin recognition complex (ORC), which is highly conser
231 origins of DNA replication are bound by the origin recognition complex (ORC), which scaffolds assemb
233 eported that a WD repeat-containing protein, origin recognition complex (ORC)-associated (ORCA/LRWD1)
234 ne response element directly adjacent to the origin recognition complex (ORC)-binding site in the II/
235 MCM) double hexamer, its precursors, and the origin recognition complex (ORC)-Cdc6-Cdt1-Mcm2-7 (OCCM)
237 o chromatin states during the cell cycle: an origin recognition complex (ORC)-dependent post-replicat
238 in S phase requires the prior assembly of an origin recognition complex (ORC)-dependent pre-replicati
262 the two pre-replicative complex components (origin recognition complex [ORC] and minichromosome main
263 in components of the prereplicative complex (origin recognition complex [ORC], Cdc6, and minichromoso
265 the gene encoding the second subunit of the origin recognition complex, ORC, and MCM3, another membe
267 cerevisiae Orc2 protein is a subunit of the origin recognition complex, ORC, which binds in a sequen
269 gest subunit of the Saccharomyces cerevisiae origin recognition complex (Orc1p) functions in transcri
270 of subunit 5 of the Drosophila melanogaster origin recognition complex (Orc5) and have characterized
271 ition correlate with the activity of hamster origin recognition complexes (ORCs) and the appearance o
272 mammalian chromosomes, the time when hamster origin recognition complexes (ORCs) became functional wa
276 Here we report that LANA associates with origin recognition complexes (ORCs) when bound to its 17
277 protein (Orc1p), the largest subunit of the origin recognition complex, plays an important role in t
278 In Drosophila, the largest subunit of the origin recognition complex protein 1 (ORC1) is degraded
279 binding patterns of EBNA1 with those of the origin recognition complex protein ORC2, the chromatin b
281 ised the interaction of the Aeropyrum pernix origin recognition complex proteins (ORC1 and ORC2) with
282 rget sites that in tissue-culture cells bind origin recognition complex proteins and function as repl
283 enetically interacts and coprecipitates with origin recognition complex proteins Orp1/Orc1 and Orp2/O
285 , and restriction (including subunits of the origin recognition complex, replication factor C protein
286 n turn, suggest the existence of a mammalian origin recognition complex, similar to that found in yea
287 o OriP in vivo as well as for assembling the origin recognition complex subunit 2 (ORC2) and trimethy
289 encodes the Drosophila homolog of the yeast origin recognition complex subunit 2 (Orc2p), a protein
292 We report that the smallest of Drosophila origin recognition complex subunits, Orc6, was found in
293 n an orderly association, beginning with the origin recognition complex, that culminates in the initi
294 ard B2, adjacent to the binding site for the origin recognition complex, the putative initiator prote
295 consisting of a single binding site for the origin recognition complex, the replication initiator pr
296 Strikingly, DUP protein colocalizes with the origin recognition complex to specific sites in the ovar
298 which constitute the core of the replication origin recognition complex, were among the most signific
300 atin before licensing can occur: the Xenopus origin recognition complex (XORC) [8] [9] and Xenopus Cd