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1 yeast CHL12 and has similarity to mammalian replication factor C.
2 teracts with multiple subunits of Drosophila replication factor C.
3 al DNA template was dependent on PCNA and on replication factor C.
4 nt on proliferating cell nuclear antigen and replication factor C.
5 ncy in stimulation of the ATPase activity of replication factor C.
6 imase, DNA polymerase alpha, DNA ligase, and replication factor C.
7 provides a binding site for the clamp-loader Replication Factor C.
8 lity of PCNA to be loaded onto primed DNA by replication factor C.
9 egions of homology with the five subunits of Replication factor C.
10 pha, proliferating cell nuclear antigen, and replication factor C activate MutLalpha endonuclease to
12 h three- and four-subunit complexes required replication factor C and proliferating cell nuclear anti
13 dition of M. thermoautotrophicum homologs of replication factor C and proliferating cell nuclear anti
14 rms a replication complex in the presence of replication factor C and proliferating cell nuclear anti
16 n A, proliferating cell nuclear antigen, and replication factor C and was active in the SV40 DNA repl
18 ntenance (MCM) 3' --> 5' DNA helicase, PolB, replication factor C, and proliferating cell nuclear ant
19 sence of proliferating cell nuclear antigen, replication factor C, and single-stranded binding protei
20 d circular DNA do in fact support MutSbeta-, replication factor C-, and PCNA-dependent activation of
23 These functions include loading onto DNA by replication factor C, as well as Okazaki fragment synthe
24 athway, FEN1 was functional without PCNA and replication factor C but required the DNA synthesis, whi
26 structural gene for the large subunit of DNA replication factor C (cdc44/rfc1) causes striking increa
27 ith mutations affecting the large subunit of replication factor C (Cdc44p or Rfc1p) in Saccharomyces
31 tion in the large subunit of the replicative replication factor C complex (rfc1-1) increased the expa
32 ase delta/proliferating cell nuclear antigen/replication factor C complex on telomeric templates that
33 pendent phosphorylation; associates with the replication factor C complex, a critical component of th
34 ion: proliferating cell nuclear antigen, the replication factor C complex, DNA polymerase delta, flap
35 FC3 encode three of the five subunits of the replication factor C complex, which is required to load
41 ved in spindle-associated, Ctf18-alternative replication factor C (Ctf18-RFC) clamp loader complex, a
42 log 6, Exonuclease 1, replication protein A, replication factor C-Delta1N, proliferating cell nuclear
43 liferating cell nuclear antigen clamp loader replication factor C, DNA polymerase delta, and DNA liga
45 ng cell nuclear antigen and the clamp loader replication factor C facilitated DNA synthesis with Dpo3
46 ticipation that the discovery of this unique replication factor C homolog will lead to critical insig
49 a its non-conserved C-terminal domain (CTD); replication factor C interaction results in approximatel
52 conformations matching the helical pitch of Replication Factor C, it is not biased toward a right-ha
54 factor is loaded onto DNA by the Rad24-RFC (replication factor C-like complex with Rad24) clamp load
55 es now present data strongly implicating the replication factor C-like complex, Elg1/ATAD5-RLC, in th
57 the nascent strand from polymerase alpha to replication factor C, one possibility is that this step
59 ix purified human proteins: AP endonuclease, replication factor C, PCNA, flap endonuclease 1 (FEN1),
60 S. pombe Uve1p, Rad2p, DNA polymerase delta, replication factor C, proliferating cell nuclear antigen
61 system comprised of MutS alpha, MutL alpha, replication factor C, proliferating cell nuclear antigen
62 th the 9-1-1 heterotrimer reminiscent of the replication factor C/proliferating cell nuclear antigen
63 Condensin, minichromosome maintenance, and replication factor C protein complexes were identified a
64 subunits of the origin recognition complex, replication factor C proteins, MCM DNA-licensing factors
65 ating cell nuclear antigen (PCNA) loading by replication factor C, providing a potential mechanism fo
67 ation factors, and the clamp loader complex (replication factor C) remained tethered to chromatin.
76 ating cell nuclear antigen (PCNA) loading by replication factor C (RFC) acts as the initial sensor of
77 oliferating cell nuclear antigen (PCNA), and replication factor C (RFC) and a reconstituted Mlh1-Pms1
78 , proliferating cell nuclear antigen (PCNA), replication factor C (RFC) and DNA polymerase delta.
79 plication clamp PCNA is loaded around DNA by replication factor C (RFC) and functions in DNA replicat
82 en (PCNA), and show that PCNA, together with replication factor C (RFC) and replication protein A (RP
87 of the Saccharomyces cerevisiae clamp loader Replication Factor C (RFC) bound to its cognate sliding
91 However, unlike the loading of PCNA by the replication factor C (RFC) clamp loader onto 3'-recessed
93 , and D subunits of Saccharomyces cerevisiae replication factor C (RFC) clamp loader, respectively, a
95 ell nuclear antigen (PCNA) sliding clamp and replication factor C (RFC) clamp-loading complex, using
96 ELG1 protein, which comprises an alternative replication factor C (RFC) complex and plays an importan
98 visiae, this process involves an alternative replication factor C (RFC) complex that contains the fou
99 oliferating cell nuclear antigen (PCNA), the replication factor C (RFC) complex, DNA polymerase delta
101 s, sliding clamps are loaded onto DNA by the replication factor C (RFC) complex, which consists of fi
102 igated the communication between subunits in replication factor C (RFC) from Archaeoglobus fulgidus.
104 of the Saccharomyces cerevisiae clamp loader Replication Factor C (RFC) in absence of sliding clamp o
110 ing cell nuclear antigen loading onto DNA by replication factor C (RFC) is a key step in eukaryotic D
112 netic experiments reveal that ATP binding to replication factor C (RFC) is sufficient for loading the
113 tural studies of the eukaryotic clamp loader replication factor C (RFC) revealed that it functions us
114 Rad17 homologs have extensive homology with replication factor C (RFC) subunits (p36, p37, p38, p40,
115 tin by a complex of Rad17 and the four small replication factor C (RFC) subunits (Rad17-RFC) in respo
116 d DNA binding site in the yeast clamp loader replication factor C (RFC) that aids in binding to nicke
117 Pase, is the bacterial homolog of eukaryotic replication factor C (RFC) that loads the sliding clamp
118 24 interacts with the four small subunits of replication factor C (RFC) to form the RFC-Rad24 complex
119 Additionally, we show a unique ability of replication factor C (RFC) to stimulate Poldelta lesion
121 ometry to contain Rfc2 and Rfc3, subunits of replication factor C (RFC), a five subunit protein that
124 and DNA binding by Saccharomyces cerevisiae replication factor C (RFC), and present the first kineti
125 tein A (RFA), the 3' primer binding complex, replication factor C (RFC), and proliferating cell nucle
126 l nuclear antigen (PCNA) and show that PCNA, replication factor C (RFC), and replication protein A (R
127 y the Saccharomyces cerevisiae clamp loader, replication factor C (RFC), and the DNA damage checkpoin
129 When loaded onto primed DNA templates by replication factor C (RFC), PCNA acts to tether the poly
130 the processivity factor PCNA and its loader, replication factor C (RFC), preventing normal fork resta
131 tionation of these crude extracts identified replication factor C (RFC), proliferating cell nuclear a
132 several DNA replication proteins, including replication factor C (RFC), proliferating cell nuclear a
133 on, hLigI interacts with and is inhibited by replication factor C (RFC), the clamp loader complex tha
134 is study, we describe an association between replication factor C (RFC), the clamp loader, and DNA li
136 dogenous and transfected Brd4 interacts with replication factor C (RFC), the conserved five-subunit c
137 utation in RFC4, encoding a small subunit of replication factor C (RFC), was found to display allele-
138 around DNA by the ATP-dependent clamp loader replication factor C (RFC), which acts at single-strande
140 A function, we have designed a new assay for replication factor C (RFC)-catalyzed loading of PCNA ont
141 proliferating cell nuclear antigen (PCNA) in replication factor C (RFC)-catalyzed loading of the clam
142 e-molecule analysis, we demonstrate that the replication factor C (RFC)-CTF18 clamp loader (RFC(CTF18
143 hat Ctf18, Ctf8, and Dcc1, the subunits of a Replication Factor C (RFC)-like complex, are essential f
152 DNA requires the activity of a clamp-loader [replication factor C (RFC)] complex and the energy deriv
153 a nucleotide-bound eukaryotic clamp loader [replication factor C (RFC)] revealed a different and mor
157 ating cell nuclear antigen (PCNA, clamp) and replication factor C (RFC, clamp loader), we have examin
160 CTF7/ECO1, POL30 (PCNA), and CHL12/CTF18 (a replication factor C [RFC] homolog) genetically interact
162 re of the five-protein clamp loader complex (replication factor-C, RFC) of the yeast Saccharomyces ce
163 the structural gene for the large subunit of replication factor C (rfc1), which loads PCNA onto DNA,
164 s two similar small subunits (M. acetivorans replication factor C small subunit (MacRFCS)) and one la
166 lelic intronic AAGGG repeat expansion in the replication factor C subunit 1 (RFC1) gene as the cause
167 repeat sequence motifs are possible in RFC1 (replication factor C subunit 1), encoding the DNA replic
168 ding proteins have been reported previously: replication factor C (the PCNA clamp loader), family B D
169 loaded onto the template-primer junction by replication factor C, the C-terminal domain of PCNA medi
170 this process through a pathway that includes replication factor C, the chromatin assembly factor Asf1
173 a circular substrate without the addition of replication factor C, which is the protein responsible f
174 nterfaces by the ATP-dependent clamp loader, Replication Factor C, whose clamp-interacting sites form
175 loaded onto DNA by a dedicated complex, the replication factor C, whose mechanism has been studied i
177 gammaS), a nonhydrolyzable analog of ATP, to replication factor C with a N-terminal truncation (Delta
178 Our results demonstrate that S. cerevisiae Replication Factor C (yRFC) can load yPCNA onto 5'-ssDNA