ライフサイエンスコーパス: RFC

1 RFC 80A and 5-aminoimidazole-4-carboxamide ribonucleotid

2 RFC does not appreciably destabilize the closed state of

3 RFC is a multipass transmembrane protein.

4 RFC loaded PCNA through two intermediate states on DNA,

5 RFC subunits belong to the AAA(+) superfamily, and their

6 RFC was expressed in mouse Muller cells that had been al

7 RFC, a folate transporter, is a potential receptor for t

8 RFC-C-dependent activation of RFC also enables ptDNA bin

9 inity for the reduced folate carrier type 1 (RFC-1).

10 Eighty-nine (36 cryoballoon and 53 RFC) patients were included in this study.

11 tive enables assessment of individual RFC-A, RFC-B, RFC-C, RFC-D, and RFC-E subunit functions in the

12 M. acetivorans RFC (RFC(Ma)), which represents an intermediate between

13 own that ptDNA entry inside an ATP-activated RFC-PCNA complex accelerates clamp opening and ATP hydro

14 strand, and CMG protects Pol epsilon against RFC inhibition on the leading strand.

15 LG1 distinct from its role as an alternative RFC complex because knockdowns of any other RFC subunits

16 g depends on the Elg1-containing alternative RFC complex, ubiquitination of PCNA, and the checkpoint

17 any other RFC subunits or other alternative RFCs did not affect PCNA monoubiquitination.

18 Thus, hpr-17 defines an RFC-like complex that facilitates telomerase activity in

19 ings assign the uloader role primarily to an RFC-like (RLC) complex, in which the largest RFC subunit

20 e plasma membrane expression of FR-alpha and RFC transporter isoforms without affecting global protei

21 an extended interface between the clamp and RFC.

22 ) that most likely include clamp closing and RFC dissociation.

23 and 182 days (P=0.54) in the cryoballoon and RFC cohorts, respectively.

24 f individual RFC-A, RFC-B, RFC-C, RFC-D, and RFC-E subunit functions in the reaction mechanism.

25 n II (CFII) included pol delta, pol eta, and RFC.

26 plication are common features of FAM111A and RFC, IRF2 is a transcriptional regulator.

27 PI-1 protein and the host IRF2, FAM111A, and RFC complex likely form an interaction network that infl

28 This interaction among ZMP, folates, and RFC, a folate/organic phosphate antiporter, is consisten

29 regulating the interaction between hLigI and RFC, which is required for efficient DNA replication and

30 ndent upon the interaction between hLigI and RFC.

31 h high nitrate concentration but that LR and RFC may better describe bulk conditions in the aquifer.

32 the asymmetric distribution of MutSgamma and RFC-PCNA on meiotic recombination intermediates may driv

33 PCFT and RFC produced comparable increases in pemetrexed activity

34 and of HepG2 cells expressing both PCFT and RFC.

35 variously transported by FRalpha, PCFT, and RFC and, unlike PMX, inhibited de novo purine nucleotide

36 These could be replaced by purified PCNA and RFC to retain full activity.

37 polymerase alpha in the presence of PCNA and RFC.

38 is that requires polymerase delta, PCNA, and RFC and support a role for aRPA in DNA repair.

39 without Msh2-Msh6 (or Msh2-Msh3), PCNA, and RFC but did not require nicking of the substrate, follow

40 oloenzyme complexes that include PCNA123 and RFC.

41 d ATP hydrolysis upon contact with ptDNA and RFC-D Arg-101 serving as a brake that confers specificit

42 Replication-Factor-C (RFC) and RFC-like complexes (RLCs) mediate chromatin engagement o

43 an intermediate between the common archaeal RFC and the eukaryotic RFC, comprises two different smal

44 subunit response to ATP binding decreases as RFC-C>RFC-D>RFC-B, with RFC-A being unnecessary.

45 These findings demonstrate that augmenting RFC functional expression at the BBB could effectively c

46 ables assessment of individual RFC-A, RFC-B, RFC-C, RFC-D, and RFC-E subunit functions in the reactio

47 eaction, particularly at a checkpoint before RFC commits to ATP hydrolysis.

48 lta), loaded PCNA is captured from DNA-bound RFC which subsequently dissociates, leaving behind the h

49 tion assay showed that the PCNA assembled by RFC is functional.

50 CNA is bound by Rad24-RFC than when bound by RFC.

51 es not interact with and is not inhibited by RFC, demonstrating that inhibition of ligation is depend

52 he addition of PCNA alleviates inhibition by RFC.

53 esenting a general model for PCNA loading by RFC in archaea and eukaryotes.

54 Analysis of PCNA opening by RFC revealed a two-step reaction in which RFC binds PCNA

55 DNA polymerase delta that loading of PCNA by RFC targets DNA polymerase delta to the D loop formed by

56 g may relate to the opening of PCNA rings by RFC during the loading reaction.

57 igen (PCNA) loading by replication factor C (RFC) acts as the initial sensor of telomere damage to es

58 ar antigen (PCNA), and replication factor C (RFC) and a reconstituted Mlh1-Pms1-dependent 3' nick-dir

59 actions that contained replication factor C (RFC) and proliferating cell nuclear antigen (PCNA) were

60 The human clamp loader replication factor C (RFC) and sliding clamp proliferating cell nuclear antige

61 Replication factor C (RFC) and the proliferating cell nuclear antigen (PCNA) a

62 The eukaryotic replication factor C (RFC) clamp loader is an AAA+ spiral-shaped heteropentame

63 We find that the replication factor C (RFC) clamp loader specifically inhibits Pol epsilon on t

64 ccharomyces cerevisiae replication factor C (RFC) clamp loader, respectively, and assessed the impact

65 e loaded onto DNA by a replication factor C (RFC) clamp loader.

66 mprises an alternative replication factor C (RFC) complex and plays an important role in preserving g

67 The multi-subunit replication factor C (RFC) complex loads circular proliferating cell nuclear a

68 on between subunits in replication factor C (RFC) from Archaeoglobus fulgidus.

69 vorans clamp loader or replication factor C (RFC) homolog.

70 Replication factor C (RFC) is a five-subunit complex that loads proliferating

71 Replication factor C (RFC) is an AAA+ heteropentamer that couples the energy o

72 al that ATP binding to replication factor C (RFC) is sufficient for loading the heterotrimeric PCNA12

73 Replication factor C (RFC), a heteropentamer of RFC1-5, loads PCNA onto DNA du

74 ccharomyces cerevisiae replication factor C (RFC), and present the first kinetic model of a eukaryoti

75 revisiae clamp loader, replication factor C (RFC), and the DNA damage checkpoint clamp loader, Rad24-

76 de extracts identified replication factor C (RFC), proliferating cell nuclear antigen (PCNA), and pol

77 th and is inhibited by replication factor C (RFC), the clamp loader complex that loads PCNA onto DNA.

78 NA sliding clamp, and, replication factor C (RFC), the clamp loader.

79 lear antigen (PCNA) in replication factor C (RFC)-catalyzed loading of the clamp onto primer template

80 e demonstrate that the replication factor C (RFC)-CTF18 clamp loader (RFC(CTF18)) controls the veloci

81 ll nuclear antigen and replication factor C (RFC).

82 der molecular machine, replication factor C (RFC).

83 r-template junction by replication factor C (RFC).

84 igen (PCNA, clamp) and replication factor C (RFC, clamp loader), we have examined the assembly of the

85 Replication-Factor-C (RFC) and RFC-like complexes (RLCs) mediate chromatin eng

86 ssessment of individual RFC-A, RFC-B, RFC-C, RFC-D, and RFC-E subunit functions in the reaction mecha

87 The reduced folate carrier (RFC) 80A allele and the thymidylate synthase (TS) 3'-unt

88 specificity over the reduced folate carrier (RFC) and inhibition of de novo purine nucleotide biosynt

89 ess PCFT without the reduced folate carrier (RFC) and of HepG2 cells expressing both PCFT and RFC.

90 ed SLC19A1, a feline reduced folate carrier (RFC) and potential receptor for TG35-2-phenotypic virus.

91 s transported by the reduced folate carrier (RFC) and proton-coupled folate transporter (PCFT).

92 The reduced folate carrier (RFC) and the proton-coupled folate transporter (PCFT) ar

93 Reduced folate carrier (RFC) is the major membrane transporter for folates and a

94 iquitously expressed reduced folate carrier (RFC) is the major transport system for folate cofactors

95 The reduced folate carrier (RFC) is the major transport system for folates in mammal

96 ssed FRs but not the reduced folate carrier (RFC) or proton-coupled folate transporter (PCFT).

97 rter (PCFT) over the reduced folate carrier (RFC), 3a was not.

98 at express FR alpha, reduced folate carrier (RFC), and PCFT.

99 by 3 major pathways, reduced folate carrier (RFC), proton-coupled folate transporter (PCFT), and fola

100 The reduced folate carrier (RFC), proton-coupled folate transporter (PCFT), and fola

101 t substrates for the reduced folate carrier (RFC), the major facilitative folate transporter, RFC exp

102 lls that express the reduced folate carrier (RFC).

103 nsporter (PCFT), and reduced folate carrier (RFC).

104 s expressing PCFT or reduced folate carrier (RFC).

105 action catalyzed by Saccharomyces cerevisiae RFC and present a comprehensive kinetic model based on g

106 transient events in Saccharomyces cerevisiae RFC-catalyzed PCNA loading, including ATP-induced RFC ac

107 long-hypothesized structure of an open clamp-RFC complex as an intermediate in loading has remained e

108 on algorithms: Random Forest Classification (RFC) and Support Vector Classification (SVC) with linear

109 gression (LR), random forest classification (RFC), and random forest regression (RFR).

110 DNA binding commits RFC to ATP hydrolysis, which is followed by PCNA closure

111 activation of replication factor C complex (RFC) subunits.

112 n is complex, involving multiple components (RFC, PCNA, DNA, and ATP) and events (minimally: PCNA ope

113 e (IPCC) identified 5 "reasons for concern" (RFCs).

114 co-striatal resting functional connectivity (RFC).

115 Our results suggest that the Ctf18 RFC-like complex modifies telomeric chromatin to make it

116 Ctf18-RFC is an alternative PCNA loader that links all these p

117 Ctf18-RFC loads PCNA with a slight preference for the leading

118 he 'alternative clamp loader' known as Ctf18-RFC acts by an unknown mechanism to activate the checkpo

119 oint signaling or chromosome cohesion, Ctf18-RFC functions in parallel to Chl1 and Mrc1 to protect re

120 rily conserved 'Pol binding module' in Ctf18-RFC that is produced by interaction of the carboxyl term

121 actors," including the multifunctional Ctf18-RFC complex, aid this process in as yet unknown ways.

122 The downstream effector of Ctf18-RFC is cohesin acetylation, which we place toward a late

123 dings indicate that the association of Ctf18-RFC with Pol at defective replication forks is a key ste

124 ored to the leading strand polymerase, Ctf18-RFC can rapidly signal fork stalling to activate the S p

125 Our results suggest that Ctf18-RFC enriches and balances PCNA levels at the replication

126 highlight the specific functions that Ctf18-RFC plays within the leading strand machinery via an int

127 Here, we show that Ctf18-RFC's role in sister chromatid cohesion correlates with

128 the cohesion establishment factor, the Ctf18-RFC (replication factor C) complex.

129 ding at replication forks requires the Ctf18-RFC complex.

130 Here we show that budding yeast Ctf18-RFC associates with DNA polymerase epsilon, via an evolu

131 g cryoballoon versus radiofrequency current (RFC) ablation in patients with drug refractory, symptoma

132 for yeast DNA polymerase delta (Pol delta), RFC and PCNA in LLR repair synthesis.

133 In the presence of purified FEN1, Pol delta, RFC and PCNA, repair occurred on heteroduplexes with loo

134 eplication system in which polymerase delta, RFC, and PCNA were replaced with T4 DNA polymerase and g

135 Also, in addition to polymerase delta, RFC, and PCNA, an as yet unidentified factor(s) is requi

136 Thus, polymerase delta, RFC, PCNA, and the MCM complex, along with the virally e

137 ps between various impacts reflected in each RFC and increases in global mean temperature (GMT) were

138 Either RFC or PCFT cDNA was stably transfected into a transport

139 n the common archaeal RFC and the eukaryotic RFC, comprises two different small subunits (RFCS1 and R

140 Finally, the MutLgamma-MutSgamma-EXO1-RFC-PCNA nuclease ensemble preferentially cleaves DNA wi

141 tion of R1-11-RFC6 HeLa cells, which express RFC without PCFT.

142 y more than C1 or C2 at pH 7.2, which favors RFC transport over PCFT.

143 Binding of ring-open PCNA to all five RFC subunits transforms the free-energy landscape underl

144 ds 2-5 had negligible substrate activity for RFC but showed variably potent (nanomolar) and selective

145 The high affinity of pralatrexate for RFC-1 significantly improves its internalization into ce

146 Dissociation of PCNA.ptDNA from RFC leads to catalytic turnover.

147 t response to ATP binding decreases as RFC-C>RFC-D>RFC-B, with RFC-A being unnecessary.

148 onse to ATP binding decreases as RFC-C>RFC-D>RFC-B, with RFC-A being unnecessary.

149 e show that hChlR1 interacts with the hCtf18-RFC complex, human proliferating cell nuclear antigen, a

150 It remains controversial how RFC and RLCs cooperate to regulate PCNA loading and unlo

151 rast to the inhibitory effect of RFC, hRad17-RFC stimulates joining by DNA ligase I.

152 eracts with the hRad17 subunit of the hRad17-RFC cell cycle checkpoint clamp loader, and with each of

153 Feline and human RFC cDNAs conferred susceptibility to TG35-2-pseudotyped

154 eviously demonstrated the existence of human RFC (hRFC) homo-oligomers and established the importance

155 Here, we report the structure of human RFC bound to PCNA by cryogenic electron microscopy to an

156 pite decades of study, no structure of human RFC has been resolved.

157 es in transmembrane domain (TMD) 11 of human RFC.

158 nt study examines the possibility that human RFC (hRFC) exists as higher order homo-oligomers.

159 ccessful after several failed attempts; (ii) RFC does not act catalytically on a primed 45-mer templa

160 are intramolecular conformational changes in RFC and PCNA that control clamp opening and closure, and

161 al or Ala and mutant constructs expressed in RFC-null HeLa cells.

162 s study, we examined the roles of individual RFC subunits in opening the PCNA clamp.

163 perspective enables assessment of individual RFC-A, RFC-B, RFC-C, RFC-D, and RFC-E subunit functions

164 atalyzed PCNA loading, including ATP-induced RFC activation, PCNA opening, ptDNA binding, ATP hydroly

165 Extracellular ZMP inhibited RFC-mediated folate influx, and the presence of intracel

166 ATP binding to this subunit initiates RFC activation, and the clamp loader adopts a spiral con

167 X, wild-type (wt) RFC was labeled; for K411A RFC, radiolabeling was abolished.

168 > 1 > 4; inhibition was abolished for K411A RFC.

169 For wt and K411A RFCs, inhibitory potencies were in the order 4 > 5 > 1 >

170 RFC-null K562 cells expressing wt and K411A RFCs.

171 Ala, Arg, Gln, Glu, Leu, and Met, only K411E RFC showed substantially decreased transport.

172 ve enhanced activities toward tumors lacking RFC function, reflecting contraction of THF cofactor poo

173 RFC-like (RLC) complex, in which the largest RFC subunit, RFC1, has been replaced with ATAD5 (ELG1 in

174 the sliding clamp PCNA, and the clamp loader RFC slightly increase the processivity of yeast pol eta

175 human enzymes show that PCNA and its loader RFC are sufficient to activate the MutLgamma endonucleas

176 polymerase delta, the PCNA clamp, its loader RFC, and completed by DNA ligase I.

177 Pol delta, together with PCNA and its loader RFC.

178 plication factor C (RFC)-CTF18 clamp loader (RFC(CTF18)) controls the velocity, spacing and restart a

179 study the clamp (PCNA) and the clamp loader (RFC) from the mesophilic archaeon Methanosarcina acetivo

180 The clamp loader (RFC) loads a sliding clamp (PCNA) onto a primer/template

181 PCNA opening locks RFC into an active state, and the resulting RFC.ATP.PCNA

182 For this purpose, we measured RFC in seven thalamic nuclei using fMRI and brain glucos

183 ATP binding to multiple RFC subunits initiates a slow conformational change in t

184 hat is activated in a mismatch-, MutSalpha-, RFC-, PCNA-, and ATP-dependent manner.

185 clamp opening in the presence and absence of RFC allowed us to substantiate the role of RFC in the in

186 n pemetrexed activity even in the absence of RFC, tumor cells are unlikely to become resistant to pem

187 RFC-C-dependent activation of RFC also enables ptDNA binding, leading to the formation

188 udies suggest that the unloading activity of RFC maximizes the utilization of PCNA by inhibiting the

189 s switched off, resulting in low affinity of RFC for DNA and ejection of RFC from the site of PCNA lo

190 The affinity of RFC for PCNA is about an order of magnitude lower in the

191 ivity required the ATP-bound conformation of RFC.

192 Previous considerations of RFC structure and mechanism were based on the notion tha

193 reover, human cells with genomic deletion of RFC were nonpermissive for TG35-2-pseudotyped virus infe

194 In contrast to the inhibitory effect of RFC, hRad17-RFC stimulates joining by DNA ligase I.

195 low affinity of RFC for DNA and ejection of RFC from the site of PCNA loading.

196 a phenomenon intrinsic to the energetics of RFC-mediated folate transport.

197 orted in vitro that functional expression of RFC at the blood-brain barrier (BBB) and its upregulatio

198 The unexpected finding of RFC expression and activity in cultured Muller cells may

199 mplexes and that the nonreplicative forms of RFC are strongly deleterious to cells that have genomewi

200 The importance of RFC subunit response to ATP binding decreases as RFC-C>R

201 e of thiamine pyrophosphate, an inhibitor of RFC.

202 roperties of selective FR targeting, lack of RFC transport, and GARFTase inhibition resulting in pote

203 dissociation was observed in the presence of RFC-loaded PCNA.

204 to a mechanistic explanation for the role of RFC in human health.

205 f RFC allowed us to substantiate the role of RFC in the initial stage of the clamp-loading cycle.

206 The active sites of RFC are fully bound to adenosine 5'-triphosphate (ATP) a

207 about an order magnitude weaker than that of RFC for PCNA, similar to the RFC-PCNA interaction in the

208 cies disassemble through either unloading of RFC.PCNA from DNA or dissociation of PCNA into its compo

209 to progress rapidly without ESCO1, ESCO2, or RFC(CTF18).

210 RFC complex because knockdowns of any other RFC subunits or other alternative RFCs did not affect PC

211 ecarious balance between Rfc1p and the other RFC complexes and that the nonreplicative forms of RFC a

212 antifolate drugs via transport by PCFT over RFC by exploiting the acidic tumor microenvironment.

213 ive chemotherapy drug delivery via PCFT over RFC, a process that takes advantage of a unique biologic

214 mplete selectivity for FRalpha and PCFT over RFC.

215 to selective transport by FRs and PCFT over RFC.

216 analogs were selective for FR and PCFT over RFC.

217 vely] are selective substrates for PCFT over RFC.

218 we show that the ability of PCNA to overcome RFC-mediated inhibition of Cdc9 is dependent upon both t

219 ted system of yeast Rad51, Rad54, RPA, PCNA, RFC, and DNA polymerase delta that loading of PCNA by RF

220 The number of (predominantly RFC) lesions applied during reablation was significantly

221 ed in the presence of the accessory proteins RFC, PCNA and RPA and are consistent with the establishe

222 LigI51A was defective in binding to purified RFC and in associating with RFC in cell extracts.

223 tumor cells including wild-type (WT) and R5 (RFC-null) HeLa cells express high levels of PCFT protein

224 We propose that Rad.RFC may clear PCNA from DNA to facilitate shutdown of re

225 Interestingly, the Rad.RFC DNA damage checkpoint clamp loader unloads PCNA clam

226 The C. elegans Rad17 RFC clamp loader homolog, hpr-17, functions in the same

227 ent of replication protein A, Claspin, Rad17-RFC, and Rad9-Rad1-Hus1 was not detected in these experi

228 s1 (9-1-1) clamp complex together with Rad17-RFC clamp loader.

229 Although Rad24-RFC alone does not bind to naked partial double-stranded

230 lexes are formed when PCNA is bound by Rad24-RFC than when bound by RFC.

231 Ddc2 and loading of the 9-1-1 clamp by Rad24-RFC, but not Rad9 or Mrc1.

232 he DNA damage checkpoint clamp loader, Rad24-RFC, using two separate fluorescence intensity-based ass

233 The affinity of Rad24-RFC for PCNA in the presence of ATP is about an order ma

234 plication protein A) causes binding of Rad24-RFC via interactions with RPA.

235 ponse factor is loaded onto DNA by the Rad24-RFC (replication factor C-like complex with Rad24) clamp

236 tly fewer reconnected PVs, which may reflect RFC catheter instability in certain left atrial regions,

237 activity, but also at neutral pH, reflecting RFC function.

238 RFC into an active state, and the resulting RFC.ATP.PCNA((open)) intermediate is ready for the entry

239 M. acetivorans RFC (RFC(Ma)), which represents an intermediate between the c

240 Conversely, the canonical Rfc1-RFC complex preferentially loads PCNA onto the lagging s

241 lease 1 (Exo1), replication protein A (RPA), RFC, PCNA, and DNA polymerase delta.

242 ture of Msh2-Msh6 (or Msh2-Msh3), Exo1, RPA, RFC-Delta1N, PCNA, and Pol epsilon was found to catalyze

243 ture of Msh2-Msh6 (or Msh2-Msh3), Exo1, RPA, RFC-Delta1N, PCNA, and Pol epsilon was found to catalyze

244 te the SDSA pathway using Rad51, Rad54, RPA, RFC, DNA Polymerase delta with different forms of PCNA.

245 CC authors did not assess whether any single RFC was more important than any other; nor did they conc

246 pecific interactions between S. solfataricus RFC clamp loader and PCNA permit us to superimpose our d

247 The central subunit RFC-C serves as a critical swivel point in the clamp loa

248 , and that ATP binding and hydrolysis switch RFC between conformations with high and low affinities,

249 Unexpectedly, we discovered that RFC can assemble a PCNA ring from monomers in solution.

250 There is little evidence that RFC-mediated influx is posttranscriptionally regulated.

251 and mechanism were based on the notion that RFC monomers were sufficient to mediate transport of fol

252 The RFC subunits are AAA+ family proteins and the complex co

253 lls that lacked FRs but contained either the RFC or PCFT.

254 on a primed 45-mer templated fork; (iii) the RFC.PCNA.DNA complex formed in the presence of ATP is de

255 rent for the large and small subunits in the RFC complex.

256 onnected PVs was significantly higher in the RFC than the cryoballoon group (2.1+/-1.4 versus 1.4+/-1

257 ngthening the biological significance of the RFC complex as a host restriction factor for poxviruses.

258 The pivotal role of the RFC-B/C/D subunit ATPase core in clamp loading is consis

259 d binding of ptDNA leads to formation of the RFC.ATP.PCNA(open).ptDNA complex, which catalyzes a burs

260 DNA binding, leading to the formation of the RFC.ATP.PCNA(open).ptDNA complex.

261 oader), we have examined the assembly of the RFC.PCNA.DNA complex and its progression to holoenzyme u

262 We show that upon clamp opening the RFC/PCNA complex undergoes a large conformational rearra

263 elicase, the Pol epsilon DNA polymerase, the RFC clamp loader, the PCNA sliding clamp, and the RPA si

264 reak-induced telomere synthesis requires the RFC-PCNA-Pol delta axis, but is independent of other can

265 er than that of RFC for PCNA, similar to the RFC-PCNA interaction in the absence of ATP.

266 of poldelta only one species converts to the RFC.PCNA.DNA.poldelta holoenzyme.

267 as selected from a HeLa subline in which the RFC gene was deleted and PCFT was highly overexpressed.

268 functions of individual subunits within the RFC(Ma) complex.

269 scribe revisions of the sensitivities of the RFCs to increases in GMT and a more thorough understandi

270 Functions have been ascribed to RFC subunits previously based on a steady-state analysis

271 e reaction mechanism are that ATP binding to RFC initiates slow activation of the clamp loader, enabl

272 ATP binding to RFC powers recruitment and opening of PCNA and activates

273 uired for high-affinity substrate binding to RFC, whereas the gamma-carboxyl is not essential.

274 PCNA closure severs contact to RFC subunits D and E (RFC2 and RFC5), and the gamma-phos

275 es of this and other antifolates relative to RFC at physiological pH.

276 Activity toward RFC-expressing cells was negligible.

277 , the major facilitative folate transporter, RFC expression may alter drug efficacies by affecting ce

278 Unlike RFC, PCFT is active at acidic pH levels characterizing t

279 e transported into tumor cells primarily via RFC.

280 In vivo, RFC facilitates MutLgamma-dependent crossing over in bud

281 by RFC revealed a two-step reaction in which RFC binds PCNA before opening PCNA rather than capturing

282 is in vitro by yeast pol zeta alone and with RFC, PCNA and RPA.

283 ding to purified RFC and in associating with RFC in cell extracts.

284 binding decreases as RFC-C>RFC-D>RFC-B, with RFC-A being unnecessary.

285 aloyl-l-ornithine (PT523) in comparison with RFC irrespective of the folate growth source.

286 e an open yeast PCNA clamp in a complex with RFC through fluorescence energy transfer experiments.

287 drolysis leads to complex dissociation, with RFC-D activity contributing the most to rapid ptDNA rele

288 Unable to slide away, PCNA re-engages with RFC and is unloaded.

289 g cell nuclear antigen, the interaction with RFC is regulated by hLigI phosphorylation.

290 on negatively regulates the interaction with RFC.

291 ablations were predominantly performed with RFC and resulted in similar acute success, duration of h

292 ver, their actions are subunit-specific with RFC-C Arg-88 serving as an accelerator that enables rapi

293 y than WT cells or R5 cells transfected with RFC.

294 ere used to inhibit [(3)H]MTX transport with RFC-null K562 cells expressing wt and K411A RFCs.

295 greater in patients originally treated with RFC (3.3+/-1.3 versus 2.5+/-1.5; P=0.015) with no differ

296 , 2, and 4 were used to covalently modify wt RFC, inhibitory potencies were in the order 2 > 1 > 4; i

297 labeling with NHS-[(3)H]MTX, wild-type (wt) RFC was labeled; for K411A RFC, radiolabeling was abolis

298 rimpose our data upon the structure of yeast RFC-PCNA complex, thereby presenting a general model for

299 re has many similarities to a previous yeast RFC:PCNA crystal structure, suggesting that eukaryotic c

300 unctionally homologous human proteins, yeast RFC interacts with and inhibits Cdc9 DNA ligase whereas