ライフサイエンスコーパス: dCTP

1 dCTP was both a substrate (apparent K(m) = 0.4 mm) and c

2 aeal enzyme specifically recognizes dCTP; 2) dCTP deamination and dUTP diphosphatase activities occur

3 3'-dCTP inhibited the elongation of nascent negative-strand

4 ion with similar efficiency compared with 3'-dCTP under the reaction conditions.

5 potency of NS5B inhibition compared with 3'-dCTP.

6 -positive bacteria and their phages, and (3) dCTP/dUTPases in enterobacterial T4-like phages.

7 ha,4 alpha-diaza-s-indacene (Bodipy)-FL-510, dCTP-PC-Bodipy-650, and dUTP-PC-6-carboxy-X-rhodamine (R

8 In the Dpo4.DNA-dG(1,8).dCTP ternary structure, the aminopyrene moiety of the dG

9 nucleotide biosynthesis using two enzymes: a dCTP deaminase catalyzes the formation of dUTP and a dUT

10 incorrect bases vary from 0.0031 s(-1) for a dCTP:C mispair to 1.16 s(-1) for a dGTP:T mispair.

11 dATP:A mispair to a high of 360 microM for a dCTP:T mispair.

12 that although yeast Rev1 could incorporate a dCTP opposite the cross-linked guanine, no evidence was

13 These first structures of a dCTP deaminase reveal a probable role for an unstructure

14 dines, including two transition mismatches A-dCTP and G-dTTP.

15 non-cognate incoming nucleotides including A:dCTP, A:dGTP, A(syn):dGTP, A:dATP, A(syn):dATP, T:dCTP,

16 dGTP<A(syn):dATP<T:dCTP<A:dGTP<A(syn):dGTP<A:dCTP<A:dATP.

17 and absence of substrates and the activator dCTP.

18 uction is diminished by a mutation affecting dCTP deaminase, Escherichia coli is known to use an alte

19 trations and was kinetically slower with all dCTP analogues tested.

20 Although dCTP deaminase and dUTPase activities are usually found

21 e X-ray structures revealed that (1) CTP and dCTP bind in a very similar fashion, (2) UTP, in the pre

22 complexes for the Y567A mutant with dATP and dCTP opposite a templating 8-oxoG in a 13/18mer primer-t

23 re and after the chemical step with dATP and dCTP opposite an 8-oxoG template started from partially

24 ctor, activating the degradation of dATP and dCTP with dGTP also being consumed in the reaction with

25 e hydrolyzed all rNTPs efficiently, dATP and dCTP with moderate efficiency, while it showed less hydr

26 d competing endogenous nucleotides (dATP and dCTP) in 47 healthy women.

27 ame active site is involved in both dCMP and dCTP deaminations.

28 )-dG adduct opposite incoming dGTP, dTTP and dCTP nucleotides, as well as unmodified guanine opposite

29 , encoding nucleoside diphosphate kinase and dCTP deaminase, respectively, had a strongly suppressive

30 P concentration increased 2-fold normal, and dCTP and dGTP concentrations rose less than 1-fold norma

31 ation increased more than 4-fold normal, and dCTP, dGTP, and dATP concentrations rose 1-2 times norma

32 hows diminished "bursts" for dATP:8-oxoG and dCTP:8-oxoG incorporation, indicative of non-productive

33 within the ternary complex of polymerase and dCTP.

34 cleotides during DNA synthesis when rCTP and dCTP are at equimolar concentration.

35 Bodipy-FL-510, dUTP-PC-R6G, dATP-PC-ROX, and dCTP-PC-Bodipy-650) (PC, photocleavable; Bodipy, 4,4-dif

36 low motion, in contrast to the 8-oxoG (anti):dCTP system.

37 uctures, both Watson-Crick (anti-8-oxoG:anti-dCTP) and Hoogsteen (syn-8-oxoG:anti-dATP) base pairing

38 d L-dCTP analogs activated dCMP deaminase as dCTP.

39 lowed because only one hydrogen bond between dCTP and the (+)-trans-anti-[BP]-N(2)-dG residue evolved

40 t exhibits an unusual preference for binding dCTP opposite a templating adenine over the cognate dTTP

41 All of these adducts strongly blocked dCTP incorporation opposite the adducts.

42 Both dCTP and dTTP base paired with the Hoogsteen edge of O(6

43 ere less for O(6)-BzG than O(6)-MeG for both dCTP and dTTP insertion.

44 ii has an enzyme, DCD-DUT, that harbors both dCTP deaminase and dUTP pyrophosphatase activities.

45 ase beta, which is known to incorporate both dCTP (no mutation) and dATP (G-->T substitution) opposit

46 kinetic parameters for the addition of both dCTP and dCDP onto a 13/20mer primer/template with an ex

47 In the BrG.dCTP ternary structure, BrG adopts anti conformation and

48 dCMP deaminase activity that is activated by dCTP and inhibited by dTTP.

49 being allosterically regulated, activated by dCTP, and inhibited by dTTP.

50 ntitatively efficient of these in catalyzing dCTP incorporation opposite bulky guanine N(2)-adducts,

51 The complementary dCTP is preferentially inserted opposite G* in all of th

52 se beta's conformational closing for correct dCTP versus incorrect dATP incoming nucleotide opposite

53 ound that Pol eta binds the incoming correct dCTP opposite both G and 8-oxoG with similar affinities,

54 tightly with DNA in the presence of correct dCTP, but the adduct weakens binding with no nucleotide

55 The addition of either a correct (dCTP) or incorrect nucleotides showed only minor differe

56 inds at a site that does not overlap the CTP/dCTP site, and (3) the triphosphates of the two nucleoti

57 Similar values of K(d(dCTP)) and K(d(DNA)) and k(off) rates of DNA substrates

58 The measured K(d)(,dCTP) was 15-fold lower for an oligonucleotide containin

59 rototype Y-family DNA polymerase, DNA, and D-dCTP, D-dCDP, L-dCDP, or the diphosphates and triphospha

60 nonical ternary structure of Pollambda-DNA-D-dCTP, L-dCTP, (-)3TC-TP, and (-)FTC-TP all have their ri

61 These structures reveal that relative to D-dCTP, each of these L-nucleotides has its sugar ring rot

62 lative to D-deoxycytidine 5'-triphosphate (D-dCTP) in the canonical ternary structure of Pollambda-DN

63 res of polbeta complexed with dG*dTTP and dA*dCTP mismatches in the presence of Mg2+ or Mn2+.

64 und ground-state structures show that the dA*dCTP-Mg2+ complex adopts an 'intermediate' protein confo

65 mplex is structurally very similar to the dA*dCTP-Mg2+ complex, whereas the dG*dTTP-Mn2+ complex unde

66 chemistry-state' structures show that the dA*dCTP-Mn2+ complex is structurally very similar to the dA

67 crystal structure of the variant bound to dA:dCTP, the fingers domain closes around the mismatched ba

68 s show that Arg-363 is responsible for dATP, dCTP, and dGTP hydrolysis, whereas Arg-504 and Ser-319 c

69 With ddCTP, dCTP, and dATP the phosphodiester bonds were formed even

70 N2-AnthG decreased dCTP binding affinity (2.6-fold) and increased DNA subst

71 Pol X prebinds MgdCTP weakly, the correct dG:dCTP ternary complex is readily formed in the presence o

72 dG:dGTP ternary complex formation but not dG:dCTP ternary complex formation.

73 at the differences in incorporation of dGTP, dCTP, and dTTP are due to the effects of imperfect geome

74 as well as dNMPs were also formed with dGTP, dCTP, or dTTP.

75 es of nucleotides, including dGTP/dATP, dGTP/dCTP, dGTP/dTTP, and dGTP/dUTP.

76 The X-ray crystal structure of the Rev1p-DNA-dCTP ternary complex showed that Rev1p utilizes an unusu

77 ter thymidine (dT)-induced inhibition of DNP dCTP synthesis by switching to NSP-mediated dCTP product

78 template base opposite to the incoming dNTP (dCTP, dATP, dGTP) is oxoG.

79 y use of selected (13)C/(15)N-labeled dNTPs (dCTPs) in PCR amplification of the target region in tand

80 ed and used as substitutes for natural dTTP, dCTP, dATP, and dGTP in PCR.

81 bda did not modulate a preference for either dCTP or dATP when opposite 8-oxodG in single-nucleotide

82 ectively, the results indicate that elevated dCTP and dTTP pools increase mismatch formation and decr

83 deficient diploid yeast strain with elevated dCTP and dTTP concentrations.

84 evidence that hUGDH and the unrelated enzyme dCTP deaminase have converged to very similar atypical a

85 n bonds were observed in the N(2),3-epsilonG:dCTP base pair, whereas only one appears to be present i

86 between different DPs and deoxy-NTPs, except dCTP.

87 stal structures explain the slightly favored dCTP insertion for pol iota in steady-state kinetic anal

88 on (PCR), using incorporation of fluorescent dCTP and detection via electrophoresis.

89 uboptimal for catalysis in the polbeta-Fm7dG:dCTP complex, which partially explains the slow insertio

90 The E(a) for dCTP insertion opposite 8-oxoG was lower than for opposi

91 sertion opposite the O(6)-alkylG adducts for dCTP and dTTP with pol eta and kappa; pol iota showed a

92 is archaeal enzyme has a higher affinity for dCTP and its steady-state turnover is faster than the ba

93 the PBCV-1 enzyme has a higher affinity for dCTP than for dCMP, (ii) dCTP serves as a positive heter

94 ing the alpha-thiotriphosphate analogues for dCTP and dGTP, respectively, suggest that phosphoryl tra

95 To reveal a structural basis for dCTP incorporation opposite dG(1,8), we solved the cryst

96 a showed pre-steady-state kinetic bursts for dCTP incorporation opposite G and O(6)-MeG but little, i

97 t identical to that previously described for dCTP, protonation of N3 in deoxythymidine and not deoxyc

98 r and has similar insertion efficiencies for dCTP and dATP.

99 lts in an increased enzymatic efficiency for dCTP insertion and makes formation of a Hoogsteen pair b

100 s showed moderately rapid burst kinetics for dCTP incorporations, even opposite the bulky methyl(9-an

101 tic analysis showed decreases of kcat/Km for dCTP insertion opposite N2-G adducts according to size,

102 howed a decrease of 10(3) in k(cat)/K(m) for dCTP incorporation opposite N(2)-MeG and a further large

103 :T to 1 error in 2.3 x 10(6) nucleotides for dCTP:C.

104 teady-state kinetic bursts were observed for dCTP incorporation throughout the series (N2-MeG to N2-A

105 ically, we determined kinetic parameters for dCTP insertion opposite a chemically stable m7dG analogu

106 havior, steady-state kinetic parameters (for dCTP), and PCR performance.

107 All complexes are well poised for dCTP insertion.

108 rate constant describing polymerization, for dCTP incorporation opposite O6-MeG was approximately 6-f

109 tion for dATP or dTTP incorporation than for dCTP or dGTP into complementary, homopolymeric DNA templ

110 m) values approximately 10(-3) less than for dCTP with all adducts; a similar differential was found

111 rase beta (pol beta) discriminates dATP from dCTP when processing 8-oxoguanine (8-oxoG), we analyze a

112 re fidelity is highest, k(pol) for correct G-dCTP incorporation by Pol nu is ~15-fold faster than k(p

113 TGA sequence, while stacking for anti-Fapy.G:dCTP pairs was similar in the two sequences.

114 uence, whereas stacking for the anti-8-oxo-G:dCTP pair was similar in both 5'-TGT and 5'-TGA sequence

115 These structures with G:dCTP following either 8-oxoG:C or 8-oxoG:A pairs exhibit

116 pectedly, however, the viral enzyme also has dCTP deaminase activity, producing dUTP.

117 Helicase-R504A hydrolyzes dCTP far better than wild-type helicase, and the hydroly

118 -nitro-dATP, 7-deaza-7-nitro-dGTP, 5-hydroxy-dCTP, and 5-hydroxy-dUTP, which have increased chemical

119 e metabolism in leukemic cells, and identify dCTP biosynthesis as a potential new therapeutic target

120 higher affinity for dCTP than for dCMP, (ii) dCTP serves as a positive heterotropic effector for the

121 showed proportional decreases of kcat/Km in dCTP insertion opposite N2-AnthG and N2-BPG (73 and 320-

122 functional group on C4 (O in dTTP and NH2 in dCTP) makes interactions with nonconserved protein resid

123 However, the role of the NSP in dCTP production and DNA synthesis in cancer cells is cur

124 The metabolic switch in dCTP production triggered by DNP inhibition is accompani

125 is dependent on both substrates: an incoming dCTP and a templating base dG.

126 rnary structures of polbeta with an incoming dCTP or dTTP analogue base-paired with O6MeG in the pres

127 in the Dpo4 active site opposite an incoming dCTP, using molecular modeling and molecular dynamics si

128 Template G and incoming dCTP do not pair with each other.

129 coming dTTP and with template G and incoming dCTP have revealed that in the Pol iota active site, the

130 6)-methylG as the template base and incoming dCTP or dTTP were solved and showed that O(6)-methylG is

131 ternary hpol eta-DNA complexes and incoming dCTP, dATP, or dGTP opposite 8-oxoG reveal that an argin

132 Also, unlike other DNA polymerases, incoming dCTP pairs with an arginine rather than the templating b

133 Watson-Crick base pairing with the incoming dCTP analog.

134 The incoming dCTP likely skips the first available template base and

135 e, (ii) the O5' and C5 atoms of the incoming dCTP, and (iii) the OH group of S565 and the aromatic fa

136 with the primer terminus dC and the incoming dCTP, providing the structural basis for the accurate by

137 the adducted template base and the incoming dCTP.

138 g-324 forms hydrogen bonds with the incoming dCTP.

139 th the templating Fm7dG paired with incoming dCTP or dTTP analogues.

140 Ternary complexes with incoming dCTP resemble the wild-type enzyme, with templating anti

141 aphthyl-Tyr115 RT inefficiently incorporated dCTP at low concentrations and was kinetically slower wi

142 polymerase beta preferentially incorporated dCTP over dATP, DNA polymerase lambda did not modulate a

143 Aminomethyl-Phe115 RT incorporated dCTP more efficiently than the WT and was resistant to t

144 n pocket, with Dpo4 capable of incorporating dCTP, dTTP or dATP opposite the adduct reasonably well.

145 ternary structures of polbeta incorporating dCTP opposite the templating Pt-GG lesion in the presenc

146 In the presence of an increased dCTP pool resulting from the loss of nucleotide diphosph

147 dCMP deaminase gene (SPBC2G2.13c) increases dCTP approximately 30-fold and decreases dTTP approximat

148 formed in the presence of indodicarbocyanine-dCTP and another pair of degenerate primers also broadly

149 tant, while only dCDP but not rCDP inhibited dCTP incorporation by the parental enzyme and the Y416F

150 also found that both dCDP and rCDP inhibited dCTP incorporation by the Y416A mutant, while only dCDP

151 endonuclease was used to assess initiation, dCTP incorporation by DNA polymerase (pol) beta was used

152 cisplatin lesions requires Pol eta to insert dCTP opposite the 3' guanine and Pol zeta4 to extend the

153 eas DNA Pol 1(KF(-)) preferentially inserted dCTP.

154 HIV-1 RT inserted dCTP and dTTP with approximately equal frequencies oppos

155 irected mechanism to preferentially instruct dCTP incorporation.

156 Intriguingly, dCTP pool depletion, RS, and hematopoietic defects induc

157 None of the D- and L-dCTP analogs activated dCMP deaminase as dCTP.

158 ry crystal structures of hPolbeta, DNA and L-dCTP or the triphosphate forms of antiviral drugs lamivu

159 ternary structure of Pollambda-DNA-D-dCTP, L-dCTP, (-)3TC-TP, and (-)FTC-TP all have their ribose rot

160 DNA, and L-deoxycytidine 5'-triphosphate (L-dCTP), or the triphosphates of lamivudine ((-)3TC-TP) an

161 cilitates efficient incorporation of matched dCTP or mismatched dATP.

162 in stable Hoogsteen base pairing with 1-MeA, dCTP fails to gain a "foothold" and is largely disordere

163 dCTP synthesis by switching to NSP-mediated dCTP production.

164 g inducer of RS in vivo through TK1-mediated dCTP pool depletion.

165 tT also catalyzes the hydrolysis of 5-methyl-dCTP.

166 revealed that it was able to misincorporate dCTP opposite template C and dGTP opposite template G wi

167 Intriguingly, the mismatched dCTP has an affinity similar to that of the matched nucl

168 on, and post-PCR incorporation of a modified dCTP, the latter of which allows resolution of amplicons

169 Moreover, dCTP forms a Watson-Crick base pair with dG, two nucleot

170 easing the enzyme's affinity for the natural dCTP substrate but increasing its affinity for 3TC-triph

171 steady-state analysis indicates that neither dCTP nor dTTP insertion is strongly preferred during pol

172 arts of the substrates lacked dCMP; thus, no dCTP was required for leading-strand synthesis and no dG

173 In contrast to the noncognate dCTP, neither the cognate dTTP nor its nonhydrolyzable a

174 ibose of AraCTP is similar to that of normal dCTP, the conformation of dFdCTP is significantly differ

175 facilitate hydrogen bonding of dTTP but not dCTP and may result in a higher affinity of dTTP to the

176 econd gene, at locus MJ0430, encodes a novel dCTP deaminase that releases dUMP, ammonia, and pyrophos

177 nt for incorporation of a normal nucleotide (dCTP) is determined solely by the rate of binding (inclu

178 und structures reveal that, whereas the O6Me.dCTP-Mn(2+) complex assumes the similar altered conforma

179 +)-bound structures show that both the O6MeG.dCTP/dTTP-Mg(2+) complexes adopt an open protein conform

180 dZTP opposite template dG in the absence of dCTP.

181 ility that was relaxed only upon addition of dCTP, which forms a Watson-Crick base pair with template

182 Protonation of the N3 atom of dCTP and bifurcation of the N3 hydrogen between the N7 a

183 The inhibitor blocks binding of dCTP by docking at the Pol alpha active site and by rota

184 ntrast, for the wild-type enzyme, binding of dCTP induces an allosteric effect that affects the subun

185 nearly equal affinities, but the binding of dCTP never reaches equilibrium.

186 cally as the first step in the conversion of dCTP to dTTP.

187 ntermediates are generated by deamination of dCTP, either spontaneously or enzymatically as the first

188 d 90-fold higher incorporation efficiency of dCTP > dATP opposite 8-oxoG and 4-fold higher efficiency

189 ly contribute to the increased efficiency of dCTP incorporation.

190 ed that the high incorporation efficiency of dCTP is dependent on both substrates: an incoming dCTP a

191 n, although, the incorporation efficiency of dCTP opposite the first and second cross-linked guanine

192 First, Dbh shows a bias in favor of dCTP, such that the rate of incorporation of dCTP opposi

193 an wild-type helicase, and the hydrolysis of dCTP fuels unwinding of DNA.

194 eventing dUTP production via inactivation of dCTP deaminase.

195 d DNA primers showed >/=95% incorporation of dCTP > dATP opposite 8-oxoG.

196 er activity than Dbh on the incorporation of dCTP (correct) and dATP (incorrect) opposite the G (norm

197 er efficiency in pol beta's incorporation of dCTP compared with G by affecting the requisite active-s

198 duct strongly coded for the incorporation of dCTP during trans lesion DNA replication, both in Escher

199 dCTP, such that the rate of incorporation of dCTP opposite a template G is about 10-fold faster than

200 ow that the near error-free incorporation of dCTP opposite the major benzo[a]pyrene-derived dG lesion

201 ing base, which ensures the incorporation of dCTP over other incoming nucleotides.

202 conformation may facilitate incorporation of dCTP via Hoogsteen-type templating with deoxyinosine, th

203 fold higher efficiency than incorporation of dCTP.

204 T(m) and strongly inhibited incorporation of dCTP.

205 rase IV (Dpo4), for the correct insertion of dCTP opposite 8-oxoguanine using the quantum mechanics/m

206 ytic efficiency (k(cat)/Km) for insertion of dCTP opposite a series of N2-alkylguanine templates of i

207 hotspot, the rate of frameshift insertion of dCTP opposite a template G that is one residue 5' to the

208 ich partially explains the slow insertion of dCTP opposite Fm7dG by polbeta.

209 , k(cat)/K(m)) were similar for insertion of dCTP opposite the lesions and for extension beyond the N

210 iclosed conformation during the insertion of dCTP opposite the templating Pt-GG, explaining the ineff

211 For pol beta, the insertion of dCTP was preferred opposite the dG-FAF adduct in a singl

212 y-state kinetics, we found that insertion of dCTP was the least favored insertion product opposite th

213 te guanine is comparable to the insertion of dCTP, while the insertion opposite adenine is only appro

214 BPG when alpha-thio-dCTP was used instead of dCTP, implying rate-limiting phosphodiester bond formati

215 ydro-8-oxodeoxyguanosine (8-oxoG) instead of dCTP, to the extent of >90% with some polymerases.

216 Increased levels of dCTP diminish the effective levels of gemcitabine throug

217 was due to the preferred misincorporation of dCTP with templating bases dA, dT, and dC over correct d

218 ication forks by depleting cellular pools of dCTP, induces a novel DNA damage response that, uniquely

219 similar fashion, (2) UTP, in the presence of dCTP or CTP, binds at a site that does not overlap the C

220 emplates is also stronger in the presence of dCTP.

221 dG(1,8) lesion in the absence or presence of dCTP.

222 steady-state kinetics showed faster rates of dCTP incorporation opposite 8-oxoG than G.

223 the preferential use of dATP and the use of dCTP, a nucleotide not normally used.

224 lowering the dCTP concentration, by omitting dCTP altogether, by adding ddCTP, or with a single abasi

225 DCD-DUT has highest activity on dCTP, followed by dUTP, and dTTP inhibits both the deami

226 both the structures with O(6)- MeG opposite dCTP and dC display sheared configuration of base pairs

227 n the anti conformation when paired opposite dCTP, but it flips to a syn conformation forming a Hoogs

228 vity was stimulated when either ATP, CTP, or dCTP was provided to the extract, an unusual observation

229 eta with an incoming nonhydrolyzable dGTP or dCTP analog paired with templating BrG.

230 addition of dATP or dGTP, but not of dTTP or dCTP.

231 bound to template 1-MeA and incoming dTTP or dCTP.

232 ntrast, the structure of the ternary 8-oxodG:dCTP complex is almost identical to the replicating comp

233 polymerase-gamma activity measured by (32)P-dCTP incorporation into a single-nucleotide gap oligonuc

234 3+/+ cells more efficiently stimulated (32)P-dCTP incorporation into a uracil-oligonucleotide.

235 to either cell doubling time or alpha (32)P-dCTP incorporation was increased in patients with thymid

236 sum sativum) root tips incubated with [(32)P]dCTP during a 1-h period when no cell death occurs yield

237 rporated a significant amount of alpha[(32)P]dCTP in DNA that contained HNE-dG adducts by comparison

238 ith template guanine and Watson-Crick paired dCTP as the nascent base pair.

239 modified guanine opposite its normal partner dCTP as a control, to compare with our previous simulati

240 However, with the normal partner dCTP, the anti conformation with close to Watson-Crick a

241 within the active site of T7 DNA polymerase, dCTP fit poorly opposite the adduct, adopting an orienta

242 Rather, dCTP and 3TC-TP bind with nearly equal affinities, but t

243 the archaeal enzyme specifically recognizes dCTP; 2) dCTP deamination and dUTP diphosphatase activit

244 ive site almost identically to the substrate dCTP, providing a structural basis for Pol gamma-mediate

245 olymerase bound to gapped DNA and substrate, dCTP) forms; these different states have long been used

246 on of transversions resulting from T.dTTP, T.dCTP, and C.dTTP mispairs.

247 A:dGTP, A(syn):dGTP, A:dATP, A(syn):dATP, T:dCTP, and T:dGTP to study the structure-function relatio

248 m insertions by pol mu: T:dGTP<A(syn):dATP<T:dCTP<A:dGTP<A(syn):dGTP<A:dCTP<A:dATP.

249 orated with a 432-fold lower efficiency than dCTP.

250 that do occur are 2-fold more efficient than dCTP:G insertion events.

251 ite 7dG than dG and only slightly lower than dCTP incorporation opposite either 7dG or dG.

252 lso revealed relatively low fidelity in that dCTP would be incorporated only 90% of the time.

253 Steady-state kinetics revealed that dCTP incorporation is preferred opposite N(2),3-epsilonG

254 The dCTP insertion efficiencies, f(ins) = (V(max)/K(m))(ins)

255 The dCTP pool shrank by about 50%, and the dATP pool was ess

256 The dCTP pyrophosphatase 1 (dCTPase) is a nucleotide pool "h

257 The dCTP pyrophosphatase 1 (dCTPase) is involved in the regu

258 The dCTP: (+)-trans-anti-[BP]-N(2)-dG system had the least n

259 Among the dCTP and TTP analogs examined, D- and L-FMAUTP were the

260 this inhibitor binds to the same site as the dCTP activator.

261 y and a positive homotropic effector for the dCTP deaminase activity, and (iii) the enzymatic efficie

262 s hydrogen bond was directly across from the dCTP glycosidic bond.

263 ing lagging-strand synthesis by lowering the dCTP concentration, by omitting dCTP altogether, by addi

264 ted, and these rates were independent of the dCTP concentration.

265 is about four times higher than that of the dCTP deaminase activity.

266 Rotation about the glycosidic bond of the dCTP residue to this abnormal position was allowed becau

267 mal controls, whereas during quiescence, the dCTP and dGTP pools decrease to 50% of the control.

268 and dGTP pools to expand significantly, the dCTP pool to drop significantly, and the dATP pool to dr

269 tion with 6-Cl-2APTP, 2-thio-dTTP, or 2-thio-dCTP, the nanocircuit uncovered an alternative conformat

270 were abolished opposite BPG when alpha-thio-dCTP was used instead of dCTP, implying rate-limiting ph

271 Large elemental effects with thio-dCTP(alphaS) were observed with N(2)-EtG (6- and 72-fold

272 eimidazolinone (MBI) labels were attached to dCTP through a propargyl linker, and the resulting label

273 e beta barrel core that likely contribute to dCTP specificity and deamination.

274 ve, proposed to be 3'-keto-deoxycytidine, to dCTP and a small amount of cytosine.

275 (EC90) ratios of TFVdp to dATP and FTCtp to dCTP (alone and in combination) for protection against H

276 s of pol iota with N(2),3-epsilonG paired to dCTP and dTTP revealed Hoogsteen-like base pairing mecha

277 intramitochondrial pool of dTTP relative to dCTP in cells from patients with TK2 deficiency and TWIN

278 imer but with reduced efficiency relative to dCTP.

279 pairing (G:C), was saturable with respect to dCTP concentration, and occurred in the absence of phosp

280 with correct deoxycytidine 5'-triphosphate (dCTP) and its syn-conformation forming a Hoogsteen base

281 d incoming 2'-deoxycytidine 5'-triphosphate (dCTP), which reveals that the polymerase itself dictates

282 Deoxycytidine (dC) triphosphate (dCTP) can be produced both by the de novo pathway (DNP)

283 in mice depletes deoxycytidine triphosphate (dCTP) pools and induces RS, early S-phase arrest, and DN

284 rinsic levels of deoxycytidine triphosphate (dCTP).

285 a model that explains how TK1 and dCK "tune" dCTP pools to both trigger and resolve RS in vivo.

286 viously characterized Salmonella typhimurium dCTP deaminase in its reaction products, this archaeal e

287 des with automated docking experiments using dCTP, dUTP, and dTTP.

288 d by GTP, dATP, or dGTP but not by CTP, UTP, dCTP, or dTTP.

289 ation but pairs differently with dTTP versus dCTP.

290 e relative k(pol)/K(d) for incorporation was dCTP > araCTP, dFdCTP >> rCTP.

291 ith DNA containing an abasic lesion and with dCTP as the incoming nucleotide.

292 F-dG to be Watson-Crick hydrogen-bonded with dCTP with modest polymerase perturbation, but other nucl

293 2A and structures of DCD-DUT in complex with dCTP and dUTP to resolutions of 1.77A and 2.10A, respect

294 omplex containing a template-primer DNA with dCTP opposite the 10-mer peptide DPC revealed that this

295 catalytic efficiency for these events (with dCTP or C) was similar for G and 8-oxoG templates.

296 ethylG allow base pairing of the lesion with dCTP.

297 orms a canonical Watson-Crick base pair with dCTP, but metal ion coordination is suboptimal for catal

298 ormation and forming Watson-Crick pairs with dCTP or dC.

299 was followed by extension of the primer with dCTP-PC-Bodipy-650 and the subsequent detection of the f

300 e.g., T x dGTP) than for its complement (A x dCTP).

301 d greatly increased the rate of all three 'X-dCTP' mispairs, which Polzeta4 alone made extremely inef