ライフサイエンスコーパス: uracil-DNA glycosylase

1 6 exonuclease) and DNA repair enzymes (e.g., uracil-DNA glycosylase).

2 deaminase and generation of abasic sites by uracil DNA glycosylase.

3 omolog 2/MutS homolog 6 heterodimers and for uracil DNA glycosylase.

4 repair enzymes such as T4 endonuclease V and uracil DNA glycosylase.

5 a backup role to the more efficient general uracil DNA glycosylase.

6 by inhibition of the DNA repair enzyme human uracil DNA glycosylase.

7 NdU) is a nanomolar competitive inhibitor of uracil DNA glycosylase.

8 nary divergence of TDG and mismatch-specific uracil DNA-glycosylase.

9 utagenesis is increased upon inactivation of uracil-DNA glycosylase.

10 combination, but only in a strain possessing uracil-DNA glycosylase.

11 nduced cytosine deaminase and its removal by uracil-DNA glycosylase.

12 se loss produced by the excision activity of uracil-DNA glycosylase.

13 removal of the uracil base by the action of uracil-DNA glycosylase.

14 d that human cells contain multiple forms of uracil-DNA glycosylase.

15 kinase, an alkaline endo-exonuclease, and a uracil-DNA glycosylase.

16 ith a single G/U located at position 21 with uracil-DNA glycosylase.

17 nations were reduced, but not eliminated, by uracil-DNA glycosylase.

18 ious reports with Escherichia coli mispaired uracil-DNA glycosylase.

19 has led to the isolation of a new family of uracil-DNA glycosylases.

20 d inhibitory effects, we observed that human uracil-DNA glycosylase 1 (UNG1) and AP endonuclease I (A

21 ells can be selectively killed by inhibiting uracil DNA glycosylase 2 (UNG) and that this synthetic l

22 posite to that observed in mice deficient in uracil DNA glycosylase 2 (UNG2)(7), which suggests that

23 gase to induce the proteasome degradation of Uracil DNA glycosylase 2 (UNG2), a pivotal enzyme of the

24 In a pull-down assay, uracil DNA glycosylase 2 (UNG2), an important enzyme in

25 One host protein, uracil DNA glycosylase 2 (UNG2), binds to multiple viral

26 One of the identified proteins was uracil DNA glycosylase 2 (UNG2).

27 rate adaptor to ubiquitinate and degrade the uracil-DNA glycosylase 2 (UNG2) base excision repair fac

28 ith several host cellular proteins including uracil DNA glycosylase-2 (UNG2) and a cullin-RING E3 ubi

29 degradation of nascent viral DNA mediated by uracil DNA glycosylases-2 (UNG2) and apurinic/apyrimidin

30 We examined the role of the viral uracil DNA glycosylase, a protein conserved among all he

31 Although these mutations abolished uracil DNA glycosylase activity, they did not prevent vi

32 g the transcription factor to interfere with uracil DNA glycosylase activity.

33 of transitions, which may relate to reduced uracil DNA-glycosylase activity, suggest a role for AICD

34 t a role for AICDA in regulating POL eta and uracil DNA-glycosylase activity.

35 as extensively purified and found to possess uracil-DNA glycosylase activity and was identified as th

36 he E. coli Ndk polypeptide lacked detectable uracil-DNA glycosylase activity and, hence, was incapabl

37 Repair was largely dependent on uracil-DNA glycosylase activity because addition of the

38 A complementary uracil-DNA glycosylase activity detected in ung(-/-) mur

39 was based on the following observations: (i) uracil-DNA glycosylase activity did not copurify with Nd

40 li Ndk polypeptide does not possess inherent uracil-DNA glycosylase activity.

41 hin the superfamily studied thus far exhibit uracil-DNA glycosylase activity.

42 om E. coli ung(-) cells showed no detectable uracil-DNA glycosylase activity; and (iii) Ndk failed to

43 With the exception of uracil DNA glycosylase all the glycosylases tested bind

44 Deficiency in UNG uracil-DNA glycosylase alone is sufficient to distort th

45 f CPDs, followed by cleavage of the DNA with uracil DNA glycosylase, an AP lyase activity, and ligati

46 lycosylase inhibitor protein (Ugi)-sensitive uracil-DNA glycosylase, an apurinic/apyrimidiniclyase, a

47 Uracils in DNA can be recognized by uracil DNA glycosylase and abasic endonuclease to produc

48 cognized by the base excision repair protein uracil DNA glycosylase and by the mismatch repair protei

49 s transposon-based library construction with uracil DNA glycosylase and endonuclease VIII to specific

50 the scaffold was enzymatically removed with uracil DNA glycosylase and exonuclease III.

51 e, UL114, whose product is homologous to the uracil DNA glycosylase and is highly conserved in all he

52 BER activity was stimulated by addition of uracil DNA glycosylase and polymerase gamma.

53 hosphorylase, phosphoribosyltransferases, or uracil DNA glycosylase and thus represents a novel archi

54 created by AID/APOBEC enzymes, here we used uracil-DNA glycosylase and an alkoxyamine to covalently

55 amine distinct steps of BER, DNA cleavage by uracil-DNA glycosylase and Ape1 endonuclease was used to

56 Subsequent to actions of uracil-DNA glycosylase and apurinic/apyrimidinic endonuc

57 us, and the VACV D4 protein serves both as a uracil-DNA glycosylase and as an essential component req

58 spermatogenesis in young animals, limited by uracil-DNA glycosylase and DNA ligase in young animals,

59 Uracil-DNA glycosylase and DNA ligase were determined to

60 cleavage by a combined treatment of E. coli uracil-DNA glycosylase and endonuclease IV.

61 om DNA by base excision repair, initiated by uracil-DNA glycosylase and endonuclease V, respectively.

62 cy is limited by the reduced activity of the uracil-DNA glycosylases and DNA polymerase beta on nucle

63 erformed with a known monofunctional enzyme (uracil DNA glycosylase) and a known bifunctional glycosy

64 mes (formamidopyrimidine DNA glycosylase and uracil-DNA glycosylase) and corresponding blockers.

65 enine DNA glycosylase, MutY DNA glycosylase, uracil DNA glycosylase, and APE1 activity.

66 vities of oxoguanine DNA glycosylase (OGG1), uracil DNA glycosylase, and endonuclease III homologue 1

67 BER assay of mitochondrial lysates with pure uracil DNA glycosylase, AP endonuclease and/or the catal

68 When human uracil DNA glycosylase, AP endonuclease, DNA polymerase

69 ude a complete base excision repair pathway (uracil DNA glycosylase, AP endonuclease, DNA polymerase

70 We found that the lysate contained uracil DNA glycosylase, AP endonuclease, DNA polymerase,

71 Near the dyad, uracil DNA glycosylase/APE1 removes an outwardly oriente

72 within the GRE, there was a reduced rate of uracil-DNA glycosylase/Ape1 activity following GR-DBD bi

73 R substrate and five purified human enzymes: uracil-DNA glycosylase, apurinic/apyrimidinic endonuclea

74 stituted with the recombinant human proteins uracil-DNA glycosylase, apurinic/apyrimidinic endonuclea

75 hosphatase (dUTPase) or package host-derived uracil DNA glycosylase as a means to limit the accumulat

76 the base-flipping enzymes HhaI methylase and uracil DNA glycosylase, as well as with TATA-binding pro

77 Thus, AP endo, like uracil DNA glycosylase, behaves in a quasi processive fa

78 When uracil DNA glycosylase binds to AB-APoppin the presence

79 xists, which could reflect action by another uracil-DNA glycosylase but might alternatively be explai

80 lative expression levels of both dUTPase and uracil-DNA glycosylase can have great influence over the

81 The DNA repair enzyme uracil DNA glycosylase catalyzes the first step in the u

82 Uracil-DNA glycosylase catalyzes the excision of uracils

83 or double mutations (D68N and H181L) in the uracil DNA glycosylase conserved catalytic site by using

84 Uracil DNA glycosylase could hydrolyze deoxyuracils of t

85 -resistance, which was further elevated in a uracil DNA glycosylase-deficient background.

86 egion, transformed into bacteria (wild-type, uracil DNA glycosylase-deficient, ung-, or exonuclease I

87 In contrast, replication of a uracil DNA glycosylase deletion mutant occurred only in

88 Despite the requirement for DNA deamination, uracil DNA glycosylase did not modulate APOBEC3G-depende

89 Escherichia coli double-strand uracil-DNA glycosylase (Dug) was purified to apparent ho

90 acil-DNA glycosylase (Ung)- or double-strand uracil-DNA glycosylase (Dug)-proficient and -deficient i

91 ce deficient in the evolutionarily conserved uracil-DNA glycosylase encoded by the UNG gene surprisin

92 isense (AS) oligonucleotide directed against uracil-DNA glycosylase encoded by the UNG gene to deplet

93 Uracil-DNA glycosylase, encoded by the UNG1 gene in Sacc

94 eltavpr virions contained readily detectable uracil-DNA glycosylase enzymatic activity, while the act

95 Furthermore, the Smug1, but not the Ung, uracil-DNA glycosylase excises FU from DNA and protects

96 osylases from Escherichia coli, and AfUDG, a uracil DNA glycosylase from Archeoglobus fulgidus, are a

97 The family 4 uracil-DNA glycosylase from the hyperthermophilic organi

98 Unlike uracil-DNA glycosylases from diverse sources, where the

99 cluding virion association, interaction with uracil DNA glycosylase, G(2) arrest, or enhancement of m

100 time quantitative PCRs (qPCRs) targeting the uracil DNA glycosylase gene (udg) or the 23S rRNA gene a

101 1 when combined with inactivation of the Ung uracil-DNA glycosylase gene leads to a loss of nearly al

102 Therefore, the uracil DNA glycosylase has an essential role in DNA repl

103 The DNA repair enzyme uracil DNA glycosylase has been crystallized with a cati

104 Mice deficient in the Ung uracil-DNA glycosylase have an increased level of uracil

105 Human uracil DNA glycosylase (hUNG) plays a central role in DN

106 ies have established that depletion of human uracil DNA glycosylase (hUNG) sensitizes some cell lines

107 ate backbone in sliding and hopping by human uracil DNA glycosylase (hUNG), which is an exemplar that

108 DNA repair enzymes such as human uracil-DNA glycosylase (hUNG) perform the initial step i

109 genic cell line that had no detectable human uracil DNA glycosylase (hUNG2) activity, establishing th

110 measured the probability that nuclear human uracil DNA glycosylase (hUNG2) excised two uracil lesion

111 nt proteins, including a human major nuclear uracil-DNA glycosylase (hUNG2) involved in immediate pos

112 ion for abasic site recognition, the rate of uracil-DNA glycosylase hydrolysis of the N-glycosidic bo

113 observed in herpesviruses, a requirement for uracil DNA glycosylase in DNA replication has been obser

114 ctures of the core catalytic domain of human uracil-DNA glycosylase in complex with uracil-containing

115 concentration of AdoMet, and the activity of uracil-DNA glycosylase in human colon tissues, and searc

116 ed to identify the SMUG1 enzyme as the major uracil-DNA glycosylase in UNG-deficient mice.

117 il residues are removed from DNA by specific uracil-DNA glycosylases in the base excision repair path

118 ogether with the presence of a virus-encoded uracil DNA glycosylase indicates that HSV-1 has the capa

119 tivity of hUNG by lentiviral transduction of uracil DNA glycosylase inhibitor protein into a large pa

120 Bacteriophage PBS2 uracil-DNA glycosylase inhibitor (Ugi) protein inactivat

121 The bacteriophage PBS2 uracil-DNA glycosylase inhibitor (Ugi) protein inactivat

122 ylase activity because addition of the PBS-2 uracil-DNA glycosylase inhibitor (Ugi) protein reduced (

123 residues in DNA by acting sequentially as a uracil-DNA glycosylase inhibitor protein (Ugi)-sensitive

124 d irreversably inhibited by the thermostable uracil-DNA glycosylase inhibitor protein (Ugi).

125 nt proteins formed a stable complex with the uracil-DNA glycosylase inhibitor protein in vitro, indic

126 since the addition of the bacteriophage PBS2 uracil-DNA glycosylase inhibitor protein to extracts sig

127 on was insensitive to inhibition by the PBS2 uracil-DNA glycosylase inhibitor protein, implying the i

128 Coupled with a uracil-DNA glycosylase inhibitor, dCas9-AIDx converted t

129 human proteins that perform all the steps of uracil DNA glycosylase-initiated base excision repair.

130 e excision repair activity changes with age, uracil-DNA glycosylase-initiated base excision repair ac

131 of elevated DNA repair gene expression, high uracil-DNA glycosylase-initiated base excision repair, a

132 In this study, uracil-DNA glycosylase-initiated BER activity was measur

133 This study indicates a DSB is formed when uracil DNA glycosylase initiates repair of two closely o

134 antly, we demonstrate that the WXXF motif of uracil DNA glycosylase is implicated in the interaction

135 Previous findings that the vaccinia virus uracil DNA glycosylase is required for virus DNA replica

136 st efficient and well characterized of these uracil-DNA glycosylases is UDG (also known as UNG and pr

137 G DNA mismatch that is normally repaired via uracil DNA glycosylase, is also inhibited by CEBPB bindi

138 The activities of dUTPase and uracil-DNA glycosylase, key enzymes in uracil-DNA metabo

139 the candidates and selected UdgX as the only uracil-DNA glycosylase known to form covalent bonds with

140 Escherichia coli mismatch-specific uracil DNA-glycosylase lacks significant oxoA activity,

141 rget transcripts containing dUTP degraded by Uracil DNA glycosylase, leaving only those transcripts p

142 Although uracil DNA glycosylases limit APOBEC-induced mutation, i

143 tion and subsequent conversion to thymidine, uracil-DNA glycosylase-mediated repair, mismatch repair,

144 We studied mtDNA repair by measuring the uracil DNA glycosylase (mtUDG) and base excision repair

145 lecting the combined action of mitochondrial uracil DNA glycosylase (mtUDG) and mitochondrial apurini

146 Mismatch uracil DNA glycosylase (Mug) from Escherichia coli is an

147 Family 2 mismatch-specific uracil DNA glycosylase (MUG) from Escherichia coli is kn

148 The gene for the mismatch-specific uracil DNA glycosylase (MUG) was identified in the Esche

149 y to be a primary substrate for the mismatch uracil-DNA glycosylase (Mug).

150 f an additional (fifth) viral gene, encoding uracil-DNA glycosylase (MVADelta5-HIV); or (iii) represe

151 eventing uracil excision via inactivation of uracil DNA-glycosylase or by preventing dUTP production

152 Treatment of the DNA with uracil-DNA glycosylase or 3-methyladenine DNA glycosylas

153 Uracil DNA glycosylase, oxoguanine DNA glycosylase and D

154 dy, we report a direct interaction between a uracil-DNA glycosylase (Pa-UDGa) and a PCNA homolog (Pa-

155 Uracil DNA glycosylase plays a key role in DNA maintenan

156 ficient mice, as evidenced by an increase in uracil DNA glycosylase protein (30%, p < 0.01) and activ

157 nockdown of SMUG1 or thymine-DNA glycosylase uracil-DNA glycosylases, proving that it is base excisio

158 ficantly contribute to removal of uracils by uracil DNA glycosylase regardless of the translational o

159 y, Vpr variants deficient for binding to the uracil DNA glycosylase repair enzyme were observed to in

160 efective in one or both of the two mammalian uracil-DNA glycosylase repair enzymes, we were able to t

161 enomenon was observed with the mitochondrial uracil-DNA glycosylase responsible for repair of mutagen

162 4'-azido-2'-deoxyuridine, when treated with uracil-DNA glycosylase, results in quantitative release

163 bacteriophage-encoded protein that inhibits uracil-DNA glycosylase shifts the pattern of IgV gene mu

164 Blocking the activity of uracil-DNA glycosylase should instead lead to replicatio

165 Single-strand-selective monofunctional uracil DNA glycosylase (SMUG1) belongs to Family 3 of th

166 or by single-strand selective monofunctional uracil DNA glycosylase (SMUG1).

167 lase, single-strand-selective monofunctional uracil-DNA glycosylase (SMUG1), and localizes to oxidati

168 The uracil DNA glycosylase superfamily consists of several d

169 is the first report of cooperativity in the uracil DNA glycosylase superfamily of enzymes, and forms

170 Those three glycosylases, UNG (uracil-DNA glycosylase), TDG (thymine-DNA glyscosylase),

171 Family 4 UDGa is a robust uracil DNA glycosylase that only acts on double-stranded

172 equentially to repair the uracil lesion: (i) uracil-DNA glycosylase that excises uracil from single-s

173 d during normal cell growth by altered human uracil-DNA glycosylases that remove undamaged cytosines

174 similarity to the two established classes of uracil-DNA glycosylases, the SMUG1 enzymes contain motif

175 id DNA containing the gene was digested with uracil-DNA glycosylase to remove uracil, and apurinic/ap

176 y positioned 2'-deoxyuridine (dU) residue by uracil DNA glycosylase (UDG) and apurinic/apyrimidinic e

177 The catalytic activities of uracil DNA glycosylase (UDG) and apyrimidinic/apurinic e

178 ated the inhibition of the DNA repair enzyme uracil DNA glycosylase (UDG) by an 11-mer oligonucleotid

179 We have tested this hypothesis with uracil DNA glycosylase (UDG) by constructing a series of

180 Enzymes like uracil DNA glycosylase (UDG) can achieve ground state de

181 The DNA repair enzyme uracil DNA glycosylase (UDG) catalyzes hydrolytic cleava

182 Escherichia coli uracil DNA glycosylase (UDG) catalyzes the hydrolysis of

183 Uracil DNA glycosylase (UDG) cleaves the glycosidic bond

184 The DNA repair enzyme uracil DNA glycosylase (UDG) hydrolyzes the glycosidic b

185 The structure of uracil DNA glycosylase (UDG) in complex with a nonamer d

186 s an abundant mutagenic lesion recognized by uracil DNA glycosylase (UDG) in the first step of base e

187 for investigating enzymatic base flipping by uracil DNA glycosylase (UDG) in which a bulky pyrene nuc

188 Uracil DNA glycosylase (UDG) is a base excision repair e

189 Uracil DNA glycosylase (UDG) is a paradigm enzyme that u

190 The DNA repair enzyme uracil DNA glycosylase (UDG) is a powerful N-glycohydrol

191 The DNA repair enzyme uracil DNA glycosylase (UDG) locates unwanted uracil bas

192 The DNA repair enzyme uracil DNA glycosylase (UDG) pinches the phosphodiester

193 reaction catalyzed by the DNA repair enzyme uracil DNA glycosylase (UDG) proceeds through an unprece

194 During DNA repair, uracil DNA glycosylase (UDG) pulls unwanted uracil into

195 on the role of D4, which also functions as a uracil DNA glycosylase (UDG) repair enzyme.

196 Enzymes in Uracil DNA glycosylase (UDG) superfamily are essential f

197 UDGb belongs to family 5 of the uracil DNA glycosylase (UDG) superfamily.

198 ycosylase (SMUG1) belongs to Family 3 of the uracil DNA glycosylase (UDG) superfamily.

199 The DNA repair enzyme uracil DNA glycosylase (UDG) utilizes base flipping to r

200 n the reaction catalyzed by Escherichia coli uracil DNA glycosylase (UDG) was investigated using X-ra

201 A classic example is the DNA repair enzyme uracil DNA glycosylase (UDG) which recognizes and excise

202 n vitro system was developed that uses human uracil DNA glycosylase (UDG), apyrimidinic/apurinic endo

203 own to interact with D4, the virally encoded uracil DNA glycosylase (UDG), by yeast-two hybrid and in

204 e catalytic pathway of the DNA repair enzyme uracil DNA glycosylase (UDG).

205 D4 is also an enzymatically active uracil DNA glycosylase (UDG).

206 olynucleotide kinase, the DNA repair enzymes uracil-DNA glycosylase (UDG) and formamido-pyrimidine-DN

207 Uracil-DNA glycosylase (UDG) compromises the replication

208 the activity of both bacterial and mammalian uracil-DNA glycosylase (UDG) enzymes.

209 showed that the base excision repair enzyme uracil-DNA glycosylase (UDG) exploits electrostatic inte

210 The 25-kDa Family 4 uracil-DNA glycosylase (UDG) from Pyrobaculum aerophilum

211 Uracil-DNA glycosylase (UDG) is a ubiquitous enzyme foun

212 Uracil-DNA glycosylase (UDG) is an essential enzyme for

213 Uracil-DNA glycosylase (UDG) is responsible for the remo

214 In contrast, uracil-DNA glycosylase (UDG) is specific for uracil and

215 igations identified five families within the uracil-DNA glycosylase (UDG) superfamily.

216 Yet human uracil-DNA glycosylase (UDG), an archetypical enzyme tha

217 bitors of herpes simplex virus type 1 (HSV1) uracil-DNA glycosylase (UDG), an enzyme of DNA repair th

218 In reactions reconstituted with uracil-DNA glycosylase (UDG), apurinic/apyrimidinic (AP)

219 NA complexes with wild-type and mutant human uracil-DNA glycosylase (UDG), coupled kinetic characteri

220 Uracil-DNA glycosylase (UDG), which is a critical enzyme

221 In bacteria, uracil is excised by uracil-DNA glycosylases (UDG) related to E. coli UNG, an

222 9,000 processed form of the highly conserved uracil-DNA glycosylase (UDG1) located in the mitochondri

223 with partial homology to a cyclin-like human uracil DNA glycosylase (UDG2), a member of an important

224 The activity of uracil DNA glycosylases (UDGs), which recognize and exci

225 ity normally associated with the Ung and Mug uracil-DNA glycosylases (UDGs) in E. coli.

226 Uracil-DNA glycosylases (UDGs) initiate the excision rep

227 oreover, UL30, in conjunction with the viral uracil DNA glycosylase (UL2), cellular apurinic/apyrimid

228 tide incorporation is dependent on the HSV-1 uracil DNA glycosylase (UL2), human AP endonuclease, and

229 reviously been shown to bind to the cellular uracil DNA glycosylase UNG.

230 on, and the dU bases are then excised by the uracil DNA glycosylase UNG; the resulting abasic sites a

231 Recent studies of mice deficient for the uracil-DNA glycosylase UNG, which removes U from DNA, su

232 Wild-type mice and those deficient in uracil DNA glycosylase (Ung(-/-)) were placed on a folat

233 ing the sensitivity of DNA to digestion with uracil DNA glycosylase (UNG) and abasic endonuclease.

234 sequent excision of the resulting uracils by uracil DNA glycosylase (UNG) and by mismatch repair prot

235 , one encoding the putative L. monocytogenes uracil DNA glycosylase (ung) and one encoding a protein

236 cuss a new, comprehensive model for how AID, uracil DNA glycosylase (UNG) and the mismatch repair sys

237 The enzyme uracil DNA glycosylase (UNG) excises unwanted uracil bas

238 human APOBEC3G and also lacks the endogenous uracil DNA glycosylase (Ung) gene and show that UNG remo

239 Uracil DNA glycosylase (UNG) is a host enzyme that excis

240 Uracil DNA glycosylase (UNG) is a powerful DNA repair en

241 Uracil DNA glycosylase (UNG) is an important DNA repair

242 Uracil DNA glycosylase (UNG) is required for most CSR ac

243 Uracil DNA glycosylase (UNG) is the primary enzyme for t

244 abasic sites with a reduced accumulation in uracil DNA glycosylase (UNG) null cells.

245 Subsequent excision of dU by uracil DNA glycosylase (UNG) of the base excision repair

246 ils in the Ig gene loci can be recognized by uracil DNA glycosylase (UNG) or mutS homologs 2 and 6 (M

247 The DNA repair enzyme human uracil DNA glycosylase (UNG) scans short stretches of ge

248 We show that depletion of the uracil DNA glycosylase (UNG) sensitizes tumor cells to F

249 Processing of dUs by uracil DNA glycosylase (UNG) yields abasic sites, which

250 In the absence of uracil DNA glycosylase (UNG), genomic uracil accumulates

251 rotein implicated in the DNA repair process, uracil DNA glycosylase (UNG), we have explored the contr

252 One example is the enzyme uracil DNA glycosylase (UNG), which captures and excises

253 stribution of mutations was compared between uracil DNA glycosylase (Ung)-deficient and wild-type mic

254 g uracil-guanine mismatches are processed by uracil DNA glycosylase (UNG)-mediated base-excision repa

255 n S regions to uracils, which are excised by uracil DNA glycosylase (UNG).

256 nism that depends on the S phase activity of uracil DNA glycosylase (UNG).

257 bases from DNA is accomplished by the enzyme uracil DNA glycosylase (UNG).

258 Uracil DNA glycosylases (UNG) are highly conserved prote

259 -induced cytidine deaminase are processed by uracil-DNA glycosylase (UNG) and mismatch repair (MMR) p

260 In the absence of uracil-DNA glycosylase (UNG) and the homologue of bacter

261 Because uracil-DNA glycosylase (Ung) and Vsr are known to repair

262 cosylase inhibitor (Ugi) protein inactivates uracil-DNA glycosylase (Ung) by acting as a DNA mimic to

263 cosylase inhibitor (Ugi) protein inactivates uracil-DNA glycosylase (Ung) by forming an exceptionally

264 Uracil-DNA glycosylase (UNG) is the key enzyme responsib

265 e excision repair (BER), either initiated by uracil-DNA glycosylase (UNG) or by single-strand selecti

266 Complementary pathways, initiated by the uracil-DNA glycosylase (UNG) or the mismatch repair fact

267 viruses and retroviruses encode a dUTPase or uracil-DNA glycosylase (UNG) to counteract uracil incorp

268 ucine intercalation loop of Escherichia coli uracil-DNA glycosylase (Ung) was investigated.

269 In this study, the activity of uracil-DNA glycosylase (UNG) was successfully detected a

270 e epsilon C is not found in E. coli DNA, and uracil-DNA glycosylase (Ung), a distinct enzyme, is much

271 tion-induced cytidine deaminase (AICDA), and uracil-DNA glycosylase (UNG), associated with autosomal

272 galovirus gene UL114, a homolog of mammalian uracil-DNA glycosylase (UNG), is required for efficient

273 We investigated the enzyme uracil-DNA glycosylase (UNG), which detects and cleaves

274 mplete uracil-DNA repair were measured using uracil-DNA glycosylase (Ung)- or double-strand uracil-DN

275 n immunoprecipitation assays in B cells from uracil-DNA glycosylase (UNG)-deficient mice stimulated e

276 f a Cas9 nickase, a cytidine deaminase and a uracil-DNA glycosylase (Ung).

277 e affinity column that tightly bound E. coli uracil-DNA glycosylase (Ung).

278 roliferation depends on protective repair by uracil-DNA glycosylase (UNG).

279 no known enzymatic activity, D4 is an active uracil-DNA glycosylase (UNG).

280 ognized by proteins from both base excision (uracil-DNA glycosylase, UNG) and mismatch recognition (M

281 A yeast strain lacking the enzyme uracil DNA glycosylase (Ung1), which excises uracil from

282 ddition, Vpr causes rapid degradation of the uracil-DNA glycosylases UNG2 and SMUG1.

283 nteractions with base excision repair enzyme uracil DNA glycosylase (UNG2) and crossover junction end

284 -excision repair pathway by antagonizing the uracil DNA glycosylase (Ung2) enzyme.

285 Human nuclear uracil DNA glycosylase (UNG2) is a cellular DNA repair e

286 Uracil DNA Glycosylase (UNG2) is the primary enzyme in h

287 into virus particles of the nuclear form of uracil DNA glycosylase (UNG2), a cellular DNA repair enz

288 imilar to the recruitment of another target, uracil DNA glycosylase (UNG2), to the CRL4-DCAF1 E3 by V

289 ation-induced cytidine deaminase (AICDA) and uracil-DNA glycosylase (UNG2), were up-regulated in norm

290 PPM1D interacts with the nuclear isoform of uracil DNA glycosylase, UNG2, and suppresses base excisi

291 The human uracil-DNA glycosylases, UNG2 and SMUG1, were able to re

292 iversification that are largely dependent on uracil-DNA glycosylase (uracil-N-glycolase [UNG]).

293 bstrate to assess enzyme processivity, human uracil-DNA glycosylase was shown to use a processive sea

294 By using uracil and uracil DNA glycosylase, we first prepared a 250-bp DNA t

295 To accomplish this, uracil-DNA glycosylases were affinity purified from HeLa

296 residues are eliminated from cellular DNA by uracil-DNA glycosylase, which cleaves the N-glycosylic b

297 ggered by AID is enhanced by a deficiency of uracil-DNA glycosylase, which indicates that AID functio

298 ties of two model enzymes, exonuclease I and uracil DNA glycosylase with high sensitivity and selecti

299 cosylase is implicated in the interaction of uracil DNA glycosylase with Vpr intracellularly.

300 bilize the abasic site during treatment with uracil-DNA glycosylase with a reducing agent.