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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

51 Uracil-DNA glycosylase and DNA ligase were determined to

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

73 Uracil-DNA glycosylase catalyzes the excision of uracils

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

91 1 when combined with inactivation of the Ung uracil-DNA glycosylase gene leads to a loss of nearly al

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

138 Uracil DNA glycosylase, oxoguanine DNA glycosylase and D

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

140 Uracil DNA glycosylase plays a key role in DNA maintenan

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

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

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

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

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

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

147 4'-azido-2'-deoxyuridine, when treated with uracil-DNA glycosylase, results in quantitative release

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

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

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

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

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

153 The uracil DNA glycosylase superfamily consists of several d

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

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

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

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

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

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

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

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

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

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

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

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

166 Uracil DNA glycosylase (UDG) cleaves the glycosidic bond

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

190 Uracil-DNA glycosylase (UDG) compromises the replication

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

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

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

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

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

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

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

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

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

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

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

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

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

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

205 9,000 processed form of the highly conserved uracil-DNA glycosylase (UDG1) located in the mitochondri

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

235 Uracil DNA glycosylases (UNG) are highly conserved prote

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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