ライフサイエンスコーパス: HIV-1 reverse transcriptase

1 he removal of different chain terminators by HIV-1 reverse transcriptase.

2 e (NgoM IV) cleavage site at its 3'-end, and HIV-1 reverse transcriptase.

3 AZT P3Ms exhibited very potent inhibition of HIV-1 reverse transcriptase.

4 ch was previously reported in a complex with HIV-1 reverse transcriptase.

5 domain of human tRNA(Lys,3), the primer for HIV-1 reverse transcriptase.

6 f AZTMP from the end of the primer strand by HIV-1 reverse transcriptase.

7 ainst hepatitis C virus (HCV) polymerase and HIV-1 reverse transcriptase.

8 n compared with the complex of nevirapine in HIV-1 reverse transcriptase.

9 osophila pol gamma complex resemble those of HIV-1 reverse transcriptase.

10 in CEM-SS cell culture and for inhibition of HIV-1 reverse transcriptase.

11 accessory subunit and the RNase H domain of HIV-1 reverse transcriptase.

12 e observed for other polymerases such as the HIV-1 reverse transcriptase.

13 f DNA strand transfer reactions catalyzed by HIV-1 reverse transcriptase.

14 was found to target the RNase H activity of HIV-1 reverse transcriptase.

15 etroviral reverse transcription catalyzed by HIV-1 reverse transcriptase.

16 sphates into a primer-template complex using HIV-1 reverse transcriptase.

17 eries of 12 TIBO nonnucleoside inhibitors of HIV-1 reverse transcriptase.

18 ich line the nonnucleoside binding pocket of HIV-1 reverse transcriptase.

19 for two complexes of catechol diethers with HIV-1 reverse transcriptase.

20 erleukin 8, and the ribonuclease H domain of HIV-1 reverse transcriptase.

21 nal changes are critical for the function of HIV-1 reverse transcriptase.

22 tors of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase.

23 itor of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase.

24 tion of HIV-1 induced syncytia formation and HIV-1 reverse transcriptase activity.

25 transcriptase variants for their effects on HIV-1 reverse transcriptase activity.

26 F61A in human immunodeficiency virus type 1 (HIV-1) reverse transcriptase affect strand displacement

27 op and validate the platform, we evolved the HIV-1 reverse transcriptase against N(1)-methyladenosine

28 ymidine 5'-triphosphate (AZTTP) by wild-type HIV-1 reverse transcriptase and a clinically important A

29 e of these hybrids was examined with p66/p51 HIV-1 reverse transcriptase and a mutant carrying an alt

30 Human tRNA(Lys,3) is the specific primer for HIV-1 reverse transcriptase and also requires nucleoside

31 d 20th nucleotides from the recessed end for HIV-1 reverse transcriptase and between the 17th and 20t

32 Phylogenetic analyses of HIV-1 reverse transcriptase and env DNA sequences isolat

33 tRNA(Lys,3), is the specific tRNA primer for HIV-1 reverse transcriptase and has a similar modificati

34 HIV-1 reverse transcriptase and protease gene sequences,

35 inhibited CDK2-dependent phosphorylation of HIV-1 reverse transcriptase and significantly reduced th

36 in more insight into the interaction between HIV-1 reverse transcriptase and the alkenyldiarylmethane

37 /2 = 61 h) along with the ability to inhibit HIV-1 reverse transcriptase and the cytopathic effect of

38 hing by human immunodeficiency virus type 1 (HIV-1) reverse transcriptase and the role of template di

39 e context of our results, related studies on HIV-1 reverse transcriptase, and previous structural stu

40 teraction between the p66 thumb subdomain of HIV-1 reverse transcriptase, and the DNA template in the

41 Specific applications for inhibition of HIV-1 reverse transcriptase are reported.

42 s) and evaluated their inhibitory effects on HIV-1 reverse transcriptase as well as their stability i

43 he dynamic behavior of the RNase H domain of HIV-1 reverse transcriptase at a more physiological pH (

44 on studies of the isolated RNase H domain of HIV-1 reverse transcriptase at low pH have revealed that

45 tent inhibitory activity against recombinant HIV-1 reverse transcriptase at submicromolar concentrati

46 V structure superimposed upon a structure of HIV-1 reverse transcriptase bound to an RNA/DNA hybrid s

47 t function in template and primer binding in HIV-1 reverse transcriptase, but the integrity of the re

48 ic basis for understanding the inhibition of HIV-1 reverse transcriptase by 3TC.

49 r machinery, and identify the suppression of HIV-1 reverse transcriptase by a directly interacting ho

50 HIV-1 reverse transcriptase can remove chain terminators

51 Our results show that actinomycin D inhibits HIV-1 reverse transcriptase catalyzed DNA strand transfe

52 ycin D was found to be a potent inhibitor of HIV-1 reverse transcriptase catalyzed DNA strand transfe

53 level, we investigated the inhibition of the HIV-1 reverse transcriptase-catalyzed viral DNA synthesi

54 main of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase cleaves the tRNA 1 nucleoti

55 ucleoside inhibitor and was absent in mutant HIV-1 reverse transcriptase deficient in polymerase acti

56 HIV-1 reverse transcriptase discriminates poorly between

57 everse transcription products indicated that HIV-1 reverse transcriptase efficiently used the HIV-2 P

58 All four ADAMs were found to inhibit HIV-1 reverse transcriptase enzyme activity, to inhibit

59 antiviral efficacy and activity against the HIV-1 reverse transcriptase enzyme.

60 Moreover, HIV-1 reverse transcriptase extends this binary complex

61 s bacteriophage DNA polymerase T7- (T7-) and HIV-1 reverse transcriptase for comparison with previous

62 nst the ribonuclease H (RNase H) activity of HIV-1 reverse transcriptase has been developed.

63 pre-steady-state kinetic investigations with HIV-1 reverse transcriptase (HIV-1 RT) have reported sub

64 HIV-1 reverse transcriptase (HIV-1 RT) is a multifunctio

65 The active site of HIV-1 reverse transcriptase (HIV-1 RT) was investigated

66 otide (FANA) aptamer (referred to as FA1) to HIV-1 reverse transcriptase (HIV-1 RT) was selected.

67 has been identified as a potent inhibitor of HIV-1 reverse transcriptase (HIV-1 RT).

68 The mechanism by which HIV-1 reverse transcriptase (HIV-RT) discriminates betwe

69 n be understood in light of the structure of HIV-1 reverse transcriptase in a complex with an RNA/DNA

70 hlorines in the aromatic rings might bind to HIV-1 reverse transcriptase in a slightly different mode

71 the 3.0 A resolution structure of wild-type HIV-1 reverse transcriptase in complex with an RNA:DNA o

72 effective as ddATP in reactions catalyzed by HIV-1 reverse transcriptase in that both analogs have si

73 Mutant HIV-1 reverse transcriptase in the viral isolates from t

74 was well tolerated in the catalytic site of HIV-1 reverse transcriptase in the wild-type virus.

75 nhibits human immunodeficiency virus type 1 (HIV-1) reverse transcriptase in a cell-free system.

76 ture of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase in a complex with an RNA-DN

77 ing by human immunodeficiency virus, type 1 (HIV-1) reverse transcriptase in front of the primer term

78 utations in the connection subdomain (cn) of HIV-1 reverse transcriptase increase AZT resistance by a

79 non-nucleoside human immunodeficiency virus (HIV)-1 reverse transcriptase inhibitor (NNRTI), was safe

80 Here we analyzed whether abacavir, an HIV-1 reverse transcriptase inhibitor often inducing sev

81 rmittently dosed vaginal gels containing the HIV-1 reverse transcriptase inhibitor tenofovir protecte

82 ring containing dapivirine, a non-nucleoside HIV-1 reverse-transcriptase inhibitor, involving women b

83 trate these new features with a simple case (HIV-1 reverse transcriptase/inhibitor interaction) and w

84 When HIV-1 reverse transcriptase inhibitors, protease inhibit

85 significant increase in activity against the HIV-1 reverse transcriptase/integrase and P2/nucleocapsi

86 accuracy of plus-strand primer selection by HIV-1 reverse transcriptase is not immediately clear.

87 DNA by human immunodeficiency virus, type 1 (HIV-1) reverse transcriptase is accompanied by RNase H d

88 itor of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase, is a promising addition to

89 e applied the assay to phi29 DNA polymerase, HIV-1 reverse transcriptase, lambda exonuclease and Esch

90 by CPHM was found to be highly specific for HIV-1 reverse transcriptase; little or no inhibition of

91 uggests that large A3G oligomers could block HIV-1 reverse transcriptase-mediated DNA synthesis, ther

92 such as human immunodeficiency virus type 1 (HIV-1) reverse transcriptase monomers and homodimers.

93 -1 replication and can select for a specific HIV-1 reverse transcriptase mutation (V75I) with concomi

94 Non-nucleoside inhibitors of HIV-1 reverse transcriptase (NNRTIs) are part of the com

95 or more than 200 nonnucleoside inhibitors of HIV-1 reverse transcriptase (NNRTIs) representing eight

96 e highly potent non-nucleoside inhibitors of HIV-1 reverse transcriptase (NNRTIs).

97 nhibitors of human immunodeficiency virus-1 (HIV-1) reverse transcriptase (NNRTIs).

98 ocused on three widely studied drug targets, HIV-1 reverse transcriptase, p38 MAP kinase, and cyclin-

99 al entry and did not affect formation of the HIV-1 reverse transcriptase products R/U5 and long termi

100 mpounds showed detectable activities against HIV-1 reverse transcriptase, protease, virus attachment,

101 V75I and other mutations in HIV-1 reverse transcriptase reported from in vitro acycl

102 ochemical, and crystallographic studies with HIV-1 reverse transcriptase revealed that alpha-CNPs mim

103 For HIV-1 reverse transcriptase, reverse transcription (RNA-

104 tion by human immunodeficiency virus type 1 (HIV-1) reverse transcriptase RNase H is critical for gen

105 d precise cleavage at the PPT/U3 junction by HIV-1 reverse transcriptase/RNase H.

106 ar carbocyclic deoxyribose ring that acts on HIV-1 reverse transcriptase (RT(WT)) as a molecular targ

107 ques infected with an SIV variant containing HIV-1 reverse transcriptase (RT) (RT-simian-human immuno

108 tase inhibitors (NNRTIs) specifically target HIV-1 reverse transcriptase (RT) and do not effectively

109 Inhibition of HIV-1 reverse transcriptase (RT) and HIV protease are ef

110 for viral replication: HIV-1 protease (PR), HIV-1 reverse transcriptase (RT) and HIV-1 integrase (IN

111 wealth of structural and biochemical data on HIV-1 reverse transcriptase (RT) and mutants.

112 thione), is an extremely potent inhibitor of HIV-1 reverse transcriptase (RT) and of HIV-1 infection

113 entary dNTP by the binary complex containing HIV-1 reverse transcriptase (RT) and primer-template ind

114 The contribution of HIV-1 reverse transcriptase (RT) and protease (PR) allel

115 e of all four nucleotides revealed that both HIV-1 reverse transcriptase (RT) and T7 DNA polymerase s

116 triphosphate form of ETV with wild type (WT) HIV-1 reverse transcriptase (RT) and the nucleoside reve

117 Drug-resistant variants of HIV-1 reverse transcriptase (RT) are also known to be re

118 Nucleic acid aptamers to HIV-1 reverse transcriptase (RT) are potent inhibitors o

119 flipping at the single molecule level, using HIV-1 reverse transcriptase (RT) as a model system.

120 o facilitate HDX analysis of multimers using HIV-1 reverse transcriptase (RT) as a model.

121 rts 13-15 in HIV-1 infected cells and in the HIV-1 reverse transcriptase (RT) assays is here describe

122 n of amino acids in the fingers subdomain of HIV-1 reverse transcriptase (RT) at positions 69 and 70.

123 of 99 available X-ray crystal structures of HIV-1 reverse transcriptase (RT) at the flexible non-nuc

124 Crystal structures for HIV-1 reverse transcriptase (RT) bound to double-strande

125 oxy-3'-thiacytidine (3TC), and AZT-resistant HIV-1 reverse transcriptase (RT) can increase the virus

126 at some conjugates act as dNTP analogues and HIV-1 reverse transcriptase (RT) catalytically incorpora

127 HIV-1 reverse transcriptase (RT) catalyzes the conversio

128 While many point mutations in the HIV-1 reverse transcriptase (RT) confer resistance to an

129 348I mutation at the connection subdomain of HIV-1 reverse transcriptase (RT) confers clinically sign

130 protein footprinting methodology to dissect HIV-1 reverse transcriptase (RT) contacts to the viral R

131 HIV-1 reverse transcriptase (RT) contains a C-terminal r

132 HIV-1 reverse transcriptase (RT) contributes to the deve

133 HIV-1 reverse transcriptase (RT) degrades the plus stran

134 solution structure of the RNase H domain of HIV-1 reverse transcriptase (RT) determined by NMR metho

135 Although HIV-1 reverse transcriptase (RT) DNA polymerase and ribo

136 Because HIV-1 reverse transcriptase (RT) does not possess 3'- to

137 ling of T7 DNA polymerase exo(-) (T7(-)) and HIV-1 reverse transcriptase (RT) during replication of p

138 Biochemical simulations demonstrate that HIV-1 reverse transcriptase (RT) efficiently incorporate

139 During reverse transcription of viral RNA, HIV-1 reverse transcriptase (RT) encounters RNA stem-loo

140 ion from methionine-184 to valine (M184V) of HIV-1 reverse transcriptase (RT) evokes the 1000-fold 3T

141 HIV-1 reverse transcriptase (RT) frequently incorporates

142 he cleavage and functional expression of the HIV-1 reverse transcriptase (RT) from the modified RV ge

143 sizing a double-stranded DNA from viral RNA, HIV-1 reverse transcriptase (RT) generates an RNA/DNA in

144 Mutations at either Tyr181 or Tyr188 within HIV-1 reverse transcriptase (RT) give high level resista

145 Mutations in HIV-1 reverse transcriptase (RT) give rise to 3'-azido-3

146 e 1 (HIV-1) can induce the development of an HIV-1 reverse transcriptase (RT) harboring a dipeptide i

147 dideoxy-3'-thiacytidine drug-resistant M184I HIV-1 reverse transcriptase (RT) has been shown to synth

148 orophenyl)benzimidazole analogues (BPBIs) to HIV-1 reverse transcriptase (RT) have been determined us

149 nd 20 nevirapine nonnucleoside inhibitors of HIV-1 reverse transcriptase (RT) have been explored in a

150 ole of patient-derived C-terminal domains of HIV-1 reverse transcriptase (RT) in NRTI resistance.

151 RNA aptamers that bind HIV-1 reverse transcriptase (RT) inhibit HIV-1 replicati

152 RNA aptamers that bind HIV-1 reverse transcriptase (RT) inhibit RT in enzymatic

153 ile groups at the wings of the nonnucleoside HIV-1 reverse transcriptase (RT) inhibitor TMC278 are bo

154 rt to develop novel and potent nonnucleoside HIV-1 reverse transcriptase (RT) inhibitors that are eff

155 In a search of HIV-1 reverse transcriptase (RT) inhibitors, a new chemo

156 HIV-1 reverse transcriptase (RT) is a heterodimeric enzy

157 HIV-1 reverse transcriptase (RT) is a highly error prone

158 HIV-1 reverse transcriptase (RT) is a major target of an

159 HIV-1 reverse transcriptase (RT) is a primary target for

160 HIV-1 reverse transcriptase (RT) is an essential enzyme,

161 ry and characterization of new inhibitors of HIV-1 reverse transcriptase (RT) is an important step to

162 HIV-1 reverse transcriptase (RT) is an important target

163 teraction of the NNRTI nevirapine (NVP) with HIV-1 reverse transcriptase (RT) is characterized by a p

164 The polymerase activity of HIV-1 reverse transcriptase (RT) is entirely dependent o

165 The biologically active form of HIV-1 reverse transcriptase (RT) is the p66/p51 heterodi

166 al and biochemical analysis of 3TC-resistant HIV-1 reverse transcriptase (RT) led to a model in which

167 We employed an HIV-1 reverse transcriptase (RT) mutant (Q151N), which i

168 ndings show that AZT resistance mutations in HIV-1 reverse transcriptase (RT) not only reduce suscept

169 These silent K65K and K66K mutations in the HIV-1 reverse transcriptase (RT) occur in over 35% of dr

170 The effect of the K103N mutation of HIV-1 reverse transcriptase (RT) on the activity of efav

171 Formation of the mature HIV-1 reverse transcriptase (RT) p66/p51 heterodimer req

172 ts, we suggest that the polymerase domain of HIV-1 reverse transcriptase (RT) plays a critical role i

173 We have discovered that an HIV-1 reverse transcriptase (RT) polymorphism (RT(172K))

174 HIV-1 reverse transcriptase (RT) possesses both DNA poly

175 le, Val106Ala and Val108Ile are mutations in HIV-1 reverse transcriptase (RT) that are observed in th

176 tors (NNRTIs) that are capable of inhibiting HIV-1 reverse transcriptase (RT) through an allosteric m

177 We used HIV-1 reverse transcriptase (RT) to monitor the annealin

178 HIV-1 reverse transcriptase (RT) undergoes a series of c

179 e reverse transcriptase inhibitor (NNRTI) of HIV-1 reverse transcriptase (RT) used for the treatment

180 However, clinical data suggest that while HIV-1 reverse transcriptase (RT) usually uses an ATP-dep

181 We characterized HIV-1 reverse transcriptase (RT) variants either with or

182 HIV-1 reverse transcriptase (RT) was found to bind with

183 nection subdomain (CN) and RNase H domain of HIV-1 reverse transcriptase (RT) were observed to exhibi

184 have identified fragment-sized inhibitors of HIV-1 reverse transcriptase (RT) with distinct chemical

185 ed clinically as anti-HIV drugs which target HIV-1 reverse transcriptase (RT), (-)-2', 3'-dideoxy-3'-

186 HIV-1 reverse transcriptase (RT), a critical enzyme of t

187 y host DNA-dependent RNA polymerase II or by HIV-1 reverse transcriptase (RT), but the relative contr

188 dynamics simulations of a ternary complex of HIV-1 reverse transcriptase (RT), double-stranded DNA, a

189 wo nucleoside analog resistance mutations in HIV-1 reverse transcriptase (RT), E89G and M184V, were p

190 luding non-nucleoside inhibitors (NNRTIs) of HIV-1 reverse transcriptase (RT), has been limited by th

191 tRNA(Lys)(3) interacts directly with HIV-1 reverse transcriptase (RT), is packaged into viral

192 lides are nonnucleoside inhibitors (NNIs) of HIV-1 reverse transcriptase (RT), of potential clinical

193 6A, 181C, 188C, and 190A), with mutations in HIV-1 reverse transcriptase (RT), singly and in combinat

194 id substitutions within the coding region of HIV-1 reverse transcriptase (RT), such as the 3'-azido-3

195 3) in the fingers and palm subdomains of the HIV-1 reverse transcriptase (RT), the enzyme that replic

196 on in the ribonuclease H (RNase H) domain of HIV-1 reverse transcriptase (RT), which increases resist

197 ine undergoes conformational changes to bind HIV-1 reverse transcriptase (RT), which is an essential

198 the decreased binding affinity to wild-type HIV-1 reverse transcriptase (RT), which may be one of th

199 ions have been biochemically shown to impact HIV-1 reverse transcriptase (RT)-mediated strand transfe

200 of the host nucleus, we opted for developing HIV-1 reverse transcriptase (RT)-specific 2'-deoxynucleo

201 s on dimerization of p66 and p51 subunits of HIV-1 reverse transcriptase (RT).

202 se targeting the essential viral polymerase, HIV-1 reverse transcriptase (RT).

203 d using T7 DNA polymerase exo(-) (T7(-)) and HIV-1 reverse transcriptase (RT).

204 ve excellent antiretroviral activity against HIV-1 reverse transcriptase (RT).

205 icient mouse cells are higher than the KM of HIV-1 reverse transcriptase (RT).

206 forms and assessed their ability to inhibit HIV-1 reverse transcriptase (RT).

207 ity, as well as the viral target protein, WT HIV-1 reverse transcriptase (RT).

208 e sites of wild-type (WT) and drug-resistant HIV-1 reverse transcriptase (RT).

209 riphosphates (dNTP) for incorporation by the HIV-1 reverse transcriptase (RT).

210 closed that RHA enhances the processivity of HIV-1 reverse transcriptase (RT).

211 simian immunodeficiency virus containing the HIV-1 reverse transcriptase (RT).

212 ranscriptase inhibitors (NNRTI) 3 and 4 with HIV-1 reverse transcriptase (RT).

213 rm a group of related sequences that inhibit HIV-1 reverse transcriptase (RT).

214 genic simian immunodeficiency virus encoding HIV-1 reverse transcriptase (RT-SHIV) to examine the imp

215 simian immunodeficiency virus (SIV) carrying HIV-1 reverse transcriptase (RT-SHIV), compared to uninf

216 ions of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) (T69S mutations follow

217 tors of human immunodeficiency virus type-1 (HIV-1) reverse transcriptase (RT) active against the dru

218 itor of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) activity and of HIV-1

219 Human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) and protease sequences

220 lity of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) and protease sequencin

221 ld-type human immunodeficiency virus type-1 (HIV-1) reverse transcriptase (RT) and two RT mutants, Y1

222 gion of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) are associated with re

223 /A/K in human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) are rilpivirine resist

224 loop to human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) between residues 230 a

225 fic for human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) bind at the template-p

226 ture of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) bound to an RNA/DNA hy

227 HIV type I (HIV-1) reverse transcriptase (RT) catalyzes the conversi

228 tion in human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) causes resistance to l

229 ity of human immunodeficiency virus, type 1 (HIV-1) reverse transcriptase (RT) cleaves the viral geno

230 AMs) at human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) codons 41, 67, 70, 210

231 ations in the human immunodeficiency type 1 (HIV-1) reverse transcriptase (RT) connection domain sign

232 grip of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) contacts the DNA prime

233 Human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) contains four structur

234 Human immunodeficiency virus-type 1 (HIV-1) reverse transcriptase (RT) coordinates DNA polyme

235 A synthesis, human immunodeficiency virus 1 (HIV-1) reverse transcriptase (RT) degrades the RNA genom

236 Human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) displays a characteris

237 The human immunodeficiency virus type-1 (HIV-1) reverse transcriptase (RT) functions as a heterod

238 idue of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) greatly enhance RT fid

239 lthough human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) has been extensively s

240 of the human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) have yet to be develop

241 of the human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) heterodimer.

242 ains of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) increase 3'-azido-3'-d

243 Human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) initiates DNA synthesi

244 vity of human immunodeficiency virus type I (HIV-1) reverse transcriptase (RT) is a critical componen

245 Human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) is a dimeric enzyme co

246 The human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) is a heterodimer compr

247 Human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) is a major target of a

248 Human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) is a putative source o

249 of the human immunodeficiency virus type-1 (HIV-1) reverse transcriptase (RT) is comprised of a clus

250 tion in human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) is selected in vitro b

251 ve (ts) human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) mutant was generated b

252 ge library of immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) mutants with amino aci

253 y using human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) mutants with unique cy

254 ed with human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) mutants with unique cy

255 ntified human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) mutants, Q151N and V14

256 The human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) resistance mutation K6

257 ting by human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) result from template s

258 ants of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) that displayed higher

259 ants of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) that influence its tem

260 ance of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) to nucleoside analogs:

261 Human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) variants with the K65R

262 tion in human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT), a variety of non-natu

263 itor of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT), acting through the PP

264 tion in human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT), I132M, which confers

265 Human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT), like all retroviral R

266 Human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT), nucleocapsid protein

267 nhibitors of human immunodeficiency virus-1 (HIV-1) reverse transcriptase (RT)-associated RNase H act

268 are allosteric inhibitors of the HIV type 1 (HIV-1) reverse transcriptase (RT).

269 ld-type human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT).

270 tion in human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT).

271 ively effective inhibitors of drug-resistant HIV-1 reverse transcriptases (RTs) that are excision pro

272 d therefore effective against drug-resistant HIV-1 reverse transcriptases (RTs) that are proficient a

273 LV) and human immunodeficiency virus type 1 (HIV-1) reverse transcriptases (RTs) during RNA-dependent

274 We reviewed all GenBank submissions of HIV-1 reverse transcriptase sequences with or without pr

275 HIV-1 reverse transcriptase shares the key features of h

276 l structure of the complex of 3v (739W94) in HIV-1 reverse transcriptase showed an overlap in the bin

277 al structure of the active sites of MuLV and HIV-1 reverse transcriptases shows the presence of a lys

278 emplate/primers were not altered if bound to HIV-1 reverse transcriptase, signifying that the deposit

279 oth for the isolated domain and for the full HIV-1 reverse transcriptase structure, suggests that the

280 ption with a slightly higher efficiency than HIV-1 reverse transcriptase, suggesting that the activit

281 a nucleotide-dependent reaction catalyzed by HIV-1 reverse transcriptase that can efficiently remove

282 to bind human immunodeficiency virus type 1 (HIV-1) reverse transcriptase tightly, are potent inhibit

283 ecifically, we evaluated the contribution of HIV-1 reverse transcriptase to proviral DNA uracilation

284 urified human immunodeficiency virus type 1 (HIV-1) reverse transcriptase to convert single-stranded

285 HIV-1 reverse transcriptase uses human tRNA(Lys,3) as a

286 C on RNA 5'-end-directed RNase H cleavage by HIV-1 reverse transcriptase, using an RNA.DNA hybrid in

287 HIV-1 reverse transcriptase utilizes a metamorphic polym

288 ants of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (V106A, V179D, and Y181C),

289 ectiveness of the compounds as inhibitors of HIV-1 reverse transcriptase was determined using a fluor

290 he initiation of (-) strand DNA synthesis by HIV-1 reverse transcriptase was examined using a transie

291 Sequencing of HIV-1 reverse transcriptase was simultaneously performed

292 er complexes, in the absence and presence of HIV-1 reverse transcriptase, were irradiated with high-e

293 The F61W mutant form of HIV-1 reverse transcriptase, which is partially impaired

294 ADAM 28 inhibited HIV-1 reverse transcriptase with an IC(50) of 0.3 microM

295 ADAM II inhibited HIV-1 reverse transcriptase with an IC50 of 0.3 microM b

296 res were determined with wild-type and K103N HIV-1 reverse transcriptase with etravirine (TMC125) and

297 a potent competitive inhibitor of wild-type HIV-1 reverse transcriptase with K(i) close to ddATP.

298 n the two previously published structures of HIV-1 reverse transcriptase with mutations at 181 or 188

299 and two strong noncompetitive inhibitors of HIV-1 reverse transcriptase with one series of inhibitor

300 plex of human immunodeficiency virus-type 1 (HIV-1) reverse transcriptase with a DNA template:primer