ライフサイエンスコーパス: HIV-1 integrase

1 e 3'-processing and strand transfer steps of HIV-1 integrase.

2 med between subunits of a dimer of dimers of HIV-1 integrase.

3 GT) aptamer, a potent nanomolar inhibitor of HIV-1 integrase.

4 differed markedly in their interactions with HIV-1 integrase.

5 n aryl di-O-acetyl group but did not inhibit HIV-1 integrase.

6 om the nucleus and abolish nuclear import of HIV-1 integrase.

7 the molecular interactions between DKAs and HIV-1 integrase.

8 ccumulation of an otherwise unstable form of HIV-1 integrase.

9 n as hSNF5, is a protein that interacts with HIV-1 integrase.

10 first receptor-based pharmacophore model for HIV-1 integrase.

11 o the solution structure of this domain from HIV-1 integrase.

12 T30695 plays a key role in the inhibition of HIV-1 integrase.

13 xicity, anti-HIV activity, and inhibition of HIV-1 integrase.

14 ure of the isolated catalytic core domain of HIV-1 integrase.

15 linear orientation were potent inhibitors of HIV-1 integrase.

16 a lead compound against purified recombinant HIV-1 integrase.

17 sugar modifications affect the inhibition of HIV-1 integrase.

18 curcumin confer inhibitory activity against HIV-1 integrase.

19 resides in the central 50-212 amino acids of HIV-1 integrase.

20 sed upon guanosine quarters as inhibitors of HIV-1 integrase.

21 rs, possessing novel structural features, on HIV-1 integrase.

22 sed on nucleotide analogues as inhibitors of HIV-1 integrase.

23 ntroduced the same mutation into full-length HIV-1 integrase.

24 sed to analyze amino acid covariation within HIV-1 integrase.

25 l as a bimolecular G-quadruplex that targets HIV-1 integrase.

26 pha-hydroxytropolones) were found to inhibit HIV-1 integrase.

27 logous human immunodeficiency virus, type 1 (HIV-1) integrase.

28 ases such as human immunodeficiency virus-1 (HIV-1) integrase.

29 tors of human immunodeficiency virus type 1 (HIV-1) integrase.

30 ainst human immunodeficiency virus type one (HIV-1) integrase.

31 compounds with: (1) improved potency against HIV-1 integrase, (2) improved anti-HIV effect in tissue

32 it was shown to exhibit potent inhibition of HIV-1 integrase (3'-processing IC50 = 0.6 microgram/mL).

33 mics simulation has been carried out for the HIV-1 integrase-5CITEP complex in order to understand th

34 Models for clinical inhibitors bound at the HIV-1 integrase active site were also constructed and co

35 itor of human immunodeficiency virus type 1 (HIV-1) integrase active against HIV-1 susceptible or res

36 tetrad structure and the capacity to inhibit HIV-1 integrase activity and between thermal stability o

37 g the efficacy of these compounds to inhibit HIV-1 integrase activity and HIV-1 replication in cell c

38 apparent decrease in the ability to inhibit HIV-1 integrase activity and in the inhibition of HIV-1

39 , T30695 demonstrated a strong inhibition of HIV-1 integrase activity as the K+-form structure, but a

40 K+-form structure, but a poor inhibition of HIV-1 integrase activity as the Li+-form structure.

41 ntrations, suggesting that they may regulate HIV-1 integrase activity in cells.

42 etained the ability to efficiently stimulate HIV-1 integrase activity in vitro.

43 nd T30177, plays a key role in inhibition of HIV-1 integrase activity.

44 rowth-factor-p75 (LEDGF/p75)-binding site on HIV-1 integrase, an attractive target for antiviral chem

45 1 blocked viral infection by complexing with HIV-1 integrase and aborting chromosomal integration.

46 enzyme targets as they are both specific for HIV-1 integrase and active against HIV-1 in tissue cultu

47 atin-binding factor LEDGF/p75 interacts with HIV-1 integrase and directs integration to active transc

48 s bearing a mutated E2C-binding site or when HIV-1 integrase and E2C were added to the reaction as se

49 ed the solubility of the catalytic domain of HIV-1 integrase and enabled the structure to be determin

50 h are important for potency against purified HIV-1 integrase and for reported cytoprotective effects

51 In HIV-1 virions, A3G interacted with HIV-1 integrase and nucleocapsid, key viral factors for

52 concurrent inhibition of two viral targets, HIV-1 integrase and protease.

53 ify hRad18 as a novel interacting partner of HIV-1 integrase and suggest a role for post-replication/

54 nt constituents for optimal activity against HIV-1 integrase and that new derivatives can be develope

55 Because HIV-1 integrase and Tn5 transposase have similar active

56 opy to study stable complexes formed between HIV-1 integrase and viral DNA and their interaction with

57 can be used to investigate the link between HIV-1 integrase and viral particle morphogenesis.

58 ex with human immunodeficiency virus type 1 (HIV-1) integrase and is essential for nuclear localizati

59 ts with human immunodeficiency virus type 1 (HIV-1) integrase and is incorporated into HIV-1 virions.

60 ding of human immunodeficiency virus type 1 (HIV-1) integrase and the effect of cofactors and inhibit

61 tor of human immunodeficiency virus, type I (HIV-1) integrase and the K(+)-induced loop folding of T3

62 he binding site of a nucleotide inhibitor of HIV-1 integrase, and possibly a component of the enzyme

63 amined for their inhibitory activity against HIV-1 integrase, and two pharmacophores associated with

64 rus type 1 (HIV-1); therefore, inhibitors of HIV-1 integrase are candidates for antiretroviral therap

65 Active site inhibitors of HIV-1 integrase are clinically validated for the treatme

66 feline immunodeficiency virus protease, and HIV-1 integrase are rationalized in terms of the dehydro

67 se compounds were selected and tested in the HIV-1 integrase assay.

68 ogical ribonucleotides ATP and GTP inhibited HIV-1 integrase at or near cellular concentrations, sugg

69 ants by replacing the SNV integrase with the HIV-1 integrase, based on multiple sequence alignments a

70 nces between wild-type and the double-mutant HIV-1 integrase, because they chelate the magnesium or m

71 HIV-1 integrase binds site-specifically to the ends of t

72 ith its ability to exclusively interact with HIV-1 integrase but not with other retroviral integrases

73 d (DKA) compounds have been shown to inhibit HIV-1 integrase by a mechanism that involves sequestrati

74 ort, we examine the Zn2+ content of purified HIV-1 integrase by atomic absorption spectroscopy and by

75 e propose that this site could interact with HIV-1 integrase by chelation of the metal in the integra

76 nt the first class of compounds that inhibit HIV-1 integrase by interacting with the enzyme N-termina

77 We compared the inhibition of HIV-1 integrase by six DKA derivatives using the wild-ty

78 n the integrase active site as inhibition of HIV-1 integrase catalytic activity and DNA binding were

79 rystal structure of the first complex of the HIV-1 integrase catalytic core domain with an inhibitor

80 ied out on completely hydrated models of the HIV-1 integrase catalytic domain, one with no metal ions

81 Human immunodeficiency virus type-1 (HIV-1) integrase catalyzes the irreversible insertion of

82 Finally, we observed that HIV-1 integrase co-localized with hRad18 in nuclear stru

83 have constructed an active-site model of the HIV-1 integrase complexed with viral DNA using the cryst

84 e have solved the structure of a fragment of HIV-1 integrase comprising the N-terminal and catalytic

85 Our findings suggest that HIV-1 integrase contacts with conserved features of the

86 The N-terminal domain of HIV-1 integrase contains a pair of His and Cys residues

87 main of human immunodeficiency virus type 1 (HIV-1) integrase contains elements necessary for specifi

88 previously reported crystal structure of the HIV-1 integrase core domain revealed that this domain be

89 determined the structure of a complex of the HIV-1 integrase core domain with a novel inhibitor, 5ClT

90 city of human immunodeficiency virus type 1 (HIV-1) integrase could be assigned to the central domain

91 ansfer assays were developed to characterize HIV-1 integrase dimerization and the interaction between

92 We used two HIV-1 integrase-DNA cross-linking assays to probe the bi

93 acids (DKAs) represent a major lead in anti-HIV-1 integrase drug design.

94 ds (DKAs) represent a major advance for anti-HIV-1 integrase drug development.

95 acity of the folded oligomers to inhibit the HIV-1 integrase enzyme in vitro or HIV-1 infection in ce

96 bitors thought to bind in the active site of HIV-1 integrase fit the dynamic model but not the static

97 derived human immunodeficiency virus type 1 (HIV-1) integrases for alterations in the choice of nonvi

98 metalloproteinases, farnesyltransferase, and HIV-1 integrase, for the treatments of cardiovascular di

99 We show that HIV-1 integrase forms stable synaptic complexes in which

100 d the binding of both viral and human DNA to HIV-1 integrase, fully flexible dinucleotides were docke

101 uncated human immunodeficiency virus type 1 (HIV-1) integrase fused to the synthetic polydactyl zinc

102 inciple, we demonstrate the detection of the HIV-1 integrase gene with the microBAR using the Loop-Me

103 dies of human immunodeficiency virus type 1 (HIV-1) integrase have been impeded by the low solubility

104 Two viral proteins, HIV-1 protease and HIV-1 integrase, have been targeted for inhibitor design

105 gonucleotide is the most potent inhibitor of HIV-1 integrase identified to date, with IC50 values in

106 ants of human immunodeficiency virus type 1 (HIV-1) integrase important for replication in T lymphocy

107 The most active compound against HIV-1 integrase in biochemical assays [2,4,6-cycloheptat

108 oylquinic acid, and L-chicoric acid, inhibit HIV-1 integrase in biochemical assays at concentrations

109 The presence of normal levels of HIV-1 integrase in mutant particles produced at the nonp

110 ession system for the synthesis of authentic HIV-1 integrase in the absence of other viral proteins.

111 idges were significantly less potent against HIV-1 integrase in vitro and were inactive against HIV-1

112 n tissue culture and catalytic activities of HIV-1 integrase in vitro.

113 ligonucleotide that is a potent inhibitor of HIV-1 integrase in vitro.

114 tide that inhibits the catalytic activity of HIV-1 integrase in vitro.

115 itor of human immunodeficiency virus type 1 (HIV-1) integrase in vitro and of HIV-1 replication in ti

116 des a variable fragment antibody recognizing HIV-1 integrase (IN#33),was injected into the human thym

117 To identify functional contacts between HIV-1 integrase (IN) and its viral DNA substrate, we dev

118 HIV-1 integrase (IN) and reverse transcriptase-associate

119 mpound that disrupts the interaction between HIV-1 integrase (IN) and the cellular factor lens epithe

120 separate analyses of binding specificity of HIV-1 integrase (IN) and viral B-DNA forms through ligan

121 low solubility and aggregation properties of HIV-1 integrase (IN) are major obstacles for biochemical

122 privileged" fragment 8-hydroxyquinoline with HIV-1 integrase (IN) at the IN-lens epithelium-derived g

123 INI1/hSNF5 is an HIV-1 integrase (IN) binding protein specifically incorp

124 Recent evidence indicates that inhibition of HIV-1 integrase (IN) binding to the viral RNA genome by

125 ribed dynamic pharmacophore model studies of HIV-1 integrase (IN) by considering more key residues in

126 HIV-1 integrase (IN) catalyzes the insertion of the vira

127 utations at amino acids 143, 148, and 155 in HIV-1 integrase (IN) define primary resistance pathways

128 HIV-1 integrase (IN) displays multiple functions, thanks

129 While an essential role of HIV-1 integrase (IN) for integration of viral cDNA into

130 ng of its structure and enzymatic mechanism, HIV-1 integrase (IN) has become a promising target for d

131 recently identified as a binding partner for HIV-1 integrase (IN) in human cells.

132 Resistance to raltegravir (RAL), the first HIV-1 integrase (IN) inhibitor approved by the FDA, invo

133 Fourteen analogues of the anti-HIV-1 integrase (IN) inhibitor L-chicoric acid (L-CA) we

134 in, we report the identification of a unique HIV-1 integrase (IN) inhibitor-binding site using photoa

135 Allosteric HIV-1 integrase (IN) inhibitors (ALLINIs) are a promisin

136 Allosteric HIV-1 integrase (IN) inhibitors (ALLINIs) are a promisin

137 Allosteric HIV-1 integrase (IN) inhibitors (ALLINIs) are a very pro

138 The pyridine-based multimerization selective HIV-1 integrase (IN) inhibitors (MINIs) are a distinct s

139 The bis-salicylhydrazides class of HIV-1 integrase (IN) inhibitors has been postulated to f

140 -yl)-acetic acids (tBPQA) are a new class of HIV-1 integrase (IN) inhibitors that are structurally di

141 ve led to the discovery of a large number of HIV-1 integrase (IN) inhibitors.

142 HIV-1 integrase (IN) is a validated target for developin

143 HIV-1 Integrase (IN) is an essential enzyme for viral re

144 nique role in the viral replication process, HIV-1 integrase (IN) is an important antiretroviral drug

145 HIV-1 integrase (IN) is an important target for contempo

146 HIV-1 integrase (IN) is an important target for designin

147 HIV-1 integrase (IN) is essential for virus replication

148 Nuclear localization signal (NLS) of HIV-1 integrase (IN) is implicated in nuclear import of

149 HIV-1 integrase (IN) is implicated to play a role in the

150 HIV-1 integrase (IN) is one of three enzymes encoded by

151 HIV-1 integrase (IN) is the molecular target of the newl

152 Insolubility of full-length HIV-1 integrase (IN) limited previous structure analyses

153 HIV-1 integrase (IN) non-covalently juxtaposes two viral

154 on.IMPORTANCE Recent evidence indicates that HIV-1 integrase (IN) plays a key role during particle ma

155 The HIV-1 integrase (IN) protein is responsible for the inte

156 A tetramer of HIV-1 integrase (IN) stably associates with the viral DN

157 There are currently three HIV-1 integrase (IN) strand transfer inhibitors (INSTIs)

158 INI1/SMARCB1 binds to HIV-1 integrase (IN) through its Rpt1 domain and exhibit

159 We observed that stable introduction of HIV-1 integrase (IN) transcription units into cells made

160 A tetramer model for HIV-1 integrase (IN) with DNA representing 20 bp of the

161 plasmid acceptor, purified bacterium-derived HIV-1 integrase (IN), and host HMG protein family member

162 plasmid acceptor, purified bacterial-derived HIV-1 integrase (IN), and host HMG-I(Y) protein.

163 rary of random, single-amino-acid mutants in HIV-1 integrase (IN), covering >40% of amino acid positi

164 EDGF/p75 is the major cellular interactor of HIV-1 integrase (IN), critical to efficient viral replic

165 entary features of the active site region of HIV-1 integrase (IN), which was developed from a series

166 (3'-P) and strand transfer (ST) functions of HIV-1 integrase (IN), while 7-aminosubstituted quinolino

167 INI1/hSNF5/BAF47/SMARCB1 is an HIV-1 integrase (IN)-binding protein that modulates vira

168 ed agents which exhibit potent inhibition of HIV-1 integrase (IN)-catalyzed strand transfer (ST) proc

169 e (PR), HIV-1 reverse transcriptase (RT) and HIV-1 integrase (IN).

170 ible for the drug-induced multimerization of HIV-1 integrase (IN).

171 sted for their inhibitory activities against HIV-1 integrase (IN).

172 1 replication, specifically interacting with HIV-1 integrase (IN).

173 ed by direct interaction between TRN-SR2 and HIV-1 integrase (IN).

174 ge number of human immunodeficiency virus 1 (HIV-1) integrase (IN) alterations, referred to as class

175 of the human immunodeficiency virus type 1 (HIV-1) integrase (IN) catalytic domain were analyzed for

176 ysis by human immunodeficiency virus-type 1 (HIV-1) integrase (IN) connects two DNA strands (disinteg

177 main of human immunodeficiency virus type 1 (HIV-1) integrase (IN) contains a D,D(35)E motif, named f

178 CCD) of human immunodeficiency virus type 1 (HIV-1) integrase (IN) harbors the enzyme active site and

179 CTD) of human immunodeficiency virus type 1 (HIV-1) integrase (IN) important for IN-IN and IN-DNA int

180 Human immunodeficiency virus type 1 (HIV-1) integrase (IN) inserts the viral DNA genome into

181 The human immunodeficiency virus type 1 (HIV-1) integrase (IN) is a critical enzyme involved in i

182 GF) and human immunodeficiency virus type 1 (HIV-1) integrase (IN) is essential for HIV-1 replication

183 The human immunodeficiency virus type 1 (HIV-1) integrase (IN) protein augments the initiation of

184 uLV and human immunodeficiency virus type 1 (HIV-1) integrase (IN) proteins.

185 Human immunodeficiency virus type 1 (HIV-1) integrase (IN) undergoes a reversible metal-induc

186 tion of human immunodeficiency virus type 1 (HIV-1) integrase (IN) using monoclonal antibodies (mAbs)

187 del for human immunodeficiency virus type 1 (HIV-1) integrase (IN) with DNA representing long termina

188 ains of human immunodeficiency virus type 1 (HIV-1) integrase (IN), there is no structure of the enti

189 tors of human immunodeficiency virus type 1 (HIV-1) integrase (IN).

190 against human immunodeficiency virus type 1 (HIV-1) integrase (IN).

191 ) binds human immunodeficiency virus type 1 (HIV-1) integrase (IN).

192 itor of human immunodeficiency virus type 1 (HIV-1) integrase (IN); caffeic acid phenethyl ester (CAP

193 n of TRN-SR2 with a truncated variant of the HIV-1 integrase, including both the CCD and CTD.

194 n was greatest in a 50-amino-acid segment of HIV-1 integrase incorporating the catalytic aspartic aci

195 Experiments with truncated HIV-1 integrases indicate that the N-terminal region con

196 as not able to compete off T30177 binding to HIV-1 integrase, indicating a tight binding of G4s to th

197 orty-two of these compounds were assayed for HIV-1 integrase inhibition, and of these, 27 had inhibit

198 cal asymmetric total synthesis of the potent HIV-1 integrase inhibitor 5 is described.

199 slow progress toward a clinically effective HIV-1 integrase inhibitor can at least in part be attrib

200 For this purpose, we used a known HIV-1 integrase inhibitor containing aryl di-O-acetyl gr

201 and are promising lead compounds for further HIV-1 integrase inhibitor development.

202 572), a human immunodeficiency virus type 1 (HIV-1) integrase inhibitor, has limited cross-resistance

203 -daily, human immunodeficiency virus type 1 (HIV-1) integrase inhibitor, was evaluated for distributi

204 Allosteric HIV-1 integrase inhibitors (ALLINIs) have garnered speci

205 Two-metal binding HIV-1 integrase inhibitors (INIs) are potent inhibitors

206 The structures of a large number of HIV-1 integrase inhibitors have in common two aryl units

207 Allosteric HIV-1 integrase inhibitors promote aberrant IN multimeri

208 discovery of 10 novel, structurally diverse HIV-1 integrase inhibitors, four of which have an IC50 v

209 Based upon a class of known HIV-1 integrase inhibitors, several pharmacophore models

210 Based on data derived from a large number of HIV-1 integrase inhibitors, similar structural features

211 A separate class of HIV-1 integrase inhibitors, the allosteric integrase inh

212 Among all the HIV-1 integrase inhibitors, the beta-diketo acids (DKAs)

213 tegy toward the potential design of improved HIV-1 integrase inhibitors.

214 his water molecule could open a route to new HIV-1 integrase inhibitors.

215 Human immunodeficiency virus type 1 (HIV-1) integrase inhibitors are in clinical trials, and

216 of the human immunodeficiency virus type-1 (HIV-1) integrase inhibitors dolutegravir (S/GSK1349572)

217 les were made in order to examine effects on HIV-1 integrase inhibitory potencies.

218 The development of HIV-1 integrase (INT) inhibitors has been hampered by in

219 Moreover, HIV-1 integrase interacted with recombinant transportin

220 owed that the C-terminal domain of wild-type HIV-1 integrase interacted with RT.

221 riginally developed to inhibit the LEDGF/p75-HIV-1 integrase interaction.

222 These findings indicate that the HIV-1 integrase is a physiological substrate of the N-en

223 HIV-1 integrase is an essential enzyme in the life cycle

224 nserved residue Q146 in the flexible loop of HIV-1 integrase is critical for productive viral DNA bin

225 HIV-1 integrase is essential for viral replication and c

226 This demonstrated that HIV-1 integrase is functional in the SNV gag-pol orf wit

227 HIV-1 integrase is one of the three essential enzymes re

228 The viral protein HIV-1 integrase is required for insertion of the viral g

229 ous binding of LEDGF/p75 to chromatin and to HIV-1 integrase is required for its cofactor activity.

230 y shown that human immunodeficiency virus-1 (HIV-1) integrase is an unstable protein and a substrate

231 Human immunodeficiency virus type 1 (HIV-1) integrase is one of three virally encoded enzymes

232 urified human immunodeficiency virus type-1 (HIV-1) integrase is stimulated by the addition of exogen

233 n immunodeficiency virus type one integrase (HIV-1 integrase) is required for integration of a double

234 g 1, which has no inhibitory potency against HIV-1 integrase, is comprised of roughly a 1:1 mixture o

235 nt manner compared to protein treatment with HIV-1 integrase, maltose binding protein (MBP), and MBP-

236 explains MAP30's apparent inhibition of the HIV-1 integrase, MAP30's ability to irreversibly relax s

237 inks to human immunodeficiency virus type 1 (HIV-1) integrase mapped predominantly to integrase proto

238 the 5CITEP inhibitor to snapshots of a 2 ns HIV-1 integrase MD trajectory indicated a previously unc

239 n also be efficiently used as a substrate in HIV-1 integrase-mediated integration both in vitro and i

240 The compound inhibits HIV-1 integrase-mediated strand transfer, and its antivi

241 SV40-based HIV-1 integrase mutant replication in otherwise nonpermi

242 nal crystal structures of the core domain of HIV-1 integrase mutants, crystallized in the presence an

243 The human immunodeficiency virus type 1 (HIV-1) integrase mutations N155H and Q148R(H)(K) that re

244 ects on human immunodeficiency virus type 1 (HIV-1) integrase of the nucleotides of three nucleoside

245 have now studied the activity of recombinant HIV-1 integrase on a linear 4.7 kb double-stranded DNA,

246 or TNPO3 either through its interaction with HIV-1 integrase or capsid.

247 experiments with different concentrations of HIV-1 integrase or DNA substrate found that the effect o

248 of the human immunodeficiency virus type 1 (HIV-1) integrase or ribonuclease (RNase) H.

249 binding site of known LEDGF/p75 interactors-HIV-1 integrase, PogZ, and JPO2.

250 um-derived growth factor/p75-binding site on HIV-1 integrase promote dimerization and inhibit integra

251 We have investigated the binding of zinc to HIV-1 integrase protein and find that it binds zinc with

252 so able to act as a molecular tether linking HIV-1 integrase protein to chromatin, a phenomenon likel

253 ned to the central domain of the 288-residue HIV-1 integrase protein, composed of amino acids 50-212.

254 nformation regarding ligand interaction with HIV-1 integrase protein.

255 The human immunodeficiency virus type 1 (HIV-1) integrase protein (IN) is essential for integrati

256 urified human immunodeficiency virus type 1 (HIV-1) integrase protein in vitro have supported mainly

257 tor for human immunodeficiency virus type 1 (HIV-1) integrase protein, determining its nuclear locali

258 In this study, eight different HIV-1 integrase proteins containing mutations observed i

259 e assayed inhibition of reactions containing HIV-1 integrase purified from an Escherichia coli expres

260 the 34 analogues had potent activity against HIV-1 integrase ranging from 0.07 to >10 microM.

261 This splice site overlaps the HIV-1 integrase reading frame, and thus, the NLD2up muta

262 HIV-1 integrase residues Ser119, Arg231, and Lys258 were

263 Analysis of the crystal structure of HIV-1 integrase reveals a cluster of lysine residues nea

264 ensitivity targeting the integrase region of HIV-1 (integrase single-copy assay [iSCA] v1.0) has been

265 HIV-1 integrase specifically recognizes and cleaves vira

266 Human immunodeficiency virus, type 1 (HIV-1), integrase specifically recognizes the terminal s

267 In phase 1 trials, the HIV-1 integrase strand transfer inhibitor cabotegravir (

268 Cabotegravir (GSK1265744) is an HIV-1 integrase strand transfer inhibitor with potent an

269 HIV-1 integrase strand transfer inhibitors are an import

270 d the efficacy and safety of raltegravir, an HIV-1 integrase strand-transfer inhibitor.

271 d structure of the C-terminal two domains of HIV-1 integrase; superposition of the conserved catalyti

272 Based upon the assay of inhibition of HIV-1 integrase, T30695 demonstrated a strong inhibition

273 Here we describe allosteric inhibitors of HIV-1 integrase that bind to the LEDGF/p75 interaction s

274 26 and 29 as potent allosteric inhibitors of HIV-1 integrase that exhibited low nanomolar antiviral p

275 s such as L-731,988 are potent inhibitors of HIV-1 integrase that inhibit integration and viral repli

276 dentified a residue in the central domain of HIV-1 integrase that interacts with or influences intera

277 eport, we describe diketo acid inhibitors of HIV-1 integrase that manifest antiviral activity as a co

278 ans the chromatin, and upon interaction with HIV-1 integrase, their complex is locked on chromatin.

279 echanism for LEDGF/p75-mediated tethering of HIV-1 integrase to chromatin.

280 tive nucleotides tested inhibited binding of HIV-1 integrase to its substrate DNA an inhibited an int

281 The binding of HIV-1 integrase to mini-HIV DNA was visualized.

282 130 of human immunodeficiency virus type 1 (HIV-1) integrase to determine their effects on integrati

283 Molecular modeling of HIV-1 integrase, together with biochemical data, indicat

284 be dependent on monitoring the evolution of HIV-1 integrase under drug selection pressure.

285 hat the human immunodeficiency virus type 1 (HIV-1) integrase uses either manganese or magnesium to a

286 We find that the Zn2+ content of HIV-1 integrase varies from 0.1 to 0.92 equiv of Zn2+ pe

287 HIV-1 integrase was presented with substrates that conta

288 yzed by human immunodeficiency virus type 1 (HIV-1) integrase was decreased after compaction of this

289 s to DNA transposases and integrases such as HIV-1 integrase, we sought to determine how integrase in

290 inds to both the acceptor and donor sites of HIV-1 integrase, whereas the monofunctional L-708,906 de

291 The HIV-1 integrase, which is essential for viral replicatio

292 of L-870,810, a small-molecule inhibitor of HIV-1 integrase with potent antiviral activity in cell c

293 h binds human immunodeficiency virus type 1 (HIV-1) integrase with high specificity and affinity but

294 T30177 binds to HIV-1 integrase without being processed and blocks the b