ライフサイエンスコーパス: HIV-1 protease

1 enced an insert representing the gene of the HIV-1 protease.

2 g factor in the evolutionary optimization of HIV-1 protease.

3 arbonyl or amide NH in the S2-subsite of the HIV-1 protease.

4 nd (2)H and observe the catalytic effects in HIV-1 protease.

5 structure of a novel inhibitor bound to the HIV-1 protease.

6 o an artificial zymogen that is activated by HIV-1 protease.

7 backbone atoms in the S1' and S2 subsites of HIV-1 protease.

8 substrate envelope, to develop inhibitors of HIV-1 protease.

9 vir, located in the catalytic site of enzyme HIV-1 protease.

10 w nM inhibitory activities against wild-type HIV-1 protease.

11 highly potent inhibitory activities against HIV-1 protease.

12 l structure of inhibitor 1 (UIC-94017)-bound HIV-1 protease.

13 s preferred by the S(1)-S(2) active sites of HIV-1 protease.

14 t can be generated by platelet activation or HIV-1 protease.

15 ution at amino acid residue 50 (I50L) of the HIV-1 protease.

16 Pr55 precursor was processed properly by the HIV-1 protease.

17 ml), possibly because of the cytotoxicity of HIV-1 protease.

18 n inactive drug-resistant mutant (D25N/V82A) HIV-1 protease.

19 nvolved in development of drug resistance in HIV-1 protease.

20 tions in the encoded proteins, including the HIV-1 protease.

21 affect the interaction of small ligands with HIV-1 protease.

22 phase and employed as the substrate for the HIV-1 protease.

23 by cleavage of a phage display library with HIV-1 protease.

24 s are mainly focused with the active site of HIV-1 protease.

25 y that is unmatched in a continuous assay of HIV-1 protease.

26 on a number of PI analogues in complex with HIV-1 protease.

27 le in maintaining the closed conformation of HIV-1 protease.

28 ite amino acid residues (Asp29 and Asp30) of HIV-1 protease.

29 PIs, including the dimerization interface of HIV-1 protease.

30 group-specific antigen (Gag) polyprotein by HIV-1 protease.

31 was established for label-free detection of HIV-1 protease.

32 e transfer resistance after injection of the HIV-1 protease.

33 X-ray crystal structure of inhibitor 3-bound HIV-1 protease (1.35 A resolution) revealed extensive in

34 vement of 10%, 17.5%, and 10% is seen for 37 HIV-1 protease, 32 thrombin, and 23 CDK2 ligands, respec

35 general approach with simulated data for the HIV-1 protease, a globular homodimeric protein.

36 alter the structure and dynamic ensemble of HIV-1 protease active site.

37 statin A into picoliter-scale droplets of an HIV-1 protease activity assay to model ultraminiaturized

38 to demonstrate dose-response screening in an HIV-1 protease activity assay.

39 ity within the hydrophobic core can modulate HIV-1 protease activity, supporting the hypothesis that

40 Primary applications of the software on the HIV-1 protease allowed us to quickly identify new inhibi

41 ved by human immunodeficiency virus, type 1 (HIV-1) protease, although at different sites.

42 h our previous XN structure of the wild-type HIV-1 protease-amprenavir complex suggests that the thre

43 probe dynamics-function correlations for the HIV-1 protease, an enzyme that has received considerable

44 , we have characterized a mutant form of the HIV-1 protease, ANAM-11, identified in clinical isolates

45 (2 A or better) X-ray crystal structures of HIV-1 protease and compare the effects of different inhi

46 ) and two cases of dissociation (homodimeric HIV-1 protease and heterodimeric ribonucleotide reductas

47 Two viral proteins, HIV-1 protease and HIV-1 integrase, have been targeted f

48 estigate the dynamic properties of wild-type HIV-1 protease and its two multi-drug-resistant variants

49 embled virus-like particles with recombinant HIV-1 protease and monitor the process with biochemical

50 ve synthesis of optimized ACC substrates for HIV-1 protease and plasmin.

51 uencing to detect minor sequence variants in HIV-1 protease and reverse transcriptase (RT) genes from

52 entification of drug resistance mutations in HIV-1 protease and reverse transcriptase (RT).

53 viral test vector containing patient-derived HIV-1 protease and reverse transcriptase gene segments.

54 ssion, and least angle regression) to relate HIV-1 protease and reverse transcriptase mutations to in

55 resistance testing produces large amounts of HIV-1 protease and reverse transcriptase sequences.

56 entification of drug resistance mutations in HIV-1 protease and RT genes.

57 0.83 and 0.77 for data sets of experimental HIV-1 protease and T4 lysozyme mutants, respectively.

58 used for docking complexes using the dimeric HIV-1 protease and the EIN-HPr complexes as examples.

59 ying the mutation effects on the dynamics of HIV-1 protease and the inhibition by APV and DRV, provid

60 he unliganded form of nitroxide spin-labeled HIV-1 protease and three different complexes with inhibi

61 potent binding affinities against wild-type HIV-1 protease and three multidrug resistant (MDR) varia

62 ystal structures of TMC114 complexed with wt HIV-1 protease and TMC114 and APV complexed with an MDR

63 tudy the gated association rate constants of HIV-1 proteases and drugs.

64 n automated mutation analysis of HIV Type 1 (HIV-1) protease and reverse transcriptase (RT) from appr

65 btype B human immunodeficiency virus type 1 (HIV-1) protease and reverse transcriptase (RT).

66 ions in human immunodeficiency virus type 1 (HIV-1) protease and reverse transcriptase (RT).

67 in the human immunodeficiency virus type 1 (HIV-1) protease and reverse transcriptase sequences.

68 athepsin D, plasmepsin 2 from P. falciparum, HIV-1 protease, and the secreted aspartic proteinase 2 (

69 mical mechanisms underlying the evolution of HIV-1 protease are addressed through molecular simulatio

70 ffinities of seven aliphatic cyclic ureas to HIV-1 protease are calculated using a predominant states

71 zed complexes of the macrocyclic PIs and the HIV-1 protease are presented, analyzed, and discussed.

72 rgy of ligand binding in different resistant HIV-1 proteases are correlated with the creation of wate

73 s is to target the dimerization interface of HIV-1 protease because disruption of the dimer will inhi

74 To provide a structural rationale for HIV-1 protease binding to the NC-p1 cleavage site, we so

75 This HIV-1 protease biosensor represents a new detection appr

76 The inhibition of HIV-1 protease by each of the fluorinated inhibitors was

77 teral drug expulsion from the active site of HIV-1 protease, by conducting all atom molecular dynamic

78 ially available antiviral drugs which target HIV-1 protease can be divided into two classes, those wh

79 HIV-1 protease cleavage subsequently increases k(cat)/K(

80 Casp8p41, a novel protein generated when HIV-1 protease cleaves caspase 8, independently causes N

81 lecules observed in the crystal structure of HIV-1 protease complexed with KNI-272, a potent inhibito

82 s ("cross-decoys") for six trypsin and seven HIV-1 protease complexes.

83 ational sampling and backbone dynamics of an HIV-1 protease construct containing four specific natura

84 The flap conformations of two drug-resistant HIV-1 protease constructs were characterized by molecula

85 Nearly 50 % of the amino acid residues of HIV-1 protease contain methyl side-chains, most of which

86 al samples are analyzed, and the activity of HIV-1 protease could be accurately detected.

87 d and sensitive: picomolar concentrations of HIV-1 protease could be detected in ~10 min.

88 s by which the viral proteins, in particular HIV-1 protease, develop resistance.

89 showed an unusual second binding site on the HIV-1 protease dimer surface of the V32I drug resistant

90 sphocarrier protein HPr and to the symmetric HIV-1 protease dimer.

91 agents based on a minimal pharmacophore for HIV-1 protease dimerization inhibition.

92 onsidered as the key residue mutation of the HIV-1 protease drug resistance because it can significan

93 (EC 3.5.1.5), trypsin (EC 3.4.21.4), and the HIV-1 protease (EC 3.4.21.16); (iv) lyase activity of he

94 ained efficacy against mutant strains of the HIV-1 protease enzyme as compared to Indinavir.

95 and crystallized a multidrug-resistant (MDR) HIV-1 protease enzyme derived from a patient failing on

96 -15-membered cycloamides and evaluated their HIV-1 protease enzyme inhibitory and antiviral activitie

97 of both linear and macrocyclic PIs with the HIV-1 protease enzyme were prepared and analyzed.

98 of the human immunodeficiency virus type 1 (HIV-1) protease enzyme, we set out to develop a modular

99 tors of human immunodeficiency virus type 1 (HIV-1) protease (enzyme, E) that values for the inhibiti

100 PCR (RT-PCR) assay that allows genotyping of HIV-1 protease even when viremia is present at levels as

101 The differences in success when targeting HIV-1 protease, feline immunodeficiency virus protease,

102 The K(i) value of wild-type HIV-1 protease for GW0385, calculated from these values

103 Self-cleavage at the N terminus of HIV-1 protease from the Gag-Pol precursor (autoprocessin

104 lity of human immunodeficiency virus type 1 (HIV-1) protease from treated and untreated patients infe

105 Taken together, these data indicate that HIV-1 protease functions best when residue 80 is a small

106 ermutated and normal sequences in the 297-bp HIV-1 protease gene amplified from patient PBMC.

107 and the emergence of resistance mutations in HIV-1 protease has become an area of significant interes

108 Human immunodeficiency virus type 1 (HIV-1) protease has been continuously evolving and devel

109 none-based ligands in complex with wild-type HIV-1 protease have been determined.

110 effect mutations outside the active site of HIV-1 protease have on inhibitor binding and virus viabi

111 ies of tetrahydropyrimidine-2-ones (THPs) as HIV-1 protease (HIV-1 PR) inhibitors.

112 HIV-1 Protease (HIV-1 PR) is one of the three enzymes es

113 00 microM), and selectively inhibit purified HIV-1 protease (HIV-1P) (IC(50) values for alpha(1)()1,

114 ulations have demonstrated that the flaps of HIV-1 protease (HIV-1p) adopt a range of conformations t

115 tes (POMs) of the Wells-Dawson class inhibit HIV-1 protease (HIV-1P) by a new mode based on kinetics,

116 acterize conformational population shifts in HIV-1 protease (HIV-1PR) upon interaction with various i

117 onitor the conformations of the flaps in apo HIV-1 protease (HIV-1PR), subtypes B, C, and F, CRF01_A/

118 and parameters of the overall tumbling: the HIV-1 protease homodimer and Maltose Binding Protein.

119 estigate the folding landscape of the mature HIV-1 protease homodimer.

120 onformations suitable for alignment with the HIV-1 protease; however, these results indicate that the

121 18)O KIEs for native and multidrug-resistant HIV-1 protease (I84V).

122 rotease inhibitor maintains activity against HIV-1 protease (IC(50) = 19 nM) and, additionally, it is

123 ng of the cleavage of a peptide substrate by HIV-1 protease in a nanopore.

124 This inhibitor binds to the active site of HIV-1 protease in a novel manner, displacing the conserv

125 studies characterized flap conformations in HIV-1 protease in an inhibited and uninhibited form and

126 al structures of wild-type and NFV-resistant HIV-1 protease in complex with p1-p6 substrate peptide v

127 ry cost of the major resistance mutations in HIV-1 protease in terms of protein stability.

128 ated by (i) processing of HERV-K(CON) Gag by HIV-1 protease in virions, (ii) coimmunoprecipitation of

129 he virus life cycle but does not inhibit the HIV-1 protease in vitro or interfere with virus assembly

130 prepare a series of unique analogues of the HIV-1 protease in which the flexibility of the "flap" st

131 al structures of inactive (D25N) WT and V82A HIV-1 proteases in complex with their respective WT and

132 casp8p41 is specific to HIV-1 protease-induced death but not other caspase 8-dep

133 P1' side chain furnished an even more potent HIV-1 protease inhibitor (K(i) = 0.8 nM, EC(50) = 0.04 m

134 We report that GRL-09510, a novel HIV-1 protease inhibitor (PI) containing a newly-generat

135 lated significantly with the activity of the HIV-1 protease inhibitor (PI) saquinavir for both P-gp (

136 the complex mutational patterns required for HIV-1 protease inhibitor resistance.

137 Nelfinavir (NFV) is an HIV-1 protease inhibitor with demonstrated antiviral act

138 Tipranavir, a nonpeptidic HIV-1 protease inhibitor, has been recently approved for

139 pharmacodynamically linked variable for this HIV-1 protease inhibitor.

140 lective human immunodeficiency virus type 1 (HIV-1) protease inhibitor (PI) widely used in antiretrov

141 8) is a human immunodeficiency virus type 1 (HIV-1) protease inhibitor (PRI) recently approved for th

142 e first human immunodeficiency virus type 1 (HIV-1) protease inhibitor approved for once-daily admini

143 2 is a potent human immunodeficiency type 1 (HIV-1) protease inhibitor with a half-life that allows f

144 esigned human immunodeficiency virus type 1 (HIV-1) protease inhibitor, is extremely potent against b

145 ings show that human immunodeficiency virus (HIV)-1 protease inhibitors designed to specifically inhi

146 However, only three of nine FDA-approved HIV-1 protease inhibitors (PI) are active against HIV-2.

147 HIV-1 protease inhibitors (PIs) are among the most effec

148 Here, we identified three novel HIV-1 protease inhibitors (PIs) containing a tetrahydrop

149 We previously showed that HIV-1 protease inhibitors (PIs) slowed the proliferation

150 A series of new HIV-1 protease inhibitors (PIs) were designed using a ge

151 ven novel tertiary alcohol containing linear HIV-1 protease inhibitors (PIs), decorated at the para p

152 We identified three nonpeptidic HIV-1 protease inhibitors (PIs), GRL-015, -085, and -097

153 viously reported tertiary-alcohol-comprising HIV-1 protease inhibitors (PIs), three new 14- and 15-me

154 As (the 3D regimen) with commonly prescribed HIV-1 protease inhibitors (PIs).

155 is, and biological evaluation of a series of HIV-1 protease inhibitors [(-)-6, (-)-7, (-)-23, (+)-24]

156 HIV-1 protease inhibitors are crucial for treatment of H

157 d biological evaluation of a series of novel HIV-1 protease inhibitors are described.

158 HIV-1 protease inhibitors are essential components of pr

159 HIV-1 protease inhibitors are part of the highly active

160 Drug resistance mutations in response to HIV-1 protease inhibitors are selected not only in the d

161 A series of novel HIV-1 protease inhibitors based on two pseudosymmetric d

162 HIV-1 protease inhibitors continue to play an important

163 ty of a series of diastereomeric cyclic urea HIV-1 protease inhibitors has been examined using the Lo

164 nce has sharply limited the effectiveness of HIV-1 protease inhibitors in AIDS therapy.

165 ynthesis, and biological evaluation of novel HIV-1 protease inhibitors incorporating N-phenyloxazolid

166 is, and biological evaluation of a series of HIV-1 protease inhibitors incorporating stereochemically

167 , the elucidation of the mechanisms by which HIV-1 protease inhibitors maintain antiviral activity in

168 resent study, we demonstrate that all of the HIV-1 protease inhibitors tested affect DC maturation.

169 In our quest for HIV-1 protease inhibitors that are not affected by the V

170 sted a second generation set of C2-symmetric HIV-1 protease inhibitors that contain a cyclohexane gro

171 rate-envelope hypothesis which predicts that HIV-1 protease inhibitors that fit within the overlappin

172 HIV-1 protease inhibitors that have little or no effect

173 To evaluate this hypothesis, over 130 HIV-1 protease inhibitors were designed and synthesized

174 Treatment with HIV-1 protease inhibitors, a component of highly active

175 Selective pressure exerted by HIV-1 protease inhibitors, a mainstay of current anti-HI

176 n effort to identify a new class of druglike HIV-1 protease inhibitors, four different stereopure bet

177 M enzyme, which is resistant to all approved HIV-1 protease inhibitors, referred to as the inhibitor-

178 In the case of HIV-1 protease inhibitors, resistance originates from mu

179 cture-based design strategies to develop new HIV-1 protease inhibitors.

180 d biological evaluation of a series of novel HIV-1 protease inhibitors.

181 high propensity to mutate in the presence of HIV-1 protease inhibitors.

182 n to the design of more potent and effective HIV-1 protease inhibitors.

183 uences on the long-term viability of current HIV-1 protease inhibitors.

184 ed for characterizing the next generation of HIV-1 protease inhibitors.

185 application in our recent work on antiviral HIV-1 protease inhibitors.

186 HIV type 1 (HIV-1) protease inhibitors (PI) have been shown to have

187 various human immunodeficiency virus type 1 (HIV-1) protease inhibitors (PIs) challenges the effectiv

188 tion of human immunodeficiency virus type 1 (HIV-1) protease inhibitors (PIs) markedly improved the c

189 ance to human immunodeficiency virus type 1 (HIV-1) protease inhibitors challenges the effectiveness

190 ance to human immunodeficiency virus type 1 (HIV-1) protease inhibitors.

191 HIV-1 protease is a key drug target due to its role in t

192 he spacer peptide 1|nucleocapsid junction by HIV-1 protease is accelerated in the presence of single-

193 HIV-1 protease is an essential enzyme for viral particle

194 HIV-1 protease is an important target for the developmen

195 HIV-1 protease is an important target for the treatment

196 ethod for the measurement of the activity of HIV-1 protease is developed by real-time monitoring of t

197 However, TMC114 binding to the MDR HIV-1 protease is reduced by a factor of 13.3, whereas t

198 of the human immunodeficiency virus type 1 (HIV-1) protease is an essential step in viral replicatio

199 Human immunodeficiency virus Type-1 (HIV-1) protease is crucial for viral maturation and infe

200 g the mature human immunodeficiency virus-1 (HIV-1) protease is presented that facilitates NMR studie

201 ild type (WT) and three resistant mutants of HIV-1 protease: L90M, G48V, and G48V/L90M.

202 Overall, the WT NC-p1 peptide binds HIV-1 protease less optimally than the AP2V mutant, as i

203 s in DeltaGag upon proteolytic processing by HIV-1 protease, monitored by NMR in real-time, demonstra

204 present the first solution structure of the HIV-1 protease monomer spanning the region Phe1-Ala95 (P

205 A series of HIV-1 protease mutants has been designed in an effort to

206 In HIV-1 protease, mutations at I50 are associated with suc

207 etermined the three-dimensional structure of HIV-1 protease NL4-3 in complex with the potent protease

208 probabilistically modeling mutations in the HIV-1 protease or reverse transcriptase (RT) isolated fr

209 profiles against several common variants of HIV-1 protease over those of the other peptidomimetic in

210 In the other substrates of HIV-1 protease, P1 is usually either a hydrophobic or an

211 DK2, COX2, estrogen receptor, neuraminidase, HIV-1 protease, p38 MAP kinase, thrombin) have been asse

212 HIV-1 protease peptide substrate conjugated to magnetic

213 The conformational dynamics in the flaps of HIV-1 protease plays a crucial role in the mechanism of

214 Human immunodeficiency virus type 1 (HIV-1) protease plays a fundamental role in the maturati

215 In summary, nearly one-half of HIV-1 protease positions are under selective drug pressu

216 te analogs maintain high binding affinity to HIV-1 protease, potent antiretroviral activity, and unli

217 forms strong hydrogen-bond-interactions with HIV-1 protease (PR) active-site amino acids and is bulki

218 res of UIC-94017 in complexes with wild-type HIV-1 protease (PR) and mutant proteases PR(V82A) and PR

219 The crystal structures of the wild-type HIV-1 protease (PR) and the two resistant variants, PR(V

220 An extremely drug resistant mutant of HIV-1 protease (PR) bearing 20 mutations (PR20) has been

221 Extreme drug resistant mutant of HIV-1 protease (PR) bearing 20 mutations (PR20) has been

222 The mature HIV-1 protease (PR) bearing the L76V drug resistance mut

223 unavir) is a promising clinical inhibitor of HIV-1 protease (PR) for treatment of drug resistant HIV/

224 ent new antiviral inhibitor GRL-98065 (1) of HIV-1 protease (PR) has been studied with PR variants co

225 w antiviral inhibitor TMC-114 (UIC-94017) of HIV-1 protease (PR) has been studied with three PR varia

226 t each P1 position in Gag, using recombinant HIV-1 protease (PR) in an in vitro processing reaction o

227 GRL-02031 (1) is an HIV-1 protease (PR) inhibitor containing a novel P1' (R)

228 urrent Food and Drug Administration-approved HIV-1 protease (PR) inhibitors drives the need to unders

229 The successful development of a number of HIV-1 protease (PR) inhibitors for the treatment of AIDS

230 The HIV-1 protease (PR) is a 99-amino-acid enzyme that is tr

231 V-1) Gag and Gag-Pro-Pol polyproteins by the HIV-1 protease (PR) is essential for the production of i

232 HIV-1 protease (PR) is the target for several important

233 The HIV-1 protease (PR) is translated as part of GagPol and

234 -0519 (1) is a potent antiviral inhibitor of HIV-1 protease (PR) possessing tris-tetrahydrofuran (tri

235 the Gag and Gag-Pro-Pol polyproteins by the HIV-1 protease (PR) remain obscure.

236 Mutations in HIV-1 protease (PR) that produce resistance to antiviral

237 pol polyprotein placed in the active site of HIV-1 protease (PR) with an open flap conformation.

238 ree enzymes essential for viral replication: HIV-1 protease (PR), HIV-1 reverse transcriptase (RT) an

239 HIV-1 protease (PR), reverse transcriptase (RT), and int

240 closely in the active, dimeric structure of HIV-1 protease (PR).

241 f a novel imaging probe that is specific for HIV-1 protease (PR).

242 ld and evaluated their antidimer activity on HIV-1 protease (PR).

243 ld-type human immunodeficiency virus type 1 (HIV-1) protease (PR) and resistant mutants PR(L24I), PR(

244 Human immunodeficiency virus type 1 (HIV-1) protease (PR) and reverse transcriptase (RT) gene

245 The human immunodeficiency virus 1 (HIV-1) protease (PR) is an aspartyl protease essential f

246 The human immunodeficiency virus type 1 (HIV-1) protease (PR) makes five obligatory cleavages in

247 Human immunodeficiency virus type 1 (HIV-1) protease (PR) permits viral maturation by process

248 e show that the CE-CBA platform can identify HIV-1 protease present in cellular extractions and facil

249 We applied this approach to the HIV-1 protease (pro) gene to view the distribution of se

250 HIV-1 protease processes the Gag and Gag-Pol polyprotein

251 Human immunodeficiency virus type 1 (HIV-1) protease processes and cleaves the Gag and Gag-Po

252 High-purity homodimeric HIV-1 protease protein was obtained in excellent yield a

253 o most potent inhibitors in complex with the HIV-1 protease provided valuable information on the inte

254 compounds cocrystallized with the wild-type HIV-1 protease provided valuable information on the inte

255 IV) and human immunodeficiency virus type 1 (HIV-1) proteases (PRs) share only 23% amino acid identit

256 l to predict the tolerated sequence space of HIV-1 protease reachable by single mutations.

257 An HIV-1 protease recognition sequence is inserted into one

258 group-specific antigen (Gag) polyprotein by HIV-1 protease represents the critical first step in the

259 high resolution X-ray structure of 26-bound HIV-1 protease revealed important molecular insight into

260 olution X-ray crystal structure of 16a-bound HIV-1 protease revealed important molecular insights int

261 -ligand X-ray crystal structure of 19b-bound HIV-1 protease revealed that the P1'-pyrrolidinone heter

262 115,118 human immunodeficiency virus type 1 (HIV-1) protease, reverse transcriptase, and integrase se

263 Mutations in HIV-1 protease selected under the pressure of protease i

264 Drug resistance mutations in HIV-1 protease selectively alter inhibitor binding witho

265 HIV-1 protease sequences from patients subjected to diff

266 the observed variability in more than 50,000 HIV-1 protease sequences, one of the most comprehensive

267 We demonstrate that HIV-1 protease specifically cleaves procaspase 8 to crea

268 are influenced by mutations at residue 50 in HIV-1 protease, structural and binding thermodynamics st

269 those residues differentiated in the various HIV-1 protease subtypes, shortly referred to as the phyl

270 ized a multiple-drug-resistant mutant of the HIV-1 protease that affects indinavir, nelfinavir, saqui

271 conformational dynamics within the flaps of HIV-1 protease that form the lid over the catalytic clef

272 , all-atom molecular dynamics simulations of HIV-1 protease that sample large conformational changes

273 complex Gag polypeptide proteolysis than the HIV-1 protease, thus hypothetically generating slightly

274 We used unliganded HIV-1 protease to develop and validate this method.

275 ynthesis of unique chemical analogues of the HIV-1 protease to further elucidate the molecular basis

276 ed the critical self-association of immature HIV-1 protease to its extended amino-terminal recognitio

277 ble structural model for the adaptability of HIV-1 protease to recognize substrates in the presence o

278 e ability of human immunodeficiency virus-1 (HIV-1) protease to develop mutations that confer multi-d

279 However, the HIV-1 protease transition state has not been previously

280 o X-ray structures of trypsin, thrombin, and HIV-1-protease, using protein structures bound to severa

281 nal ensemble shifts in a multidrug resistant HIV-1 protease variant, MDR769, are characterized by sit

282 udy, we report two crystal structures of two HIV-1 protease variants bound with their corresponding n

283 clinically relevant panel of drug-resistant HIV-1 protease variants, losing no more than 6-13-fold a

284 ructures of complexes of atazanavir with two HIV-1 protease variants, namely, (i) an enzyme optimized

285 APV or DRV binds with HIV-1 protease via both hydrophobic and hydrogen bonding

286 ce regions were prepared; all four inhibited HIV-1 protease via perturbation of dimerization.

287 A fluorogenic substrate for HIV-1 protease was designed and used as the basis for a

288 n-ligand X-ray crystal structure of 3d-bound HIV-1 protease was determined.

289 d the drug-resistant V82F/I84V mutant of the HIV-1 protease was investigated by molecular dynamics (M

290 Recombinant HIV-1 protease was obtained from bacteria grown on a 98%

291 as that had previously been shown to inhibit HIV-1 protease was tested.

292 In the case of the HIV-1 protease, we reported earlier that proteases from

293 binding of clinical inhibitors to resistant HIV-1 protease, we used room-temperature joint X-ray/neu

294 ally designed to inhibit the closely related HIV-1 protease were evaluated as privileged structures a

295 nal interface residues (96-99) of the mature HIV-1 protease were shown to be essential for dimerizati

296 -decoy recognition for CHARMm in the case of HIV-1 protease, whereas DrugScore and ChemScore, as well

297 duces apoptosis and is a specific product of HIV-1 protease which may contribute to death of HIV-1-in

298 is remarkable - particularly in the case of HIV-1 protease, which has a large conformational change

299 ystal structures of drug resistant I50V/A71V HIV-1 protease with p1-p6 substrates bearing coevolved m

300 we report the enzymatic characterization of HIV-1 proteases with sequences found in drug-naive Ugand