ライフサイエンスコーパス: HIV-1 protease

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

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

3 less efficient cleavage of the R peptide by 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 he p66 homodimer precursor is susceptible to HIV-1 protease.

9 substrate envelope, to develop inhibitors of 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 group-specific antigen (Gag) polyprotein by HIV-1 protease.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

42 (2 A or better) X-ray crystal structures of HIV-1 protease and compare the effects of different inhi

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

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

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

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

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

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

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

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

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

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

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

54 0.83 and 0.77 for data sets of experimental HIV-1 protease and T4 lysozyme mutants, respectively.

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

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

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

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

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

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

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

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

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

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

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

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

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

68 ng simulation has been carried out using the HIV-1 protease as receptor, thus paving the way to study

69 e a useful tool for drug discovery targeting HIV-1 protease autoprocessing and for quantification of

70 HIV-1 protease autoprocessing liberates the free mature

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

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

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

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

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

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

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

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

79 Further proteolytic attack by HIV-1 protease cleaves the ribonuclease H (RNase H) doma

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

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

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

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

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

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

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

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

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

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

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

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

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

93 -15-membered cycloamides and evaluated their HIV-1 protease enzyme inhibitory and antiviral activitie

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

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

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

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

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

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

100 and either prior to or following excision by HIV-1 protease forms a 66 kDa chain (p66) homodimer prec

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

129 Phosphate and amino acid prodrugs of the HIV-1 protease inhibitor (PI) atazanavir (1) were prepar

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

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

132 nantiomer (-)-6 has been converted to potent HIV-1 protease inhibitor 3.

133 is a key subunit of darunavir, a widely used HIV-1 protease inhibitor drug for the treatment of HIV/A

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

135 higher body mass index with higher ATX, and HIV-1 protease inhibitor use with higher sCD14 levels.

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

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

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

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

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

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

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

143 sis, and X-ray structural analysis of hybrid HIV-1 protease inhibitors (PIs) containing bis-tetrahydr

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

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

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

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

148 HIV-1 protease inhibitors (PIs), such as darunavir (DRV)

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

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

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

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

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

154 HIV-1 protease inhibitors are essential components of pr

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

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

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

158 as used to improve the resistance profile of HIV-1 protease inhibitors by optimizing hydrogen bonding

159 HIV-1 protease inhibitors continue to play an important

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

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

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

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

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

165 defective viral particles by treatment with HIV-1 protease inhibitors or by genetic manipulation of

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

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

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

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

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

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

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

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

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

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

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

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

178 e Gag-protein of HIV-1 variants resistant to HIV-1 protease inhibitors.

179 ty P2 ligands for a variety of highly potent HIV-1 protease inhibitors.

180 uences on the long-term viability of current 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 ed for characterizing the next generation of HIV-1 protease inhibitors.

184 vide insights for optimizing these promising HIV-1 protease inhibitors.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

211 HIV-1 protease peptide substrate conjugated to magnetic

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

233 -0519 (1) is a potent antiviral inhibitor of HIV-1 protease (PR) possessing tris-tetrahydrofuran (tri

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

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

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

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

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

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

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 cleavage between CA and SP1 catalyzed by the 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 stal structures of inhibitors with wild-type HIV-1 protease revealed that the bis-THF moiety retained

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

263 115,118 human immunodeficiency virus type 1 (HIV-1) protease, reverse transcriptase, and integrase se

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

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

266 HIV-1 protease sequences from patients subjected to diff

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

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

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

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

271 proteolytic cleavage of precursor p66/p66 by HIV-1 protease, suggesting that it stabilizes the produc

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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