ライフサイエンスコーパス: HIV protease

1 hods were used to study the role of Thr80 in HIV protease.

2 anisms that are independent of inhibition of HIV protease.

3 inked peptides derived from the interface of HIV protease.

4 ew inhibitors predicted to be active against HIV protease.

5 independent from its ability to inhibit the HIV protease.

6 olymers substitute for salts as effectors of HIV protease.

7 se, inosine monophosphate dehydrogenase, and HIV protease.

8 egy to kill HIV-infected cells by exploiting HIV protease.

9 ffinity of fullerene-based inhibitors of the HIV protease.

10 a small molecule template for inhibition of HIV protease.

11 offset the inhibitor resistance acquired by HIV protease.

12 r targets of antimicrobial drugs such as the HIV protease.

13 ch to build potent active site inhibitors of HIV protease.

14 predicting the cleavage sites in proteins by HIV protease.

15 t potent integrase inhibitors also inhibited HIV protease.

16 d, have proven to be effective inhibitors of HIV protease.

17 eir activity, such as the proteasome and the HIV protease.

18 roduced from p66 by C-terminal truncation by HIV protease.

19 d Arg-8 side chain in the S1'-subsite of the HIV protease.

20 o analyze the association of amprenavir with HIV protease.

21 eveloped to combat the resistant variants of HIV protease.

22 activity as a function of the inhibition of HIV-protease.

23 loop in conferring inhibitor specificity in HIV proteases.

24 developed for human immunodeficiency viral (HIV) protease.

25 rocaspase 8 by human immunodeficiency virus (HIV) protease.

26 to predict the cleavability of a peptide by HIV protease?

27 Lastly, the cell rounds up and HIV protease activation induces diffuse fluorescence thr

28 ing of the hypothetical derivatives into the HIV protease active site and assessment of the model com

29 tion) revealed extensive interactions in the HIV protease active site including strong hydrogen bondi

30 ization of hydrophobic interactions with the HIV protease active site produced ritonavir, with excell

31 pecifically to interact with the backbone of HIV protease active site to combat drug resistance.

32 sistant clones to establish how variation in HIV protease affects CARD8 activation.

33 We have determined a minimal epitope of HIV protease, amino acids 76 to 84, towards which a CD8(

34 HIV protease, an aspartyl protease crucial to the life c

35 volves a fluorogenic continuous assay of the HIV protease, analyzed by the differential-equation orie

36 et provides a nearly complete mutagenesis of HIV protease and enables the calculation of statisticall

37 h NSC 158393 derivatives that inhibited both HIV protease and integrase, and the most potent integras

38 excellent antiviral efficacy against mutant HIV protease and resistant HIV strains.

39 Since 2006, HIV protease and reverse transcriptase gene (pol) sequen

40 nzyme will complement the therapeutic use of HIV protease and reverse transcriptase inhibitors.

41 o discovered 163 new amino acid mutations in HIV protease and RT that are strong candidates for drug

42 Substrate kinetics of the HIV protease and the unfolding kinetics of UMP/CMP kinas

43 induced injury via mechanisms independent of HIV protease and viral replication.

44 alues (antiviral resistance) for each of the HIV proteases and the viruses containing the identical e

45 ted protease inhibitors, including aspartic (HIV protease) and metallo (ACE and thermolysin) protease

46 e study displayed decent binding affinity to HIV protease, and several compounds were shown to posses

47 tive importance and roles of each subsite in HIV protease, and the constraints on robust inhibitor de

48 f actin filaments, toward the functioning of HIV protease, and toward the process of angiogenesis.

49 vity in cell culture, were selective for the HIV protease, and were orally available in three animal

50 tion of HIV-1 reverse transcriptase (RT) and HIV protease are effective mechanisms for anti-retrovira

51 analysis is that inhibitor-resistant mutant HIV proteases are very unlikely to contribute to viral v

52 A series of novel aminodiol inhibitors of HIV protease based on the lead compound 1 with structura

53 Purified bcl-2 is cleaved by HIV protease between phenylalanine 112 and alanine 113.

54 , however, produces compounds with excellent HIV protease binding affinity and antiviral activity.

55 ing the structure of compound 3 bound to the HIV protease, bis tertiary amide inhibitor 9 was designe

56 ery similar to human immunodeficiency virus (HIV) protease but exhibits distinct substrate and inhibi

57 on-derived S(rel)(2) values in ubiquitin and HIV protease, but also identify a fraction of residues f

58 c cytochalasin L-696,474 (2, an inhibitor of HIV protease) by using common precursors.

59 been developed to explore the specificity of HIV protease cleavage activity.

60 called a sum-product function for extracting HIV protease cleavage discriminant rules using genetic p

61 ave noncleavable alterations surrounding the HIV protease cleavage site.

62 When applied to the prediction of HIV protease cleavage sites, the new method has shown a

63 Trypsin cleavage sites and the prediction of HIV protease cleavage sites.

64 studying and understanding the mechanism of HIV protease cleavage specification is critical.

65 Using these HTRF detection conditions, HIV protease cleaved the substrate in 50 mM NaOAc, 150 m

66 y viral proteins, including the finding that HIV protease cleaves eIF3d, a subunit of eukaryotic tran

67 Our previous studies showed that HIV protease cleaves the host protein procaspase 8 to ge

68 hange when the human immunodeficiency virus (HIV) protease cleaves it free from the Pr55(Gag) polypro

69 ave shown that human immunodeficiency virus (HIV) protease cleaves procaspase 8 to a fragment, termed

70 The crystal structure of phenprocoumon/HIV protease complex initiated a structure-based design

71 stal structure of the 4-hydroxy-2-pyrone III/HIV protease complex, a series of analogues incorporatin

72 ing the crystal structures of three chimeric HIV proteases complexed with SB203386, a tripeptide anal

73 Igg-binding domain of protein G (GB3) and in HIV protease, complexed with the inhibitor DMP323.

74 the threat of human immunodeficiency virus (HIV) protease drug resistance still exists, there will b

75 cted based on the structural features of the HIV protease-drug inhibitor complex.

76 A number of cytokines and the HIV Protease, for example, dimerize through beta-sheet m

77 s can result in high-affinity ligands of the HIV protease, for which they are highly complementary in

78 sures on the same amino acid sequence of the HIV protease gene and, thus, can influence viral sequenc

79 Analysis of the HIV protease gene from the plasma of HIV-infected patien

80 ugh characterizing location contributions to HIV protease gene region differences associated with a p

81 olution of the human immunodeficiency virus (HIV) protease gene (pro), we analyzed a database of 213

82 ostintegration HIV replication can result in HIV protease generation of Casp8p41, which activates BAK

83 was constructed to improve the separation of HIV protease genes varying in sequence at 12 codons asso

84 ile the role of drug resistance mutations in HIV protease has been studied comprehensively, mutations

85 specificity in human immunodeficiency virus (HIV) protease has been investigated by determining the c

86 eries of potent nonpeptide inhibitors of the HIV protease have been identified.

87 The structure of HIV protease (HIV Pr) bound to JE-2147 (also named AG177

88 y resistant to inhibitors of targets such as HIV protease (HIV PR).

89 described for a novel series of nonpeptidic HIV protease (HIV Pr)inhibitors.

90 on of the design of the cyclic urea class of HIV protease (HIVPR) inhibitors suggests a general appro

91 uses small inhibitory molecules that target HIV protease; however, the emergence of resistant HIV st

92 e properties first ascribed to inhibition of HIV protease; however, they have pleiotropic antitumour

93 e energy contribution of each residue in the HIV protease in binding to one of its substrates and to

94 esign antihypertensives and the structure of HIV protease in design of AIDS antivirals.

95 catalytic efficiency of mutant and wild type HIV protease in the presence or absence of inhibitors.

96 The role of HIV protease in viral replication has made it a signific

97 of the human immunodeficiency virus type 1 (HIV) protease in cultured cells leads to apoptosis, prec

98 Order-disorder changes in HIV protease indicate a mechanism of entropy compensatio

99 mides has been synthesized and evaluated for HIV protease inhibition and antiviral activity.

100 sed in vitro and in vivo models to show that HIV protease inhibitor (PI) class ARVs induced neuronal

101 GS-8374 is a potent HIV protease inhibitor (PI) with a unique diethyl-phosph

102 an allophenylnorstatine-containing dipeptide HIV protease inhibitor (PI), which is potent against a w

103 fragment to fill S1' and S2' afforded potent HIV protease inhibitor 49 [IC50 = 10 nM, 3-[(2-tert-buty

104 are amino alcohol 1, the core portion of the HIV protease inhibitor A-792611, in 46% yield from pheny

105 The HIV protease inhibitor amprenavir inhibits calpain activ

106 ed that peptidomimetic FISLE-412,1 a reduced HIV protease inhibitor analogue, was well-tolerated, alt

107 The HIV protease inhibitor class of antiretroviral drug caus

108 or the progeria-like side effects of certain HIV protease inhibitor drugs, but also highlight new app

109 ease, monofluorinated analogues of the Merck HIV protease inhibitor indinavir, are described.

110 ing to the potent and clinically efficacious HIV protease inhibitor ritonavir are described.

111 or inhibition of glucose transport with the HIV protease inhibitor ritonavir elicited growth arrest

112 lines and primary cells by the FDA-approved HIV protease inhibitor ritonavir, which exerts a selecti

113 The HIV protease inhibitor ritonavir, which inhibits calpain

114 Ritonavir is a HIV protease inhibitor routinely prescribed to HIV patie

115 enzyl P1/P1' moiety of the cyclic urea based HIV protease inhibitor series.

116 uct FK506, we have synthetically modified an HIV protease inhibitor such that it acquires high affini

117 We examined the effect of nelfinavir, an HIV protease inhibitor that inhibits Akt signaling, on V

118 hat it is an important regulator involved in HIV protease inhibitor toxicity and host-microbial patho

119 uran, a high-affinity nonpeptidal ligand for HIV protease inhibitor UIC-94017, is described.

120 d UIC-94017 (TMC-114) is a second-generation HIV protease inhibitor with improved pharmacokinetics th

121 with three probes (a thrombin inhibitor, an HIV protease inhibitor, and a model for angiotensin II).

122 of (2R)-indandiol, a chiral precursor of the HIV protease inhibitor, Crixivan.

123 We demonstrate that the HIV protease inhibitor, indinavir, dramatically inhibits

124 Notably, Indinavir; an HIV protease inhibitor, may be effective in reducing the

125 The molecular mechanisms of action of a HIV protease inhibitor, ritonavir, on hepatic function w

126 a Merck compound synthesized as a potential HIV protease inhibitor, was investigated using recombina

127 Starting from palinavir (1), our lead HIV protease inhibitor, we have discovered a new series

128 type 2 diabetes mellitus, and nelfinavir, an HIV protease inhibitor, when used alone or in combinatio

129 t role in the gender differences observed in HIV protease inhibitor-induced atherosclerosis.

130 er, the cellular/molecular mechanisms of the HIV protease inhibitor-induced lipid dysregulation and a

131 nants of CARD8 sensing, we tested a panel of HIV protease inhibitor-resistant clones to establish how

132 s a once-daily human immunodeficiency virus (HIV) protease inhibitor (PI) shown to be effective and w

133 a nonpeptidic human immunodeficiency virus (HIV) protease inhibitor (PI), containing 3(R),3a(S),6a(R

134 Human immunodeficiency virus (HIV) protease inhibitor (PI)-induced adverse effects hav

135 Ritonavir is a human immunodeficiency virus (HIV) protease inhibitor and an inhibitor of cytochrome P

136 poorly soluble human immunodeficiency virus (HIV) protease inhibitor based upon in vivo test results.

137 trate that the human immunodeficiency virus (HIV) protease inhibitor ritonavir binds SXR and activate

138 anism by which human immunodeficiency virus (HIV) protease inhibitor therapy adversely induces lipody

139 mprenavir is a human immunodeficiency virus (HIV) protease inhibitor with a favorable pharmacokinetic

140 f lopinavir, a human immunodeficiency virus (HIV) protease inhibitor, coformulated with ritonavir as

141 macologically recapitulated by combining the HIV-protease inhibitor nelfinavir with ISRIB, an experim

142 we tested the hypothesis that indinavir, an HIV-protease inhibitor, directly induces insulin resista

143 ed the safety and efficacy of saquinavir, an HIV-protease inhibitor, given with one or two nucleoside

144 cess an important synthetic precursor to the HIV-protease inhibitor, saquinavir, by formation of an N

145 Crystallographic studies of HIV protease-inhibitor complexes help explain the perhap

146 inhibitors, utilizing crystal structures of HIV protease/inhibitor complexes, provided a rational ba

147 HIV protease inhibitors (HIV PI) are a class of antiretr

148 HIV protease inhibitors (HIV-PIs) are key components of

149 HIV protease inhibitors (HIV-PIs) target the HIV asparty

150 Inhibitors of the HIV aspartyl protease [HIV protease inhibitors (HIV-PIs)] are the cornerstone o

151 The HIV protease inhibitors (HPI) amprenavir, nelfinavir, an

152 and diabetes are recognized side effects of HIV protease inhibitors (HPIs), suggesting that these ag

153 HIV protease inhibitors (PIs) acutely and reversibly inh

154 First-generation HIV protease inhibitors (PIs) alter proteasome activity,

155 Pharmacologic HIV protease inhibitors (PIs) and structurally related o

156 While drugs like HIV protease inhibitors (PIs) and trimethoprim-sulfameth

157 HIV protease inhibitors (PIs) avert apoptosis in part by

158 The use of HIV protease inhibitors (PIs) has been associated with s

159 , and oral administration of prodrugs of the HIV protease inhibitors (PIs) lopinavir and ritonavir.

160 This study examined the effects of HIV protease inhibitors (PIs) on bone resorption, bone f

161 In this article, we show that HIV protease inhibitors (PIs) prescribed to HIV-infected

162 tiretroviral therapy (HAART), which includes HIV protease inhibitors (PIs), has been associated with

163 drug classes such as nucleoside analogs and HIV protease inhibitors (PIs), has increased HIV-patient

164 , which appears to be exacerbated by certain HIV protease inhibitors (PIs).

165 s study, we demonstrate that three different HIV protease inhibitors (ritonavir, indinavir, and ataza

166 daily 10 mg/kg intraperitoneal injection of HIV protease inhibitors (ritonavir, lopinavir/ritonavir

167 inal tyrosine peptide aldehydes based on the HIV protease inhibitors (S)-MAPI and GE 20372 A.

168 HIV protease inhibitors acutely block glucose transporte

169 iseases like atherosclerosis it appears that HIV protease inhibitors affect the cardiovascular system

170 We also resolved binding of zinc, lipids and HIV protease inhibitors and showed that drug binding blo

171 poor pharmacokinetic properties of existing HIV protease inhibitors and, potentially, other drug cla

172 HIV protease inhibitors are a key component of anti-retr

173 tructure-based design and synthesis of novel HIV protease inhibitors are described.

174 nd synthesis of a series of novel nonpeptide HIV protease inhibitors are described.

175 ation of a series of nonpeptidic macrocyclic HIV protease inhibitors are described.

176 Interestingly, HIV protease inhibitors are distinct from previously kno

177 HIV protease inhibitors are thus a new class of anticanc

178 We conclude that HIV protease inhibitors as a class are capable of select

179 or the discovery of more potent non-peptidic HIV protease inhibitors as potential therapeutic agents

180 s an illustration, the core structure of the HIV protease inhibitors DMP 323 and DMP 450 has been pre

181 ination antiretroviral therapy that includes HIV protease inhibitors experience atrophy of peripheral

182 rying mutations known to cause resistance to HIV protease inhibitors faithfully recapitulated the rep

183 Since HIV protease inhibitors have "off target" cellular effec

184 d rapid biliary excretion of peptide-derived HIV protease inhibitors have limited their utility as po

185 he present study, we examined the effects of HIV protease inhibitors in female LDL-R null mice.

186 cal approaches used to determine the role of HIV protease inhibitors in the development of cardiovasc

187 bitors, the AlphaLISA assay confirmed all 11 HIV protease inhibitors in the library capable of suppre

188 trials have established the critical role of HIV protease inhibitors in the treatment of acquired imm

189 block for several clinical and experimental HIV protease inhibitors including the highly important d

190 sity lipoprotein receptor (LDL-R) null mice, HIV protease inhibitors induce atherosclerotic lesions a

191 The clinical use of HIV protease inhibitors is associated with insulin resis

192 Treatment of patients infected with HIV with HIV protease inhibitors is unfortunately associated with

193 In vitro and in vivo data suggest that the HIV protease inhibitors lopinavir/ritonavir may have pot

194 Poor adherence to HIV protease inhibitors may compromise the effectiveness

195 iscuss possible molecular mechanisms whereby HIV protease inhibitors may promote atherogenesis.

196 In conclusion, HIV protease inhibitors may, by blocking the caspase-dep

197 rrently available data strongly suggest that HIV protease inhibitors negatively impact the cardiovasc

198 We investigated the effects of HIV protease inhibitors on adipogenesis and adipocyte su

199 on mass spectrometry to study the effects of HIV protease inhibitors on the human zinc metalloproteas

200 d screening program to discover non-peptidic HIV protease inhibitors previously identified compound I

201 rovide possible cellular mechanisms by which HIV protease inhibitors promote atherosclerosis and card

202 Preclinically, HIV protease inhibitors radiosensitize tumors with activ

203 lues for inhibition of HIV-1 protease by the HIV protease inhibitors ranged from 0.24 nM to 1.0 micro

204 esistant HIV strains, the development of new HIV protease inhibitors remains a high priority for the

205 The design of new HIV protease inhibitors requires an improved understandi

206 Finally, the HIV protease inhibitors saquinavir and ritonavir were po

207 Antiretroviral regimens containing HIV protease inhibitors suppress viremia in HIV-infected

208 , in the presence of dilated cardiomyopathy, HIV protease inhibitors that impair glucose transport in

209 The potential for HIV protease inhibitors to contribute to or exacerbate c

210 A series of symmetry-based HIV protease inhibitors was designed and synthesized.

211 HIV protease inhibitors were developed in the early 1990

212 Several HIV protease inhibitors were found either to inhibit pre

213 rapeutic concentrations (5-15 microM), these HIV protease inhibitors were found to increase the level

214 d from S-aryl-D-cysteine proved to be potent HIV protease inhibitors which also exhibited potent whol

215 ided an example of a promising new series of HIV protease inhibitors with significantly improved enzy

216 an immunodeficiency virus (HIV) treated with HIV protease inhibitors, a complication develops that re

217 . 2c) were identified as potent, nonpeptidic HIV protease inhibitors, but these compounds lacked sign

218 ding lupus medications, thrombin inhibitors, HIV protease inhibitors, DNA gyrase inhibitors and many

219 ause for the loss of sensitivity toward many HIV protease inhibitors, including our first-generation

220 chemotherapeutic agents, antipsychotics, and HIV protease inhibitors, into and out of the central ner

221 anti-retroviral therapies, which incorporate HIV protease inhibitors, resolve many AIDS-defining illn

222 chiral building blocks for the synthesis of HIV protease inhibitors, such as atazanavir and darunavi

223 e (HAPA) transition-state isostere series of HIV protease inhibitors, which initially resulted in the

224 >4-fold in the presence of ritonavir-boosted HIV protease inhibitors, while pibrentasvir concentratio

225 template provided a series of highly potent HIV protease inhibitors, with structure-activity relatio

226 e and robust classification of resistance to HIV protease inhibitors.

227 ease in HIV-1 infected patients treated with HIV protease inhibitors.

228 atives could have potential use as effective HIV protease inhibitors.

229 on glucose transport were observed for other HIV protease inhibitors.

230 d the urgent need for a second generation of HIV protease inhibitors.

231 (3)-P(2) position of hydroxyethylamine-based HIV protease inhibitors.

232 al protease increase the binding affinity of HIV protease inhibitors.

233 of HIV with resistance to a wide variety of HIV protease inhibitors.

234 now being used and the more frequent use of HIV protease inhibitors.

235 useful for designing specific and efficient HIV protease inhibitors.

236 10 pi-aromatic system of Ro 31-8959 class of HIV protease inhibitors.

237 roviral drugs, such as efavirenz and boosted HIV protease inhibitors.

238 Compound 2a is a key intermediate toward HIV protease inhibitors.

239 ituent effects to the analysis and design of HIV protease inhibitors.

240 of epi-aortic lesions in patients receiving HIV protease inhibitors.

241 Human immunodeficiency virus (HIV) protease inhibitors (HIV PIs) are the core componen

242 Human immunodeficiency virus (HIV) protease inhibitors (PIs) act as reversible noncomp

243 onstrated that human immunodeficiency virus (HIV) protease inhibitors (PIs) exert inhibitory effects

244 Human immunodeficiency virus (HIV) protease inhibitors (PIs) have been used successful

245 Human immunodeficiency virus (HIV) protease inhibitors (PIs) recently have been report

246 efficacy of 5 human immunodeficiency virus (HIV) protease inhibitors (PIs) was examined by the effec

247 (RTV)-boosted human immunodeficiency virus (HIV) protease inhibitors are coadministered in healthy v

248 Human immunodeficiency virus (HIV) protease inhibitors have been successfully used in

249 fectiveness of human immunodeficiency virus (HIV) protease inhibitors in acquired immunodeficiency sy

250 of non-peptide human immunodeficiency virus (HIV) protease inhibitors in short analysis time and auto

251 Human immunodeficiency virus (HIV) protease inhibitors show activity against Plasmodiu

252 several potent human immunodeficiency virus (HIV) protease inhibitors such as LY289612.

253 patients with human immunodeficiency virus (HIV) protease inhibitors such as ritonavir can result in

254 ivity of three human immunodeficiency virus (HIV) protease inhibitors was investigated in human prima

255 e made the intriguing discovery that several HIV-protease inhibitors can function as decoy antigens t

256 Computational modeling revealed that HIV-protease inhibitors comprised structural features pr

257 le resistance at entry became susceptible to HIV-protease inhibitors within 16 weeks after the discon

258 reviously identified as a lead template with HIV protease inhibitory activity.

259 HIV protease is a primary target for the design of viros

260 en the geometric mean efficiency of a mutant HIV protease is less than 61% of the wild type activity

261 mpounds with superb binding affinity for the HIV protease (Ki values in the 10-50 pM range).

262 IV-1 protease bound to SB203386 reveals that HIV protease ligand specificity is imparted by residues

263 tural basis of human immunodeficiency virus (HIV) protease ligand specificity, we have crystallized a

264 f CD4 T cells that replicate HIV can involve HIV protease-mediated cleavage of procaspase 8 to genera

265 to a series of diastereomeric inhibitors of HIV protease, monofluorinated analogues of the Merck HIV

266 ion suggested a Kd of 9.4 +/- 2.7 nM for the HIV protease monomer-dimer equilibrium.

267 he ability to predict the drug resistance of HIV protease mutants may be useful in developing more ef

268 ide a rational context for understanding why HIV protease mutations that arise in drug resistant stra

269 were also found to decrease the activity of HIV protease near neutral pH values, while incorporating

270 The peptides selected were substrates of HIV protease or of avian sarcoma virus protease, both of

271 mice, which develop HIVAN in the absence of HIV protease or reverse transcriptase.

272 ped to handle genotype-phenotype datasets of HIV protease (PR) and reverse transcriptase (RT).

273 ng variants of human immunodeficiency virus (HIV) protease (PR) monomers.

274 Cleavage of the doubly labeled substrate by HIV protease precludes complex formation, thereby decrea

275 polyprotein by human immunodeficiency virus (HIV) protease present the virus with severe limitations

276 usly unappreciated interpatient variation in HIV protease processing efficiency that impacts viral in

277 The overall catalytic efficiency of a mutant HIV protease relative to the wild type enzyme is given b

278 sp3 becomes processed into an active form by HIV protease, resulting in apoptosis of the infected cel

279 cessful molecular modeling of inhibitors for HIV protease suggests that this may be an attainable obj

280 s indicate that pepsin is a better model for HIV protease than for avian leukemia virus protease.

281 tent peptide (G12: GIXVSL; X=pBzF) inhibited HIV protease through the formation of a covalent Schiff

282 the reduction in binding affinity to the MDR HIV protease, TMC114 still binds with an affinity that i

283 For HIV protease, two separate crystal structures that diffe

284 subsequently used to evolve an inhibitor of HIV protease using a selection based on cellular viabili

285 ree energies between different dimers of the HIV protease using molecular dynamics and a continuum mo

286 ran-2-one) was modeled in the active site of HIV protease utilizing a similar binding mode found for

287 the isolation and DNA sequencing of minority HIV protease variants is presented here.

288 ne cassettes appeared to be reduced when the HIV protease was active.

289 ed as any active site or primary mutation in HIV protease, was detected in virus isolates from 51 lop

290 hydro-4-hydroxy-2-pyrones complexed with the HIV protease were also determined to provide better unde

291 and glycine conformations is exemplified by HIV protease, where different inhibitors are associated

292 eine sulfone, 17c, was a 3.5 nM inhibitor of HIV protease which inhibited the spread of virus in MT4

293 ic resistance required multiple mutations in HIV protease, which emerged subsequently in an ordered,

294 viral particle as well as the activation of HIV protease, which is needed to cleave the polyproteins

295 region of the human immunodeficiency virus (HIV) protease, which houses the active site of the enzym

296 ce in searching for the proper inhibitors of HIV protease will be greatly expedited if one can find a

297 owledge of the polyprotein cleavage sites by HIV protease will refine our understanding of its specif

298 es culminated in compound VI, which inhibits HIV protease with a Ki value of 8 pM and shows an IC90 v

299 s have been shown to be potent inhibitors of HIV protease with Ki < 0.050 nM and IC90 < 20 nM for vir

300 pic changes in human immunodeficiency virus (HIV) protease with reduced in vitro susceptibility to th