ABT-538 is a potent inhibitor of human immunodeficiency virus protease and has high oral bioavailability in humans
about
Potencies of human immunodeficiency virus protease inhibitors in vitro against Plasmodium falciparum and in vivo against murine malariaElucidation of crystal form diversity of the HIV protease inhibitor ritonavir by high-throughput crystallizationNeuroprotection mediated by inhibition of calpain during acute viral encephalitisUnderstanding the mechanism of cytochrome P450 3A4: recent advances and remaining problemsViability of a drug-resistant human immunodeficiency virus type 1 protease variant: structural insights for better antiviral therapyDesign and Synthesis of HIV-1 Protease Inhibitors Incorporating Oxazolidinones as P2/P2‘ Ligands in Pseudosymmetric Dipeptide IsosteresHIV-1 Protease Inhibitors from Inverse Design in the Substrate Envelope Exhibit Subnanomolar Binding to Drug-Resistant VariantsEvaluating the Substrate-Envelope Hypothesis: Structural Analysis of Novel HIV-1 Protease Inhibitors Designed To Be Robust against Drug ResistanceStructure and mechanism of the complex between cytochrome P4503A4 and ritonavirThe crystal structure of protease Sapp1p from Candida parapsilosis in complex with the HIV protease inhibitor ritonavirInteraction of human cytochrome P4503A4 with ritonavir analogsStructure of a G48H mutant of HIV-1 protease explains how glycine-48 replacements produce mutants resistant to inhibitor drugsMolecular recognition of cyclic urea HIV-1 protease inhibitorsExploring the active site of herpes simplex virus type-1 thymidine kinase by X-ray crystallography of complexes with aciclovir and other ligandsBMS-232632, a highly potent human immunodeficiency virus protease inhibitor that can be used in combination with other available antiretroviral agentsIn vitro resistance profile of the human immunodeficiency virus type 1 protease inhibitor BMS-232632Inhibition of human immunodeficiency virus type 1 transcription and replication by DNA sequence-selective plant lignansIn vitro selection and characterization of human immunodeficiency virus type 1 variants with increased resistance to ABT-378, a novel protease inhibitor.ABT-378, a highly potent inhibitor of the human immunodeficiency virus proteaseHuman immunodeficiency virus type 1 viral background plays a major role in development of resistance to protease inhibitorsSecond locus involved in human immunodeficiency virus type 1 resistance to protease inhibitorsAntiviral properties of palinavir, a potent inhibitor of the human immunodeficiency virus type 1 proteaseAntiviral activity of the dihydropyrone PNU-140690, a new nonpeptidic human immunodeficiency virus protease inhibitorIn vitro combination of PNU-140690, a human immunodeficiency virus type 1 protease inhibitor, with ritonavir against ritonavir-sensitive and -resistant clinical isolatesGenetic correlates of in vivo viral resistance to indinavir, a human immunodeficiency virus type 1 protease inhibitorOngoing trials in HIV protease inhibitors.The distribution of ligand-binding pockets around protein-protein interfaces suggests a general mechanism for pocket formation.Alteration of substrate and inhibitor specificity of feline immunodeficiency virus protease.Using the Tools and Resources of the RCSB Protein Data Bank.Computational study of the resistance shown by the subtype B/HIV-1 protease to currently known inhibitors.Liposome-mediated delivery of antiviral agents to human immunodeficiency virus-infected cells.Multidose pharmacokinetics of ritonavir and zidovudine in human immunodeficiency virus-infected patientsPharmacokinetic interaction between ritonavir and indinavir in healthy volunteersEffect of fluoxetine on pharmacokinetics of ritonavir.Identification of a key target sequence to block human immunodeficiency virus type 1 replication within the gag-pol transframe domain.Mechanism of the Association Pathways for a Pair of Fast and Slow Binding Ligands of HIV-1 Protease.How an inhibitor of the HIV-I protease modulates proteasome activity.Strength of hydrogen bond network takes crucial roles in the dissociation process of inhibitors from the HIV-1 protease binding pocket.HIV-1 protease inhibitors.Comparison of human immunodeficiency virus type 1 Pr55(Gag) and Pr160(Gag-pol) processing intermediates that accumulate in primary and transformed cells treated with peptidic and nonpeptidic protease inhibitors
P2860
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P2860
ABT-538 is a potent inhibitor of human immunodeficiency virus protease and has high oral bioavailability in humans
description
1995 nî lūn-bûn
@nan
1995 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի մարտին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
ABT-538 is a potent inhibitor ...... oral bioavailability in humans
@ast
ABT-538 is a potent inhibitor ...... oral bioavailability in humans
@en
ABT-538 is a potent inhibitor ...... oral bioavailability in humans
@nl
type
label
ABT-538 is a potent inhibitor ...... oral bioavailability in humans
@ast
ABT-538 is a potent inhibitor ...... oral bioavailability in humans
@en
ABT-538 is a potent inhibitor ...... oral bioavailability in humans
@nl
prefLabel
ABT-538 is a potent inhibitor ...... oral bioavailability in humans
@ast
ABT-538 is a potent inhibitor ...... oral bioavailability in humans
@en
ABT-538 is a potent inhibitor ...... oral bioavailability in humans
@nl
P2093
P2860
P3181
P356
P1476
ABT-538 is a potent inhibitor ...... oral bioavailability in humans
@en
P2093
C A Flentge
E McDonald
J F Denissen
S Vasavanonda
P2860
P304
P3181
P356
10.1073/PNAS.92.7.2484
P407
P577
1995-03-28T00:00:00Z