about
Bile pigments as HIV-1 protease inhibitors and their effects on HIV-1 viral maturation and infectivity in vitroVirus maturation as a new HIV-1 therapeutic targetMolecular mechanisms for the conversion of zymogens to active proteolytic enzymesA brief history of macromolecular crystallography, illustrated by a family tree and its Nobel fruitsInhibition of the HIV-1 and HIV-2 proteases by a monoclonal antibodyCrystal structure of an in vivo HIV-1 protease mutant in complex with saquinavir: Insights into the mechanisms of drug resistance1.9 A x-ray study shows closed flap conformation in crystals of tethered HIV-1 PRLack of synergy for inhibitors targeting a multi-drug-resistant HIV-1 proteaseViability of a drug-resistant human immunodeficiency virus type 1 protease variant: structural insights for better antiviral therapySolution structure of the mature HIV-1 protease monomer: insight into the tertiary fold and stability of a precursorCrystal Structure of Lysine Sulfonamide Inhibitor Reveals the Displacement of the Conserved Flap Water Molecule in Human Immunodeficiency Virus Type 1 ProteasePotent New Antiviral Compound Shows Similar Inhibition and Structural Interactions with Drug Resistant Mutants and Wild Type HIV-1 Protease †Effect of the Active Site D25N Mutation on the Structure, Stability, and Ligand Binding of the Mature HIV-1 ProteaseStructure of the unbound form of HIV-1 subtype A protease: comparison with unbound forms of proteases from other HIV subtypesCrystal Structures of Inhibitor Complexes of Human T-Cell Leukemia Virus (HTLV-1) ProteaseCrystal structure of XMRV protease differs from the structures of other retropepsinsSynthesis, X-ray Analysis, and Biological Evaluation of a New Class of Stereopure Lactam-Based HIV-1 Protease InhibitorsExtreme Entropy–Enthalpy Compensation in a Drug-Resistant Variant of HIV-1 ProteaseStructures of Darunavir-Resistant HIV-1 Protease Mutant Reveal Atypical Binding of Darunavir to Wide Open FlapsEffects of Hinge Region Natural Polymorphisms on Human Immunodeficiency Virus-1 Protease Structure, Dynamics and Drug-Pressure EvolutionCrystal structure of a tethered dimer of HIV-1 proteinase complexed with an inhibitorCrystal structure of human immunodeficiency virus (HIV) type 2 protease in complex with a reduced amide inhibitor and comparison with HIV-1 protease structuresMolecular recognition of cyclic urea HIV-1 protease inhibitorsPatient-specific simulation as a basis for clinical decision-makingA potent human immunodeficiency virus type 1 protease inhibitor, UIC-94003 (TMC-126), and selection of a novel (A28S) mutation in the protease active site.Antiviral properties of aminodiol inhibitors against human immunodeficiency virus and proteaseSelection and analysis of human immunodeficiency virus type 1 variants with increased resistance to ABT-538, a novel protease inhibitorGenotypic and phenotypic characterization of human immunodeficiency virus type 1 variants isolated from patients treated with the protease inhibitor nelfinavir.Potency and selectivity of inhibition of human immunodeficiency virus protease by a small nonpeptide cyclic urea, DMP 323Comparison of inhibitor binding to feline and human immunodeficiency virus proteases: structure-based drug design and the resistance problemSelection of multiple human immunodeficiency virus type 1 variants that encode viral proteases with decreased sensitivity to an inhibitor of the viral proteaseEfficacy of constant infusion of A-77003, an inhibitor of the human immunodeficiency virus type 1 (HIV-1) protease, in limiting acute HIV-1 infection in vitroAntiviral properties of palinavir, a potent inhibitor of the human immunodeficiency virus type 1 proteaseDrug resistance during indinavir therapy is caused by mutations in the protease gene and in its Gag substrate cleavage sitesAntiviral and resistance studies of AG1343, an orally bioavailable inhibitor of human immunodeficiency virus proteaseThe universal statistical distributions of the affinity, equilibrium constants, kinetics and specificity in biomolecular recognitionThe folding free-energy surface of HIV-1 protease: insights into the thermodynamic basis for resistance to inhibitors.Point mutations and sequence variability in proteins: redistributions of preexisting populations.Statistical potentials for fold assessment.Bioinformatics and Drug Discovery.
P2860
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P2860
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh
1993年學術文章
@zh-hant
name
Structure-based inhibitors of HIV-1 protease.
@en
type
label
Structure-based inhibitors of HIV-1 protease.
@en
prefLabel
Structure-based inhibitors of HIV-1 protease.
@en
P1476
Structure-based inhibitors of HIV-1 protease.
@en
P2093
Erickson JW
Wlodawer A
P304
P356
10.1146/ANNUREV.BI.62.070193.002551
P577
1993-01-01T00:00:00Z