How does a symmetric dimer recognize an asymmetric substrate? A substrate complex of HIV-1 protease
about
Predicting deleterious amino acid substitutionsHIV-1 protease molecular dynamics of a wild-type and of the V82F/I84V mutant: possible contributions to drug resistance and a potential new target site for drugsViability 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 precursorX-Ray Crystal Structures of Human Immunodeficiency Virus Type 1 Protease Mutants Complexed with AtazanavirCrystal Structure of Lysine Sulfonamide Inhibitor Reveals the Displacement of the Conserved Flap Water Molecule in Human Immunodeficiency Virus Type 1 ProteaseDesign and Synthesis of HIV-1 Protease Inhibitors Incorporating Oxazolidinones as P2/P2‘ Ligands in Pseudosymmetric Dipeptide IsosteresComputational design and experimental study of tighter binding peptides to an inactivated mutant of HIV-1 proteaseCaught in the Act: The 1.5 Å Resolution Crystal Structures of the HIV-1 Protease and the I54V Mutant Reveal a Tetrahedral Reaction Intermediate †Effect of the Active Site D25N Mutation on the Structure, Stability, and Ligand Binding of the Mature HIV-1 ProteaseHIV-1 Protease Inhibitors from Inverse Design in the Substrate Envelope Exhibit Subnanomolar Binding to Drug-Resistant VariantsHighly conserved glycine 86 and arginine 87 residues contribute differently to the structure and activity of the mature HIV-1 proteaseAmprenavir complexes with HIV-1 protease and its drug-resistant mutants altering hydrophobic clustersStructure-Based Design, Synthesis, and Structure−Activity Relationship Studies of HIV-1 Protease Inhibitors Incorporating PhenyloxazolidinonesNine crystal structures determine the substrate envelope of the MDR HIV-1 proteaseStructural, kinetic, and thermodynamic studies of specificity designed HIV-1 proteaseSubstrate Envelope-Designed Potent HIV-1 Protease Inhibitors to Avoid Drug ResistanceDesign, Synthesis, and Biological and Structural Evaluations of Novel HIV-1 Protease Inhibitors To Combat Drug ResistanceExtreme Entropy–Enthalpy Compensation in a Drug-Resistant Variant of HIV-1 ProteaseHIV-1 Protease-Substrate Coevolution in Nelfinavir ResistanceDrug Resistance Conferred by Mutations Outside the Active Site through Alterations in the Dynamic and Structural Ensemble of HIV-1 ProteaseStructural Basis of Why Nelfinavir-Resistant D30N Mutant of HIV-1 Protease Remains Susceptible to SaquinavirThe folding free-energy surface of HIV-1 protease: insights into the thermodynamic basis for resistance to inhibitors.Crystal structure of an HIV assembly and maturation switch.ModBase, a database of annotated comparative protein structure models and associated resources.HIV-1 protease substrate binding and product release pathways explored with coarse-grained molecular dynamics.Kinetic characterization of the critical step in HIV-1 protease maturationReplacement of the P1 amino acid of human immunodeficiency virus type 1 Gag processing sites can inhibit or enhance the rate of cleavage by the viral proteaseDiversification and specialization of HIV protease function during in vitro evolution.Mining the protein data bank to differentiate error from structural variation in clustered static structures: an examination of HIV protease.Identification of structural mechanisms of HIV-1 protease specificity using computational peptide docking: implications for drug resistance.Computational study of protein specificity: the molecular basis of HIV-1 protease drug resistance.Virion instability of human immunodeficiency virus type 1 reverse transcriptase (RT) mutated in the protease cleavage site between RT p51 and the RT RNase H domain.Effects of HIV-1 protease on cellular functions and their potential applications in antiretroviral therapy.Rationale for more diverse inhibitors in competition with substrates in HIV-1 protease.Structure-based prediction of potential binding and nonbinding peptides to HIV-1 proteaseMechanism of substrate recognition by drug-resistant human immunodeficiency virus type 1 protease variants revealed by a novel structural intermediateRole of invariant Thr80 in human immunodeficiency virus type 1 protease structure, function, and viral infectivityCurrent and Novel Inhibitors of HIV ProteaseImpact of M36I polymorphism on the interaction of HIV-1 protease with its substrates: insights from molecular dynamics.
P2860
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P2860
How does a symmetric dimer recognize an asymmetric substrate? A substrate complex of HIV-1 protease
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2000 nî lūn-bûn
@nan
2000 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի սեպտեմբերին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
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2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
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2000年论文
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name
How does a symmetric dimer rec ...... rate complex of HIV-1 protease
@ast
How does a symmetric dimer rec ...... rate complex of HIV-1 protease
@en
How does a symmetric dimer rec ...... rate complex of HIV-1 protease
@nl
type
label
How does a symmetric dimer rec ...... rate complex of HIV-1 protease
@ast
How does a symmetric dimer rec ...... rate complex of HIV-1 protease
@en
How does a symmetric dimer rec ...... rate complex of HIV-1 protease
@nl
prefLabel
How does a symmetric dimer rec ...... rate complex of HIV-1 protease
@ast
How does a symmetric dimer rec ...... rate complex of HIV-1 protease
@en
How does a symmetric dimer rec ...... rate complex of HIV-1 protease
@nl
P2093
P3181
P356
P1476
How does a symmetric dimer rec ...... rate complex of HIV-1 protease
@en
P2093
C A Schiffer
E Nalivaika
M Prabu-Jeyabalan
P304
P3181
P356
10.1006/JMBI.2000.4018
P407
P577
2000-09-01T00:00:00Z