Autocatalytic maturation, physical/chemical properties, and crystal structure of group N HIV-1 protease: Relevance to drug resistance

Autocatalytic maturation, physical/chemical properties, and crystal structure of group N HIV-1 protease: Relevance to drug resistance

Item
http://www.wikidata.org/entity/Q27664164
The L76V Drug Resistance Mutation Decreases the Dimer Stability and Rate of Autoprocessing of HIV-1 Protease by Reducing Internal Hydrophobic ContactsCritical differences in HIV-1 and HIV-2 protease specificity for clinical inhibitorsTerminal Interface Conformations Modulate Dimer Stability Prior to Amino Terminal Autoprocessing of HIV-1 ProteaseExtreme Multidrug Resistant HIV-1 Protease with 20 Mutations Is Resistant to Novel Protease Inhibitors with P1′-Pyrrolidinone or P2-Tris-tetrahydrofuranHIV-1 Protease with 20 Mutations Exhibits Extreme Resistance to Clinical Inhibitors through Coordinated Structural RearrangementsStructures of Darunavir-Resistant HIV-1 Protease Mutant Reveal Atypical Binding of Darunavir to Wide Open FlapsStructural Studies of a Rationally Selected Multi-Drug Resistant HIV-1 Protease Reveal Synergistic Effect of Distal Mutations on Flap DynamicsTransition states of native and drug-resistant HIV-1 protease are the same.Inhibition of autoprocessing of natural variants and multidrug resistant mutant precursors of HIV-1 protease by clinical inhibitors.Substituted Bis-THF Protease Inhibitors with Improved Potency against Highly Resistant Mature HIV-1 Protease PR20Mechanism of dissociative inhibition of HIV protease and its autoprocessing from a precursor.Binding of Clinical Inhibitors to a Model Precursor of a Rationally Selected Multidrug Resistant HIV-1 Protease Is Significantly Weaker Than That to the Released Mature EnzymeEnhanced stability of monomer fold correlates with extreme drug resistance of HIV-1 protease.Mutations Proximal to Sites of Autoproteolysis and the α-Helix That Co-evolve under Drug Pressure Modulate the Autoprocessing and Vitality of HIV-1 Protease.Drug Resistance Mutation L76V Alters Nonpolar Interactions at the Flap-Core Interface of HIV-1 Protease
P2860

Autocatalytic maturation, physical/chemical properties, and crystal structure of group N HIV-1 protease: Relevance to drug resistance

Item
http://www.wikidata.org/entity/Q27664164
description
2010 nî lūn-bûn
@nan
2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Autocatalytic maturation, phys ...... : Relevance to drug resistance
@ast
Autocatalytic maturation, phys ...... : Relevance to drug resistance
@en
Autocatalytic maturation, phys ...... : Relevance to drug resistance
@nl
type
label
Autocatalytic maturation, phys ...... : Relevance to drug resistance
@ast
Autocatalytic maturation, phys ...... : Relevance to drug resistance
@en
Autocatalytic maturation, phys ...... : Relevance to drug resistance
@nl
prefLabel
Autocatalytic maturation, phys ...... : Relevance to drug resistance
@ast
Autocatalytic maturation, phys ...... : Relevance to drug resistance
@en
Autocatalytic maturation, phys ...... : Relevance to drug resistance
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P433
P478
P50
P577
P5875
P698
P921
P932
P356
P1433
P1476
Autocatalytic maturation, phys ...... : Relevance to drug resistance
@en
P2093
P2860
P304
P31
P356
P433
P478
P50
P577
P5875
P698
P921
P932