Structural basis for coevolution of a human immunodeficiency virus type 1 nucleocapsid-p1 cleavage site with a V82A drug-resistant mutation in viral protease.
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The choreography of HIV-1 proteolytic processing and virion assemblyHIV-1 protease and reverse transcriptase control the architecture of their nucleocapsid partnerIn silico prediction of mutant HIV-1 proteases cleaving a target sequenceComputational design and experimental study of tighter binding peptides to an inactivated mutant of HIV-1 proteaseStructural Analysis of Human Immunodeficiency Virus Type 1 CRF01_AE Protease in Complex with the Substrate p1-p6The Effect of Clade-Specific Sequence Polymorphisms on HIV-1 Protease Activity and Inhibitor Resistance PathwaysNine crystal structures determine the substrate envelope of the MDR HIV-1 proteaseStructural and Thermodynamic Basis of Amprenavir/Darunavir and Atazanavir Resistance in HIV-1 Protease with Mutations at Residue 50Structural, kinetic, and thermodynamic studies of specificity designed HIV-1 proteaseExtreme Entropy–Enthalpy Compensation in a Drug-Resistant Variant of HIV-1 ProteaseHIV-1 Protease-Substrate Coevolution in Nelfinavir ResistanceA novel substrate-based HIV-1 protease inhibitor drug resistance mechanismGag mutations strongly contribute to HIV-1 resistance to protease inhibitors in highly drug-experienced patients besides compensating for fitness lossIdentification of structural mechanisms of HIV-1 protease specificity using computational peptide docking: implications for drug resistance.Rationale for more diverse inhibitors in competition with substrates in HIV-1 protease.Molecular basis for substrate recognition and drug resistance from 1.1 to 1.6 angstroms resolution crystal structures of HIV-1 protease mutants with substrate analogs.Substrate envelope and drug resistance: crystal structure of RO1 in complex with wild-type human immunodeficiency virus type 1 protease.Mechanism 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 infectivityImproved Generalized Born Solvent Model Parameters for Protein Simulations.Molecular Basis for Drug Resistance in HIV-1 ProteaseClinical management of HIV drug resistance.Modulation of HIV protease flexibility by the T80N mutationFunction-based mutation-resistant synthetic signaling device activated by HIV-1 proteolysisModulation of HIV-1 Gag NC/p1 cleavage efficiency affects protease inhibitor resistance and viral replicative capacityElucidation of the Molecular Mechanism Driving Duplication of the HIV-1 PTAP Late Domain.Mutations in multiple domains of Gag drive the emergence of in vitro resistance to the phosphonate-containing HIV-1 protease inhibitor GS-8374.HIV-1 drug resistance mutations: an updated framework for the second decade of HAARTImproving Viral Protease Inhibitors to Counter Drug Resistance.Resilience to resistance of HIV-1 protease inhibitors: profile of darunavir.New approaches to HIV protease inhibitor drug design II: testing the substrate envelope hypothesis to avoid drug resistance and discover robust inhibitorsHuman immunodeficiency virus type 1 protease-correlated cleavage site mutations enhance inhibitor resistance.HIV-1 assembly, budding, and maturation.Human Immunodeficiency Virus Gag and protease: partners in resistance.Analysis of correlated mutations in HIV-1 protease using spectral clusteringRole of Gag in HIV Resistance to Protease InhibitorsThree residues in HIV-1 matrix contribute to protease inhibitor susceptibility and replication capacity.Evolution of gag and gp41 in Patients Receiving Ritonavir-Boosted Protease Inhibitors.Positive impact of HIV-1 gag cleavage site mutations on the virological response to darunavir boosted with ritonavir.Protease-Mediated Maturation of HIV: Inhibitors of Protease and the Maturation Process
P2860
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P2860
Structural basis for coevolution of a human immunodeficiency virus type 1 nucleocapsid-p1 cleavage site with a V82A drug-resistant mutation in viral protease.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh
2004年學術文章
@zh-hant
name
Structural basis for coevoluti ...... nt mutation in viral protease.
@en
Structural basis for coevoluti ...... nt mutation in viral protease.
@nl
type
label
Structural basis for coevoluti ...... nt mutation in viral protease.
@en
Structural basis for coevoluti ...... nt mutation in viral protease.
@nl
prefLabel
Structural basis for coevoluti ...... nt mutation in viral protease.
@en
Structural basis for coevoluti ...... nt mutation in viral protease.
@nl
P2093
P2860
P1433
P1476
Structural basis for coevoluti ...... nt mutation in viral protease.
@en
P2093
Celia A Schiffer
Ellen A Nalivaika
Moses Prabu-Jeyabalan
Nancy M King
P2860
P304
12446-12454
P356
10.1128/JVI.78.22.12446-12454.2004
P407
P577
2004-11-01T00:00:00Z