Modulation of the oligomeric structures of HIV-1 retroviral enzymes by synthetic peptides and small molecules.
about
Novel therapeutic strategies targeting HIV integraseEffect of the Active Site D25N Mutation on the Structure, Stability, and Ligand Binding of the Mature HIV-1 ProteaseAutocatalytic maturation, physical/chemical properties, and crystal structure of group N HIV-1 protease: Relevance to drug resistanceTerminal Interface Conformations Modulate Dimer Stability Prior to Amino Terminal Autoprocessing of HIV-1 ProteaseStructural Maturation of HIV-1 Reverse Transcriptase-A Metamorphic Solution to Genomic InstabilityA symmetric region of the HIV-1 integrase dimerization interface is essential for viral replicationIdentification of the bona fide DHDPS from a common plant pathogenThe HIVToolbox 2 web system integrates sequence, structure, function and mutation analysisMutations that abrogate human immunodeficiency virus type 1 reverse transcriptase dimerization affect maturation of the reverse transcriptase heterodimer.Conformational changes in HIV-1 reverse transcriptase induced by nonnucleoside reverse transcriptase inhibitor binding.Peptides that inhibit HIV-1 integrase by blocking its protein-protein interactions.Probing nonnucleoside inhibitor-induced active-site distortion in HIV-1 reverse transcriptase by transient kinetic analysesThe Need for Development of New HIV-1 Reverse Transcriptase and Integrase Inhibitors in the Aftermath of Antiviral Drug ResistanceTargeting human immunodeficiency virus type 1 assembly, maturation and budding.HIV Drug Resistance and the Advent of Integrase Inhibitors.Inhibiting the HIV integration process: past, present, and the future.Homodimerization of the p51 subunit of HIV-1 reverse transcriptase.The N137 and P140 amino acids in the p51 and the P95 amino acid in the p66 subunit of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase are instrumental to maintain catalytic activity and to design new classes of anti-HIV-1 drugs.A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility.Development of peptide inhibitors of HIV transmission.On the Molecular Modeling Analyses of Novel HIV-1 Protease Inhibitors Based on Modified Chitosan Dimer
P2860
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P2860
Modulation of the oligomeric structures of HIV-1 retroviral enzymes by synthetic peptides and small molecules.
description
2002 nî lūn-bûn
@nan
2002 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Modulation of the oligomeric s ...... peptides and small molecules.
@ast
Modulation of the oligomeric s ...... peptides and small molecules.
@en
Modulation of the oligomeric s ...... peptides and small molecules.
@nl
type
label
Modulation of the oligomeric s ...... peptides and small molecules.
@ast
Modulation of the oligomeric s ...... peptides and small molecules.
@en
Modulation of the oligomeric s ...... peptides and small molecules.
@nl
prefLabel
Modulation of the oligomeric s ...... peptides and small molecules.
@ast
Modulation of the oligomeric s ...... peptides and small molecules.
@en
Modulation of the oligomeric s ...... peptides and small molecules.
@nl
P2860
P1433
P1476
Modulation of the oligomeric s ...... peptides and small molecules.
@en
P2093
Nicolas Sluis-Cremer
P2860
P304
P356
10.1046/J.1432-1033.2002.03216.X
P407
P577
2002-11-01T00:00:00Z