Protein design of a bacterially expressed HIV-1 gp41 fusion inhibitor.
about
HIV enters cells via endocytosis and dynamin-dependent fusion with endosomesMicrobicides: a new hope for HIV preventionFusion of mature HIV-1 particles leads to complete release of a gag-GFP-based content marker and raises the intraviral pHStructural and biological mimicry of protein surface recognition by / -peptide foldamersDevelopment of an HIV-1 Microbicide Based on Caulobacter crescentus: Blocking Infection by High-Density Display of Virus Entry Inhibitors.Combinations of 3-hydroxyphthalic anhydride-modified ovalbumin with antiretroviral drug-based microbicide candidates display synergistic and complementary effects against HIV-1 infection.Inhibition of HIV-1 endocytosis allows lipid mixing at the plasma membrane, but not complete fusion.Early steps of HIV-1 fusion define the sensitivity to inhibitory peptides that block 6-helix bundle formation.Intercellular adhesion molecule 1 promotes HIV-1 attachment but not fusion to target cells.Potent strategy to inhibit HIV-1 by binding both gp120 and gp41.Sub-inhibitory concentrations of human α-defensin potentiate neutralizing antibodies against HIV-1 gp41 pre-hairpin intermediates in the presence of serum.Single-chain protein mimetics of the N-terminal heptad-repeat region of gp41 with potential as anti-HIV-1 drugs.One percent tenofovir applied topically to humanized BLT mice and used according to the CAPRISA 004 experimental design demonstrates partial protection from vaginal HIV infection, validating the BLT model for evaluation of new microbicide candidatesDistinct requirements for HIV-cell fusion and HIV-mediated cell-cell fusion.High-Throughput HIV-Cell Fusion Assay for Discovery of Virus Entry InhibitorsTargeting HIV-1 gp41-induced fusion and pathogenesis for anti-viral therapyVisualization of retrovirus uptake and delivery into acidic endosomes.Multifaceted mechanisms of HIV-1 entry inhibition by human α-defensinThe potent human immunodeficiency virus type 1 (HIV-1) entry inhibitor HR212 blocks formation of the envelope glycoprotein gp41 six-helix bundle.Mutations of Gln64 in the HIV-1 gp41 N-terminal heptad repeat render viruses resistant to peptide HIV fusion inhibitors targeting the gp41 pocket.Fusion Stage of HIV-1 Entry Depends on Virus-Induced Cell Surface Exposure of Phosphatidylserine.The C34 Peptide Fusion Inhibitor Binds to the Six-Helix Bundle Core Domain of HIV-1 gp41 by Displacement of the C-Terminal Helical Repeat Region.The role of the N-terminal segment of CCR5 in HIV-1 Env-mediated membrane fusion and the mechanism of virus adaptation to CCR5 lacking this segment.Efficient Fusion at Neutral pH by Human Immunodeficiency Virus gp41 Trimers containing the Fusion Peptide and Transmembrane Domain.Functional characteristics of small proteins (70 amino acid residues) forming protein-nucleic acid complexes.HIV vs. HIV: Turning HIV-Derived Peptides into Drugs
P2860
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P2860
Protein design of a bacterially expressed HIV-1 gp41 fusion inhibitor.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Protein design of a bacterially expressed HIV-1 gp41 fusion inhibitor.
@en
type
label
Protein design of a bacterially expressed HIV-1 gp41 fusion inhibitor.
@en
prefLabel
Protein design of a bacterially expressed HIV-1 gp41 fusion inhibitor.
@en
P2093
P356
P1433
P1476
Protein design of a bacterially expressed HIV-1 gp41 fusion inhibitor.
@en
P2093
John P Moore
Thomas J Ketas
P304
P356
10.1021/BI7001289
P407
P50
P577
2007-03-20T00:00:00Z