Human immunodeficiency virus type 1 IIIB selected for replication in vivo exhibits increased envelope glycoproteins in virions without alteration in coreceptor usage: separation of in vivo replication from macrophage tropism.
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The broad anti-viral agent glycyrrhizin directly modulates the fluidity of plasma membrane and HIV-1 envelopeValidation of the SCID-hu Thy/Liv mouse model with four classes of licensed antiretroviralsAdoption of an "open" envelope conformation facilitating CD4 binding and structural remodeling precedes coreceptor switch in R5 SHIV-infected macaques.A human immunodeficiency virus type 1 isolate from an infected person homozygous for CCR5Delta32 exhibits dual tropism by infecting macrophages and MT2 cells via CXCR4.Fusion-induced apoptosis contributes to thymocyte depletion by a pathogenic human immunodeficiency virus type 1 envelope in the human thymus.Type I interferon contributes to CD4+ T cell depletion induced by infection with HIV-1 in the human thymus.Characterization of a thymus-tropic HIV-1 isolate from a rapid progressor: role of the envelope.HIV-1 replication and pathogenesis in the human thymus.HIV-1 infection and pathogenesis in a novel humanized mouse model.Conserved changes in envelope function during human immunodeficiency virus type 1 coreceptor switchingThe heptad repeat 2 domain is a major determinant for enhanced human immunodeficiency virus type 1 (HIV-1) fusion and pathogenicity of a highly pathogenic HIV-1 Env.Complex determinants in human immunodeficiency virus type 1 envelope gp120 mediate CXCR4-dependent infection of macrophages.Thymic pathogenicity of an HIV-1 envelope is associated with increased CXCR4 binding efficiency and V5-gp41-dependent activity, but not V1/V2-associated CD4 binding efficiency and viral entry.Heterogeneity of envelope molecules shown by different sensitivities to anti-V3 neutralizing antibody and CXCR4 antagonist regulates the formation of multiple-site binding of HIV-1.Adsorption and infectivity of human immunodeficiency virus type 1 are modified by the fluidity of the plasma membrane for multiple-site binding.
P2860
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P2860
Human immunodeficiency virus type 1 IIIB selected for replication in vivo exhibits increased envelope glycoproteins in virions without alteration in coreceptor usage: separation of in vivo replication from macrophage tropism.
description
2001 nî lūn-bûn
@nan
2001 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
name
Human immunodeficiency virus t ...... ation from macrophage tropism.
@ast
Human immunodeficiency virus t ...... ation from macrophage tropism.
@en
type
label
Human immunodeficiency virus t ...... ation from macrophage tropism.
@ast
Human immunodeficiency virus t ...... ation from macrophage tropism.
@en
prefLabel
Human immunodeficiency virus t ...... ation from macrophage tropism.
@ast
Human immunodeficiency virus t ...... ation from macrophage tropism.
@en
P2093
P2860
P1433
P1476
Human immunodeficiency virus t ...... ation from macrophage tropism.
@en
P2093
E D Miller
M Townsend
P2860
P304
P356
10.1128/JVI.75.18.8498-8506.2001
P577
2001-09-01T00:00:00Z