Mutations within the putative membrane-spanning domain of the simian immunodeficiency virus transmembrane glycoprotein define the minimal requirements for fusion, incorporation, and infectivity.
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Structures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeFunctional Analysis of the Transmembrane Domain in Paramyxovirus F Protein-Mediated Membrane FusionActivity of the Mason-Pfizer monkey virus fusion protein is modulated by single amino acids in the cytoplasmic tail.The membrane-spanning domain of gp41 plays a critical role in intracellular trafficking of the HIV envelope protein.Detailed topology mapping reveals substantial exposure of the "cytoplasmic" C-terminal tail (CTT) sequences in HIV-1 Env proteins at the cell surface.Progressive truncations C terminal to the membrane-spanning domain of simian immunodeficiency virus Env reduce fusogenicity and increase concentration dependence of Env for fusion.Mutagenesis of tyrosine and di-leucine motifs in the HIV-1 envelope cytoplasmic domain results in a loss of Env-mediated fusion and infectivity.Highly conserved structural properties of the C-terminal tail of HIV-1 gp41 protein despite substantial sequence variation among diverse clades: implications for functions in viral replication.Evidence against extracellular exposure of a highly immunogenic region in the C-terminal domain of the simian immunodeficiency virus gp41 transmembrane proteinThe paramyxovirus fusion protein C-terminal region: mutagenesis indicates an indivisible protein unit.Role of the membrane-spanning domain of human immunodeficiency virus type 1 envelope glycoprotein in cell-cell fusion and virus infectionMembrane structure correlates to function of LLP2 on the cytoplasmic tail of HIV-1 gp41 protein.Structural basis for membrane anchoring of HIV-1 envelope spikeTruncation of the membrane-spanning domain of human immunodeficiency virus type 1 envelope glycoprotein defines elements required for fusion, incorporation, and infectivityStructure of the transmembrane domain of HIV-1 envelope glycoprotein.A replication-competent, neutralization-sensitive variant of simian immunodeficiency virus lacking 100 amino acids of envelope.CD4-independent entry and replication of simian immunodeficiency virus in primary rhesus macaque astrocytes are regulated by the transmembrane protein.Bitopic membrane topology of the stable signal peptide in the tripartite Junín virus GP-C envelope glycoprotein complex.Atraumatic oral spray immunization with replication-deficient viral vector vaccines.Role of the stable signal peptide of Junín arenavirus envelope glycoprotein in pH-dependent membrane fusion.Expression and biochemical analysis of the entire HIV-2 gp41 ectodomain: determinants of stability map to N- and C-terminal sequences outside the 6-helix bundle core.
P2860
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P2860
Mutations within the putative membrane-spanning domain of the simian immunodeficiency virus transmembrane glycoprotein define the minimal requirements for fusion, incorporation, and infectivity.
description
2001 nî lūn-bûn
@nan
2001 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Mutations within the putative ...... ncorporation, and infectivity.
@ast
Mutations within the putative ...... ncorporation, and infectivity.
@en
type
label
Mutations within the putative ...... ncorporation, and infectivity.
@ast
Mutations within the putative ...... ncorporation, and infectivity.
@en
prefLabel
Mutations within the putative ...... ncorporation, and infectivity.
@ast
Mutations within the putative ...... ncorporation, and infectivity.
@en
P2093
P2860
P921
P1433
P1476
Mutations within the putative ...... ncorporation, and infectivity.
@en
P2093
P2860
P304
P356
10.1128/JVI.75.20.9601-9612.2001
P577
2001-10-01T00:00:00Z