Myristylation of the large surface protein is required for hepatitis B virus in vitro infectivity.
about
Viral and cellular determinants involved in hepadnaviral entryFine mapping of pre-S sequence requirements for hepatitis B virus large envelope protein-mediated receptor interactionReptilian reovirus utilizes a small type III protein with an external myristylated amino terminus to mediate cell-cell fusion.Infection process of the hepatitis B virus depends on the presence of a defined sequence in the pre-S1 domainEfficient inhibition of hepatitis B virus infection by acylated peptides derived from the large viral surface protein.Vaccinia virus penetration requires cholesterol and results in specific viral envelope proteins associated with lipid raftsRole of the pre-S2 domain of the large envelope protein in hepatitis B virus assembly and infectivityA short N-proximal region in the large envelope protein harbors a determinant that contributes to the species specificity of human hepatitis B virus.Hepatitis B virus biology.Mapping of the hepatitis B virus pre-S1 domain involved in receptor recognitionPhage display creates innovative applications to combat hepatitis B virusThe myristate moiety and amino terminus of vaccinia virus l1 constitute a bipartite functional region needed for entryHepatitis B virus large surface protein: function and fame.HBV life cycle: entry and morphogenesis.Interaction of human tumor viruses with host cell surface receptors and cell entryThe translocation motif of hepatitis B virus envelope proteins is dispensable for infectivity.Systems Analysis of Protein Fatty Acylation in Herpes Simplex Virus-Infected Cells Using Chemical ProteomicsHepatitis B surface antigen levels and sequences of natural hepatitis B virus variants influence the assembly and secretion of hepatitis d virus.The alkylated imino sugar, n-(n-Nonyl)-deoxygalactonojirimycin, reduces the amount of hepatitis B virus nucleocapsid in tissue culture.The first transmembrane domain of the hepatitis B virus large envelope protein is crucial for infectivityThe pre-S1 and antigenic loop infectivity determinants of the hepatitis B virus envelope proteins are functionally independent.Analysis of host range phenotypes of primate hepadnaviruses by in vitro infections of hepatitis D virus pseudotypesHepatitis B Virus and Hepatitis D Virus Entry, Species Specificity, and Tissue Tropism.Asialoglycoprotein receptor interacts with the preS1 domain of hepatitis B virus in vivo and in vitro.The pre-s2 domain of the hepatitis B virus is dispensable for infectivity but serves a spacer function for L-protein-connected virus assembly.Hepatitis B virus infection initiates with a large surface protein-dependent binding to heparan sulfate proteoglycans.Entry of hepatitis delta virus requires the conserved cysteine residues of the hepatitis B virus envelope protein antigenic loop and is blocked by inhibitors of thiol-disulfide exchange.Myristoylated PreS1-domain of the hepatitis B virus L-protein mediates specific binding to differentiated hepatocytes.Infectivity determinants of the hepatitis B virus pre-S domain are confined to the N-terminal 75 amino acid residues.Immunoadhesins containing pre-S domains of hepatitis B virus large envelope protein are secreted and inhibit virus infection.Role of the antigenic loop of the hepatitis B virus envelope proteins in infectivity of hepatitis delta virus.The N-terminus of B96Bom, a Bombyx mori G-protein-coupled receptor, is N-myristoylated and translocated across the membrane.Two potentially important elements of the hepatitis B virus large envelope protein are dispensable for the infectivity of hepatitis delta virus.Hepatitis B virus infection in microcarrier-attached immortalized human hepatocytes cultured in molecularporous membrane bags: a model for long-term episomal replication of HBV.Analysis of hepatitis B virus preS1 variability and prevalence of the rs2296651 polymorphism in a Spanish population.Analysis of hepatitis B virus preS1 variability and prevalence of the rs2296651 polymorphism in a Spanish population.Delivery of chimeric hepatitis B core particles into liver cells.Host functions used by hepatitis B virus to complete its life cycle: Implications for developing host-targeting agents to treat chronic hepatitis B
P2860
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P2860
Myristylation of the large surface protein is required for hepatitis B virus in vitro infectivity.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Myristylation of the large sur ...... B virus in vitro infectivity.
@en
type
label
Myristylation of the large sur ...... B virus in vitro infectivity.
@en
prefLabel
Myristylation of the large sur ...... B virus in vitro infectivity.
@en
P2093
P356
P1433
P1476
Myristylation of the large sur ...... B virus in vitro infectivity.
@en
P2093
P304
P356
10.1006/VIRO.1996.0209
P407
P577
1996-04-01T00:00:00Z