Binding to sialic acids is not an essential step for the entry of animal rotaviruses to epithelial cells in culture.
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Structural Basis of Rotavirus Strain Preference toward N-Acetyl- or N-Glycolylneuraminic Acid-Containing ReceptorsAnalysis of host range restriction determinants in the rabbit model: comparison of homologous and heterologous rotavirus infections.Viruses and cells with mutations affecting viral entry are selected during persistent rotavirus infections of MA104 cellsIntegrins alpha2beta1 and alpha4beta1 can mediate SA11 rotavirus attachment and entry into cells.The VP5 domain of VP4 can mediate attachment of rotaviruses to cells.Biochemical characterization of rotavirus receptors in MA104 cellsDifferential infection of polarized epithelial cell lines by sialic acid-dependent and sialic acid-independent rotavirus strains.Different rotavirus strains enter MA104 cells through different endocytic pathways: the role of clathrin-mediated endocytosis.VLA-2 (alpha2beta1) integrin promotes rotavirus entry into cells but is not necessary for rotavirus attachment.Initial interaction of rotavirus strains with N-acetylneuraminic (sialic) acid residues on the cell surface correlates with VP4 genotype, not species of origin.Heat shock cognate protein 70 is involved in rotavirus cell entry.Interaction of rotaviruses with Hsc70 during cell entry is mediated by VP5Monkey rotavirus binding to alpha2beta1 integrin requires the alpha2 I domain and is facilitated by the homologous beta1 subunitMapping the hemagglutination domain of rotaviruses.Integrin alpha(v)beta(3) mediates rotavirus cell entry.Genetic mapping indicates that VP4 is the rotavirus cell attachment protein in vitro and in vivo.Interactions between the two surface proteins of rotavirus may alter the receptor-binding specificity of the virusTrypsin activation pathway of rotavirus infectivity.Mutations in type 3 reovirus that determine binding to sialic acid are contained in the fibrous tail domain of viral attachment protein sigma1.Functional and structural analysis of the sialic acid-binding domain of rotavirusesSpike protein VP8* of human rotavirus recognizes histo-blood group antigens in a type-specific manner.Rotaviruses induce an early membrane permeabilization of MA104 cells and do not require a low intracellular Ca2+ concentration to initiate their replication cycle.The spike protein VP4 defines the endocytic pathway used by rotavirus to enter MA104 cells.Rotavirus interaction with isolated membrane vesiclesCharacterization of virus-like particles produced by the expression of rotavirus capsid proteins in insect cellsRotavirus contains integrin ligand sequences and a disintegrin-like domain that are implicated in virus entry into cells.Structural insights into the coupling of virion assembly and rotavirus replication.VP7 mediates the interaction of rotaviruses with integrin alphavbeta3 through a novel integrin-binding site.Rotaviruses reach late endosomes and require the cation-dependent mannose-6-phosphate receptor and the activity of cathepsin proteases to enter the cell.Relative roles of GM1 ganglioside, N-acylneuraminic acids, and α2β1 integrin in mediating rotavirus infection.Integrin alphavbeta5 is a primary receptor for adenovirus in CAR-negative cells.Virus-like particle-induced fusion from without in tissue culture cells: role of outer-layer proteins VP4 and VP7.Assay for evaluation of rotavirus-cell interactions: identification of an enterocyte ganglioside fraction that mediates group A porcine rotavirus recognition.Characterization of neuraminidase-resistant mutants derived from rotavirus porcine strain OSU.
P2860
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P2860
Binding to sialic acids is not an essential step for the entry of animal rotaviruses to epithelial cells in culture.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
Binding to sialic acids is not ...... o epithelial cells in culture.
@en
type
label
Binding to sialic acids is not ...... o epithelial cells in culture.
@en
prefLabel
Binding to sialic acids is not ...... o epithelial cells in culture.
@en
P2093
P2860
P1433
P1476
Binding to sialic acids is not ...... to epithelial cells in culture
@en
P2093
P2860
P304
P407
P577
1993-09-01T00:00:00Z