Role of VP3 in human rotavirus internalization after target cell attachment via VP7.
about
Rotavirus architecture at subnanometer resolutionpH-Induced Conformational Change of the Rotavirus VP4 Spike: Implications for Cell Entry and Antibody NeutralizationInsights into neutralization of animal viruses gained from study of influenza virusAntigenic relationships among human rotaviruses as determined by outer capsid protein VP4.The VP5 domain of VP4 can mediate attachment of rotaviruses to cells.Interaction of rotaviruses with Hsc70 during cell entry is mediated by VP5Genetic mapping indicates that VP4 is the rotavirus cell attachment protein in vitro and in vivo.Trypsin activation pathway of rotavirus infectivity.Functional and structural analysis of the sialic acid-binding domain of rotavirusesCharacterization of rotavirus electropherotypes excreted by symptomatic and asymptomatic infants.Rotaviruses induce an early membrane permeabilization of MA104 cells and do not require a low intracellular Ca2+ concentration to initiate their replication cycle.Rotavirus interaction with isolated membrane vesiclesCharacterization of virus-like particles produced by the expression of rotavirus capsid proteins in insect cellsMurine rotavirus genes encoding outer capsid proteins VP4 and VP7 are not major determinants of host range restriction and virulenceThe amino-terminal half of rotavirus SA114fM VP4 protein contains a hemagglutination domain and primes for neutralizing antibodies to the virus.Antibodies to the trypsin cleavage peptide VP8 neutralize rotavirus by inhibiting binding of virions to target cells in culture.Heterotypic passive protection induced by synthetic peptides corresponding to VP7 and VP4 of bovine rotavirusSerotype-specific epitope(s) present on the VP8 subunit of rotavirus VP4 proteinInteraction of rotavirus particles with liposomes.Rotavirus YM gene 4: analysis of its deduced amino acid sequence and prediction of the secondary structure of the VP4 protein.Rotavirus contains integrin ligand sequences and a disintegrin-like domain that are implicated in virus entry into cells.Rotaviruses specifically bind to the neutral glycosphingolipid asialo-GM1.NS35 and not vp7 is the soluble rotavirus protein which binds to target cells.Rotavirus proteins VP7, NS28, and VP4 form oligomeric structuresRotavirus-specific protein synthesis is not necessary for recognition of infected cells by virus-specific cytotoxic T lymphocytesPriming for rotavirus neutralizing antibodies by a VP4 protein-derived synthetic peptideRotavirus gene structure and function.Passive protection against rotavirus-induced diarrhea by monoclonal antibodies to the heterotypic neutralization domain of VP7 and the VP8 fragment of VP4.Noninfectious rotavirus (strain RRV) induces an immune response in mice which protects against rotavirus challengeCharacterization of the interaction between VP8 of bovine rotavirus C486 and cellular components on MA-104 cells and erythrocytesTrypsin cleavage stabilizes the rotavirus VP4 spike.Rotavirus-induced fusion from without in tissue culture cells.Virus-like particle-induced fusion from without in tissue culture cells: role of outer-layer proteins VP4 and VP7.Binding to sialic acids is not an essential step for the entry of animal rotaviruses to epithelial cells in culture.Specific interactions between rotavirus outer capsid proteins VP4 and VP7 determine expression of a cross-reactive, neutralizing VP4-specific epitope.A synthetic peptide corresponding to the cleavage region of VP3 from rotavirus SA11 induces neutralizing antibodies.Molecular and serological analyses of two bovine rotaviruses (B-11 and B-60) causing calf scours in Australia.The peptide-binding and ATPase domains of recombinant hsc70 are required to interact with rotavirus and reduce its infectivity.Liposome-mediated transfection of intact viral particles reveals that plasma membrane penetration determines permissivity of tissue culture cells to rotavirus.
P2860
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P2860
Role of VP3 in human rotavirus internalization after target cell attachment via VP7.
description
1988 nî lūn-bûn
@nan
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
1988年论文
@zh
1988年论文
@zh-cn
name
Role of VP3 in human rotavirus internalization after target cell attachment via VP7.
@en
type
label
Role of VP3 in human rotavirus internalization after target cell attachment via VP7.
@en
prefLabel
Role of VP3 in human rotavirus internalization after target cell attachment via VP7.
@en
P2093
P2860
P1433
P1476
Role of VP3 in human rotavirus internalization after target cell attachment via VP7.
@en
P2093
P2860
P304
P407
P577
1988-07-01T00:00:00Z