Intraluminal proteolytic activation plays an important role in replication of type 1 reovirus in the intestines of neonatal mice.
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Neutrophil elastase, an acid-independent serine protease, facilitates reovirus uncoating and infection in U937 promonocyte cells.Potential for Improving Potency and Specificity of Reovirus Oncolysis with Next-Generation Reovirus VariantsStructure of the reovirus outer capsid and dsRNA-binding protein sigma3 at 1.8 A resolution.Similar uptake but different trafficking and escape routes of reovirus virions and infectious subvirion particles imaged in polarized Madin-Darby canine kidney cells.Efficient norovirus and reovirus replication in the mouse intestine requires microfold (M) cells.Cleavage susceptibility of reovirus attachment protein sigma1 during proteolytic disassembly of virions is determined by a sequence polymorphism in the sigma1 neck.Proteolytic processing of the astrovirus capsidMutant cells selected during persistent reovirus infection do not express mature cathepsin L and do not support reovirus disassembly.Role of immunoglobulin A in protection against reovirus entry into Murine Peyer's patchesGut proteases target Yersinia invasin in vivo.Mechanisms of viral pathogenesis. Distinct forms of reoviruses and their roles during replication in cells and hostThe viral sigma1 protein and glycoconjugates containing alpha2-3-linked sialic acid are involved in type 1 reovirus adherence to M cell apical surfaces.Impact of host proteases on reovirus infection in the respiratory tract.Infectious subvirion particles of reovirus type 3 Dearing exhibit a loss in infectivity and contain a cleaved sigma 1 proteinReovirus variants selected during persistent infections of L cells contain mutations in the viral S1 and S4 genes and are altered in viral disassemblyMutations in reovirus outer-capsid protein sigma3 selected during persistent infections of L cells confer resistance to protease inhibitor E64Murine noroviruses comprising a single genogroup exhibit biological diversity despite limited sequence divergence.Mechanisms of reovirus bloodstream dissemination.Reovirus uses multiple endocytic pathways for cell entry.Peyer's patch dendritic cells process viral antigen from apoptotic epithelial cells in the intestine of reovirus-infected mice.From touchdown to transcription: the reovirus cell entry pathwayNorovirus capture with histo-blood group antigens reveals novel virus-ligand interactions.The oncolytic effect in vivo of reovirus on tumour cells that have survived reovirus cell killing in vitro.Protective antibodies inhibit reovirus internalization and uncoating by intracellular proteases.Proteolytic processing of reovirus is required for adherence to intestinal M cellsIsolation and genetic characterization of ethanol-resistant reovirus mutantsA carboxy-terminal fragment of protein mu 1/mu 1C is present in infectious subvirion particles of mammalian reoviruses and is proposed to have a role in penetrationMonoclonal antibodies to reovirus reveal structure/function relationships between capsid proteins and genetics of susceptibility to antibody action.Secretory immunoglobulin A antibodies against the sigma1 outer capsid protein of reovirus type 1 Lang prevent infection of mouse Peyer's patches.Parallel mechanisms in neuropathogenesis of enteric virus infections.Innate host barriers to viral trafficking and population diversity: lessons learned from poliovirus.The requirement of environmental acidification for Ibaraki virus infection to host cells.Lipid Membranes Facilitate Conformational Changes Required for Reovirus Cell Entry.Conformational changes required for reovirus cell entry are sensitive to pH.Reduction of virion-associated σ1 fibers on oncolytic reovirus variants promotes adaptation toward tumorigenic cells.The μ1 72-96 loop controls conformational transitions during reovirus cell entry.Lipids Cooperate with the Reovirus Membrane Penetration Peptide to Facilitate Particle Uncoating.Cell entry-associated conformational changes in reovirus particles are controlled by host protease activity.Sites and determinants of early cleavages in the proteolytic processing pathway of reovirus surface protein sigma3.Addition of exogenous protease facilitates reovirus infection in many restrictive cells.
P2860
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P2860
Intraluminal proteolytic activation plays an important role in replication of type 1 reovirus in the intestines of neonatal mice.
description
1990 nî lūn-bûn
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1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
1990年论文
@zh
1990年论文
@zh-cn
name
Intraluminal proteolytic activ ...... e intestines of neonatal mice.
@ast
Intraluminal proteolytic activ ...... e intestines of neonatal mice.
@en
type
label
Intraluminal proteolytic activ ...... e intestines of neonatal mice.
@ast
Intraluminal proteolytic activ ...... e intestines of neonatal mice.
@en
prefLabel
Intraluminal proteolytic activ ...... e intestines of neonatal mice.
@ast
Intraluminal proteolytic activ ...... e intestines of neonatal mice.
@en
P2093
P2860
P1433
P1476
Intraluminal proteolytic activ ...... e intestines of neonatal mice.
@en
P2093
P2860
P304
P407
P577
1990-04-01T00:00:00Z