Putative autocleavage of outer capsid protein micro1, allowing release of myristoylated peptide micro1N during particle uncoating, is critical for cell entry by reovirus.
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3.3 A cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry.Potential for Improving Potency and Specificity of Reovirus Oncolysis with Next-Generation Reovirus VariantsDiminished reovirus capsid stability alters disease pathogenesis and littermate transmissionThe picobirnavirus crystal structure provides functional insights into virion assembly and cell entryThe reovirus sigma1 aspartic acid sandwich: a trimerization motif poised for conformational changeApoptosis induction influences reovirus replication and virulence in newborn miceDeterminants of strain-specific differences in efficiency of reovirus entryRequirements for the formation of membrane pores by the reovirus myristoylated micro1N peptide.Reovirus mu1 structural rearrangements that mediate membrane penetrationReverse genetics for mammalian reovirus.Transport to late endosomes is required for efficient reovirus infectionSimilar uptake but different trafficking and escape routes of reovirus virions and infectious subvirion particles imaged in polarized Madin-Darby canine kidney cells.Independent regulation of reovirus membrane penetration and apoptosis by the mu1 phi domainNMR structure of a viral peptide inserted in artificial membranes: a view on the early steps of the birnavirus entry processAdenovirus protein VI mediates membrane disruption following capsid disassembly.Features of reovirus outer capsid protein mu1 revealed by electron cryomicroscopy and image reconstruction of the virion at 7.0 Angstrom resolution.Reovirus variants selected for resistance to ammonium chloride have mutations in viral outer-capsid protein sigma3.Sequence analysis of the genome of piscine orthoreovirus (PRV) associated with heart and skeletal muscle inflammation (HSMI) in Atlantic salmon (Salmo salar).Mammalian reovirus, a nonfusogenic nonenveloped virus, forms size-selective pores in a model membrane.Assembly of highly infectious rotavirus particles recoated with recombinant outer capsid proteins.Antibodies against outer-capsid proteins of grass carp reovirus expressed in E. coli are capable of neutralizing viral infectivity.Primed for Discovery: Atomic-Resolution Cryo-EM Structure of a Reovirus Entry IntermediateThermostabilizing mutations in reovirus outer-capsid protein mu1 selected by heat inactivation of infectious subvirion particles.Thermolabilizing pseudoreversions in reovirus outer-capsid protein micro 1 rescue the entry defect conferred by a thermostabilizing mutation.Mechanisms of reovirus-induced cell death and tissue injury: role of apoptosis and virus-induced perturbation of host-cell signaling and transcription factor activation.Reovirus variants with mutations in genome segments S1 and L2 exhibit enhanced virion infectivity and superior oncolysis.Mechanisms of reovirus bloodstream dissemination.Dissecting quasi-equivalence in nonenveloped viruses: membrane disruption is promoted by lytic peptides released from subunit pentamers, not hexamers.From touchdown to transcription: the reovirus cell entry pathwayReovirus receptors, cell entry, and proapoptotic signaling.NPXY motifs in the beta1 integrin cytoplasmic tail are required for functional reovirus entry.A role for molecular chaperone Hsc70 in reovirus outer capsid disassemblyA positive-feedback mechanism promotes reovirus particle conversion to the intermediate associated with membrane penetration.Interferon-inducible transmembrane protein 3 (IFITM3) restricts reovirus cell entry.Viroporins customize host cells for efficient viral propagation.Dissecting the functional domains of a nonenveloped virus membrane penetration peptide.Reovirus forms neo-organelles for progeny particle assembly within reorganized cell membranes.Viral weapons of membrane destruction: variable modes of membrane penetration by non-enveloped viruses.High-resolution 3D structures reveal the biological functions of reoviruses.Lipid Membranes Facilitate Conformational Changes Required for Reovirus Cell Entry.
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P2860
Putative autocleavage of outer capsid protein micro1, allowing release of myristoylated peptide micro1N during particle uncoating, is critical for cell entry by reovirus.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Putative autocleavage of outer ...... al for cell entry by reovirus.
@en
type
label
Putative autocleavage of outer ...... al for cell entry by reovirus.
@en
prefLabel
Putative autocleavage of outer ...... al for cell entry by reovirus.
@en
P2093
P2860
P1433
P1476
Putative autocleavage of outer ...... cal for cell entry by reovirus
@en
P2093
Amy L Odegard
Kartik Chandran
Max L Nibert
Timothy S Baker
Xing Zhang
P2860
P304
P356
10.1128/JVI.78.16.8732-8745.2004
P407
P577
2004-08-01T00:00:00Z