A critical phenylalanine residue in the respiratory syncytial virus fusion protein cytoplasmic tail mediates assembly of internal viral proteins into viral filaments and particles.
about
Critical role of the fusion protein cytoplasmic tail sequence in parainfluenza virus assemblyHost cytoskeleton in respiratory syncytial virus assembly and buddingNew host factors important for respiratory syncytial virus (RSV) replication revealed by a novel microfluidics screen for interactors of matrix (M) proteinArchitecture of respiratory syncytial virus revealed by electron cryotomography.The Thr205 phosphorylation site within respiratory syncytial virus matrix (M) protein modulates M oligomerization and virus productionParamyxovirus glycoprotein incorporation, assembly and budding: a three way dance for infectious particle production.Respiratory syncytial virus assembles into structured filamentous virion particles independently of host cytoskeleton and related proteinsCurrent concepts and progress in RSV vaccine development.Dimerization of matrix protein is required for budding of respiratory syncytial virus.Breaking in: human metapneumovirus fusion and entryImaging viral RNA using multiply labeled tetravalent RNA imaging probes in live cellsProgressive changes in inflammatory and matrix adherence of bronchial epithelial cells with persistent respiratory syncytial virus (RSV) infection (progressive changes in RSV infection).Packaging and Prefusion Stabilization Separately and Additively Increase the Quantity and Quality of Respiratory Syncytial Virus (RSV)-Neutralizing Antibodies Induced by an RSV Fusion Protein Expressed by a Parainfluenza Virus Vector.The Respiratory Syncytial Virus Phosphoprotein, Matrix Protein, and Fusion Protein Carboxy-Terminal Domain Drive Efficient Filamentous Virus-Like Particle Formation.Molecular mechanisms driving respiratory syncytial virus assembly.Gene sequence variability of the three surface proteins of human respiratory syncytial virus (HRSV) in TexasF-actin modulates measles virus cell-cell fusion and assembly by altering the interaction between the matrix protein and the cytoplasmic tail of hemagglutinin.Phenylalanine residues at the carboxyl terminus of the herpes simplex virus 1 UL20 membrane protein regulate cytoplasmic virion envelopment and infectious virus productionFunctional correlations of respiratory syncytial virus proteins to intrinsic disorder.RSV glycoprotein and genomic RNA dynamics reveal filament assembly prior to the plasma membraneThe respiratory syncytial virus fusion protein targets to the perimeter of inclusion bodies and facilitates filament formation by a cytoplasmic tail-dependent mechanism.The Morphology and Assembly of Respiratory Syncytial Virus Revealed by Cryo-Electron TomographyRespiratory Syncytial Virus Matrix (M) Protein Interacts with Actin In Vitro and in Cell Culture
P2860
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P2860
A critical phenylalanine residue in the respiratory syncytial virus fusion protein cytoplasmic tail mediates assembly of internal viral proteins into viral filaments and particles.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
A critical phenylalanine resid ...... viral filaments and particles.
@ast
A critical phenylalanine resid ...... viral filaments and particles.
@en
type
label
A critical phenylalanine resid ...... viral filaments and particles.
@ast
A critical phenylalanine resid ...... viral filaments and particles.
@en
prefLabel
A critical phenylalanine resid ...... viral filaments and particles.
@ast
A critical phenylalanine resid ...... viral filaments and particles.
@en
P2093
P2860
P356
P1433
P1476
A critical phenylalanine resid ...... viral filaments and particles.
@en
P2093
Aaron W Lifland
Anne L Hotard
Fyza Y Shaikh
Martin L Moore
Philip J Santangelo
Reagan G Cox
P2860
P356
10.1128/MBIO.00270-11
P577
2012-02-07T00:00:00Z