Coronavirus particle assembly: primary structure requirements of the membrane protein.
about
Rewiring the severe acute respiratory syndrome coronavirus (SARS-CoV) transcription circuit: engineering a recombination-resistant genomeAssembly of the coronavirus envelope: homotypic interactions between the M proteinsThe M, E, and N structural proteins of the severe acute respiratory syndrome coronavirus are required for efficient assembly, trafficking, and release of virus-like particles.Immune responses against severe acute respiratory syndrome coronavirus induced by virus-like particles in mice.Interaction of the coronavirus infectious bronchitis virus membrane protein with beta-actin and its implication in virion assembly and buddingPathogenicity of severe acute respiratory coronavirus deletion mutants in hACE-2 transgenic mice.Analysis of constructed E gene mutants of mouse hepatitis virus confirms a pivotal role for E protein in coronavirus assemblyRetargeting of coronavirus by substitution of the spike glycoprotein ectodomain: crossing the host cell species barrierSelf-assembly of severe acute respiratory syndrome coronavirus membrane protein.Structural maturation of the transmissible gastroenteritis coronavirus.Production and immunogenicity of chimeric virus-like particles containing the spike glycoprotein of infectious bronchitis virus.A major determinant for membrane protein interaction localizes to the carboxy-terminal domain of the mouse coronavirus nucleocapsid protein.Contribution of trafficking signals in the cytoplasmic tail of the infectious bronchitis virus spike protein to virus infection.The coronavirus nucleocapsid is a multifunctional protein.An interaction between the nucleocapsid protein and a component of the replicase-transcriptase complex is crucial for the infectivity of coronavirus genomic RNA.A conserved domain in the coronavirus membrane protein tail is important for virus assembly.Genetic evidence for a structural interaction between the carboxy termini of the membrane and nucleocapsid proteins of mouse hepatitis virus.Coronaviruses maintain viability despite dramatic rearrangements of the strictly conserved genome organizationEvolved variants of the membrane protein can partially replace the envelope protein in murine coronavirus assembly.Switching species tropism: an effective way to manipulate the feline coronavirus genome.The small envelope protein E is not essential for murine coronavirus replication.Incorporation of spike and membrane glycoproteins into coronavirus virions.A severe acute respiratory syndrome coronavirus that lacks the E gene is attenuated in vitro and in vivo.Development of a real-time reverse transcription loop-mediated isothermal amplification method for the rapid detection of porcine epidemic diarrhea virus.Exceptional flexibility in the sequence requirements for coronavirus small envelope protein functionImportance of the penultimate positive charge in mouse hepatitis coronavirus A59 membrane protein.Identification of a conserved linear B-cell epitope in the M protein of porcine epidemic diarrhea virusDifference in receptor usage between severe acute respiratory syndrome (SARS) coronavirus and SARS-like coronavirus of bat origin.Identifying SARS-CoV membrane protein amino acid residues linked to virus-like particle assembly.A key role for the carboxy-terminal tail of the murine coronavirus nucleocapsid protein in coordination of genome packagingMolecular targets for diagnostics and therapeutics of severe acute respiratory syndrome (SARS-CoV).The E protein is a multifunctional membrane protein of SARS-CoV.Generation of synthetic severe acute respiratory syndrome coronavirus pseudoparticles: implications for assembly and vaccine production.Recognition of the murine coronavirus genomic RNA packaging signal depends on the second RNA-binding domain of the nucleocapsid protein.Cleavage of group 1 coronavirus spike proteins: how furin cleavage is traded off against heparan sulfate binding upon cell culture adaptation.Analyses of Coronavirus Assembly Interactions with Interspecies Membrane and Nucleocapsid Protein ChimerasMapping of the coronavirus membrane protein domains involved in interaction with the spike protein.Assembly of spikes into coronavirus particles is mediated by the carboxy-terminal domain of the spike protein.The membrane M protein carboxy terminus binds to transmissible gastroenteritis coronavirus core and contributes to core stability.Studies on membrane topology, N-glycosylation and functionality of SARS-CoV membrane protein.
P2860
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P2860
Coronavirus particle assembly: primary structure requirements of the membrane protein.
description
1998 nî lūn-bûn
@nan
1998 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Coronavirus particle assembly: primary structure requirements of the membrane protein
@nl
Coronavirus particle assembly: primary structure requirements of the membrane protein.
@ast
Coronavirus particle assembly: primary structure requirements of the membrane protein.
@en
type
label
Coronavirus particle assembly: primary structure requirements of the membrane protein
@nl
Coronavirus particle assembly: primary structure requirements of the membrane protein.
@ast
Coronavirus particle assembly: primary structure requirements of the membrane protein.
@en
prefLabel
Coronavirus particle assembly: primary structure requirements of the membrane protein
@nl
Coronavirus particle assembly: primary structure requirements of the membrane protein.
@ast
Coronavirus particle assembly: primary structure requirements of the membrane protein.
@en
P2093
P2860
P1433
P1476
Coronavirus particle assembly: primary structure requirements of the membrane protein.
@en
P2093
P2860
P304
P577
1998-08-01T00:00:00Z