The membrane M protein carboxy terminus binds to transmissible gastroenteritis coronavirus core and contributes to core stability.
about
Cooperation of an RNA packaging signal and a viral envelope protein in coronavirus RNA packagingBinding of transmissible gastroenteritis coronavirus to cell surface sialoglycoproteins.Severe acute respiratory syndrome coronavirus 3a protein is a viral structural proteinGeneration of a replication-competent, propagation-deficient virus vector based on the transmissible gastroenteritis coronavirus genome.Transmissible Gastroenteritis Coronavirus Packaging Signal Is Located at the 5' End of the Virus GenomeRibonucleocapsid Formation of Severe Acute Respiratory Syndrome Coronavirus through Molecular Action of the N-Terminal Domain of N ProteinCharacterization of an Immunodominant Epitope in the Endodomain of the Coronavirus Membrane ProteinThe 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.Cryo-electron tomography of mouse hepatitis virus: Insights into the structure of the coronavirion.Mouse hepatitis coronavirus nucleocapsid phosphorylation.Sumoylation of the nucleocapsid protein of severe acute respiratory syndrome coronavirus.Interaction of the coronavirus infectious bronchitis virus membrane protein with beta-actin and its implication in virion assembly and buddingA structural analysis of M protein in coronavirus assembly and morphology.Self-assembly of severe acute respiratory syndrome coronavirus membrane protein.A major determinant for membrane protein interaction localizes to the carboxy-terminal domain of the mouse coronavirus nucleocapsid protein.The coronavirus nucleocapsid is a multifunctional protein.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.Evolved variants of the membrane protein can partially replace the envelope protein in murine coronavirus assembly.Identification of functionally important negatively charged residues in the carboxy end of mouse hepatitis coronavirus A59 nucleocapsid protein.Nucleocapsid-independent specific viral RNA packaging via viral envelope protein and viral RNA signal.Switching species tropism: an effective way to manipulate the feline coronavirus genome.The small envelope protein E is not essential for murine coronavirus replication.Supramolecular architecture of severe acute respiratory syndrome coronavirus revealed by electron cryomicroscopy.Importance of the penultimate positive charge in mouse hepatitis coronavirus A59 membrane protein.Subcellular localization of SARS-CoV structural proteins.Identification of mouse hepatitis coronavirus A59 nucleocapsid protein phosphorylation sitesIdentifying SARS-CoV membrane protein amino acid residues linked to virus-like particle assembly.Identification of cellular proteome using two-dimensional difference gel electrophoresis in ST cells infected with transmissible gastroenteritis coronavirus.Importance of MHV-CoV A59 nucleocapsid protein COOH-terminal negative charges.Transmissible gastroenteritis coronavirus genome packaging signal is located at the 5' end of the genome and promotes viral RNA incorporation into virions in a replication-independent processGenetic analysis of determinants for spike glycoprotein assembly into murine coronavirus virions: distinct roles for charge-rich and cysteine-rich regions of the endodomain.Porcine Epidemic Diarrhea Virus 3C-Like Protease-Mediated Nucleocapsid Processing: Possible Link to Viral Cell Culture Adaptability.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.Analyses of Coronavirus Assembly Interactions with Interspecies Membrane and Nucleocapsid Protein ChimerasImmunogenicity of transmissible gastroenteritis virus (TGEV) M gene delivered by attenuated Salmonella typhimurium in mice.Localization to the nucleolus is a common feature of coronavirus nucleoproteins, and the protein may disrupt host cell division.Organization of two transmissible gastroenteritis coronavirus membrane protein topologies within the virion and core.Transcription regulatory sequences and mRNA expression levels in the coronavirus transmissible gastroenteritis virus.
P2860
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P2860
The membrane M protein carboxy terminus binds to transmissible gastroenteritis coronavirus core and contributes to core stability.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
2001年论文
@zh
2001年论文
@zh-cn
name
The membrane M protein carboxy ...... contributes to core stability.
@en
The membrane M protein carboxy ...... contributes to core stability.
@nl
type
label
The membrane M protein carboxy ...... contributes to core stability.
@en
The membrane M protein carboxy ...... contributes to core stability.
@nl
prefLabel
The membrane M protein carboxy ...... contributes to core stability.
@en
The membrane M protein carboxy ...... contributes to core stability.
@nl
P2860
P50
P1433
P1476
The membrane M protein carboxy ...... contributes to core stability.
@en
P2093
P2860
P304
P356
10.1128/JVI.75.3.1312-1324.2001
P407
P577
2001-02-01T00:00:00Z