Genetic evidence for a structural interaction between the carboxy termini of the membrane and nucleocapsid proteins of mouse hepatitis virus.
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X-Ray Structures of the N- and C-Terminal Domains of a Coronavirus Nucleocapsid Protein: Implications for Nucleocapsid FormationTransmissible 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.The spike protein of severe acute respiratory syndrome (SARS) is cleaved in virus infected Vero-E6 cells.SARS-CoV envelope protein palmitoylation or nucleocapid association is not required for promoting virus-like particle productionA structural analysis of M protein in coronavirus assembly and morphology.Self-assembly of severe acute respiratory syndrome coronavirus membrane protein.Expression, crystallization and preliminary crystallographic study of mouse hepatitis virus (MHV) nucleocapsid protein C-terminal domain.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.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.Coronavirus pathogenesis and the emerging pathogen severe acute respiratory syndrome coronavirus.Evolved variants of the membrane protein can partially replace the envelope protein in murine coronavirus assembly.Inefficient signalase cleavage promotes efficient nucleocapsid incorporation into budding flavivirus membranes.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.The 3' cis-acting genomic replication element of the severe acute respiratory syndrome coronavirus can function in the murine coronavirus genome.The nsp1, nsp13, and M proteins contribute to the hepatotropism of murine coronavirus JHM.WU.A hypervariable region within the 3' cis-acting element of the murine coronavirus genome is nonessential for RNA synthesis but affects pathogenesisExceptional flexibility in the sequence requirements for coronavirus small envelope protein functionFunctional transcriptional regulatory sequence (TRS) RNA binding and helix destabilizing determinants of murine hepatitis virus (MHV) nucleocapsid (N) protein.Importance of the penultimate positive charge in mouse hepatitis coronavirus A59 membrane protein.High fidelity of murine hepatitis virus replication is decreased in nsp14 exoribonuclease mutants.Envelope protein palmitoylations are crucial for murine coronavirus assembly.Chimeric coronavirus-like particles carrying severe acute respiratory syndrome coronavirus (SCoV) S protein protect mice against challenge with SCoVIdentifying SARS-CoV membrane protein amino acid residues linked to virus-like particle assembly.Structures of the N- and C-terminal domains of MHV-A59 nucleocapsid protein corroborate a conserved RNA-protein binding mechanism in coronavirusCharacterization of the RNA components of a putative molecular switch in the 3' untranslated region of the murine coronavirus genome.A key role for the carboxy-terminal tail of the murine coronavirus nucleocapsid protein in coordination of genome packagingCharacterization of a critical interaction between the coronavirus nucleocapsid protein and nonstructural protein 3 of the viral replicase-transcriptase complex.Importance of MHV-CoV A59 nucleocapsid protein COOH-terminal negative charges.Negatively charged residues in the endodomain are critical for specific assembly of spike protein into murine coronavirusMolecular targets for diagnostics and therapeutics of severe acute respiratory syndrome (SARS-CoV).
P2860
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P2860
Genetic evidence for a structural interaction between the carboxy termini of the membrane and nucleocapsid proteins of mouse hepatitis virus.
description
2002 nî lūn-bûn
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2002 թուականի Մայիսին հրատարակուած գիտական յօդուած
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2002 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2002年の論文
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2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
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2002年论文
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name
Genetic evidence for a structu ...... eins of mouse hepatitis virus.
@ast
Genetic evidence for a structu ...... eins of mouse hepatitis virus.
@en
Genetic evidence for a structu ...... eins of mouse hepatitis virus.
@nl
type
label
Genetic evidence for a structu ...... eins of mouse hepatitis virus.
@ast
Genetic evidence for a structu ...... eins of mouse hepatitis virus.
@en
Genetic evidence for a structu ...... eins of mouse hepatitis virus.
@nl
prefLabel
Genetic evidence for a structu ...... eins of mouse hepatitis virus.
@ast
Genetic evidence for a structu ...... eins of mouse hepatitis virus.
@en
Genetic evidence for a structu ...... eins of mouse hepatitis virus.
@nl
P2860
P1433
P1476
Genetic evidence for a structu ...... eins of mouse hepatitis virus.
@en
P2093
Paul S Masters
P2860
P304
P356
10.1128/JVI.76.10.4987-4999.2002
P407
P577
2002-05-01T00:00:00Z