Four proteins processed from the replicase gene polyprotein of mouse hepatitis virus colocalize in the cell periphery and adjacent to sites of virion assembly.
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Localization and Membrane Topology of Coronavirus Nonstructural Protein 4: Involvement of the Early Secretory Pathway in ReplicationTopology and Membrane Anchoring of the Coronavirus Replication Complex: Not All Hydrophobic Domains of nsp3 and nsp6 Are Membrane SpanningSevere Acute Respiratory Syndrome Coronavirus nsp9 Dimerization Is Essential for Efficient Viral GrowthNMR Structure of the SARS-CoV Nonstructural Protein 7 in Solution at pH 6.5The coronavirus nucleocapsid protein is dynamically associated with the replication-transcription complexes.Coronavirus replicase-reporter fusions provide quantitative analysis of replication and replication complex formation.Analysis of murine hepatitis virus strain A59 temperature-sensitive mutant TS-LA6 suggests that nsp10 plays a critical role in polyprotein processingAnalysis of intraviral protein-protein interactions of the SARS coronavirus ORFeome.Mouse hepatitis virus replicase proteins associate with two distinct populations of intracellular membranesIdentification of mouse hepatitis virus papain-like proteinase 2 activity.Expression, crystallization and preliminary crystallographic study of mouse hepatitis virus (MHV) nucleocapsid protein C-terminal domain.Exchange of the coronavirus replicase polyprotein cleavage sites alters protease specificity and processing.Coronaviruses induce entry-independent, continuous macropinocytosisStructural genomics of the severe acute respiratory syndrome coronavirus: nuclear magnetic resonance structure of the protein nsP7The nsp2 replicase proteins of murine hepatitis virus and severe acute respiratory syndrome coronavirus are dispensable for viral replication.RNA replication of mouse hepatitis virus takes place at double-membrane vesicles.Membrane association and dimerization of a cysteine-rich, 16-kilodalton polypeptide released from the C-terminal region of the coronavirus infectious bronchitis virus 1a polyprotein.Systematic assembly of a full-length infectious cDNA of mouse hepatitis virus strain A59.A novel severe acute respiratory syndrome coronavirus protein, U274, is transported to the cell surface and undergoes endocytosis.Heterogeneous nuclear ribonucleoprotein A1 regulates RNA synthesis of a cytoplasmic virusCrystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs.Dodecamer structure of severe acute respiratory syndrome coronavirus nonstructural protein nsp10.The polypyrimidine tract-binding protein affects coronavirus RNA accumulation levels and relocalizes viral RNAs to novel cytoplasmic domains different from replication-transcription sitesMutations across murine hepatitis virus nsp4 alter virus fitness and membrane modifications.Replication of murine hepatitis virus is regulated by papain-like proteinase 1 processing of nonstructural proteins 1, 2, and 3.Suppression of coronavirus replication by inhibition of the MEK signaling pathway.Dissection of amino-terminal functional domains of murine coronavirus nonstructural protein 3.Murine hepatitis virus replicase protein nsp10 is a critical regulator of viral RNA synthesis.Temperature-sensitive mutants and revertants in the coronavirus nonstructural protein 5 protease (3CLpro) define residues involved in long-distance communication and regulation of protease activityGenetic analysis of Murine hepatitis virus nsp4 in virus replicationGenetic interactions between an essential 3' cis-acting RNA pseudoknot, replicase gene products, and the extreme 3' end of the mouse coronavirus genomeA contemporary view of coronavirus transcription.Structures of the N- and C-terminal domains of MHV-A59 nucleocapsid protein corroborate a conserved RNA-protein binding mechanism in coronavirusSARS coronavirus replicase proteins in pathogenesis.The severe acute respiratory syndrome-coronavirus replicative protein nsp9 is a single-stranded RNA-binding subunit unique in the RNA virus world.Identification and characterization of severe acute respiratory syndrome coronavirus replicase proteins.Intracellular localization and protein interactions of the gene 1 protein p28 during mouse hepatitis virus replication.In Situ Tagged nsp15 Reveals Interactions with Coronavirus Replication/Transcription Complex-Associated Proteins.Biogenesis and dynamics of the coronavirus replicative structures.Coronavirus entry and release in polarized epithelial cells: a review.
P2860
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P2860
Four proteins processed from the replicase gene polyprotein of mouse hepatitis virus colocalize in the cell periphery and adjacent to sites of virion assembly.
description
2000 nî lūn-bûn
@nan
2000 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Four proteins processed from t ...... t to sites of virion assembly.
@ast
Four proteins processed from t ...... t to sites of virion assembly.
@en
type
label
Four proteins processed from t ...... t to sites of virion assembly.
@ast
Four proteins processed from t ...... t to sites of virion assembly.
@en
prefLabel
Four proteins processed from t ...... t to sites of virion assembly.
@ast
Four proteins processed from t ...... t to sites of virion assembly.
@en
P2093
P2860
P1433
P1476
Four proteins processed from t ...... nt to sites of virion assembly
@en
P2093
P2860
P304
P356
10.1128/JVI.74.7.3379-3387.2000
P577
2000-04-01T00:00:00Z