Identification of functionally important negatively charged residues in the carboxy end of mouse hepatitis coronavirus A59 nucleocapsid protein.
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Ribonucleocapsid Formation of Severe Acute Respiratory Syndrome Coronavirus through Molecular Action of the N-Terminal Domain of N ProteinMouse hepatitis coronavirus nucleocapsid phosphorylation.Expression, crystallization and preliminary crystallographic study of mouse hepatitis virus (MHV) nucleocapsid protein C-terminal domain.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.Evolved variants of the membrane protein can partially replace the envelope protein in murine coronavirus assembly.Role of E542 and E545 missense mutations of PIK3CA in breast cancer: a comparative computational approach.Role of the coronavirus E viroporin protein transmembrane domain in virus assembly.Importance of the penultimate positive charge in mouse hepatitis coronavirus A59 membrane protein.Coronavirus envelope (E) protein remains at the site of assemblyIdentification of mouse hepatitis coronavirus A59 nucleocapsid protein phosphorylation sitesImportance of conserved cysteine residues in the coronavirus envelope protein.Structures of the N- and C-terminal domains of MHV-A59 nucleocapsid protein corroborate a conserved RNA-protein binding mechanism in coronavirusA 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.Identification of in vivo-interacting domains of the murine coronavirus nucleocapsid protein.Identification of protein functions using a machine-learning approach based on sequence-derived properties.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 ChimerasMouse hepatitis coronavirus A59 nucleocapsid protein is a type I interferon antagonist.
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P2860
Identification of functionally important negatively charged residues in the carboxy end of mouse hepatitis coronavirus A59 nucleocapsid protein.
description
2006 nî lūn-bûn
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2006 թուականի Մայիսին հրատարակուած գիտական յօդուած
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2006 թվականի մայիսին հրատարակված գիտական հոդված
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2006年の論文
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2006年学术文章
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2006年学术文章
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2006年学术文章
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2006年学术文章
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name
Identification of functionally ...... irus A59 nucleocapsid protein.
@ast
Identification of functionally ...... irus A59 nucleocapsid protein.
@en
Identification of functionally ...... irus A59 nucleocapsid protein.
@nl
type
label
Identification of functionally ...... irus A59 nucleocapsid protein.
@ast
Identification of functionally ...... irus A59 nucleocapsid protein.
@en
Identification of functionally ...... irus A59 nucleocapsid protein.
@nl
prefLabel
Identification of functionally ...... irus A59 nucleocapsid protein.
@ast
Identification of functionally ...... irus A59 nucleocapsid protein.
@en
Identification of functionally ...... irus A59 nucleocapsid protein.
@nl
P2093
P2860
P1433
P1476
Identification of functionally ...... irus A59 nucleocapsid protein.
@en
P2093
Andrew Blount
Brenda G Hogue
Sandhya Verma
Valerie Bednar
P2860
P304
P356
10.1128/JVI.80.9.4344-4355.2006
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P577
2006-05-01T00:00:00Z