Nucleocapsid incorporation into parainfluenza virus is regulated by specific interaction with matrix protein.
about
Parainfluenza virusesCritical role of the fusion protein cytoplasmic tail sequence in parainfluenza virus assemblyTrafficking of Sendai virus nucleocapsids is mediated by intracellular vesiclesCrystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoproteinThe human metapneumovirus matrix protein stimulates the inflammatory immune response in vitroStructural analysis of respiratory syncytial virus reveals the position of M2-1 between the matrix protein and the ribonucleoprotein complexMapping of the VP40-binding regions of the nucleoprotein of Ebola virus.Association of ebola virus matrix protein VP40 with microtubules.Peste des petits ruminants virus infection of small ruminants: a comprehensive review.A role for the C terminus of Mopeia virus nucleoprotein in its incorporation into Z protein-induced virus-like particles.Rescue of a chimeric rinderpest virus with the nucleocapsid protein derived from peste-des-petits-ruminants virus: use as a marker vaccineParamyxovirus assembly and budding: building particles that transmit infections.Paramyxovirus glycoprotein incorporation, assembly and budding: a three way dance for infectious particle production.The C-terminal end of parainfluenza virus 5 NP protein is important for virus-like particle production and M-NP protein interaction.Gene-specific contributions to mumps virus neurovirulence and neuroattenuation.Evidence for ubiquitin-regulated nuclear and subnuclear trafficking among Paramyxovirinae matrix proteinsQuantitative analysis of Nipah virus proteins released as virus-like particles reveals central role for the matrix protein.Critical role of Rab11a-mediated recycling endosomes in the assembly of type I parainfluenza viruses.The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded.Biarsenical labeling of vesicular stomatitis virus encoding tetracysteine-tagged m protein allows dynamic imaging of m protein and virus uncoating in infected cells.Mutations in the Transmembrane Domain and Cytoplasmic Tail of Hendra Virus Fusion Protein Disrupt Virus-Like-Particle Assembly.C-Terminal DxD-Containing Sequences within Paramyxovirus Nucleocapsid Proteins Determine Matrix Protein Compatibility and Can Direct Foreign Proteins into Budding Particles.Interaction of Human Parainfluenza Virus Type 3 Nucleoprotein with Matrix Protein Mediates Internal Viral Protein Assembly.High-throughput virtual screening and docking studies of matrix protein vp40 of ebola virus.Nontransmissible virus-like particle formation by F-deficient sendai virus is temperature sensitive and reduced by mutations in M and HN proteins.A new Sendai virus vector deficient in the matrix gene does not form virus particles and shows extensive cell-to-cell spreadingThe matrix protein of measles virus regulates viral RNA synthesis and assembly by interacting with the nucleocapsid protein.Borna disease virus matrix protein is an integral component of the viral ribonucleoprotein complex that does not interfere with polymerase activity.Ebola virus VP35-VP40 interaction is sufficient for packaging 3E-5E minigenome RNA into virus-like particles.Contribution of ebola virus glycoprotein, nucleoprotein, and VP24 to budding of VP40 virus-like particles.Altered interaction of the matrix protein with the cytoplasmic tail of hemagglutinin modulates measles virus growth by affecting virus assembly and cell-cell fusion.A catalytically and genetically optimized beta-lactamase-matrix based assay for sensitive, specific, and higher throughput analysis of native henipavirus entry characteristics.Interaction between a unique minor protein and a major capsid protein of Bluetongue virus controls virus infectivity.The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein.Electrostatic interactions between Hendra virus matrix proteins are required for efficient virus-like particle assembly.Surveillance, isolation and complete genome sequence of bovine parainfluenza virus type 3 in Egyptian cattle
P2860
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P2860
Nucleocapsid incorporation into parainfluenza virus is regulated by specific interaction with matrix protein.
description
2001 nî lūn-bûn
@nan
2001 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
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
name
Nucleocapsid incorporation int ...... teraction with matrix protein.
@ast
Nucleocapsid incorporation int ...... teraction with matrix protein.
@en
type
label
Nucleocapsid incorporation int ...... teraction with matrix protein.
@ast
Nucleocapsid incorporation int ...... teraction with matrix protein.
@en
prefLabel
Nucleocapsid incorporation int ...... teraction with matrix protein.
@ast
Nucleocapsid incorporation int ...... teraction with matrix protein.
@en
P2093
P2860
P1433
P1476
Nucleocapsid incorporation int ...... teraction with matrix protein.
@en
P2093
P2860
P304
P356
10.1128/JVI.75.3.1117-1123.2001
P577
2001-02-01T00:00:00Z