Mumps virus matrix, fusion, and nucleocapsid proteins cooperate for efficient production of virus-like particles.
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Nucleocapsid proteins: roles beyond viral RNA packagingVirus budding and the ESCRT pathwayMolecular biology, pathogenesis and pathology of mumps virusCritical role of the fusion protein cytoplasmic tail sequence in parainfluenza virus assemblyNipah virus matrix protein: expert hacker of cellular machines.Requirements for Human Respiratory Syncytial Virus Glycoproteins in Assembly and Egress from Infected Cells.Structural analysis of respiratory syncytial virus reveals the position of M2-1 between the matrix protein and the ribonucleoprotein complexPIV5 M protein interaction with host protein angiomotin-like 1Newcastle disease virus-like particles: preparation, purification, quantification, and incorporation of foreign glycoproteinsParamyxovirus assembly and budding: building particles that transmit infections.Self-assembly and release of peste des petits ruminants virus-like particles in an insect cell-baculovirus system and their immunogenicity in mice and goats.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.Efficient cellular release of Rift Valley fever virus requires genomic RNA.Parainfluenza virus 5 m protein interaction with host protein 14-3-3 negatively affects virus particle formation.Gene-specific contributions to mumps virus neurovirulence and neuroattenuation.Evidence for ubiquitin-regulated nuclear and subnuclear trafficking among Paramyxovirinae matrix proteinsRoles of Phosphorylation of the Nucleocapsid Protein of Mumps Virus in Regulating Viral RNA Transcription and Replication.Mumps Virus Is Released from the Apical Surface of Polarized Epithelial Cells, and the Release Is Facilitated by a Rab11-Mediated Transport System.Arenavirus budding: a common pathway with mechanistic differences.Mutations in the Transmembrane Domain and Cytoplasmic Tail of Hendra Virus Fusion Protein Disrupt Virus-Like-Particle Assembly.Dimerization Efficiency of Canine Distemper Virus Matrix Protein Regulates Membrane-Budding Activity.Simultaneous mutation of G275A and P276A in the matrix protein of Newcastle disease virus decreases virus replication and budding.Viral protein requirements for assembly and release of human parainfluenza virus type 3 virus-like particles.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.Roles of the three L-domains in β-retrovirus budding.A stabilized headless measles virus attachment protein stalk efficiently triggers membrane fusion.Matrix proteins of Nipah and Hendra viruses interact with beta subunits of AP-3 complexes.Structure and organization of paramyxovirus particles.The conserved YAGL motif in human metapneumovirus is required for higher-order cellular assemblies of the matrix protein and for virion production.Viral protein determinants of Lassa virus entry and release from polarized epithelial cells.Efficient budding of the tacaribe virus matrix protein z requires the nucleoprotein.Tsg101 is recruited by a late domain of the nucleocapsid protein to support budding of Marburg virus-like particles.Newcastle disease virus-like particles as a platform for the development of vaccines for human and agricultural pathogensCytoplasmic Motifs in the Nipah Virus Fusion Protein Modulate Virus Particle Assembly and Egress.Budding of Enveloped Viruses: Interferon-Induced ISG15-Antivirus Mechanisms Targeting the Release ProcessMutations in the FPIV motif of Newcastle disease virus matrix protein attenuate virus replication and reduce virus budding.Electrostatic interactions between Hendra virus matrix proteins are required for efficient virus-like particle assembly.Human Parainfluenza Virus Type 3 Matrix Protein Reduces Viral RNA Synthesis of HPIV3 by Regulating Inclusion Body Formation.
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Mumps virus matrix, fusion, and nucleocapsid proteins cooperate for efficient production of virus-like particles.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 13 May 2009
@en
vedecký článok
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vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
Mumps virus matrix, fusion, an ...... ction of virus-like particles.
@en
Mumps virus matrix, fusion, an ...... ction of virus-like particles.
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type
label
Mumps virus matrix, fusion, an ...... ction of virus-like particles.
@en
Mumps virus matrix, fusion, an ...... ction of virus-like particles.
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prefLabel
Mumps virus matrix, fusion, an ...... ction of virus-like particles.
@en
Mumps virus matrix, fusion, an ...... ction of virus-like particles.
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P2093
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P1476
Mumps virus matrix, fusion, an ...... ction of virus-like particles.
@en
P2093
Anthony P Schmitt
Phuong Tieu Schmitt
Thomas S McCrory
P2860
P304
P356
10.1128/JVI.00421-09
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P577
2009-05-13T00:00:00Z