Requirements for the assembly and release of Newcastle disease virus-like particles. - sprookjes - yvandenbroek - TriplyDB

Requirements for the assembly and release of Newcastle disease virus-like particles.

Requirements for the assembly and release of Newcastle disease virus-like particles.

http://www.wikidata.org/entity/Q35139627

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Nucleocapsid proteins: roles beyond viral RNA packaging Structure and assembly of a paramyxovirus matrix protein 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 complex Newcastle disease virus-like particles containing respiratory syncytial virus G protein induced protection in BALB/c mice, with no evidence of immunopathology.PIV5 M protein interaction with host protein angiomotin-like 1 Newcastle disease virus-like particles: preparation, purification, quantification, and incorporation of foreign glycoproteins BALB/c mice immunized with a combination of virus-like particles incorporating Kaposi sarcoma-associated herpesvirus (KSHV) envelope glycoproteins gpK8.1, gB, and gH/gL induced comparable serum neutralizing antibody activity to UV-inactivated KSHV.Assembly and biological and immunological properties of Newcastle disease virus-like particles.Vaccine potential of Nipah virus-like particles Paramyxovirus 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.Modification of the respiratory syncytial virus f protein in virus-like particles impacts generation of B cell memory.Paramyxovirus glycoprotein incorporation, assembly and budding: a three way dance for infectious particle production.Assembly and immunological properties of Newcastle disease virus-like particles containing the respiratory syncytial virus F and G proteins.Biological challenges and technological opportunities for respiratory syncytial virus vaccine development.Different regions of the newcastle disease virus fusion protein modulate pathogenicity.Molecular mechanism of arenavirus assembly and budding.Efficient cellular release of Rift Valley fever virus requires genomic RNA.Evidence for ubiquitin-regulated nuclear and subnuclear trafficking among Paramyxovirinae matrix proteins Roles of the fusion and hemagglutinin-neuraminidase proteins in replication, tropism, and pathogenicity of avian paramyxoviruses.Quantitative analysis of Nipah virus proteins released as virus-like particles reveals central role for the matrix protein.Emerging paramyxoviruses: molecular mechanisms and antiviral strategies Murine immune responses to virus-like particle-associated pre- and postfusion forms of the respiratory syncytial virus F protein Vesicle formation by self-assembly of membrane-bound matrix proteins into a fluidlike budding domain.Cotton rat immune responses to virus-like particles containing the pre-fusion form of respiratory syncytial virus fusion protein.Long-term and memory immune responses in mice against Newcastle disease virus-like particles containing respiratory syncytial virus glycoprotein ectodomains Chapter 4 - Reconstitution of membrane budding with unilamellar vesicles The YPLGVG sequence of the Nipah virus matrix protein is required for budding Mumps virus matrix, fusion, and nucleocapsid proteins cooperate for efficient production of virus-like particles.Evidence for the interaction of the human metapneumovirus G and F proteins during virus-like particle formation.Novel Epstein-Barr virus-like particles incorporating gH/gL-EBNA1 or gB-LMP2 induce high neutralizing antibody titers and EBV-specific T-cell responses in immunized mice.Virulence of Newcastle disease virus: what is known so far?Virus-like particle vaccine confers protection against a lethal newcastle disease virus challenge in chickens and allows a strategy of differentiating infected from vaccinated animals Recombinant Newcastle disease virus-vectored vaccines against human and animal infectious diseases.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.Paramyxovirus Glycoproteins and the Membrane Fusion Process.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.

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Requirements for the assembly and release of Newcastle disease virus-like particles.

http://www.wikidata.org/entity/Q35139627

description

2006 nî lūn-bûn

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2006 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2006 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

Requirements for the assembly and release of Newcastle disease virus-like particles.

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Requirements for the assembly and release of Newcastle disease virus-like particles.

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Requirements for the assembly and release of Newcastle disease virus-like particles.

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Requirements for the assembly and release of Newcastle disease virus-like particles.

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Requirements for the assembly and release of Newcastle disease virus-like particles.

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Requirements for the assembly and release of Newcastle disease virus-like particles.

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P1433

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Journal of Virology

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Requirements for the assembly and release of Newcastle disease virus-like particles.

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P2093

Homer D Pantua

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Lori W McGinnes

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Mark E Peeples

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Trudy G Morrison

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P2860

The protein network of HIV budding

Late assembly domain function can exhibit context dependence and involves ubiquitin residues implicated in endocytosis.

Budding viral hijackers co-opt the endocytic machinery to make a getaway

A matrix-less measles virus is infectious and elicits extensive cell fusion: consequences for propagation in the brain.

Efficient selection for high-expression transfectants with a novel eukaryotic vector

AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding

HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress

Escaping from the cell: assembly and budding of negative-strand RNA viruses

Retrovirus budding

Viral liposomes released from insect cells infected with recombinant baculovirus expressing the matrix protein of vesicular stomatitis virus

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11062-11073

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scholarly article

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10.1128/JVI.00726-06

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80

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2006-09-13T00:00:00Z

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16971425

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