Nuclear export of the nonenveloped parvovirus virion is directed by an unordered protein signal exposed on the capsid surface.
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Salamander limb regeneration involves the activation of a multipotent skeletal muscle satellite cell population.Role of capsid proteins in parvoviruses infectionStructure of a Packaging-Defective Mutant of Minute Virus of Mice Indicates that the Genome Is Packaged via a Pore at a 5-Fold AxisComplementary induction of immunogenic cell death by oncolytic parvovirus H-1PV and gemcitabine in pancreatic cancerVirulent variants emerging in mice infected with the apathogenic prototype strain of the parvovirus minute virus of mice exhibit a capsid with low avidity for a primary receptor.VP2 cleavage and the leucine ring at the base of the fivefold cylinder control pH-dependent externalization of both the VP1 N terminus and the genome of minute virus of mice.Parvovirus particles and movement in the cellular cytoplasm and effects of the cytoskeleton.NS1 interaction with CKII alpha: novel protein complex mediating parvovirus-induced cytotoxicity.Molecular and functional analyses of a human parvovirus B19 infectious clone demonstrates essential roles for NS1, VP1, and the 11-kilodalton protein in virus replication and infectivity.DNA-mediated anisotropic mechanical reinforcement of a virus.The parvoviral capsid controls an intracellular phase of infection essential for efficient killing of stepwise-transformed human fibroblasts.A theoretical model for the dynamic structure of hepatitis B nucleocapsidMechanical elasticity as a physical signature of conformational dynamics in a virus particleAn in-frame deletion in the NS protein-coding sequence of parvovirus H-1PV efficiently stimulates export and infectivity of progeny virions.Manipulation of the mechanical properties of a virus by protein engineering.A supraphysiological nuclear export signal is required for parvovirus nuclear export.Distinct host cell fates for human malignant melanoma targeted by oncolytic rodent parvoviruses.Enhanced cytoplasmic sequestration of the nuclear export receptor CRM1 by NS2 mutations developed in the host regulates parvovirus fitness.Virus engineering: functionalization and stabilization.Structural basis for biologically relevant mechanical stiffening of a virus capsid by cavity-creating or spacefilling mutations.Late Maturation Steps Preceding Selective Nuclear Export and Egress of Progeny Parvovirus.A slender tract of glycine residues is required for translocation of the VP2 protein N-terminal domain through the parvovirus MVM capsid channel to initiate infection.Viral oncolysis that targets Raf-1 signaling control of nuclear transport.Dynamics and interactions of parvoviral NS1 protein in the nucleus.Structural Analysis of a Temperature-Induced Transition in a Viral Capsid Probed by HDX-MS.Low pH-dependent endosomal processing of the incoming parvovirus minute virus of mice virion leads to externalization of the VP1 N-terminal sequence (N-VP1), N-VP2 cleavage, and uncoating of the full-length genome.Parvovirus Capsid Structures Required for Infection: Mutations Controlling Receptor Recognition and Protease Cleavages.Functional relevance of amino acid residues involved in interactions with ordered nucleic acid in a spherical virus.Reorganization of Nuclear Pore Complexes and the Lamina in Late-Stage Parvovirus Infection.Quantitatively probing propensity for structural transitions in engineered virus nanoparticles by single-molecule mechanical analysis.Minute virus of mice, a parvovirus, in complex with the Fab fragment of a neutralizing monoclonal antibody.Protoparvovirus Cell Entry.Optimizing the Targeting of Mouse Parvovirus 1 to Murine Melanoma Selects for Recombinant Genomes and Novel Mutations in the Viral Capsid Gene.Mutations in the Non-Structural Protein-Coding Sequence of Protoparvovirus H-1PV Enhance the Fitness of the Virus and Show Key Benefits Regarding the Transduction Efficiency of Derived Vectors.Systematic analysis of biological roles of charged amino acid residues located throughout the structured inner wall of a virus capsid.Parvoviruses: structure and infection
P2860
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P2860
Nuclear export of the nonenveloped parvovirus virion is directed by an unordered protein signal exposed on the capsid surface.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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name
Nuclear export of the nonenvel ...... exposed on the capsid surface.
@en
Nuclear export of the nonenvel ...... exposed on the capsid surface.
@nl
type
label
Nuclear export of the nonenvel ...... exposed on the capsid surface.
@en
Nuclear export of the nonenvel ...... exposed on the capsid surface.
@nl
prefLabel
Nuclear export of the nonenvel ...... exposed on the capsid surface.
@en
Nuclear export of the nonenvel ...... exposed on the capsid surface.
@nl
P2093
P2860
P1433
P1476
Nuclear export of the nonenvel ...... exposed on the capsid surface.
@en
P2093
Beatriz Maroto
José M Almendral
Noelia Valle
P2860
P304
10685-10694
P356
10.1128/JVI.78.19.10685-10694.2004
P407
P577
2004-10-01T00:00:00Z