A beta-stranded motif drives capsid protein oligomers of the parvovirus minute virus of mice into the nucleus for viral assembly
about
The NS2 proteins of parvovirus minute virus of mice are required for efficient nuclear egress of progeny virions in mouse cells.Role of capsid proteins in parvoviruses infectionStructure of Penaeus stylirostris Densovirus, a Shrimp PathogenStructure of Bombyx mori Densovirus 1, a Silkworm PathogenMinute virus of mice NS1 interacts with the SMN protein, and they colocalize in novel nuclear bodies induced by parvovirus infectionThe structure of human parvovirus B19Mutagenesis of adeno-associated virus type 2 capsid protein VP1 uncovers new roles for basic amino acids in trafficking and cell-specific transduction.Expression analysis of Bombyx mori bidensovirus structural proteins and assembly of virus-like particles in insect cells.Interaction of the Vp3 nuclear localization signal with the importin alpha 2/beta heterodimer directs nuclear entry of infecting simian virus 40.The role of nuclear localization signal in parvovirus life cycle.Phosphorylation status of the parvovirus minute virus of mice particle: mapping and biological relevance of the major phosphorylation sites.Host-selected amino acid changes at the sialic acid binding pocket of the parvovirus capsid modulate cell binding affinity and determine virulence.Mechanical disassembly of single virus particles reveals kinetic intermediates predicted by theory.The VP1 N-terminal sequence of canine parvovirus affects nuclear transport of capsids and efficient cell infectionInteraction between parvovirus NS2 protein and nuclear export factor Crm1 is important for viral egress from the nucleus of murine cells.Classic nuclear localization signals and a novel nuclear localization motif are required for nuclear transport of porcine parvovirus capsid proteins.Nucleocytoplasmic traffic disorder induced by cardioviruses.High mutant frequency in populations of a DNA virus allows evasion from antibody therapy in an immunodeficient hostParvovirus particles and movement in the cellular cytoplasm and effects of the cytoskeleton.DNA-mediated anisotropic mechanical reinforcement of a virus.Nuclear envelope disruption involving host caspases plays a role in the parvovirus replication cycle.Nuclear import of viral DNA genomes.The Mammalian Cell Cycle Regulates Parvovirus Nuclear Capsid Assembly.Pathways of cell infection by parvoviruses and adeno-associated virusesExploitation of microtubule cytoskeleton and dynein during parvoviral traffic toward the nucleus.Role of interfacial amino acid residues in assembly, stability, and conformation of a spherical virus capsid.DNA virus replication compartments.Nuclear entry of DNA viruses.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.Genome replication and postencapsidation functions mapping to the nonstructural gene restrict the host range of a murine parvovirus in human cells.Complementary roles of multiple nuclear targeting signals in the capsid proteins of the parvovirus minute virus of mice during assembly and onset of infection.Translation control by protein kinase R restricts minute virus of mice infection: role in parvovirus oncolysis.Viral oncolysis that targets Raf-1 signaling control of nuclear transport.Nuclear export of the nonenveloped parvovirus virion is directed by an unordered protein signal exposed on the capsid surface.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.Functional relevance of amino acid residues involved in interactions with ordered nucleic acid in a spherical virus.Expression and subcellular targeting of canine parvovirus capsid proteins in baculovirus-transduced NLFK cells.In vitro disassembly of a parvovirus capsid and effect on capsid stability of heterologous peptide insertions in surface loops.
P2860
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P2860
A beta-stranded motif drives capsid protein oligomers of the parvovirus minute virus of mice into the nucleus for viral assembly
description
2000 nî lūn-bûn
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A beta-stranded motif drives c ...... the nucleus for viral assembly
@ast
A beta-stranded motif drives c ...... the nucleus for viral assembly
@en
type
label
A beta-stranded motif drives c ...... the nucleus for viral assembly
@ast
A beta-stranded motif drives c ...... the nucleus for viral assembly
@en
prefLabel
A beta-stranded motif drives c ...... the nucleus for viral assembly
@ast
A beta-stranded motif drives c ...... the nucleus for viral assembly
@en
P2093
P2860
P1433
P1476
A beta-stranded motif drives c ...... the nucleus for viral assembly
@en
P2093
E Lombardo
J C Ramírez
J M Almendral
M Agbandje-McKenna
P2860
P304
P356
10.1128/JVI.74.8.3804-3814.2000
P577
2000-04-01T00:00:00Z