In vitro disassembly of a parvovirus capsid and effect on capsid stability of heterologous peptide insertions in surface loops.
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Packaging capacity of adeno-associated virus serotypes: impact of larger genomes on infectivity and postentry steps.Structural determinants of tissue tropism and in vivo pathogenicity for the parvovirus minute virus of miceMechanical disassembly of single virus particles reveals kinetic intermediates predicted by theory.Thermal stability of Cpl-7 endolysin from the streptococcus pneumoniae bacteriophage Cp-7; cell wall-targeting of its CW_7 motifs.Detecting small changes and additional peptides in the canine parvovirus capsid structureMechanical elasticity as a physical signature of conformational dynamics in a virus particleThe role of capsid maturation on adenovirus priming for sequential uncoatingManipulation of the mechanical properties of a virus by protein engineering.Role of interfacial amino acid residues in assembly, stability, and conformation of a spherical virus capsid.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.AAV-ID: A Rapid and Robust Assay for Batch-to-Batch Consistency Evaluation of AAV Preparations.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.Nuclear export of the nonenveloped parvovirus virion is directed by an unordered protein signal exposed on the capsid surface.Surface-exposed adeno-associated virus Vp1-NLS capsid fusion protein rescues infectivity of noninfectious wild-type Vp2/Vp3 and Vp3-only capsids but not that of fivefold pore mutant virions.Structural Analysis of a Temperature-Induced Transition in a Viral Capsid Probed by HDX-MS.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.Mutational analysis of narrow pores at the fivefold symmetry axes of adeno-associated virus type 2 capsids reveals a dual role in genome packaging and activation of phospholipase A2 activityExpression and subcellular targeting of canine parvovirus capsid proteins in baculovirus-transduced NLFK cells.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.Separate basic region motifs within the adeno-associated virus capsid proteins are essential for infectivity and assemblyThermal stability of RNA phage virus-like particles displaying foreign peptidesAtomic Resolution Structures of Human Bufaviruses Determined by Cryo-Electron Microscopy.Systematic analysis of biological roles of charged amino acid residues located throughout the structured inner wall of a virus capsid.
P2860
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P2860
In vitro disassembly of a parvovirus capsid and effect on capsid stability of heterologous peptide insertions in surface loops.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
In vitro disassembly of a parv ...... e insertions in surface loops.
@en
type
label
In vitro disassembly of a parv ...... e insertions in surface loops.
@en
prefLabel
In vitro disassembly of a parv ...... e insertions in surface loops.
@en
P2860
P50
P356
P1476
In vitro disassembly of a parv ...... e insertions in surface loops.
@en
P2093
José María Almendral
P2860
P304
P356
10.1074/JBC.M307662200
P407
P577
2003-12-01T00:00:00Z