Scaffolding protein regulates the polymerization of P22 coat subunits into icosahedral shells in vitro.
about
Structural basis for scaffolding-mediated assembly and maturation of a dsDNA virusBacteriophage protein-protein interactionsAcquiring Structural Information on Virus Particles with Charge Detection Mass SpectrometryAssembly of the herpes simplex virus procapsid from purified components and identification of small complexes containing the major capsid and scaffolding proteins.The bacteriophage lambda gpNu3 scaffolding protein is an intrinsically disordered and biologically functional procapsid assembly catalyst.'Let the phage do the work': using the phage P22 coat protein structures as a framework to understand its folding and assembly mutantsVisualizing virus assembly intermediates inside marine cyanobacteriaPressure denaturation of the bacteriophage P22 coat protein and its entropic stabilization in icosahedral shells.Highly specific salt bridges govern bacteriophage P22 icosahedral capsid assembly: identification of the site in coat protein responsible for interaction with scaffolding protein.Pattern formation in icosahedral virus capsids: the papova viruses and Nudaurelia capensis beta virusNucleation and growth phases in the polymerization of coat and scaffolding subunits into icosahedral procapsid shells.Exploring the paths of (virus) assemblyRole of the scaffolding protein in P22 procapsid size determination suggested by T = 4 and T = 7 procapsid structures.Solution x-ray scattering-based estimation of electron cryomicroscopy imaging parameters for reconstruction of virus particles.Mechanism of scaffolding-directed virus assembly suggested by comparison of scaffolding-containing and scaffolding-lacking P22 procapsids.Penton release from P22 heat-expanded capsids suggests importance of stabilizing penton-hexon interactions during capsid maturation.P22 viral capsids as nanocomposite high-relaxivity MRI contrast agentsLocal rule-based theory of virus shell assembly.Molecular dissection of ø29 scaffolding protein function in an in vitro assembly systemCharacterization of the Proteins Associated with Caulobacter crescentus Bacteriophage CbK ParticlesThermolabile folding intermediates: inclusion body precursors and chaperonin substrates.In vitro screening for molecules that affect virus capsid assembly (and other protein association reactions)Conformational switch-defective X174 internal scaffolding proteins kinetically trap assembly intermediates before procapsid formation.Mechanism of capsid maturation in a double-stranded DNA virus.Cloning, purification, and preliminary characterization by circular dichroism and NMR of a carboxyl-terminal domain of the bacteriophage P22 scaffolding protein.Unraveling the role of the C-terminal helix turn helix of the coat-binding domain of bacteriophage P22 scaffolding protein.A virus-like particle vaccine platform elicits heightened and hastened local lung mucosal antibody production after a single dose.Symmetry Controlled, Genetic Presentation of Bioactive Proteins on the P22 Virus-like Particle Using an External Decoration Protein.Contextual Role of a Salt Bridge in the Phage P22 Coat Protein I-Domain.Detection of intermediates and kinetic control during assembly of bacteriophage P22 procapsidMechanisms of genome propagation and helper exploitation by satellite phage P4.Self-assembly of brome mosaic virus capsids: insights from shorter time-scale experiments.Location of the bacteriophage P22 coat protein C-terminus provides opportunities for the design of capsid-based materials.ϕX174 Procapsid Assembly: Effects of an Inhibitory External Scaffolding Protein and Resistant Coat Proteins In VitroDecoding bacteriophage P22 assembly: identification of two charged residues in scaffolding protein responsible for coat protein interactionPolyhead formation in phage P22 pinpoints a region in coat protein required for conformational switching.A virally encoded chaperone specialized for folding of the major capsid protein of African swine fever virus.Sequential interactions of structural proteins in phage phi 29 procapsid assembly.Approaches to determine stoichiometry of viral assembly components.A viral scaffolding protein triggers portal ring oligomerization and incorporation during procapsid assembly.
P2860
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P2860
Scaffolding protein regulates the polymerization of P22 coat subunits into icosahedral shells in vitro.
description
1988 nî lūn-bûn
@nan
1988年の論文
@ja
1988年学术文章
@wuu
1988年学术文章
@zh
1988年学术文章
@zh-cn
1988年学术文章
@zh-hans
1988年学术文章
@zh-my
1988年学术文章
@zh-sg
1988年學術文章
@yue
1988年學術文章
@zh-hant
name
Scaffolding protein regulates ...... o icosahedral shells in vitro.
@en
Scaffolding protein regulates ...... o icosahedral shells in vitro.
@nl
type
label
Scaffolding protein regulates ...... o icosahedral shells in vitro.
@en
Scaffolding protein regulates ...... o icosahedral shells in vitro.
@nl
prefLabel
Scaffolding protein regulates ...... o icosahedral shells in vitro.
@en
Scaffolding protein regulates ...... o icosahedral shells in vitro.
@nl
P2093
P1476
Scaffolding protein regulates ...... o icosahedral shells in vitro.
@en
P2093
P304
P356
10.1016/0022-2836(88)90555-4
P407
P577
1988-08-01T00:00:00Z