Role of the scaffolding protein in P22 procapsid size determination suggested by T = 4 and T = 7 procapsid structures.
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Structure of Halothiobacillus neapolitanus carboxysomes by cryo-electron tomographyVirus maturationPrinciples of virus structural organizationStructure of the Sec13–Sec16 edge element, a template for assembly of the COPII vesicle coatStructural basis for scaffolding-mediated assembly and maturation of a dsDNA virusAdding the Third Dimension to Virus Life Cycles: Three-Dimensional Reconstruction of Icosahedral Viruses from Cryo-Electron MicrographsThe delta domain of the HK97 major capsid protein is essential for assemblyNature's favorite building block: Deciphering folding and capsid assembly of proteins with the HK97-foldAcquiring Structural Information on Virus Particles with Charge Detection Mass SpectrometryCryo-reconstructions of P22 polyheads suggest that phage assembly is nucleated by trimeric interactions among coat proteins.'Let the phage do the work': using the phage P22 coat protein structures as a framework to understand its folding and assembly mutantsOptimal architectures of elongated viruses.Identification of additional coat-scaffolding interactions in a bacteriophage P22 mutant defective in maturationSequence of the genome of Salmonella bacteriophage P22In vitro assembly of the T=13 procapsid of bacteriophage T5 with its scaffolding domain.Local rules simulation of the kinetics of virus capsid self-assemblyMechanism of scaffolding-directed virus assembly suggested by comparison of scaffolding-containing and scaffolding-lacking P22 procapsids.Identification of the sites of interaction between the scaffold and outer shell in herpes simplex virus-1 capsids by difference electron imaging.Conformational switch-defective X174 internal scaffolding proteins kinetically trap assembly intermediates before procapsid formation.Packaging of a polymer by a viral capsid: the interplay between polymer length and capsid sizeCorrect Assembly of the Bacteriophage T5 Procapsid Requires Both the Maturation Protease and the Portal ComplexInsights into head-tailed viruses infecting extremely halophilic archaea.RNA-controlled polymorphism in the in vivo assembly of 180-subunit and 120-subunit virions from a single capsid protein.Detection of intermediates and kinetic control during assembly of bacteriophage P22 procapsidGenes essential for the morphogenesis of the Shiga toxin 2-transducing phage from Escherichia coli O157:H7.ϕX174 Procapsid Assembly: Effects of an Inhibitory External Scaffolding Protein and Resistant Coat Proteins In VitroOrigin of icosahedral symmetry in virusesBacteriophage P22 capsid size determination: roles for the coat protein telokin-like domain and the scaffolding protein amino-terminus.Self-assembled cage-like protein structures.Maturation of phage T7 involves structural modification of both shell and inner core components.Roles of triplex and scaffolding proteins in herpes simplex virus type 1 capsid formation suggested by structures of recombinant particlesA P22 scaffold protein mutation increases the robustness of head assembly in the presence of excess portal protein.Virus-like particle of Macrobrachium rosenbergii nodavirus produced in Spodoptera frugiperda (Sf9) cells is distinctive from that produced in Escherichia coli.A Molecular Staple: D-Loops in the I Domain of Bacteriophage P22 Coat Protein Make Important Intercapsomer Contacts Required for Procapsid Assembly.Determinants of bacteriophage P22 polyhead formation: the role of coat protein flexibility in conformational switching.The physical basis for the head-to-tail rule that excludes most fullerene cages from self-assembly.Phage P22 procapsids equilibrate with free coat protein subunits.Conformational changes in bacteriophage P22 scaffolding protein induced by interaction with coat protein.Elasticity theory and shape transitions of viral shells.Spontaneous curvature as a regulator of the size of virus capsids.
P2860
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P2860
Role of the scaffolding protein in P22 procapsid size determination suggested by T = 4 and T = 7 procapsid structures.
description
1998 nî lūn-bûn
@nan
1998 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Role of the scaffolding protei ...... nd T = 7 procapsid structures.
@ast
Role of the scaffolding protei ...... nd T = 7 procapsid structures.
@en
Role of the scaffolding protei ...... nd T = 7 procapsid structures.
@nl
type
label
Role of the scaffolding protei ...... nd T = 7 procapsid structures.
@ast
Role of the scaffolding protei ...... nd T = 7 procapsid structures.
@en
Role of the scaffolding protei ...... nd T = 7 procapsid structures.
@nl
prefLabel
Role of the scaffolding protei ...... nd T = 7 procapsid structures.
@ast
Role of the scaffolding protei ...... nd T = 7 procapsid structures.
@en
Role of the scaffolding protei ...... nd T = 7 procapsid structures.
@nl
P2093
P2860
P1433
P1476
Role of the scaffolding protei ...... nd T = 7 procapsid structures.
@en
P2093
J A Malinski
P A Thuman-Commike
P2860
P304
P356
10.1016/S0006-3495(98)77814-2
P407
P577
1998-01-01T00:00:00Z