Structure of phage P22 coat protein aggregates formed in the absence of the scaffolding protein.
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Intermediates in the assembly pathway of the double-stranded RNA virus phi6Structural 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-foldCryo-reconstructions of P22 polyheads suggest that phage assembly is nucleated by trimeric interactions among coat proteins.Invariant polymorphism in virus capsid assembly'Let the phage do the work': using the phage P22 coat protein structures as a framework to understand its folding and assembly mutantsA docking model based on mass spectrometric and biochemical data describes phage packaging motor incorporationIdentification of additional coat-scaffolding interactions in a bacteriophage P22 mutant defective in maturationIn vitro assembly of the T=13 procapsid of bacteriophage T5 with its scaffolding domain.Role of the scaffolding protein in P22 procapsid size determination suggested by T = 4 and T = 7 procapsid structures.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.Regulation of coat protein polymerization by the scaffolding protein of bacteriophage P22.The DNA injection apparatus of phage p22.Local rule-based theory of virus shell assembly.Identification of the sites of interaction between the scaffold and outer shell in herpes simplex virus-1 capsids by difference electron imaging.Unraveling the role of the C-terminal helix turn helix of the coat-binding domain of bacteriophage P22 scaffolding protein.Correct Assembly of the Bacteriophage T5 Procapsid Requires Both the Maturation Protease and the Portal ComplexOn the sequential packaging of bacteriophage P22 DNA.In vitro incorporation of the phage Phi29 connector complex.ϕX174 Procapsid Assembly: Effects of an Inhibitory External Scaffolding Protein and Resistant Coat Proteins In VitroBacteriophage P22 capsid size determination: roles for the coat protein telokin-like domain and the scaffolding protein amino-terminus.Self-assembled cage-like protein structures.Particle polymorphism caused by deletion of a peptide molecular switch in a quasiequivalent icosahedral virus.Kinetic analysis of the role of intersubunit interactions in human immunodeficiency virus type 1 capsid protein assembly in vitro.A P22 scaffold protein mutation increases the robustness of head assembly in the presence of excess portal protein.A viral scaffolding protein triggers portal ring oligomerization and incorporation during procapsid assembly.Assembly properties of the human immunodeficiency virus type 1 CA protein.Charge Detection Mass Spectrometry Identifies Preferred Non-Icosahedral Polymorphs in the Self-Assembly of Woodchuck Hepatitis Virus Capsids.A Molecular Staple: D-Loops in the I Domain of Bacteriophage P22 Coat Protein Make Important Intercapsomer Contacts Required for Procapsid Assembly.Image reconstruction from cryo-electron micrographs reveals the morphopoietic mechanism in the P2-P4 bacteriophage system.Determinants of bacteriophage P22 polyhead formation: the role of coat protein flexibility in conformational switching.Second-site suppressors of a cold-sensitive prohead accessory protein of bacteriophage phi X174.Generalized structural polymorphism in self-assembled viral particles.Conformational changes in bacteriophage P22 scaffolding protein induced by interaction with coat protein.Exploring the parameter space of complex self-assembly through virus capsid models.Conformational transformations in the protein lattice of phage P22 procapsids.GroEL and GroES control of substrate flux in the in vivo folding pathway of phage P22 coat protein.
P2860
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P2860
Structure of phage P22 coat protein aggregates formed in the absence of the scaffolding protein.
description
1978 nî lūn-bûn
@nan
1978 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1978 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1978年の論文
@ja
1978年論文
@yue
1978年論文
@zh-hant
1978年論文
@zh-hk
1978年論文
@zh-mo
1978年論文
@zh-tw
1978年论文
@wuu
name
Structure of phage P22 coat pr ...... ce of the scaffolding protein.
@ast
Structure of phage P22 coat pr ...... ce of the scaffolding protein.
@en
Structure of phage P22 coat pr ...... ce of the scaffolding protein.
@nl
type
label
Structure of phage P22 coat pr ...... ce of the scaffolding protein.
@ast
Structure of phage P22 coat pr ...... ce of the scaffolding protein.
@en
Structure of phage P22 coat pr ...... ce of the scaffolding protein.
@nl
prefLabel
Structure of phage P22 coat pr ...... ce of the scaffolding protein.
@ast
Structure of phage P22 coat pr ...... ce of the scaffolding protein.
@en
Structure of phage P22 coat pr ...... ce of the scaffolding protein.
@nl
P1476
Structure of phage P22 coat pr ...... ce of the scaffolding protein.
@en
P2093
P304
P356
10.1016/0022-2836(78)90017-7
P407
P577
1978-12-01T00:00:00Z