Determinants of bacteriophage P22 polyhead formation: the role of coat protein flexibility in conformational switching.
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Three-dimensional structure of victorivirus HvV190S suggests coat proteins in most totiviruses share a conserved coreMultiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM ModelingNature's favorite building block: Deciphering folding and capsid assembly of proteins with the HK97-foldAcquiring Structural Information on Virus Particles with Charge Detection Mass SpectrometryStepwise molecular display utilizing icosahedral and helical complexes of phage coat and decoration proteins in the development of robust nanoscale display vehiclesCryo-reconstructions of P22 polyheads suggest that phage assembly is nucleated by trimeric interactions among coat proteins.Highly specific salt bridges govern bacteriophage P22 icosahedral capsid assembly: identification of the site in coat protein responsible for interaction with scaffolding protein.Conformational switch-defective X174 internal scaffolding proteins kinetically trap assembly intermediates before procapsid formation.Effects of an early conformational switch defect during ϕX174 morphogenesis are belatedly manifested late in the assembly pathwayAn intramolecular chaperone inserted in bacteriophage P22 coat protein mediates its chaperonin-independent folding.Architecture of a dsDNA viral capsid in complex with its maturation protease.Bacteriophage P22 capsid size determination: roles for the coat protein telokin-like domain and the scaffolding protein amino-terminus.Decoding bacteriophage P22 assembly: identification of two charged residues in scaffolding protein responsible for coat protein interactionA viral scaffolding protein triggers portal ring oligomerization and incorporation during procapsid assembly.Biocatalytic virus capsid as nanovehicle for enzymatic activation of Tamoxifen in tumor cells.A Molecular Staple: D-Loops in the I Domain of Bacteriophage P22 Coat Protein Make Important Intercapsomer Contacts Required for Procapsid Assembly.Structural evolution of the P22-like phages: comparison of Sf6 and P22 procapsid and virion architectures.The energetic contributions of scaffolding and coat proteins to the assembly of bacteriophage procapsids.Coat Protein Mutations That Alter the Flux of Morphogenetic Intermediates through the ϕX174 Early Assembly Pathway.
P2860
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P2860
Determinants of bacteriophage P22 polyhead formation: the role of coat protein flexibility in conformational switching.
description
2010 nî lūn-bûn
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2010年の論文
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2010年学术文章
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2010年学术文章
@zh-cn
2010年学术文章
@zh-hans
2010年学术文章
@zh-my
2010年学术文章
@zh-sg
2010年學術文章
@yue
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name
Determinants of bacteriophage ...... y in conformational switching.
@en
type
label
Determinants of bacteriophage ...... y in conformational switching.
@en
prefLabel
Determinants of bacteriophage ...... y in conformational switching.
@en
P2093
P2860
P1476
Determinants of bacteriophage ...... y in conformational switching.
@en
P2093
Carolyn M Teschke
Kristin N Parent
Margaret M Suhanovsky
Sarah E Dunn
Timothy S Baker
P2860
P304
P356
10.1111/J.1365-2958.2010.07311.X
P407
P577
2010-08-18T00:00:00Z