Polyhead formation in phage P22 pinpoints a region in coat protein required for conformational switching.
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Mechanisms of virus 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.'Let the phage do the work': using the phage P22 coat protein structures as a framework to understand its folding and assembly mutantsHighly specific salt bridges govern bacteriophage P22 icosahedral capsid assembly: identification of the site in coat protein responsible for interaction with scaffolding protein.In vitro assembly of the T=13 procapsid of bacteriophage T5 with its scaffolding domain.Modeling Viral Capsid Assembly.Conformational switch-defective X174 internal scaffolding proteins kinetically trap assembly intermediates before procapsid formation.Contextual Role of a Salt Bridge in the Phage P22 Coat Protein I-Domain.Rational elicitation of cold-sensitive phenotypes.An intramolecular chaperone inserted in bacteriophage P22 coat protein mediates its chaperonin-independent folding.Bacteriophage P22 capsid size determination: roles for the coat protein telokin-like domain and the scaffolding protein amino-terminus.A Molecular Staple: D-Loops in the I Domain of Bacteriophage P22 Coat Protein Make Important Intercapsomer Contacts Required for Procapsid Assembly.Multiclass maximum-likelihood symmetry determination and motif reconstruction of 3-D helical objects from projection images for electron microscopy.Determinants of bacteriophage P22 polyhead formation: the role of coat protein flexibility in conformational switching.Reciprocal space representations of helical objects and their projection images for helices constructed from motifs without spherical symmetry.Coat Protein Mutations That Alter the Flux of Morphogenetic Intermediates through the ϕX174 Early Assembly Pathway.Control of Salmonella on sprouting mung bean and alfalfa seeds by using a biocontrol preparation based on antagonistic bacteria and lytic bacteriophages.
P2860
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P2860
Polyhead formation in phage P22 pinpoints a region in coat protein required for conformational switching.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Polyhead formation in phage P2 ...... for conformational switching.
@en
Polyhead formation in phage P2 ...... for conformational switching.
@nl
type
label
Polyhead formation in phage P2 ...... for conformational switching.
@en
Polyhead formation in phage P2 ...... for conformational switching.
@nl
prefLabel
Polyhead formation in phage P2 ...... for conformational switching.
@en
Polyhead formation in phage P2 ...... for conformational switching.
@nl
P2093
P2860
P1476
Polyhead formation in phage P2 ...... for conformational switching.
@en
P2093
Carolyn M Teschke
Kristin N Parent
Margaret M Suhanovsky
P2860
P304
P356
10.1111/J.1365-2958.2007.05868.X
P407
P577
2007-08-03T00:00:00Z