Folding and assembly of phage P22 tailspike endorhamnosidase lacking the N-terminal, head-binding domain.
about
Orally administered P22 phage tailspike protein reduces salmonella colonization in chickens: prospects of a novel therapy against bacterial infectionsStructure of the Receptor-Binding Protein of Bacteriophage Det7: a Podoviral Tail Spike in a MyovirusBacteriophage P22 tailspike: structure of the complete protein and function of the interdomain linkerBiochemical and biophysical characterization of PlyGRCS, a bacteriophage endolysin active against methicillin-resistant Staphylococcus aureus.Identification and crystallisation of a heat- and protease-stable fragment of the bacteriophage T4 short tail fibre.Mechanism of phage P22 tailspike protein folding mutations.An elongated spine of buried core residues necessary for in vivo folding of the parallel beta-helix of P22 tailspike adhesin.Homotrimeric, beta-stranded viral adhesins and tail proteinsThe C-terminus of the P22 tailspike protein acts as an independent oligomerization domain for monomeric proteins.Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodies.Phage P22 tailspike protein: removal of head-binding domain unmasks effects of folding mutations on native-state thermal stability.Interactions of phage P22 tails with their cellular receptor, Salmonella O-antigen polysaccharide.The tailspike protein of Shigella phage Sf6. A structural homolog of Salmonella phage P22 tailspike protein without sequence similarity in the beta-helix domain.Equilibrium intermediates in the reversible unfolding of firefly (Photinus pyralis) luciferase.Biochemical characterization of beta2-adrenergic receptor dimers and oligomers.Structure of the Receptor-Binding Carboxy-Terminal Domain of the Bacteriophage T5 L-Shaped Tail Fibre with and without Its Intra-Molecular Chaperone.Cotranslational folding promotes beta-helix formation and avoids aggregation in vivo.Three amino acids that are critical to formation and stability of the P22 tailspike trimer.Trimeric autotransporters require trimerization of the passenger domain for stability and adhesive activityC-terminal hydrophobic interactions play a critical role in oligomeric assembly of the P22 tailspike trimer.The C-terminal cysteine annulus participates in auto-chaperone function for Salmonella phage P22 tailspike folding and assembly.A newly synthesized, ribosome-bound polypeptide chain adopts conformations dissimilar from early in vitro refolding intermediates.Interaction of Salmonella phage P22 with its O-antigen receptor studied by X-ray crystallography.
P2860
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P2860
Folding and assembly of phage P22 tailspike endorhamnosidase lacking the N-terminal, head-binding domain.
description
1993 nî lūn-bûn
@nan
1993 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Folding and assembly of phage ...... terminal, head-binding domain.
@ast
Folding and assembly of phage ...... terminal, head-binding domain.
@en
Folding and assembly of phage ...... terminal, head-binding domain.
@nl
type
label
Folding and assembly of phage ...... terminal, head-binding domain.
@ast
Folding and assembly of phage ...... terminal, head-binding domain.
@en
Folding and assembly of phage ...... terminal, head-binding domain.
@nl
prefLabel
Folding and assembly of phage ...... terminal, head-binding domain.
@ast
Folding and assembly of phage ...... terminal, head-binding domain.
@en
Folding and assembly of phage ...... terminal, head-binding domain.
@nl
P2093
P2860
P1433
P1476
Folding and assembly of phage ...... terminal, head-binding domain.
@en
P2093
P2860
P304
P356
10.1111/J.1432-1033.1993.TB18076.X
P407
P577
1993-08-01T00:00:00Z