Thermal unfolding pathway for the thermostable P22 tailspike endorhamnosidase.
about
Orally administered P22 phage tailspike protein reduces salmonella colonization in chickens: prospects of a novel therapy against bacterial infectionsBacteriophage P22 tailspike: structure of the complete protein and function of the interdomain linkerRole for cysteine residues in the in vivo folding and assembly of the phage P22 tailspikeProteomic Analysis of a Novel Bacillus Jumbo Phage Revealing Glycoside Hydrolase As Structural ComponentIdentification 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 proteinsThermolabile folding intermediates: inclusion body precursors and chaperonin substrates.Multimeric intermediates in the pathway to the aggregated inclusion body state for P22 tailspike polypeptide chains.Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodies.Beta-helix core packing within the triple-stranded oligomerization domain of the P22 tailspikeThe interdigitated beta-helix domain of the P22 tailspike protein acts as a molecular clamp in trimer stabilizationGenomic and proteomic analysis of phiEco32, a novel Escherichia coli bacteriophage.Phage P22 tailspike protein: removal of head-binding domain unmasks effects of folding mutations on native-state thermal stability.The tailspike protein of Shigella phage Sf6. A structural homolog of Salmonella phage P22 tailspike protein without sequence similarity in the beta-helix domain.Isolation of suppressors of temperature-sensitive folding mutationsThree amino acids that are critical to formation and stability of the P22 tailspike trimer.In vitro unfolding, refolding, and polymerization of human gammaD crystallin, a protein involved in cataract formation.Formation of highly stable chimeric trimers by fusion of an adenovirus fiber shaft fragment with the foldon domain of bacteriophage t4 fibritin.A concerted mechanism for the suppression of a folding defect through interactions with chaperones.Silica encapsulated SERS nanoprobe conjugated to the bacteriophage tailspike protein for targeted detection of Salmonella.Unfolding of bacteriophage P22 tailspike protein: enhanced thermal stability of an N-terminal fusion mutant.Interaction of Salmonella phage P22 with its O-antigen receptor studied by X-ray crystallography.
P2860
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P2860
Thermal unfolding pathway for the thermostable P22 tailspike endorhamnosidase.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年学术文章
@wuu
1991年学术文章
@zh
1991年学术文章
@zh-cn
1991年学术文章
@zh-hans
1991年学术文章
@zh-my
1991年学术文章
@zh-sg
1991年學術文章
@yue
1991年學術文章
@zh-hant
name
Thermal unfolding pathway for the thermostable P22 tailspike endorhamnosidase.
@en
Thermal unfolding pathway for the thermostable P22 tailspike endorhamnosidase.
@nl
type
label
Thermal unfolding pathway for the thermostable P22 tailspike endorhamnosidase.
@en
Thermal unfolding pathway for the thermostable P22 tailspike endorhamnosidase.
@nl
prefLabel
Thermal unfolding pathway for the thermostable P22 tailspike endorhamnosidase.
@en
Thermal unfolding pathway for the thermostable P22 tailspike endorhamnosidase.
@nl
P356
P1433
P1476
Thermal unfolding pathway for the thermostable P22 tailspike endorhamnosidase.
@en
P304
P356
10.1021/BI00239A026
P407
P577
1991-06-01T00:00:00Z