Phage P22 tailspike protein: removal of head-binding domain unmasks effects of folding mutations on native-state thermal stability.
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 linkerIrreversible thermal denaturation of cytochrome C studied by electrospray mass spectrometry.Tailspike interactions with lipopolysaccharide effect DNA ejection from phage P22 particles in vitroAn elongated spine of buried core residues necessary for in vivo folding of the parallel beta-helix of P22 tailspike adhesin.The C-terminus of the P22 tailspike protein acts as an independent oligomerization domain for monomeric proteins.A Plant-Produced Bacteriophage Tailspike Protein for the Control of Salmonella.The interdigitated beta-helix domain of the P22 tailspike protein acts as a molecular clamp in trimer stabilizationThe tailspike protein of Shigella phage Sf6. A structural homolog of Salmonella phage P22 tailspike protein without sequence similarity in the beta-helix domain.Complete genomic sequence of the virulent Salmonella bacteriophage SP6.A concerted mechanism for the suppression of a folding defect through interactions with chaperones.Folding of coliphage T4 short tail fiber in vitro. Analysing the role of a bacteriophage-encoded chaperone.
P2860
Q21136065-A41F3A0D-1D74-47E4-97B8-2BD5D96AF0D1Q27649311-CB32F716-C85B-4751-A164-8A3025F3A31CQ27690200-389D277F-DC73-45F2-B3C2-42C13B329705Q30374787-00B6085E-07CD-451D-AB9D-FC79AA827F3BQ34136179-A1A9EFBC-83CD-4031-B9EE-FB8C6079B3DFQ34410800-00DEE892-25A0-4067-866B-B319BA2B0D18Q36032778-02AAEBAC-9EFD-4397-8D02-0EDEB5CF6C8DQ36441987-9C91404D-2520-4EE8-88B4-964E548F4708Q36639162-A6677D1E-70E9-42F7-986B-8A43CBFC6097Q38361188-31AC0B25-CAC2-41DD-B5D1-869C11CED909Q40700920-19C85B3C-E98D-49C1-B1A3-10CE16815639Q44756926-82C79FBB-0E9A-4842-96C6-D459A12908F1Q54077446-27852A9F-91DF-43BD-B43A-A9393204AF2A
P2860
Phage P22 tailspike protein: removal of head-binding domain unmasks effects of folding mutations on native-state thermal stability.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh
1998年學術文章
@zh-hant
name
Phage P22 tailspike protein: r ...... ative-state thermal stability.
@en
type
label
Phage P22 tailspike protein: r ...... ative-state thermal stability.
@en
prefLabel
Phage P22 tailspike protein: r ...... ative-state thermal stability.
@en
P2093
P2860
P356
P1433
P1476
Phage P22 tailspike protein: r ...... ative-state thermal stability.
@en
P2093
P2860
P304
P356
10.1002/PRO.5560071021
P577
1998-10-01T00:00:00Z