The C-terminal cysteine annulus participates in auto-chaperone function for Salmonella phage P22 tailspike folding and assembly.

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Structure of the Receptor-Binding Carboxy-Terminal Domain of the Bacteriophage T5 L-Shaped Tail Fibre with and without Its Intra-Molecular Chaperone.

P2860

Q40870235-C52C0AE7-C874-45A1-B846-C32E44DCE3A1

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The C-terminal cysteine annulus participates in auto-chaperone function for Salmonella phage P22 tailspike folding and assembly.

Item

http://www.wikidata.org/entity/Q41881003

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2012 nî lūn-bûn

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2012年の論文

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2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

2012年论文

@zh

2012年论文

@zh-cn

name

The C-terminal cysteine annulu ...... ailspike folding and assembly.

@en

type

Item

label

The C-terminal cysteine annulu ...... ailspike folding and assembly.

@en

prefLabel

The C-terminal cysteine annulu ...... ailspike folding and assembly.

@en

P1476

The C-terminal cysteine annulu ...... ailspike folding and assembly.

@en

P2093

Cameron Haase-Pettingell

http://www.w3.org/2001/XMLSchema#string

Jonathan King

http://www.w3.org/2001/XMLSchema#string

Takumi Takata

http://www.w3.org/2001/XMLSchema#string

P2860

Mutations improving the folding of phage P22 tailspike protein affect its receptor binding activity

The structure of the receptor-binding domain of the bacteriophage T4 short tail fibre reveals a knitted trimeric metal-binding fold

Structure of the Receptor-Binding Protein of Bacteriophage Det7: a Podoviral Tail Spike in a Myovirus

Polysaccharide binding sites in hyaluronate lyase--crystal structures of native phage-encoded hyaluronate lyase and its complexes with ascorbic acid and lactose

Crystallographic Insights into the Autocatalytic Assembly Mechanism of a Bacteriophage Tail Spike

Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding

Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer

Phage P22 tailspike protein: crystal structure of the head-binding domain at 2.3 A, fully refined structure of the endorhamnosidase at 1.56 A resolution, and the molecular basis of O-antigen recognition and cleavage

The zipper-like folding of collagen triple helices and the effects of mutations that disrupt the zipper

Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli

P304

36-49

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.4161/BACT.19775

http://www.w3.org/2001/XMLSchema#string

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P577

2012-01-01T00:00:00Z

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P5875

225184944

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P698

22666655

http://www.w3.org/2001/XMLSchema#string

P921

molecular chaperones

P932

3357383

http://www.w3.org/2001/XMLSchema#string

The C-terminal cysteine annulus participates in auto-chaperone function for Salmonella phage P22 tailspike folding and assembly.

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P2860

P2860

The C-terminal cysteine annulus participates in auto-chaperone function for Salmonella phage P22 tailspike folding and assembly.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P5875

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P5875

P698

P921

P932