The TRiC chaperonin controls reovirus replication through outer-capsid folding.

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Reovirus Nonstructural Protein σNS Acts as an RNA-Stability Factor Promoting Viral Genome Replication.Protein Mismatches Caused by Reassortment Influence Functions of the Reovirus Capsid

P2860

Q54209646-4FEDAFFA-DDDB-4AE0-918F-7403189A3E9F Q57469919-A2F0FF46-DE45-4202-B51B-67D5B5CCCF59

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The TRiC chaperonin controls reovirus replication through outer-capsid folding.

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http://www.wikidata.org/entity/Q52358244

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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2018年学术文章

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The TRiC chaperonin controls reovirus replication through outer-capsid folding.

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The TRiC chaperonin controls reovirus replication through outer-capsid folding.

@nl

type

Item

label

The TRiC chaperonin controls reovirus replication through outer-capsid folding.

@en

The TRiC chaperonin controls reovirus replication through outer-capsid folding.

@nl

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The TRiC chaperonin controls reovirus replication through outer-capsid folding.

@en

The TRiC chaperonin controls reovirus replication through outer-capsid folding.

@nl

P1476

The TRiC chaperonin controls reovirus replication through outer-capsid folding.

@en

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Alison W Ashbrook

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

Daniel R Gestaut

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

Isabel Fernández de Castro

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

J Craig Forrest

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

Joshua A Bauer

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

Judith Frydman

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

Paula F Zamora

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

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Characterization of reemerging chikungunya virus

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Proteolytic cleavage of the reovirus sigma 3 protein results in enhanced double-stranded RNA-binding activity: identification of a repeated basic amino acid motif within the C-terminal binding region

Antibody protects against lethal infection with the neurally spreading reovirus type 3 (Dearing)

Structure of the reovirus outer capsid and dsRNA-binding protein sigma3 at 1.8 A resolution.

Structure of the reovirus membrane-penetration protein, Mu1, in a complex with is protector protein, Sigma3

The molecular architecture of the eukaryotic chaperonin TRiC/CCT

GroEL/ES Chaperonin Modulates the Mechanism and Accelerates the Rate of TIM-Barrel Domain Folding

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Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets.

P2888

s41564-018-0122-x

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481-493

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scholarly article

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10.1038/S41564-018-0122-X

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

P433

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

P478

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

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P577

2018-03-12T00:00:00Z

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

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29531365

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P932

5874176

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

The TRiC chaperonin controls reovirus replication through outer-capsid folding.

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P2860

P2860

The TRiC chaperonin controls reovirus replication through outer-capsid folding.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P50

P577

P698

P932