Chaperone-client interactions: Non-specificity engenders multifunctionality.

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Reconstitution of the core of the malaria parasite glideosome with recombinant Plasmodium class XIV myosin A and Plasmodium actin.Directed evolution to improve protein folding in vivo.Substrate specificity in the context of molecular chaperones.

P2860

Q47137117-323A4320-2041-44E5-86B5-1AE4E39ED821 Q47253797-4B12EAAF-C178-447B-9572-931B3CDCC52E Q48022737-8DDC618E-8F19-4E85-A5AD-5CC79EC151C9

P2860

Chaperone-client interactions: Non-specificity engenders multifunctionality.

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http://www.wikidata.org/entity/Q39376939

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2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh

2017年學術文章

@zh-hant

name

Chaperone-client interactions: Non-specificity engenders multifunctionality.

@en

Chaperone-client interactions: Non-specificity engenders multifunctionality.

@nl

type

Item

label

Chaperone-client interactions: Non-specificity engenders multifunctionality.

@en

Chaperone-client interactions: Non-specificity engenders multifunctionality.

@nl

prefLabel

Chaperone-client interactions: Non-specificity engenders multifunctionality.

@en

Chaperone-client interactions: Non-specificity engenders multifunctionality.

@nl

P1476

Chaperone-client interactions: Non-specificity engenders multifunctionality.

@en

P2093

James C A Bardwell

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

Philipp Koldewey

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

Scott Horowitz

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

P2860

Chaperonin chamber accelerates protein folding through passive action of preventing aggregation

What distinguishes GroEL substrates from other Escherichia coli proteins?

Just scratching the surface: an expanding view of the Cpx envelope stress response

Role of the -phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics

Domain motions in GroEL upon binding of an oligopeptide

Crystal Structures of the 70-kDa Heat Shock Proteins in Domain Disjoining Conformation

Dual Action of ATP Hydrolysis Couples Lid Closure to Substrate Release into the Group II Chaperonin Chamber

Genetic selection designed to stabilize proteins uncovers a chaperone called Spy

The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins

ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL Chaperonin

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12010-12017

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

P31

scholarly article

P356

10.1074/JBC.R117.796862

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

P407

English

P433

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

P478

292

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

P577

2017-06-15T00:00:00Z

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

P698

28620048

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

P921

molecular chaperones

P932

5519353

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

Chaperone-client interactions: Non-specificity engenders multifunctionality.

about

P2860

P2860

Chaperone-client interactions: Non-specificity engenders multifunctionality.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P921

P932