A switch point in the molecular chaperone Hsp90 responding to client interaction.

about

A switch point in the molecular chaperone Hsp90 responding to client interaction.

Item

http://www.wikidata.org/entity/Q52584576

description

2018 nî lūn-bûn

@nan

2018年の論文

@ja

2018年学术文章

@wuu

2018年学术文章

@zh

2018年学术文章

@zh-cn

2018年学术文章

@zh-hans

2018年学术文章

@zh-my

2018年学术文章

@zh-sg

2018年學術文章

@yue

2018年學術文章

@zh-hant

name

A switch point in the molecular chaperone Hsp90 responding to client interaction.

@en

A switch point in the molecular chaperone Hsp90 responding to client interaction.

@nl

type

Item

label

A switch point in the molecular chaperone Hsp90 responding to client interaction.

@en

A switch point in the molecular chaperone Hsp90 responding to client interaction.

@nl

prefLabel

A switch point in the molecular chaperone Hsp90 responding to client interaction.

@en

A switch point in the molecular chaperone Hsp90 responding to client interaction.

@nl

P1476

A switch point in the molecular chaperone Hsp90 responding to client interaction

@en

P2093

Lee Freiburger

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

Michael Sattler

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

Qi Luo

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

Ville R I Kaila

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

P2860

Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition

Glucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cycles

The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo

Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones

Modeling signal propagation mechanisms and ligand-based conformational dynamics of the Hsp90 molecular chaperone full-length dimer

Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions

Enhancing the stability and solubility of the glucocorticoid receptor ligand-binding domain by high-throughput library screening

The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop

Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase

VMD: visual molecular dynamics

P2888

s41467-018-03946-x

P304

1472

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

P31

scholarly article

P356

10.1038/S41467-018-03946-X

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

P407

English

P433

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

P478

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

P50

Johannes Buchner

Tobias Madl

Daniel Andreas Rutz

P577

2018-04-16T00:00:00Z

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

P698

29662162

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

P921

molecular chaperones

P932

5902578

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