A chemical compound inhibiting the Aha1-Hsp90 chaperone complex.

about

Proteomic interrogation of HSP90 and insights for medical research.Adapting to stress - chaperome networks in cancer.

P2860

Q47678542-2417E1EE-0A52-4150-832E-FDC1FB5D4E4A Q54425017-51B07366-C079-433C-8DED-A599CCC3FE25

P2860

A chemical compound inhibiting the Aha1-Hsp90 chaperone complex.

Item

http://www.wikidata.org/entity/Q47886847

description

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

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-hant

name

A chemical compound inhibiting the Aha1-Hsp90 chaperone complex.

@en

A chemical compound inhibiting the Aha1-Hsp90 chaperone complex.

@nl

type

Item

label

A chemical compound inhibiting the Aha1-Hsp90 chaperone complex.

@en

A chemical compound inhibiting the Aha1-Hsp90 chaperone complex.

@nl

prefLabel

A chemical compound inhibiting the Aha1-Hsp90 chaperone complex.

@en

A chemical compound inhibiting the Aha1-Hsp90 chaperone complex.

@nl

P1476

A chemical compound inhibiting the Aha1-Hsp90 chaperone complex.

@en

P2093

Christine John

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

Gunter Fischer

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

Johannes Buchner

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

Martin Rübbelke

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

Matthias Weiwad

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

Michael Sattler

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

Sandrine C Stiegler

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

Stephan A Sieber

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

Vadim S Korotkov

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

P2860

Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone

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

Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis

Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1

Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome

The 'active life' of Hsp90 complexes

Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine

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

Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent

Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling

P304

17073-17083

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P31

scholarly article

P356

10.1074/JBC.M117.797829

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P407

English

P433

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

P478

292

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

P577

2017-08-28T00:00:00Z

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

P698

28851842

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

P921

molecular chaperones

P932

5641884

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

A chemical compound inhibiting the Aha1-Hsp90 chaperone complex.

about

P2860

P2860

A chemical compound inhibiting the Aha1-Hsp90 chaperone complex.

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