Biochemical reconstitution of steroid receptor•Hsp90 protein complexes and reactivation of ligand binding

about

Biochemical reconstitution of steroid receptor•Hsp90 protein complexes and reactivation of ligand binding

Item

http://www.wikidata.org/entity/Q35591253

description

2011 nî lūn-bûn

@nan

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

2011年论文

@zh

2011年论文

@zh-cn

name

Biochemical reconstitution of ...... reactivation of ligand binding

@ast

Biochemical reconstitution of ...... reactivation of ligand binding

@en

type

Item

label

Biochemical reconstitution of ...... reactivation of ligand binding

@ast

Biochemical reconstitution of ...... reactivation of ligand binding

@en

prefLabel

Biochemical reconstitution of ...... reactivation of ligand binding

@ast

Biochemical reconstitution of ...... reactivation of ligand binding

@en

P1476

Biochemical reconstitution of ...... reactivation of ligand binding

@en

P2093

Hannah R Franklin

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

Nathan W Furukawa

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

Patrick J M Murphy

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

P2860

The Hsp organizer protein hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone system

Steroid receptor interactions with heat shock protein and immunophilin chaperones

Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery

Evidence for iterative ratcheting of receptor-bound hsp70 between its ATP and ADP conformations during assembly of glucocorticoid receptor.hsp90 heterocomplexes.

Folding of the glucocorticoid receptor by the reconstituted Hsp90-based chaperone machinery. The initial hsp90.p60.hsp70-dependent step is sufficient for creating the steroid binding conformation.

Functioning of the Hsp90 machine in chaperoning checkpoint kinase I (Chk1) and the progesterone receptor (PR).

The Hsp90 chaperone machinery regulates signaling by modulating ligand binding clefts.

High-sensitivity detection and quantitative analysis of native protein-protein interactions and multiprotein complexes by flow cytometry.

Regulation of the dynamics of hsp90 action on the glucocorticoid receptor by acetylation/deacetylation of the chaperone.

Pifithrin-alpha inhibits p53 signaling after interaction of the tumor suppressor protein with hsp90 and its nuclear translocation.

P31

scholarly article

P356

10.3791/3059

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

P433

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

P577

2011-09-21T00:00:00Z

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

P698

21968922

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

P921

ligand binding

P932

3230214

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