The steroid-binding properties of recombinant glucocorticoid receptor: a putative role for heat shock protein hsp90.
about
Mechanism of dimer formation of the 90-kDa heat-shock proteinHuman mineralocorticoid receptor interacts with actin under mineralocorticoid ligand modulationDefinition of a minimal domain of the dioxin receptor that is associated with Hsp90 and maintains wild type ligand binding affinity and specificityHistone acetyltransferase complexes can mediate transcriptional activation by the major glucocorticoid receptor activation domainInteraction of glucocorticosteroid receptor and wild-type or mutated 90-kDa heat shock protein coexpressed in baculovirus-infected Sf9 cells.Hsp90 regulates the phosphorylation and activity of serum- and glucocorticoid-regulated kinase-1.Modular structure of glucocorticoid receptor domains is not equivalent to functional independence. Stability and activity of the steroid binding domain are controlled by sequences in separate domains.Regulation and functions of stress proteins in allergy and inflammation.A metal-linked gapped zipper model is proposed for the hsp90-glucocorticoid receptor interaction.
P2860
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P2860
The steroid-binding properties of recombinant glucocorticoid receptor: a putative role for heat shock protein hsp90.
description
1990 nî lūn-bûn
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1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
1990年论文
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1990年论文
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name
The steroid-binding properties ...... for heat shock protein hsp90.
@en
The steroid-binding properties ...... for heat shock protein hsp90.
@nl
type
label
The steroid-binding properties ...... for heat shock protein hsp90.
@en
The steroid-binding properties ...... for heat shock protein hsp90.
@nl
prefLabel
The steroid-binding properties ...... for heat shock protein hsp90.
@en
The steroid-binding properties ...... for heat shock protein hsp90.
@nl
P2093
P1476
The steroid-binding properties ...... for heat shock protein hsp90.
@en
P2093
J A Gustafsson
J Carlstedt-Duke
P E Strömstedt
Y Ohara-Nemoto
P304
P356
10.1016/0960-0760(90)90391-W
P577
1990-11-01T00:00:00Z