Unliganded and hormone-bound glucocorticoid receptors interact with distinct hydrophobic sites in the Hsp90 C-terminal domain.
about
Glucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cyclesStructures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperonesChaperone machines for protein folding, unfolding and disaggregationDynamic tyrosine phosphorylation modulates cycling of the HSP90-P50(CDC37)-AHA1 chaperone machineZebrafish whole-adult-organism chemogenomics for large-scale predictive and discovery chemical biologyExploring the Functional Complementation between Grp94 and Hsp90The helix 1-3 loop in the glucocorticoid receptor LBD is a regulatory element for FKBP cochaperones.Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:Hop complex.Smyd2 controls cytoplasmic lysine methylation of Hsp90 and myofilament organization.The molecular chaperone gp96/GRP94 interacts with Toll-like receptors and integrins via its C-terminal hydrophobic domainUncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast.Estrogen receptor-alpha hinge-region lysines 302 and 303 regulate receptor degradation by the proteasomeA conformational switch in the ligand-binding domain regulates the dependence of the glucocorticoid receptor on Hsp90.A ligand-specific kinetic switch regulates glucocorticoid receptor trafficking and function.Increased age reduces DAF-16 and SKN-1 signaling and the hormetic response of Caenorhabditis elegans to the xenobiotic juglone.ATP-driven molecular chaperone machines.A C-terminal HSP90 inhibitor restores glucocorticoid sensitivity and relieves a mouse allograft model of Cushing disease.Design and synthesis of Hsp90 inhibitors: exploring the SAR of Sansalvamide A derivatives.ATP binding to Hsp90 is sufficient for effective chaperoning of p53 protein.The new platinum(IV) derivative LA-12 shows stronger inhibitory effect on Hsp90 function compared to cisplatin.Macrocycles that inhibit the binding between heat shock protein 90 and TPR-containing proteins.Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53.Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90.Mechanistic studies of Sansalvamide A-amide: an allosteric modulator of Hsp90.Osmolyte-induced conformational changes in the Hsp90 molecular chaperone.
P2860
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P2860
Unliganded and hormone-bound glucocorticoid receptors interact with distinct hydrophobic sites in the Hsp90 C-terminal domain.
description
2006 nî lūn-bûn
@nan
2006 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Unliganded and hormone-bound g ...... n the Hsp90 C-terminal domain.
@ast
Unliganded and hormone-bound g ...... n the Hsp90 C-terminal domain.
@en
type
label
Unliganded and hormone-bound g ...... n the Hsp90 C-terminal domain.
@ast
Unliganded and hormone-bound g ...... n the Hsp90 C-terminal domain.
@en
prefLabel
Unliganded and hormone-bound g ...... n the Hsp90 C-terminal domain.
@ast
Unliganded and hormone-bound g ...... n the Hsp90 C-terminal domain.
@en
P2093
P2860
P356
P1476
Unliganded and hormone-bound g ...... n the Hsp90 C-terminal domain.
@en
P2093
P2860
P304
18487-18492
P356
10.1073/PNAS.0609163103
P407
P577
2006-11-27T00:00:00Z