In vivo functional protein-protein interaction: nuclear targeted hsp90 shifts cytoplasmic steroid receptor mutants into the nucleus
about
Human MI-ER1 alpha and beta function as transcriptional repressors by recruitment of histone deacetylase 1 to their conserved ELM2 domain.Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation.A new member of the hsp90 family of molecular chaperones interacts with the retinoblastoma protein during mitosis and after heat shockHeat shock protein (Hsp) 40 mutants inhibit Hsp70 in mammalian cellsHeat shock protein 90 and the nuclear transport of progesterone receptorZinc and cadmium can promote rapid nuclear translocation of metal response element-binding transcription factor-1Dual mechanisms of repression of E2F1 activity by the retinoblastoma gene productNuclear import of the glucocorticoid receptor-hsp90 complex through the nuclear pore complex is mediated by its interaction with Nup62 and importin betaNestin modulates glucocorticoid receptor function by cytoplasmic anchoring.Hsp90 nuclear accumulation in quiescence is linked to chaperone function and spore development in yeast.Abnormal expression and distribution of heat shock protein 90: potential etiologic immunoendocrine mechanism of glucocorticoid resistance in idiopathic nephrotic syndrome.Cotransport of the heterodimeric small subunit of the Saccharomyces cerevisiae ribonucleotide reductase between the nucleus and the cytoplasmThe molecular chaperone Hsp90 can negatively regulate the activity of a glucocorticosteroid-dependent promoter.Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90Activation of the unliganded estrogen receptor by EGF involves the MAP kinase pathway and direct phosphorylationAdenovirus early region 4 34-kilodalton protein directs the nuclear localization of the early region 1B 55-kilodalton protein in primate cells.Human cytomegalovirus capsid assembly protein precursor (pUL80.5) interacts with itself and with the major capsid protein (pUL86) through two different domains.Two eukaryote-specific regions of Hsp82 are dispensable for its viability and signal transduction functions in yeast.Multiplexed In-cell Immunoassay for Same-sample Protein Expression Profiling.SGT1 is required in PcINF1/SRC2-1 induced pepper defense response by interacting with SRC2-1HSP90 protects the human T-cell leukemia virus type 1 (HTLV-1) tax oncoprotein from proteasomal degradation to support NF-κB activation and HTLV-1 replication2-phenylethynesulphonamide (PFT-μ) enhances the anticancer effect of the novel hsp90 inhibitor NVP-AUY922 in melanoma, by reducing GSH levels.Multiple roles of ligand in transforming the dioxin receptor to an active basic helix-loop-helix/PAS transcription factor complex with the nuclear protein Arnt.Non-random subcellular distribution of variant EKLF in erythroid cells.A critical role for HSP90 in cancer cell invasion involves interaction with the extracellular domain of HER-2.Geldanamycin, an inhibitor of Hsp90, blocks cytoplasmic retention of progesterone receptors and glucocorticoid receptors via their respective ligand binding domains.Control of transcription by steroid hormones.Molecular mechanisms of glucocorticoid resistance/hypersensitivity. Potential clinical implications.Heat-shock proteins in animal models for acute renal failure.The cytokine interleukin-5 (IL-5) effects cotransport of its receptor subunits to the nucleus in vitro.Identification of transactivation and repression functions of the dioxin receptor and its basic helix-loop-helix/PAS partner factor Arnt: inducible versus constitutive modes of regulation.Role of molecular chaperones and TPR-domain proteins in the cytoplasmic transport of steroid receptors and their passage through the nuclear pore.Distinct functions of the 90 kDa heat-shock protein (hsp90) in oestrogen and mineralocorticosteroid receptor activity: effects of hsp90 deletion mutants.C-terminal hydrophobic interactions play a critical role in oligomeric assembly of the P22 tailspike trimer.Stress-inducible, murine protein mSTI1. Characterization of binding domains for heat shock proteins and in vitro phosphorylation by different kinases.Inhibition of glucocorticoid receptor nucleocytoplasmic shuttling by okadaic acid requires intact cytoskeleton.The C-terminal half of Hsp90 is responsible for its cytoplasmic localization.Dimerization of Hsp90 is required for in vivo function. Design and analysis of monomers and dimers.The Gbetagamma dimer drives the interaction of heterotrimeric Gi proteins with nonlamellar membrane structures.Nucleocytoplasmic distribution is required for activation of resistance by the potato NB-LRR receptor Rx1 and is balanced by its functional domains.
P2860
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P2860
In vivo functional protein-protein interaction: nuclear targeted hsp90 shifts cytoplasmic steroid receptor mutants into the nucleus
description
1994 nî lūn-bûn
@nan
1994 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
In vivo functional protein-pro ...... eptor mutants into the nucleus
@ast
In vivo functional protein-pro ...... eptor mutants into the nucleus
@en
In vivo functional protein-pro ...... eptor mutants into the nucleus
@nl
type
label
In vivo functional protein-pro ...... eptor mutants into the nucleus
@ast
In vivo functional protein-pro ...... eptor mutants into the nucleus
@en
In vivo functional protein-pro ...... eptor mutants into the nucleus
@nl
prefLabel
In vivo functional protein-pro ...... eptor mutants into the nucleus
@ast
In vivo functional protein-pro ...... eptor mutants into the nucleus
@en
In vivo functional protein-pro ...... eptor mutants into the nucleus
@nl
P2093
P2860
P356
P1476
In vivo functional protein-pro ...... eptor mutants into the nucleus
@en
P2093
Baulieu EE
Cadepond F
Catelli MG
Guiochon-Mantel A
P2860
P304
P356
10.1073/PNAS.91.1.340
P407
P577
1994-01-01T00:00:00Z