Role of molecular chaperones and TPR-domain proteins in the cytoplasmic transport of steroid receptors and their passage through the nuclear pore. - Wikidata - wikimedia - TriplyDB

Role of molecular chaperones and TPR-domain proteins in the cytoplasmic transport of steroid receptors and their passage through the nuclear pore.

Role of molecular chaperones and TPR-domain proteins in the cytoplasmic transport of steroid receptors and their passage through the nuclear pore.

http://www.wikidata.org/entity/Q41592060

about

An interaction network predicted from public data as a discovery tool: application to the Hsp90 molecular chaperone machine Steroid Receptor-Associated Immunophilins: A Gateway to Steroid Signalling FKBP51 and FKBP52 in signaling and disease Plasmodium falciparum Hop (PfHop) Interacts with the Hsp70 Chaperone in a Nucleotide-Dependent Fashion and Exhibits Ligand Selectivity Approaches for defining the Hsp90-dependent proteome.Subcellular rearrangement of hsp90-binding immunophilins accompanies neuronal differentiation and neurite outgrowth Improved assays for determining the cytosolic access of peptides, proteins, and their mimetics.NF-κB transcriptional activity is modulated by FK506-binding proteins FKBP51 and FKBP52: a role for peptidyl-prolyl isomerase activity.Heat shock protein 83 (Hsp83) facilitates methoprene-tolerant (Met) nuclear import to modulate juvenile hormone signaling.Prenatal alcohol exposure modifies glucocorticoid receptor subcellular distribution in the medial prefrontal cortex and impairs frontal cortex-dependent learning.Regulation of steroid hormone receptor function by the 52-kDa FK506-binding protein (FKBP52).Management of cytoskeleton architecture by molecular chaperones and immunophilins.The 90-kDa heat-shock protein (Hsp90)-binding immunophilin FKBP51 is a mitochondrial protein that translocates to the nucleus to protect cells against oxidative stress.The neuroregenerative mechanism mediated by the Hsp90-binding immunophilin FKBP52 resembles the early steps of neuronal differentiation.A novel variant on chromosome 6p21.1 is associated with the risk of developing colorectal cancer: a two-stage case-control study in Han Chinese.70-kDa heat shock cognate protein hsc70 mediates calmodulin-dependent nuclear import of the sex-determining factor SRY Organization of nuclear architecture during adipocyte differentiation.On the trail of the glucocorticoid receptor: into the nucleus and back.Hsp90-binding immunophilins as a potential new platform for drug treatment.Biological relevance of Hsp90-binding immunophilins in cancer development and treatment.Enhancing nuclear translocation: perspectives in inhaled corticosteroid therapy.HSP90AB1: Helping the good and the bad.New Insights in Glucocorticoid Receptor Signaling-More Than Just a Ligand-Binding Receptor Hsp90-binding immunophilin FKBP51 forms complexes with hTERT enhancing telomerase activity.Spironolactone Prevents Endothelial Nitric Oxide Synthase Uncoupling and Vascular Dysfunction Induced by β-Adrenergic Overstimulation: Role of Perivascular Adipose Tissue.Gene expression regulation by heat-shock proteins: the cardinal roles of HSF1 and Hsp90.The Nuclear Receptor Field: A Historical Overview and Future Challenges Glucocorticoid Receptor and Adipocyte Biology The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease

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Role of molecular chaperones and TPR-domain proteins in the cytoplasmic transport of steroid receptors and their passage through the nuclear pore.

http://www.wikidata.org/entity/Q41592060

description

2010 nî lūn-bûn

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

@zh-tw

2010年论文

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2010年论文

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2010年论文

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name

Role of molecular chaperones a ...... sage through the nuclear pore.

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Role of molecular chaperones a ...... sage through the nuclear pore.

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Role of molecular chaperones a ...... sage through the nuclear pore.

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Role of molecular chaperones a ...... sage through the nuclear pore.

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Alejandra G Erlejman

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

Graciela Piwien-Pilipuk

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

Mario D Galigniana

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

P2860

Importins fulfil a dual function as nuclear import receptors and cytoplasmic chaperones for exposed basic domains

Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90

Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded

Nuclear import of the TATA-binding protein: mediation by the karyopherin Kap114p and a possible mechanism for intranuclear targeting.

Accelerating the rate of disassembly of karyopherin.cargo complexes.

Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex.

Evidence that the peptidylprolyl isomerase domain of the hsp90-binding immunophilin FKBP52 is involved in both dynein interaction and glucocorticoid receptor movement to the nucleus

Nucleotide binding states of hsp70 and hsp90 during sequential steps in the process of glucocorticoid receptor.hsp90 heterocomplex assembly

A new first step in activation of steroid receptors: hormone-induced switching of FKBP51 and FKBP52 immunophilins

Retrograde transport of the glucocorticoid receptor in neurites requires dynamic assembly of complexes with the protein chaperone hsp90 and is linked to the CHIP component of the machinery for proteasomal degradation

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299-308

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scholarly article

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10.4161/NUCL.1.4.11743

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4

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1

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Pablo C Echeverria

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2010-07-01T00:00:00Z

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49641099

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21113270

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molecular chaperones

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2990191

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