Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70 - Wikidata - wikimedia - TriplyDB

Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70

Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70

http://www.wikidata.org/entity/Q36660658

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Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions.Hsp90 cochaperones p23 and FKBP4 physically interact with hAgo2 and activate RNA interference-mediated silencing in mammalian cells Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with Hsp90 and progesterone receptor Human Fas-associated factor 1 interacts with heat shock protein 70 and negatively regulates chaperone activity Regulation of interferon-induced protein kinase PKR: modulation of P58IPK inhibitory function by a novel protein, P52rIPK Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome Small glutamine-rich protein/viral protein U-binding protein is a novel cochaperone that affects heat shock protein 70 activity The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies Hsp70 chaperones: cellular functions and molecular mechanism Mutational analysis of the hsp70-interacting protein Hip Targeting Plasmodium falciparum Hsp90: Towards Reversing Antimalarial Resistance A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins Contribution of N- and C-terminal domains to the function of Hsp90 in Saccharomyces cerevisiae.Sgt1p is a unique co-chaperone that acts as a client adaptor to link Hsp90 to Skp1p.The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90 In vivo analysis of the Hsp90 cochaperone Sti1 (p60)Cns1 is an activator of the Ssa1 ATPase activity.Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones.Specific interaction of the 70-kDa heat shock cognate protein with the tetratricopeptide repeats Evidence that the co-chaperone p23 regulates ligand responsiveness of the dioxin (Aryl hydrocarbon) receptor The Hsp organizer protein hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone system HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor Hop modulates Hsp70/Hsp90 interactions in protein folding Mechanisms of disease: the role of heat-shock protein 90 in genitourinary malignancy p50(cdc37) binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding site Characterization of the Ah receptor-associated protein, ARA9 The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors Characterization of functional domains of the eukaryotic co-chaperone Hip Identification and characterization of Harc, a novel Hsp90-associating relative of Cdc37 The tetratricopeptide repeat: a structural motif mediating protein-protein interactions Heat shock proteins in human cancer FKBP51 promotes assembly of the Hsp90 chaperone complex and regulates androgen receptor signaling in prostate cancer cells.GERp95 belongs to a family of signal-transducing proteins and requires Hsp90 activity for stability and Golgi localization.Bacterial lipopolysaccharide induces expression of the stress response genes hop and H411.Noncatalytic role of the FKBP52 peptidyl-prolyl isomerase domain in the regulation of steroid hormone signaling.HIV replication enhances production of free fatty acids, low density lipoproteins and many key proteins involved in lipid metabolism: a proteomics study

P2860

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P2860

Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70

http://www.wikidata.org/entity/Q36660658

description

1993 nî lūn-bûn

@nan

1993年の論文

@ja

1993年論文

@yue

1993年論文

@zh-hant

1993年論文

@zh-hk

1993年論文

@zh-mo

1993年論文

@zh-tw

1993年论文

@wuu

1993年论文

@zh

1993年论文

@zh-cn

name

Identification of a 60-kilodal ...... interacts with hsp90 and hsp70

@ast

Identification of a 60-kilodal ...... interacts with hsp90 and hsp70

@en

type

label

Identification of a 60-kilodal ...... interacts with hsp90 and hsp70

@ast

Identification of a 60-kilodal ...... interacts with hsp90 and hsp70

@en

prefLabel

Identification of a 60-kilodal ...... interacts with hsp90 and hsp70

@ast

Identification of a 60-kilodal ...... interacts with hsp90 and hsp70

@en

P1433

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P1476

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P2093

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P2860

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P407

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P478

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P577

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P1433

Molecular and Cellular Biology

P1476

Identification of a 60-kilodal ...... interacts with hsp90 and hsp70

@en

P2093

B Madden

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

D F Smith

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

D J McCormick

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

D O Toft

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

K Zaitsu

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

T N Marion

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

W P Sullivan

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

P2860

Association of a 59-kilodalton immunophilin with the glucocorticoid receptor complex

Molecular cloning and expression of a transformation-sensitive human protein containing the TPR motif and sharing identity to the stress-inducible yeast protein STI1

The 56-59-kilodalton protein identified in untransformed steroid receptor complexes is a unique protein that exists in cytosol in a complex with both the 70- and 90-kilodalton heat shock proteins

The common 90-kd protein component of non-transformed '8S' steroid receptors is a heat-shock protein

High resolution two-dimensional electrophoresis of proteins

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

The Hsp56 component of steroid receptor complexes binds to immobilized FK506 and shows homology to FKBP-12 and FKBP-13

Assembly of progesterone receptor with heat shock proteins and receptor activation are ATP mediated events

A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids

P304

869-876

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P31

scholarly article

P356

10.1128/MCB.13.2.869

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P407

P433

2

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P478

13

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P577

1993-02-01T00:00:00Z

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P5875

14775118

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P698

8423808

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P932

358970

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