Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70 - Test2 - elhamkhani - TriplyDB

Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70

Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70

http://www.wikidata.org/entity/Q24520314

about

Cyclophilin 40 alters UVA-induced apoptosis and mitochondrial ROS generation in keratinocytes Inhibition of cyclophilins alters lipid trafficking and blocks hepatitis C virus secretion Steroid Receptor-Associated Immunophilins: A Gateway to Steroid Signalling Ex vivo promoter analysis of antiviral heat shock cognate 70B gene in Anopheles gambiae The Hsp90 cochaperones Cpr6, Cpr7, and Cns1 interact with the intact ribosome Cyclosporin A treatment of Leishmania donovani reveals stage-specific functions of cyclophilins in parasite proliferation and viability Heat shock protein 70 inhibits the activity of Influenza A virus ribonucleoprotein and blocks the replication of virus in vitro and in vivo Systematic Proteomic Identification of the Heat Shock Proteins (Hsp) that Interact with Estrogen Receptor Alpha (ERα) and Biochemical Characterization of the ERα-Hsp70 Interaction Heat shock protein 70 interacts with aquaporin-2 and regulates its trafficking Heat shock proteins: cellular and molecular mechanisms in the central nervous system.Regulation of nuclear translocation of the Myb1 transcription factor by TvCyclophilin 1 in the protozoan parasite Trichomonas vaginalis.Interaction of heat shock protein 90 and the co-chaperone Cpr6 with Ura2, a bifunctional enzyme required for pyrimidine biosynthesis Steroid Resistant CD8+CD28null NKT-Like Pro-inflammatory Cytotoxic Cells in Chronic Obstructive Pulmonary Disease Unraveling the role of peptidyl-prolyl isomerases in neurodegeneration.Peptidyl-prolyl isomerases: a full cast of critical actors in cardiovascular diseases.HSP90AB1: Helping the good and the bad.Discovery of multiple interacting partners of gankyrin, a proteasomal chaperone and an oncoprotein--evidence for a common hot spot site at the interface and its functional relevance.Phenotyping of tianma-stimulated differentiated rat neuronal b104 cells by quantitative proteomics.The RET51/FKBP52 complex and its involvement in Parkinson disease.The Leber congenital amaurosis protein AIPL1 functions as part of a chaperone heterocomplex.The first report of direct inhibitors that target the C-terminal MEEVD region on heat shock protein 90.Virtual prototyping study shows increased ATPase activity of Hsp90 to be the key determinant of cancer phenotype.Distinct hsp70 domains mediate apoptosis-inducing factor release and nuclear accumulation.Toxicogenomic profiling of the hepatic tumor promoters indole-3-carbinol, 17beta-estradiol and beta-naphthoflavone in rainbow trout.Gene expression and biochemical characterization of Azotobacter vinelandii cyclophilins and Protein Interaction Studies of the cytoplasmic isoform with dnaK and lpxH.

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P2860

Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70

http://www.wikidata.org/entity/Q24520314

description

2004 nî lūn-bûn

@nan

2004 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2004年の論文

@ja

2004年論文

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2004年論文

@zh-hant

2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

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name

Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70

@ast

Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70

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Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70

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Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70

@nl

type

label

Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70

@ast

Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70

@en

Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70

@en-gb

Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70

@nl

prefLabel

Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70

@ast

Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70

@en

Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70

@en-gb

Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70

@nl

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Cell Stress & Chaperones

P1476

Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70

@en

P2093

Amerigo Carrello

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

Barbara A L Owen

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

Bryan K Ward

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

Danny Mok

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

David O Toft

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

Rodney F Minchin

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

Rudi K Allan

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

Sarah L Morgan

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

Thomas Ratajczak

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

P2860

Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions.

The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins

Human cyclophilin 40 is a heat shock protein that exhibits altered intracellular localization following heat shock

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

A structure-based mutational analysis of cyclophilin 40 identifies key residues in the core tetratricopeptide repeat domain that mediate binding to Hsp90

Expression and characterization of human FKBP52, an immunophilin that associates with the 90-kDa heat shock protein and is a component of steroid receptor complexes

BAG-1 modulates the chaperone activity of Hsp70/Hsc70.

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

Molecular cloning of human p48, a transient component of progesterone receptor complexes and an Hsp70-binding protein

Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with Hsp90 and progesterone receptor

P2888

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scholarly article

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4351423

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10.1379/CSC-26R.1

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2

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9

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2004-01-01T00:00:00Z

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1067173939

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15497503

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1065296

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