p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function - Test2 - elhamkhani - TriplyDB

p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function

p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function

http://www.wikidata.org/entity/Q24554532

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Hsp90 regulates p50(cdc37) function during the biogenesis of the activeconformation of the heme-regulated eIF2 alpha kinase The heat shock protein 90-CDC37 chaperone complex is required for signaling by types I and II interferons Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function JAK2 activates TFII-I and regulates its interaction with extracellular signal-regulated kinase.Meaningful relationships: the regulation of the Ras/Raf/MEK/ERK pathway by protein interactions The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR Heat-shock protein 90 and Cdc37 interact with LKB1 and regulate its stability Extracellular signal-regulated kinase binds to TFII-I and regulates its activation of the c-fos promoter Quality control and fate determination of Hsp90 client proteins Functions of the Hsp90 chaperone system: lifting client proteins to new heights The human Cdc37.Hsp90 complex studied by heteronuclear NMR spectroscopy Raf-interactome in tuning the complexity and diversity of Raf function.Sgt1p is a unique co-chaperone that acts as a client adaptor to link Hsp90 to Skp1p.Cdc37p is required for stress-induced high-osmolarity glycerol and protein kinase C mitogen-activated protein kinase pathway functionality by interaction with Hog1p and Slt2p (Mpk1p)Cdc37 has distinct roles in protein kinase quality control that protect nascent chains from degradation and promote posttranslational maturation The molecular chaperone Hsp90 is required for high osmotic stress response in Saccharomyces cerevisiae.Regulation of molecular chaperone gene transcription involves the serine phosphorylation, 14-3-3 epsilon binding, and cytoplasmic sequestration of heat shock factor 1 Requirement for a kinase-specific chaperone pathway in the production of a Cdk9/cyclin T1 heterodimer responsible for P-TEFb-mediated tat stimulation of HIV-1 transcription Phosphorylation of the myosin-binding subunit of myosin phosphatase by Raf-1 and inhibition of phosphatase activity Geldanamycin, an inhibitor of the chaperone activity of HSP90, induces MAPK-independent cell cycle arrest A comparison of Hsp90alpha and Hsp90beta interactions with cochaperones and substrates Mapping the Interactome of a Major Mammalian Endoplasmic Reticulum Heat Shock Protein 90 The ankyrin repeat-containing adaptor protein Tvl-1 is a novel substrate and regulator of Raf-1 A functional screen reveals an extensive layer of transcriptional and splicing control underlying RAS/MAPK signaling in Drosophila CK2 binds, phosphorylates, and regulates its pivotal substrate Cdc37, an Hsp90-cochaperone Identification and characterization of Harc, a novel Hsp90-associating relative of Cdc37 Estradiol-induced phosphorylation of ERK1/2 in explants of the mouse cerebral cortex: the roles of heat shock protein 90 (Hsp90) and MEK2.Functional interaction of human Cdc37 with the androgen receptor but not with the glucocorticoid receptor.Opposite effects of the Hsp90 inhibitor Geldanamycin: induction of apoptosis in PC12, and differentiation in N2A cells.Heat shock protein expression in canine malignant mammary tumours.How Genetics Has Helped Piece Together the MAPK Signaling Pathway.In vitro reconstitution of a functional duck hepatitis B virus reverse transcriptase: posttranslational activation by Hsp90.Leucine-rich repeat kinase 2 (LRRK2): a key player in the pathogenesis of Parkinson's disease Cdc37 promotes the stability of protein kinases Cdc28 and Cak1.The oncoprotein kinase chaperone CDC37 functions as an oncogene in mice and collaborates with both c-myc and cyclin D1 in transformation of multiple tissues Split Renilla luciferase protein fragment-assisted complementation (SRL-PFAC) to characterize Hsp90-Cdc37 complex and identify critical residues in protein/protein interactions.p50(Cdc37) can buffer the temperature-sensitive properties of a mutant of Hck.Chaperones in cell cycle regulation and mitogenic signal transduction: a review.The role of Hsp90N, a new member of the Hsp90 family, in signal transduction and neoplastic transformation.

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P2860

p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function

http://www.wikidata.org/entity/Q24554532

description

1999 nî lūn-bûn

@nan

1999 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

1999 թվականի մարտին հրատարակված գիտական հոդված

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1999年の論文

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1999年論文

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1999年論文

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1999年論文

@zh-hk

1999年論文

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1999年論文

@zh-tw

1999年论文

@wuu

name

p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function

@ast

p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function

@en

p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function

@nl

type

label

p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function

@ast

p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function

@en

p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function

@nl

prefLabel

p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function

@ast

p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function

@en

p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function

@nl

P1433

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P1433

Molecular and Cellular Biology

P1476

p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function

@en

P2093

A Grammatikakis

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

J H Lin

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

N Grammatikakis

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

P N Tsichlis

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

P2860

Interaction between Cdc37 and Cdk4 in human cells

Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4

The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo

Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation.

CDC37 is required for p60v-src activity in yeast

Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone

Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase

hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures.

Cdc37 is required for association of the protein kinase Cdc28 with G1 and mitotic cyclins.

The selection of S. cerevisiae mutants defective in the start event of cell division

P304

1661-1672

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scholarly article

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1072936

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P356

10.1128/MCB.19.3.1661

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3

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P478

19

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Brent H Cochran

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1999-03-01T00:00:00Z

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10022854

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P932

83960

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