Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase. - Wikidata - awgldk - TriplyDB

Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase.

Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase.

http://www.wikidata.org/entity/Q40725739

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Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones Quality control and fate determination of Hsp90 client proteins Discovery of biological networks from diverse functional genomic data.Sgt1p is a unique co-chaperone that acts as a client adaptor to link Hsp90 to Skp1p.Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast.Characterization of Hsp70 binding and nucleotide exchange by the yeast Hsp110 chaperone Sse1.Cdc37 has distinct roles in protein kinase quality control that protect nascent chains from degradation and promote posttranslational maturation Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor.Identification of Histoplasma capsulatum transcripts induced in response to reactive nitrogen species.Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function.Hsp90 cochaperone Aha1 is a negative regulator of the Saccharomyces MAL activator and acts early in the chaperone activation pathway.Hsp110 chaperones control client fate determination in the hsp70-Hsp90 chaperone system Effect of mutation of the tetratricopeptide repeat and asparatate-proline 2 domains of Sti1 on Hsp90 signaling and interaction in Saccharomyces cerevisiae HSP90 supports tumor growth and angiogenesis through PRKD2 protein stabilization.The ribosomal biogenesis protein Utp21 interacts with Hsp90 and has differing requirements for Hsp90-associated proteins.Post-translational modifications of Hsp90 and their contributions to chaperone regulation All in the family: atypical Hsp70 chaperones are conserved modulators of Hsp70 activity.Multiple 40-kDa heat-shock protein chaperones function in Tom70-dependent mitochondrial import.Functional specificity of co-chaperone interactions with Hsp90 client proteins.Function and regulation in MAPK signaling pathways: lessons learned from the yeast Saccharomyces cerevisiae Chaperoning the chaperone: a role for the co-chaperone Cpr7 in modulating Hsp90 function in Saccharomyces cerevisiae.Functioning of the Hsp90 machine in chaperoning checkpoint kinase I (Chk1) and the progesterone receptor (PR).Tumor-intrinsic and tumor-extrinsic factors impacting hsp90- targeted therapy.Novel interaction of the Hsp90 chaperone machine with Ssl2, an essential DNA helicase in Saccharomyces cerevisiae.Farnesylation of Ydj1 is required for in vivo interaction with Hsp90 client proteins.Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms.Kruppel-associated box domain-associated protein-1 as a latency regulator for Kaposi's sarcoma-associated herpesvirus and its modulation by the viral protein kinase.Characterization of celastrol to inhibit hsp90 and cdc37 interaction.Regulation of molecular chaperones through post-translational modifications: decrypting the chaperone code.Contributions of co-chaperones and post-translational modifications towards Hsp90 drug sensitivity.Ydj1 protects nascent protein kinases from degradation and controls the rate of their maturation.Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation.The Hsp110 protein chaperone Sse1 is required for yeast cell wall integrity and morphogenesis.Alteration of the protein kinase binding domain enhances function of the Saccharomyces cerevisiae molecular chaperone Cdc37.Evidence for Hsp90 Co-chaperones in Regulating Hsp90 Function and Promoting Client Protein Folding.Detecting Posttranslational Modifications of Hsp90.Mutation of essential Hsp90 co-chaperones SGT1 or CNS1 renders yeast hypersensitive to overexpression of other co-chaperones.

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P2860

Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase.

http://www.wikidata.org/entity/Q40725739

description

2004 nî lūn-bûn

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2004年の論文

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2004年学术文章

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2004年学术文章

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2004年學術文章

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2004年學術文章

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2004年學術文章

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Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase.

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Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase.

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prefLabel

Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase.

@en

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MBC.E03-07-0480

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Molecular Biology of the Cell

P1476

Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase.

@en

P2093

Arsalan Shabbir

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

Avrom J Caplan

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

Christopher Cardozo

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

Paul Lee

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

P2860

Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone

Interaction between Cdc37 and Cdk4 in human cells

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

Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1

Genetic and biochemical analysis of p23 and ansamycin antibiotics in the function of Hsp90-dependent signaling proteins

Heat-shock protein 90 and Cdc37 interact with LKB1 and regulate its stability

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

Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2−ΔΔCT Method

SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins

Cooperation of the molecular chaperone Ydj1 with specific Hsp70 homologs to suppress protein aggregation.

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1785-1792

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10.1091/MBC.E03-07-0480

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4

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15

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2004-01-23T00:00:00Z

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molecular chaperones

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379275

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