The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Hippel-Lindau tumor suppressor complex. - Wikidata - awgldk - TriplyDB

The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Hippel-Lindau tumor suppressor complex.

The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Hippel-Lindau tumor suppressor complex.

http://www.wikidata.org/entity/Q39745880

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State of the science: an update on renal cell carcinoma Misfolded proteins partition between two distinct quality control compartments Activities of the chaperonin containing TCP-1 (CCT): implications for cell cycle progression and cytoskeletal organisation Contribution of the Type II Chaperonin, TRiC/CCT, to Oncogenesis Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets.Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies Interaction of p53 with the CCT complex promotes protein folding and wild-type p53 activity The HIF prolyl hydroxylase PHD3 is a potential substrate of the TRiC chaperonin Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis The chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosol The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions.Action of the chaperonin GroEL/ES on a non-native substrate observed with single-molecule FRET.Transactivation of Schizosaccharomyces pombe cdt2+ stimulates a Pcu4-Ddb1-CSN ubiquitin ligase The Type II Hsp40 Sis1 cooperates with Hsp70 and the E3 ligase Ubr1 to promote degradation of terminally misfolded cytosolic protein.The cytosolic chaperonin CCT/TRiC and cancer cell proliferation.Glycosylation of Skp1 promotes formation of Skp1-cullin-1-F-box protein complexes in dictyostelium.Balance between synaptic versus extrasynaptic NMDA receptor activity influences inclusions and neurotoxicity of mutant huntingtin.Hsp70 clears misfolded kinases that partitioned into distinct quality-control compartments.Functional Subunits of Eukaryotic Chaperonin CCT/TRiC in Protein Folding.A direct regulatory interaction between chaperonin TRiC and stress-responsive transcription factor HSF1.Structural Basis for Modulation of Quality Control Fate in a Marginally Stable Protein.Drosophila Mgr, a Prefoldin subunit cooperating with von Hippel Lindau to regulate tubulin stability.Identification of the TRiC/CCT substrate binding sites uncovers the function of subunit diversity in eukaryotic chaperonins Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Missense mutations in the human SDHB gene increase protein degradation without altering intrinsic enzymatic function.Proteostasis modulators prolong missense VHL protein activity and halt tumor progression Chaperonin TRiC/CCT Modulates the Folding and Activity of Leukemogenic Fusion Oncoprotein AML1-ETO.Structural insights into the folding defects of oncogenic pVHL lead to correction of its function in vitro.Polyglutamine neurodegeneration: protein misfolding revisited.Cellular chaperonin CCTγ contributes to rabies virus replication during infection Chaperonin TRiC/CCT Recognizes Fusion Oncoprotein AML1-ETO through Subunit-Specific Interactions.Sgt1 associates with Hsp90: an initial step of assembly of the core kinetochore complex.The ribosome as a hub for protein quality control.Fidelity of cotranslational protein targeting by the signal recognition particle.Regulation of GPCR expression through an interaction with CCT7, a subunit of the CCT/TRiC complex.p90 ribosomal S6 kinase and p70 ribosomal S6 kinase link phosphorylation of the eukaryotic chaperonin containing TCP-1 to growth factor, insulin, and nutrient signaling.TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes Nuclear E-cadherin and VHL immunoreactivity are prognostic indicators of clear-cell renal cell carcinoma.Identification of a hTid-1 mutation which sensitizes gliomas to apoptosis.The structure of CCT-Hsc70 NBD suggests a mechanism for Hsp70 delivery of substrates to the chaperonin.

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The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Hippel-Lindau tumor suppressor complex.

http://www.wikidata.org/entity/Q39745880

description

2003 nî lūn-bûn

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2003年の論文

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年學術文章

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2003年學術文章

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2003年學術文章

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name

The Hsp70 and TRiC/CCT chapero ...... ndau tumor suppressor complex.

@en

The Hsp70 and TRiC/CCT chapero ...... ndau tumor suppressor complex.

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type

label

The Hsp70 and TRiC/CCT chapero ...... ndau tumor suppressor complex.

@en

The Hsp70 and TRiC/CCT chapero ...... ndau tumor suppressor complex.

@nl

prefLabel

The Hsp70 and TRiC/CCT chapero ...... ndau tumor suppressor complex.

@en

The Hsp70 and TRiC/CCT chapero ...... ndau tumor suppressor complex.

@nl

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MCB.23.9.3141-3151.2003

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Molecular and Cellular Biology

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The Hsp70 and TRiC/CCT chapero ...... ndau tumor suppressor complex.

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P2093

Amie J McClellan

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

Andre Darveau

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Anne S Meyer

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Mark W Melville

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P2860

The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis

HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing

Functional organization of the yeast proteome by systematic analysis of protein complexes

Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin

The von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteins

Identification of the von Hippel-lindau tumor-suppressor protein as part of an active E3 ubiquitin ligase complex

Studying interactions of four proteins in the yeast two-hybrid system: structural resemblance of the pVHL/elongin BC/hCUL-2 complex with the ubiquitin ligase complex SKP1/cullin/F-box protein

Solution structure and dynamics of yeast elongin C in complex with a von Hippel-Lindau peptide

Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation

Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry

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3141-3151

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10.1128/MCB.23.9.3141-3151.2003

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7498035

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12697815

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molecular chaperones

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153194

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