Regulation of the cytoplasmic quality control protein degradation pathway by BAG2 - Wikidata - awgldk - TriplyDB

Regulation of the cytoplasmic quality control protein degradation pathway by BAG2

Regulation of the cytoplasmic quality control protein degradation pathway by BAG2

http://www.wikidata.org/entity/Q28272894

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Identification of FAM111A as an SV40 host range restriction and adenovirus helper factor Endoplasmic reticulum protein quality control is determined by cooperative interactions between Hsp/c70 protein and the CHIP E3 ligase BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP.Cytosolic chaperones influence the fate of a toxin dislocated from the endoplasmic reticulum The nucleotide exchange factors of Hsp70 molecular chaperones Selective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradation Protein homeostasis at the plasma membrane Protein quality control in the nucleus Structural basis of nucleotide exchange and client binding by the Hsp70 cochaperone Bag2 A Decade of Boon or Burden: What Has the CHIP Ever Done for Cellular Protein Quality Control Mechanism Implicated in Neurodegeneration and Aging?BAG3 and Hsc70 interact with actin capping protein CapZ to maintain myofibrillar integrity under mechanical stress Hold me tight: Role of the heat shock protein family of chaperones in cardiac disease Bat3 deficiency accelerates the degradation of Hsp70-2/HspA2 during spermatogenesis.Ube2w and ataxin-3 coordinately regulate the ubiquitin ligase CHIP Genome evolution in the cold: Antarctic icefish muscle transcriptome reveals selective duplications increasing mitochondrial function Chaperone functions of the E3 ubiquitin ligase CHIP.The role of the UPS in cystic fibrosis.BAG2 structure, function and involvement in disease.Hsp40 chaperones promote degradation of the HERG potassium channel.Identification of factors involved in the anti-tumor activity of carnosine on glioblastomas using a proteomics approach.Ubiquitinylation of α-synuclein by carboxyl terminus Hsp70-interacting protein (CHIP) is regulated by Bcl-2-associated athanogene 5 (BAG5).Endoplasmic reticulum-associated degradation of Niemann-Pick C1: evidence for the role of heat shock proteins and identification of lysine residues that accept ubiquitin.HSP70-binding protein HSPBP1 regulates chaperone expression at a posttranslational level and is essential for spermatogenesis.The balanced regulation of Hsc70 by DNJ-13 and UNC-23 is required for muscle functionality.Brain distribution of carboxy terminus of Hsc70-interacting protein (CHIP) and its nuclear translocation in cultured cortical neurons following heat stress or oxygen-glucose deprivation.Molecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathways.Role of Hsc70 binding cycle in CFTR folding and endoplasmic reticulum-associated degradation.Targeting of KRAS mutant tumors by HSP90 inhibitors involves degradation of STK33.Crystallization and preliminary X-ray crystallographic analysis of the Bag2 amino-terminal domain from Mus musculus BAG2 promotes tumorigenesis through enhancing mutant p53 protein levels and function.BAG2 Gene-mediated Regulation of PINK1 Protein Is Critical for Mitochondrial Translocation of PARKIN and Neuronal Survival Induction of BAG2 protein during proteasome inhibitor-induced apoptosis in thyroid carcinoma cells.Carboxyl terminus of Hsp70-interacting protein (CHIP) is required to modulate cardiac hypertrophy and attenuate autophagy during exercise.Molecular chaperones as regulators of cell death.Heparin-degrading sulfatases in hepatocellular carcinoma: roles in pathogenesis and therapy targets.The tumor suppressor function of human sulfatase 1 (SULF1) in carcinogenesis.Chaperone-assisted degradation: multiple paths to destruction.Molecular chaperones as rational drug targets for Parkinson's disease therapeutics.Cross-functional E3 ligases Parkin and C-terminus Hsp70-interacting protein in neurodegenerative disorders.The role of the cytosolic HSP70 chaperone system in diseases caused by misfolding and aberrant trafficking of ion channels

P2860

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P2860

Regulation of the cytoplasmic quality control protein degradation pathway by BAG2

http://www.wikidata.org/entity/Q28272894

description

2005 nî lūn-bûn

@nan

2005 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2005年の論文

@ja

2005年論文

@yue

2005年論文

@zh-hant

2005年論文

@zh-hk

2005年論文

@zh-mo

2005年論文

@zh-tw

2005年论文

@wuu

name

Regulation of the cytoplasmic quality control protein degradation pathway by BAG2

@ast

Regulation of the cytoplasmic quality control protein degradation pathway by BAG2

@en

Regulation of the cytoplasmic quality control protein degradation pathway by BAG2

@nl

type

label

Regulation of the cytoplasmic quality control protein degradation pathway by BAG2

@ast

Regulation of the cytoplasmic quality control protein degradation pathway by BAG2

@en

Regulation of the cytoplasmic quality control protein degradation pathway by BAG2

@nl

prefLabel

Regulation of the cytoplasmic quality control protein degradation pathway by BAG2

@ast

Regulation of the cytoplasmic quality control protein degradation pathway by BAG2

@en

Regulation of the cytoplasmic quality control protein degradation pathway by BAG2

@nl

P1433

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P2860

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P1433

Journal of Biological Chemistry

P1476

Regulation of the cytoplasmic quality control protein degradation pathway by BAG2

@en

P2093

Christoph Borchers

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

David Huang

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

Douglas M Cyr

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

Holly McDonough

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

Hong Yu Ren

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

Hui-Hua Li

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

J Michael Younger

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

Qian Dai

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

Shinichi Takayama

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

Shu-Bing Qian

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

P2860

An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators

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

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

Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors

The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome

Molecular chaperone targeting and regulation by BAG family proteins

Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling

CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation

Cloning and functional analysis of BAG-1: a novel Bcl-2-binding protein with anti-cell death activity

P304

38673-81

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P31

scholarly article

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3151415

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P356

10.1074/JBC.M507986200

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P407

P433

46

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P478

280

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P577

2005-11-18T00:00:00Z

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16169850

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P921

quality control