CHIP protects from the neurotoxicity of expanded and wild-type ataxin-1 and promotes their ubiquitination and degradation (Q24296740)

HSPA (Hsp70) binding protein 1

GOA release 2020-03-11

1 reference

positive regulation of chaperone-mediated protein complex assembly

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

protein ubiquitination

1 reference

1 reference

9

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Huda Zoghbi

object named as

Huda Y Zoghbi

10

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Maria de Haro

object named as

Maria de Haro

8

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author name string

Ismael Al-Ramahi

1

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Yung C Lam

2

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Hung-Kai Chen

3

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Beatrice de Gouyon

4

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Minghang Zhang

5

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Alma M Pérez

6

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Joana Branco

7

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Juan Botas

Journal of Biological Chemistry

11

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language of work or name

English

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publication date

8 September 2006

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published in

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volume

281

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issue

36

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page(s)

26714-24

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cites work

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The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg.

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Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1.

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Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice.

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Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice

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Identification of genes that modify ataxin-1-induced neurodegeneration.

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Boat, an AXH domain protein, suppresses the cytotoxicity of mutant ataxin-1.

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The unfolding tale of the unfolded protein response

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Posttranslational quality control: folding, refolding, and degrading proteins.

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Protein quality control: U-box-containing E3 ubiquitin ligases join the fold

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Protein turnover: a CHIP programmed for proteolysis.

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

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

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CHIP: a quality-control E3 ligase collaborating with molecular chaperones

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Interaction of U-box-type ubiquitin-protein ligases (E3s) with molecular chaperones

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Overexpression of the cochaperone CHIP enhances Hsp70-dependent folding activity in mammalian cells.

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CHIP activates HSF1 and confers protection against apoptosis and cellular stress

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CHIP promotes proteasomal degradation of familial ALS-linked mutant SOD1 by ubiquitinating Hsp/Hsc70.

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The co-chaperone carboxyl terminus of Hsp70-interacting protein (CHIP) mediates alpha-synuclein degradation decisions between proteasomal and lysosomal pathways

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CHIP-Hsc70 Complex Ubiquitinates Phosphorylated Tau and Enhances Cell Survival

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CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation

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CHIP suppresses polyglutamine aggregation and toxicity in vitro and in vivo.

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Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes.

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U-box protein carboxyl terminus of Hsc70-interacting protein (CHIP) mediates poly-ubiquitylation preferentially on four-repeat Tau and is involved in neurodegeneration of tauopathy

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Co-chaperone CHIP associates with mutant Cu/Zn-superoxide dismutase proteins linked to familial amyotrophic lateral sclerosis and promotes their degradation by proteasomes

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Chaperoned ubiquitylation--crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex

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Genetic suppression of polyglutamine toxicity in Drosophila

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CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity

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Ataxin 1, a SCA1 neurodegenerative disorder protein, is functionally linked to the silencing mediator of retinoid and thyroid hormone receptors

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Serine 776 of ataxin-1 is critical for polyglutamine-induced disease in SCA1 transgenic mice

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Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's disease

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Mice lacking ataxin-1 display learning deficits and decreased hippocampal paired-pulse facilitation

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7 January 2021

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Identifiers

DOI

10.1074/JBC.M601603200

1 reference

Consolidated OpenCitations Corpus – April 2017

3151400

3151400

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference