(Q28115341)

3 January 2017

title

Co-chaperone HSJ1a dually regulates the proteasomal degradation of ataxin-3 (English)

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3 January 2017

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Xue-Chao Gao

1

1 reference

3 January 2017

Chen-Jie Zhou

2

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3 January 2017

Zi-Ren Zhou

3

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3 January 2017

Yu-Hang Zhang

4

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3 January 2017

Xue-Ming Zheng

5

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3 January 2017

Ai-Xin Song

6

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3 January 2017

Hong-Yu Hu

7

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3 January 2017

language of work or name

English

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publication date

1 January 2011

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3 January 2017

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3 January 2017

volume

6

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3 January 2017

issue

5

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3 January 2017

page(s)

e19763

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Creative Commons Attribution 4.0 International

3 January 2017

copyright license

start time

19 May 2011

1 reference

April 2022 Public Data File from Crossref

copyright status

copyrighted

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cites work

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29 September 2017

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29 September 2017

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Levels of DNAJB family members (HSP40) correlate with disease onset in patients with spinocerebellar ataxia type 3.

29 September 2017

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Inhibition of hsp70 by methylene blue affects signaling protein function and ubiquitination and modulates polyglutamine protein degradation

29 September 2017

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Hsp40 chaperones promote degradation of the HERG potassium channel

29 September 2017

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In vivo suppression of polyglutamine neurotoxicity by C-terminus of Hsp70-interacting protein (CHIP) supports an aggregation model of pathogenesis.

29 September 2017

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CHIP deletion reveals functional redundancy of E3 ligases in promoting degradation of both signaling proteins and expanded glutamine proteins

29 September 2017

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29 September 2017

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Polyglutamine diseases: emerging concepts in pathogenesis and therapy

29 September 2017

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To be, or not to be--molecular chaperones in protein degradation

29 September 2017

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Phosphorylation of ataxin-3 by glycogen synthase kinase 3beta at serine 256 regulates the aggregation of ataxin-3.

29 September 2017

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Hsp40 molecules that target to the ubiquitin-proteasome system decrease inclusion formation in models of polyglutamine disease

29 September 2017

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29 September 2017

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The chaperone-associated ubiquitin ligase CHIP is able to target p53 for proteasomal degradation

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3098244

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

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3098244

Cooperation of molecular chaperones with the ubiquitin/proteasome system

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3098244

CHIP: a link between the chaperone and proteasome systems

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3098244

Roles of molecular chaperones in protein misfolding diseases

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3098244

Molecular clearance of ataxin-3 is regulated by a mammalian E4

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3098244

Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3098244

Ubiquitin-mediated sequestration of normal cellular proteins into polyglutamine aggregates

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3098244

Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's disease

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3098244

Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, and are suppressed by the HDJ-2 chaperone

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3098244

Role of the J-domain in the cooperation of Hsp40 with Hsp70.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3098244

Involvement of the molecular chaperone Ydj1 in the ubiquitin-dependent degradation of short-lived and abnormal proteins in Saccharomyces cerevisiae

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3098244

A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3098244

Chemical manipulation of hsp70 ATPase activity regulates tau stability.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3098244

CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3098244

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

2 June 2018

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Crossref

https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0019763

Chaperone-dependent regulation of endothelial nitric-oxide synthase intracellular trafficking by the co-chaperone/ubiquitin ligase CHIP.

21 January 2018

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https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0019763

Highly efficient expression and purification system of small-size protein domains in Escherichia coli for biochemical characterization.

21 January 2018

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https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0019763

Ubiquitin-dependent degradation of certain protein substrates in vitro requires the molecular chaperone Hsc70

21 January 2018

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12 December 2020

Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease

1 reference

12 December 2020

Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract

1 reference

12 December 2020

Interaction of the human DnaJ homologue, HSJ1b with the 90 kDa heat shock protein, Hsp90

1 reference

12 December 2020

Spinocerebellar ataxia, type 3 (SCA3) is genetically identical to Machado-Joseph disease (MJD)

1 reference

12 December 2020

10.1371/JOURNAL.PONE.0019763

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