Chaperone functions of the E3 ubiquitin ligase CHIP. (Q30362083)

20 June 2017

Chaperone functions of the E3 ubiquitin ligase CHIP. (English)

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20 June 2017

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Meredith F N Rosser

1

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20 June 2017

Erin Washburn

2

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20 June 2017

Paul J Muchowski

3

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20 June 2017

Cam Patterson

4

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20 June 2017

Douglas M Cyr

5

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20 June 2017

language of work or name

English

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publication date

1 June 2007

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Journal of Biological Chemistry

20 June 2017

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20 June 2017

282

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20 June 2017

31

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20 June 2017

22267-22277

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The ubiquitin system for protein degradation

20 June 2017

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https://api.crossref.org/works/10.1074%2FJBC.M700513200

Molecular chaperones in the cytosol: from nascent chain to folded protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

Molecular chaperones and protein quality control

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

Role of quality control pathways in human diseases involving protein misfolding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

The J-protein family: modulating protein assembly, disassembly and translocation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

From the cradle to the grave: molecular chaperones that may choose between folding and degradation

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M700513200

Protein turnover: a CHIP programmed for proteolysis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

Regulation of the cytoplasmic quality control protein degradation pathway by BAG2

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

Hsp70 chaperones: cellular functions and molecular mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

A foldable CFTR{Delta}F508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

CHIP activates HSF1 and confers protection against apoptosis and cellular stress

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

AtCHIP, a U-box-containing E3 ubiquitin ligase, plays a critical role in temperature stress tolerance in Arabidopsis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

CHIP-Hsc70 Complex Ubiquitinates Phosphorylated Tau and Enhances Cell Survival

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

In vivo evidence of CHIP up-regulation attenuating tau aggregation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

Ubiquitylation of neuronal nitric-oxide synthase by CHIP, a chaperone-dependent E3 ligase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

The biological and chemical basis for tissue-selective amyloid disease

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

Hip, a novel cochaperone involved in the eukaryotic hsc70/hsp40 reaction cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

The Hsp90 Cochaperone p23 Is the Limiting Component of the Multiprotein Hsp90/Hsp70-based Chaperone System in Vivo Where It Acts to Stabilize the Client Protein·Hsp90 Complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

Identification of essential residues in the type II Hsp40 Sis1 that function in polypeptide binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

Interaction of Hsp70 chaperones with substrates

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog, Hsp40.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

Polypeptide substrate recognition by calnexin requires specific conformations of the calnexin protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

Dimerization of the human E3 ligase CHIP via a coiled-coil domain is essential for its activity.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

Structure and interactions of the helical and U-box domains of CHIP, the C terminus of HSP70 interacting protein.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

U box proteins as a new family of ubiquitin-protein ligases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

Specific interaction between Smad1 and CHIP: a surface plasmon resonance study

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

CHIP mediates degradation of Smad proteins and potentially regulates Smad-induced transcription

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

Beyond transcription--new mechanisms for the regulation of molecular chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

Redox-regulated molecular chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

Adenosine nucleotides and the regulation of GRP94-client protein interactions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

Hsp105 but not Hsp70 family proteins suppress the aggregation of heat-denatured protein in the presence of ADP

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

The hsp110 and Grp1 70 stress proteins: newly recognized relatives of the Hsp70s

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M700513200

21 January 2018

Identifiers

DOI

10.1074/JBC.M700513200

1 reference

release_rzjaq7x33rglxncmjsl2bs6yqa

20 June 2017

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/rzjaq7x33rglxncmjsl2bs6yqa

mapped directly with Wikidata item

24 November 2022

based on heuristic

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