(Q28272894)

1

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Shu-Bing Qian

2

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Hui-Hua Li

3

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Holly McDonough

4

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Christoph Borchers

5

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David Huang

6

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Shinichi Takayama

7

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J Michael Younger

8

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Hong Yu Ren

9

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Douglas M Cyr

Journal of Biological Chemistry

10

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language of work or name

English

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publication date

18 November 2005

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published in

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volume

280

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issue

46

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page(s)

38673-81

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cites work

Pathways of chaperone-mediated protein folding in the cytosol

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507986200

Quality control in the endoplasmic reticulum protein factory

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507986200

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.M507986200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507986200

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.M507986200

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.M507986200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507986200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507986200

Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507986200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507986200

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.M507986200

Ligand-dependent switching of ubiquitin-proteasome pathways for estrogen receptor

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507986200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507986200

Identification of in-gel digested proteins by complementary peptide mass fingerprinting and tandem mass spectrometry data obtained on an electrospray ionization quadrupole time-of-flight mass spectrometer.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507986200

Molecular chaperone targeting and regulation by BAG family proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507986200

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.M507986200

CHIP activates HSF1 and confers protection against apoptosis and cellular stress

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507986200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507986200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507986200

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.M507986200

An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507986200

What's in the 'BAG'?--A functional domain analysis of the BAG-family proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507986200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507986200

Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507986200

BAG-1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507986200

Bag-1M accelerates nucleotide release for human Hsc70 and Hsp70 and can act concentration-dependent as positive and negative cofactor.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507986200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507986200

Proteomic identification of Bcl2-associated athanogene 2 as a novel MAPK-activated protein kinase 2 substrate

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507986200

Bag1-Hsp70 mediates a physiological stress signalling pathway that regulates Raf-1/ERK and cell growth.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507986200

21 January 2018

Identifiers

DOI

10.1074/JBC.M507986200

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

16169850

1 reference

Consolidated OpenCitations Corpus – April 2017