(Q44151437)

30 November 2017

Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome (English)

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30 November 2017

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1 reference

Simon Alberti

1

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30 November 2017

Jens Demand

2

1 reference

30 November 2017

Claudia Esser

3

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30 November 2017

Niels Emmerich

4

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30 November 2017

Hansjorg Schild

5

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30 November 2017

Jorg Hohfeld

6

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30 November 2017

language of work or name

English

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publication date

23 September 2002

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Journal of Biological Chemistry

30 November 2017

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30 November 2017

277

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30 November 2017

48

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30 November 2017

45920-45927

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

30 November 2017

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

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.M204196200

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.M204196200

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

Ubiquitin and its kin: how close are the family ties?

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

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.M204196200

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.M204196200

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.M204196200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

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.M204196200

The U box is a modified RING finger — a common domain in ubiquitination

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

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.M204196200

GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

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.M204196200

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.M204196200

Protein turnover: a CHIP programmed for proteolysis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

Distinct isoforms of the cofactor BAG-1 differentially affect Hsc70 chaperone function.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

The human 26 S and 20 S proteasomes generate overlapping but different sets of peptide fragments from a model protein substrate.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

In vitro assembly and recognition of Lys-63 polyubiquitin chains

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

Cell cycle-regulated modification of the ribosome by a variant multiubiquitin chain

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

Characterization of two polyubiquitin binding sites in the 26 S protease subunit 5a

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

Proteasome subunit Rpn1 binds ubiquitin-like protein domains

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

Physical association of ubiquitin ligases and the 26S proteasome

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

A HECT domain E3 enzyme assembles novel polyubiquitin chains

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

Role of the ubiquitin-selective CDC48(UFD1/NPL4 )chaperone (segregase) in ERAD of OLE1 and other substrates

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204196200

21 January 2018

Identifiers

DOI

10.1074/JBC.M204196200

1 reference

30 November 2017

1 reference