Biochemical and Proteomic Analysis of Ubiquitination of Hsc70 and Hsp70 by the E3 Ligase CHIP (Q28262433)

20 October 2023

Kristie L Rose

2

Kristie L

Rose

1 reference

20 October 2023

Salisha Hill

3

Salisha

Hill

1 reference

20 October 2023

Sophie Jouan

4

Sophie

Jouan

1 reference

20 October 2023

Walter J Chazin

5

Walter J

Chazin

1 reference

Creative Commons Attribution 4.0 International

20 October 2023

language of work or name

English

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publication date

2015

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published in

PLOS One

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volume

10

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issue

5

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page(s)

e0128240

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copyright license

start time

26 May 2015

1 reference

April 2022 Public Data File from Crossref

copyright status

copyrighted

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cites work

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

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Insights into the conformational dynamics of the E3 ubiquitin ligase CHIP in complex with chaperones and E2 enzymes.

2 June 2018

1 reference

Crossref

https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0128240

The size of the proteasomal substrate determines whether its degradation will be mediated by mono- or polyubiquitylation

21 January 2018

1 reference

Crossref

https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0128240

Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker

21 January 2018

1 reference

https://pubmed.ncbi.nlm.nih.gov/26010904

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1371/JOURNAL.PONE.0128240

1 reference

ADS bibcode

2015PLoSO..1028240S

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1 reference

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