Molecular chaperones: How J domains turn on Hsp70s (Q33606901)

28 July 2017

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title

Molecular chaperones: How J domains turn on Hsp70s (English)

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28 July 2017

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W L Kelley

1

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PubMed ID

10226023

28 July 2017

language of work or name

English

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publication date

1 April 1999

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28 July 2017

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28 July 2017

9

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28 July 2017

8

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28 July 2017

R305-8

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The Hsp70 and Hsp60 chaperone machines

28 July 2017

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https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7

7 January 2021

Interaction of Hsp70 chaperones with substrates

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https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7

7 January 2021

An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators

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https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7

7 January 2021

The J-domain family and the recruitment of chaperone power

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7

7 January 2021

A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7

7 January 2021

Specific molecular chaperone interactions and an ATP-dependent conformational change are required during posttranslational protein translocation into the yeast ER.

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7

7 January 2021

Mitochondrial Hsp70 cannot replace BiP in driving protein translocation into the yeast endoplasmic reticulum

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7

7 January 2021

Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1.

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7

7 January 2021

NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7

7 January 2021

A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7

7 January 2021

The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7

7 January 2021

Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone.

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7

7 January 2021

Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ.

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7

7 January 2021

J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7

7 January 2021

10.1016/S0960-9822(99)80185-7

Identifiers

DOI

1 reference

28 July 2017

1 reference

PubMed ID

10226023