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Molecular chaperones: How J domains turn on Hsp70s
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instance of
scholarly article
1 reference
stated in
Europe PubMed Central
PubMed ID
10226023
retrieved
28 July 2017
review article
1 reference
stated in
Europe PubMed Central
title
Molecular chaperones: How J domains turn on Hsp70s
(English)
1 reference
stated in
Europe PubMed Central
PubMed ID
10226023
retrieved
28 July 2017
main subject
molecular chaperones
0 references
author name string
W L Kelley
series ordinal
1
1 reference
stated in
Europe PubMed Central
PubMed ID
10226023
retrieved
28 July 2017
language of work or name
English
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publication date
1 April 1999
1 reference
stated in
Europe PubMed Central
PubMed ID
10226023
retrieved
28 July 2017
published in
Current Biology
1 reference
stated in
Europe PubMed Central
PubMed ID
10226023
retrieved
28 July 2017
volume
9
1 reference
stated in
Europe PubMed Central
PubMed ID
10226023
retrieved
28 July 2017
page(s)
R305-8
1 reference
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Europe PubMed Central
PubMed ID
10226023
retrieved
28 July 2017
issue
8
1 reference
stated in
Europe PubMed Central
PubMed ID
10226023
retrieved
28 July 2017
cites work
The Hsp70 and Hsp60 chaperone machines
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Interaction of Hsp70 chaperones with substrates
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
The J-domain family and the recruitment of chaperone power
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
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
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Specific molecular chaperone interactions and an ATP-dependent conformational change are required during posttranslational protein translocation into the yeast ER.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Mitochondrial Hsp70 cannot replace BiP in driving protein translocation into the yeast endoplasmic reticulum
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1.
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Role of the J-domain in the cooperation of Hsp40 with Hsp70.
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980185-7
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Identifiers
DOI
10.1016/S0960-9822(99)80185-7
1 reference
stated in
Europe PubMed Central
PubMed ID
10226023
retrieved
28 July 2017
PubMed ID
10226023
1 reference
stated in
Europe PubMed Central
PubMed ID
10226023
retrieved
28 July 2017
ResearchGate publication ID
13072494
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