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Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast
scientific article
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scholarly article
1 reference
stated in
PubMed
PubMed ID
15342786
retrieved
1 December 2016
title
Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast
(English)
1 reference
stated in
PubMed
PubMed ID
15342786
retrieved
1 December 2016
main subject
cell biology
0 references
cystic fibrosis
0 references
molecular chaperones
0 references
transmembrane protein
0 references
Type I HSP40 co-chaperone YDJ1 YNL064C
1 reference
stated in
GOA release 2020-03-11
Type I HSP40 co-chaperone HLJ1 YMR161W
1 reference
stated in
GOA release 2020-03-11
author
Trevor Lithgow
series ordinal
4
0 references
Traude H. Beilharz
object named as
Traude Beilharz
series ordinal
3
0 references
author name string
Robert T Youker
series ordinal
1
0 references
Peter Walsh
series ordinal
2
0 references
Jeffrey L Brodsky
series ordinal
5
0 references
language of work or name
English
0 references
publication date
November 2004
0 references
published in
Molecular Biology of the Cell
1 reference
stated in
PubMed
PubMed ID
15342786
retrieved
1 December 2016
volume
15
0 references
page(s)
4787-97
0 references
issue
11
0 references
cites work
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The human DnaJ homologue (Hdj)-1/heat-shock protein (Hsp) 40 co-chaperone is required for the in vivo stabilization of the cystic fibrosis transmembrane conductance regulator by Hsp70
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SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins
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Regulation of the heat shock conjugate Hsc70 in the mammalian cell: the characterization of the anti-apoptotic protein BAG-1 provides novel insights
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stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=524727
retrieved
2 June 2018
Involvement of heat shock protein 90 in the degradation of mutant insulin receptors by the proteasome.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=524727
retrieved
2 June 2018
Functional expression of the cystic fibrosis transmembrane conductance regulator in yeast.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=524727
retrieved
2 June 2018
MSI3, a multicopy suppressor of mutants hyperactivated in the RAS-cAMP pathway, encodes a novel HSP70 protein of Saccharomyces cerevisiae.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=524727
retrieved
2 June 2018
Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=524727
retrieved
2 June 2018
Use of modular substrates demonstrates mechanistic diversity and reveals differences in chaperone requirement of ERAD.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=524727
retrieved
27 November 2018
Expression and degradation of the cystic fibrosis transmembrane conductance regulator in Saccharomyces cerevisiae
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=524727
retrieved
27 November 2018
Apoprotein B degradation is promoted by the molecular chaperones hsp90 and hsp70.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=524727
retrieved
27 November 2018
Both the N- and C-terminal chaperone sites of Hsp90 participate in protein refolding
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=524727
retrieved
27 November 2018
Post-translational disruption of the delta F508 cystic fibrosis transmembrane conductance regulator (CFTR)-molecular chaperone complex with geldanamycin stabilizes delta F508 CFTR in the rabbit reticulocyte lysate.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=524727
retrieved
27 November 2018
Geldanamycin, an hsp90/GRP94-binding drug, induces increased transcription of endoplasmic reticulum (ER) chaperones via the ER stress pathway
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=524727
retrieved
27 November 2018
The molecular chaperone Hsc70 assists the in vitro folding of the N-terminal nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=524727
retrieved
27 November 2018
Structural organization of procaryotic and eucaryotic Hsp90. Influence of divalent cations on structure and function.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=524727
retrieved
27 November 2018
Multiple proteolytic systems, including the proteasome, contribute to CFTR processing.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=524727
retrieved
27 November 2018
Limited proteolysis as a probe for arrested conformational maturation of delta F508 CFTR
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/15342786
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
CFTR expression and ER-associated degradation in yeast
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/15342786
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Localization and suppression of a kinetic defect in cystic fibrosis transmembrane conductance regulator folding
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/15342786
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
In vitro evidence that hsp90 contains two independent chaperone sites
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/15342786
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
A Toxic Fusion Protein Accumulating between the Mitochondrial Membranes Inhibits Protein Assemblyin Vivo
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/15342786
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/15342786
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Control of estrogen receptor ligand binding by Hsp90
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/15342786
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1091/MBC.E04-07-0584
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
406018
OpenCitations bibliographic resource ID
406018
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
406018
PMCID
524727
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
406018
PubMed ID
15342786
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
406018
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