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Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor
scientific article
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scholarly article
1 reference
stated in
PubMed
PubMed ID
16688211
retrieved
1 December 2016
title
Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor
(English)
1 reference
stated in
PubMed
PubMed ID
16688211
retrieved
1 December 2016
main subject
molecular chaperones
0 references
Adenyl-nucleotide exchange factor SSE2 YBR169C
1 reference
stated in
GOA release 2020-03-11
Hsp70 family ATPase SSB1 YDL229W
1 reference
stated in
GOA release 2020-03-11
Adenyl-nucleotide exchange factor SSE1 YPL106C
1 reference
stated in
GOA release 2020-03-11
Hsp70 family ATPase SSA1 YAL005C
1 reference
stated in
GOA release 2020-03-11
author
Bernd Bukau
series ordinal
5
object named as
Bernd Bukau
0 references
author name string
Holger Raviol
series ordinal
1
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Heather Sadlish
series ordinal
2
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Fernanda Rodriguez
series ordinal
3
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Matthias P Mayer
series ordinal
4
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language of work or name
English
0 references
publication date
7 June 2006
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published in
The EMBO Journal
1 reference
stated in
PubMed
PubMed ID
16688211
retrieved
1 December 2016
volume
25
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issue
11
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page(s)
2510-8
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cites work
Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells
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=1478168
retrieved
20 March 2017
The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family
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=1478168
retrieved
20 March 2017
Coordinated activation of Hsp70 chaperones
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=1478168
retrieved
20 March 2017
Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p
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=1478168
retrieved
20 March 2017
Functional organization of the yeast proteome by systematic analysis of protein complexes
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=1478168
retrieved
20 March 2017
Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors
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=1478168
retrieved
20 March 2017
Sls1p stimulates Sec63p-mediated activation of Kar2p in a conformation-dependent manner in the yeast endoplasmic reticulum.
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=1478168
retrieved
20 March 2017
A generic protein purification method for protein complex characterization and proteome exploration
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=1478168
retrieved
20 March 2017
The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone
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=1478168
retrieved
20 March 2017
Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins
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=1478168
retrieved
20 March 2017
Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1.
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=1478168
retrieved
20 March 2017
Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
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=1478168
retrieved
20 March 2017
The refolding activity of the yeast heat shock proteins Ssa1 and Ssa2 defines their role in protein translocation
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=1478168
retrieved
20 March 2017
Isolation and characterization of SSE1 and SSE2, new members of the yeast HSP70 multigene family
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=1478168
retrieved
20 March 2017
Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase
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=1478168
retrieved
20 March 2017
Molecular chaperones in the cytosol: from nascent chain to folded protein
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=1478168
retrieved
20 March 2017
Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange
2 references
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=1478168
retrieved
20 March 2017
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=1478168
retrieved
7 April 2017
The Hsp70 and Hsp60 chaperone machines
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=1478168
retrieved
7 April 2017
Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase
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=1478168
retrieved
29 September 2017
Overexpression of yeast Hsp110 homolog Sse1p suppresses ydj1-151 thermosensitivity and restores Hsp90-dependent activity
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=1478168
retrieved
29 September 2017
The hsp110 and Grp1 70 stress proteins: newly recognized relatives of the Hsp70s
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=1478168
retrieved
29 September 2017
DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.
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=1478168
retrieved
29 September 2017
The molecular chaperone Sse1 and the growth control protein kinase Sch9 collaborate to regulate protein kinase A activity 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=1478168
retrieved
2 June 2018
Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase
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=1478168
retrieved
2 June 2018
Interaction of Hsp70 chaperones with substrates
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=1478168
retrieved
2 June 2018
Human and yeast Hsp110 chaperones exhibit functional differences
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=1478168
retrieved
27 November 2018
Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding
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=1478168
retrieved
27 November 2018
The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1.
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=1478168
retrieved
27 November 2018
Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers
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=1478168
retrieved
27 November 2018
Deletion of DnaK's lid strengthens binding to the nucleotide exchange factor, GrpE: a kinetic and thermodynamic analysis
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=1478168
retrieved
27 November 2018
Bag-1M accelerates nucleotide release for human Hsc70 and Hsp70 and can act concentration-dependent as positive and negative cofactor.
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=1478168
retrieved
27 November 2018
Investigation of the interaction between DnaK and DnaJ by surface plasmon resonance spectroscopy.
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=1478168
retrieved
27 November 2018
Characterization of interactions between the anti-apoptotic protein BAG-1 and Hsc70 molecular chaperones
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=1478168
retrieved
27 November 2018
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/16688211
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Folding and refolding of thermolabile and thermostable bacterial luciferases: the role of DnaKJ heat-shock proteins
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/16688211
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Distinct but overlapping functions of Hsp70, Hsp90, and an Hsp70 nucleotide exchange factor during protein biogenesis in yeast
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/16688211
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
The yeast Hsp110 Sse1 functionally interacts with the Hsp70 chaperones Ssa and Ssb
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/16688211
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1038/SJ.EMBOJ.7601139
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
286919
OpenCitations bibliographic resource ID
286919
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
286919
PMCID
1478168
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
286919
PubMed ID
16688211
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
286919
ResearchGate publication ID
7093536
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