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Role of the mitochondrial DnaJ homolog Mdj1p as a chaperone for mitochondrially synthesized and imported proteins
scientific article
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scholarly article
1 reference
stated in
PubMed
PubMed ID
8943361
retrieved
1 December 2016
title
Role of the mitochondrial DnaJ homolog Mdj1p as a chaperone for mitochondrially synthesized and imported proteins
(English)
1 reference
stated in
PubMed
PubMed ID
8943361
retrieved
1 December 2016
main subject
molecular chaperones
0 references
Mdj1p YFL016C
1 reference
stated in
GOA release 2020-03-11
mitochondrion
1 reference
based on heuristic
inferred from title
author name string
B Westermann
series ordinal
1
0 references
B Gaume
series ordinal
2
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J M Herrmann
series ordinal
3
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W Neupert
series ordinal
4
0 references
E Schwarz
series ordinal
5
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language of work or name
English
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publication date
December 1996
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published in
Molecular and Cellular Biology
1 reference
stated in
PubMed
PubMed ID
8943361
retrieved
1 December 2016
volume
16
0 references
issue
12
0 references
page(s)
7063-71
0 references
cites work
Role of the mitochondrial DnaJ homologue, Mdj1p, in the prevention of heat-induced protein aggregation.
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PubMed Central
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Extragenic suppressors of mutations in the cytoplasmic C terminus of SEC63 define five genes in Saccharomyces cerevisiae
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A mitochondrial homolog of bacterial GrpE interacts with mitochondrial hsp70 and is essential for viability
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20 March 2017
Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding
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PubMed Central
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20 March 2017
A role for a eukaryotic GrpE-related protein, Mge1p, in protein translocation
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Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria
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20 March 2017
Mitochondrial Hsp70/MIM44 complex facilitates protein import
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Dynamic interaction between Isp45 and mitochondrial hsp70 in the protein import system of the yeast mitochondrial inner membrane
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20 March 2017
A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s
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Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria
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A positive selection for mutants lacking orotidine-5'-phosphate decarboxylase activity in yeast: 5-fluoro-orotic acid resistance
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A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome
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The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE
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Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast
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Binding protein BiP is required for translocation of secretory proteins into the endoplasmic reticulum in Saccharomyces cerevisiae
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Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeast
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Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins
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7 April 2017
Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
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7 April 2017
Protein biogenesis: chaperones for nascent polypeptides
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Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.
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Hsp60-independent protein folding in the matrix of yeast mitochondria
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29 September 2017
The delta psi- and Hsp70/MIM44-dependent reaction cycle driving early steps of protein import into mitochondria
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29 September 2017
A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates.
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29 September 2017
The role of molecular chaperones in protein folding
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29 September 2017
Mitochondrial GrpE modulates the function of matrix Hsp70 in translocation and maturation of preproteins
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29 September 2017
Heat shock proteins: molecular chaperones of protein biogenesis.
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29 September 2017
Eukaryotic DnaJ homologs and the specificity of Hsp70 activity
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29 September 2017
Genetic interactions between KAR2 and SEC63, encoding eukaryotic homologues of DnaK and DnaJ in the endoplasmic reticulum
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29 September 2017
Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides
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29 September 2017
Mitochondrial molecular chaperones: their role in protein translocation
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29 September 2017
DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70.
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29 September 2017
NMR structure determination of the Escherichia coli DnaJ molecular chaperone: secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domain.
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29 September 2017
DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.
1 reference
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PubMed Central
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29 September 2017
The conserved G/F motif of the DnaJ chaperone is necessary for the activation of the substrate binding properties of the DnaK chaperone
1 reference
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PubMed Central
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29 September 2017
The role of the GrpE homologue, Mge1p, in mediating protein import and protein folding in mitochondria.
1 reference
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29 September 2017
Initiation of lambda DNA replication with purified host- and bacteriophage-encoded proteins: the role of the dnaK, dnaJ and grpE heat shock proteins
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29 September 2017
Analysis of mitochondrial protein import using translocation intermediates and specific antibodies.
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29 September 2017
Sequential action of mitochondrial chaperones in protein import into the matrix
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29 September 2017
The emergence of the chaperone machines
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29 September 2017
Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
1 reference
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29 September 2017
Mitochondrial heat shock protein 70, a molecular chaperone for proteins encoded by mitochondrial DNA.
1 reference
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2 June 2018
Mitochondrial GrpE is present in a complex with hsp70 and preproteins in transit across membranes
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=231709
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2 June 2018
Mitochondrial protein import: biochemical and genetic evidence for interaction of matrix hsp70 and the inner membrane protein MIM44
1 reference
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PubMed Central
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=231709
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2 June 2018
Escherichia coli heat shock gene mutants are defective in proteolysis
1 reference
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PubMed Central
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=231709
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2 June 2018
Physical interaction between heat shock proteins DnaK, DnaJ, and GrpE and the bacterial heat shock transcription factor sigma 32
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=231709
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2 June 2018
DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli
1 reference
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PubMed Central
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=231709
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2 June 2018
Substitution of PIM1 protease in mitochondria by Escherichia coli Lon protease.
1 reference
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PubMed Central
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27 November 2018
ATP-induced protein-Hsp70 complex dissociation requires K+ but not ATP hydrolysis.
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=231709
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27 November 2018
YGE1 is a yeast homologue of Escherichia coli grpE and is required for maintenance of mitochondrial functions.
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=231709
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27 November 2018
The NH2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lambda replication.
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=231709
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27 November 2018
How ATP drives proteins across membranes.
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PubMed Central
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27 November 2018
Successive action of Escherichia coli chaperones in vivo.
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27 November 2018
Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria.
1 reference
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PubMed Central
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27 November 2018
Heat shock protein-mediated disassembly of nucleoprotein structures is required for the initiation of bacteriophage lambda DNA replication
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PubMed Central
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27 November 2018
Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis
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PubMed Central
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27 November 2018
Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
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PubMed
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12 December 2020
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inferred from PubMed ID database lookup
The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria
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PubMed
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https://pubmed.ncbi.nlm.nih.gov/8943361
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12 December 2020
based on heuristic
inferred from PubMed ID database lookup
1H and 15N magnetic resonance assignments, secondary structure, and tertiary fold of Escherichia coli DnaJ(1-78)
1 reference
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PubMed
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https://pubmed.ncbi.nlm.nih.gov/8943361
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12 December 2020
based on heuristic
inferred from PubMed ID database lookup
The role of ATP in the functional cycle of the DnaK chaperone system
1 reference
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PubMed
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https://pubmed.ncbi.nlm.nih.gov/8943361
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12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Topogenesis of cytochrome oxidase subunit II. Mechanisms of protein export from the mitochondrial matrix
1 reference
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PubMed
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https://pubmed.ncbi.nlm.nih.gov/8943361
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12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Transport of proteins into mitochondria: translocational intermediates spanning contact sites between outer and inner membranes
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/8943361
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12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Function of DnaJ and DnaK as chaperones in origin-specific DNA binding by RepA
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/8943361
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1128/MCB.16.12.7063
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PMCID
231709
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PubMed ID
8943361
1 reference
stated in
PubMed
PubMed ID
8943361
retrieved
1 December 2016
ResearchGate publication ID
14264633
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