Molecular chaperones as essential mediators of mitochondrial biogenesis (Q34793186)

4 August 2017

1 reference

title

Molecular chaperones as essential mediators of mitochondrial biogenesis (English)

1 reference

4 August 2017

0 references

Wolfgang Voos

1

1 reference

PubMed ID

12191768

4 August 2017

Karin Röttgers

series ordinal

2

1 reference

PubMed ID

12191768

4 August 2017

language of work or name

English

0 references

publication date

1 September 2002

1 reference

Biochimica et Biophysica Acta

4 August 2017

1 reference

4 August 2017

1592

1 reference

4 August 2017

1

1 reference

4 August 2017

51-62

1 reference

The Hsp70 and Hsp60 chaperone machines

4 August 2017

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Protein folding in the cytosol: chaperonin-dependent and -independent mechanisms

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Molecular chaperones in cellular protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

HSP100/Clp proteins: a common mechanism explains diverse functions

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Molecular chaperones: towards a characterization of the heat-shock protein 70 family.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

SSC1, a member of the 70-kDa heat shock protein multigene family of Saccharomyces cerevisiae, is essential for growth

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

The mitochondrial protein import machinery. Role of ATP in dissociation of the Hsp70.Mim44 complex

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Molecular basis for interactions of the DnaK chaperone with substrates.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Polypeptides traverse the mitochondrial envelope in an extended state

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

The Structure of Precursor Proteins during Import into Mitochondria

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

The dimensions of the protein import channels in the outer and inner mitochondrial membranes

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Genetic and biochemical dissection of the mitochondrial protein-import machinery

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

A precursor protein partly translocated into yeast mitochondria is bound to a 70 kd mitochondrial stress protein.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

A dual role for mitochondrial heat shock protein 70 in membrane translocation of preproteins

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Membrane potential-driven protein import into mitochondria. The sorting sequence of cytochrome b(2) modulates the deltapsi-dependence of translocation of the matrix-targeting sequence

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Protein import into mitochondria: the requirement for external ATP is precursor-specific whereas intramitochondrial ATP is universally needed for translocation into the matrix

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Presequence and mature part of preproteins strongly influence the dependence of mitochondrial protein import on heat shock protein 70 in the matrix

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

The requirement of matrix ATP for the import of precursor proteins into the mitochondrial matrix and intermembrane space.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Multiple interactions of components mediating preprotein translocation across the inner mitochondrial membrane

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

A mitochondrial homolog of bacterial GrpE interacts with mitochondrial hsp70 and is essential for viability

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Yge1p, a eukaryotic Grp-E homolog, is localized in the mitochondrial matrix and interacts with mitochondrial Hsp70

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Mge1 functions as a nucleotide release factor for Ssc1, a mitochondrial Hsp70 of Saccharomyces cerevisiae

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Role of mitochondrial GrpE and phosphate in the ATPase cycle of matrix Hsp70.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Mitochondrial GrpE modulates the function of matrix Hsp70 in translocation and maturation of preproteins

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

A role for a eukaryotic GrpE-related protein, Mge1p, in protein translocation

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

The role of the GrpE homologue, Mge1p, in mediating protein import and protein folding in mitochondria.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Mitochondrial GrpE is present in a complex with hsp70 and preproteins in transit across membranes

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Identification of a 45-kDa protein at the protein import site of the yeast mitochondrial inner membrane

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

The essential yeast protein MIM44 (encoded by MPI1) is involved in an early step of preprotein translocation across the mitochondrial inner membrane.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Domain structure and lipid interaction of recombinant yeast Tim44

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Mitochondrial protein import: biochemical and genetic evidence for interaction of matrix hsp70 and the inner membrane protein MIM44

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Dynamic interaction between Isp45 and mitochondrial hsp70 in the protein import system of the yeast mitochondrial inner membrane

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Mitochondrial Hsp70/MIM44 complex facilitates protein import

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Interaction between BiP and Sec63p is required for the completion of protein translocation into the ER of Saccharomyces cerevisiae

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

The mitochondrial protein import motor: dissociation of mitochondrial hsp70 from its membrane anchor requires ATP binding rather than ATP hydrolysis

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Differential requirement for the mitochondrial Hsp70-Tim44 complex in unfolding and translocation of preproteins.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Mitochondrial protein import motor: the ATPase domain of matrix Hsp70 is crucial for binding to Tim44, while the peptide binding domain and the carboxy-terminal segment play a stimulatory role

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

The Hsp70 peptide-binding domain determines the interaction of the ATPase domain with Tim44 in mitochondria

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Separation of structural and dynamic functions of the mitochondrial translocase: Tim44 is crucial for the inner membrane import sites in translocation of tightly folded domains, but not of loosely folded preproteins

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

What drives the translocation of proteins?

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Modular structure of the TIM23 preprotein translocase of mitochondria

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Protein translocation into mitochondria: the role of TIM complexes

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Mitochondrial import driving forces: enhanced trapping by matrix Hsp70 stimulates translocation and reduces the membrane potential dependence of loosely folded preproteins

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Can Hsp70 proteins act as force-generating motors?

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Protein sorting. Pulling in the proteins

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Recognition of preproteins by the isolated TOM complex of mitochondria

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Effect of the protein import machinery at the mitochondrial surface on precursor stability

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Import of cytochrome b2 to the mitochondrial intermembrane space: the tightly folded heme-binding domain makes import dependent upon matrix ATP.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Unfolding of preproteins upon import into mitochondria

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Mitochondria Unfold Precursor Proteins by Unraveling Them From Their N-termini

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

The mitochondrial Hsp70-dependent import system actively unfolds preproteins and shortens the lag phase of translocation

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Active unfolding of precursor proteins during mitochondrial protein import

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

The protein import motor of mitochondria: unfolding and trapping of preproteins are distinct and separable functions of matrix Hsp70

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Protein unfolding by mitochondria. The Hsp70 import motor

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Mitochondrial heat shock protein 70, a molecular chaperone for proteins encoded by mitochondrial DNA.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Mdj2p, a novel DnaJ homolog in the mitochondrial inner membrane of the yeast Saccharomyces cerevisiae

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Role of the mitochondrial DnaJ homologue, Mdj1p, in the prevention of heat-induced protein aggregation.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Sequential action of two hsp70 complexes during protein import into mitochondria

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Two distinct mechanisms operate in the reactivation of heat-denatured proteins by the mitochondrial Hsp70/Mdj1p/Yge1p chaperone system

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Dual role of the mitochondrial chaperone Mdj1p in inheritance of mitochondrial DNA in yeast

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Ecm10, a novel hsp70 homolog in the mitochondrial matrix of the yeast Saccharomyces cerevisiae

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

The cold sensitivity of a mutant of Saccharomyces cerevisiae lacking a mitochondrial heat shock protein 70 is suppressed by loss of mitochondrial DNA.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron homeostasis

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

The mitochondrial proteins Ssq1 and Jac1 are required for the assembly of iron sulfur clusters in mitochondria

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Biogenesis of iron-sulfur proteins in eukaryotes: a novel task of mitochondria that is inherited from bacteria

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Role of the mitochondrial Hsp70s, Ssc1 and Ssq1, in the maturation of Yfh1

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

The two mitochondrial heat shock proteins 70, Ssc1 and Ssq1, compete for the cochaperone Mge1.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Suppressors of superoxide dismutase (SOD1) deficiency in Saccharomyces cerevisiae. Identification of proteins predicted to mediate iron-sulfur cluster assembly

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Jac1, a mitochondrial J-type chaperone, is involved in the biogenesis of Fe/S clusters in Saccharomyces cerevisiae

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

J-domain protein, Jac1p, of yeast mitochondria required for iron homeostasis and activity of Fe-S cluster proteins

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Molecular chaperones and mitochondrial protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Structure and function in GroEL-mediated protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Identification of a groES-like chaperonin in mitochondria that facilitates protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Cloning and disruption of the gene encoding yeast mitochondrial chaperonin 10, the homolog of E. coli groES.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Putting a lid on protein folding: structure and function of the co-chaperonin, GroES.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Directionality of polypeptide transfer in the mitochondrial pathway of chaperone-mediated protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Cyclophilin catalyzes protein folding in yeast mitochondria

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

The chaperonin cycle cannot substitute for prolyl isomerase activity, but GroEL alone promotes productive folding of a cyclophilin-sensitive substrate to a cyclophilin-resistant form

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Molecular chaperones. Resurrection or destruction?

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Heat-shock protein 104 expression is sufficient for thermotolerance in yeast

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Protein disaggregation mediated by heat-shock protein Hsp104.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

The mitochondrial ClpB homolog Hsp78 cooperates with matrix Hsp70 in maintenance of mitochondrial function

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

Mcx1p, a ClpX homologue in mitochondria of Saccharomyces cerevisiae

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

A human homologue of Escherichia coli ClpP caseinolytic protease: recombinant expression, intracellular processing and subcellular localization

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

AAA proteases: cellular machines for degrading membrane proteins

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4889%2802%2900264-1

7 January 2021

10.1016/S0167-4889(02)00264-1

Identifiers

DOI

1 reference

4 August 2017

1 reference

PubMed ID

12191768