Mitochondrial protein import: molecular basis of the ATP-dependent interaction of MtHsp70 with Tim44. (Q34104076)

31 July 2017

Mitochondrial protein import: molecular basis of the ATP-dependent interaction of MtHsp70 with Tim44. (English)

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31 July 2017

Fernando Moro

1

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31 July 2017

Koji Okamoto

2

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31 July 2017

Mariel Donzeau

3

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31 July 2017

Walter Neupert

4

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31 July 2017

Michael Brunner

5

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31 July 2017

language of work or name

English

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publication date

30 November 2001

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Journal of Biological Chemistry

31 July 2017

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31 July 2017

277

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31 July 2017

9

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31 July 2017

6874-6880

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

31 July 2017

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107935200

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

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M107935200

Mitochondrial Hsp70/MIM44 complex facilitates protein import

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M107935200

The TIM17.23 preprotein translocase of mitochondria: composition and function in protein transport into the matrix

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M107935200

Protein translocation into mitochondria: the role of TIM complexes

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M107935200

The MIM complex mediates preprotein translocation across the mitochondrial inner membrane and couples it to the mt-Hsp70/ATP driving system

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107935200

The Hsp70 and Hsp60 chaperone machines

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M107935200

Structural analysis of substrate binding by the molecular chaperone DnaK

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M107935200

The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107935200

Molecular chaperones in cellular protein folding

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M107935200

Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107935200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107935200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107935200

Mitochondrial Hsp70 Ssc1: role in protein folding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107935200

Translocation arrest by reversible folding of a precursor protein imported into mitochondria. A means to quantitate translocation contact sites

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107935200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107935200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107935200

The sugar kinase/heat shock protein 70/actin superfamily: implications of conserved structure for mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107935200

Peptide-binding specificity of the molecular chaperone BiP

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107935200

Multistep mechanism of substrate binding determines chaperone activity of Hsp70

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M107935200

Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107935200

ATP hydrolysis is required for the DnaJ-dependent activation of DnaK chaperone for binding to both native and denatured protein substrates

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107935200

The role of ATP in the functional cycle of the DnaK chaperone system

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107935200

Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107935200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107935200

The mitochondrial hsp70 chaperone system. Effect of adenine nucleotides, peptide substrate, and mGrpE on the oligomeric state of mhsp70

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M107935200

21 January 2018

Identifiers

DOI

10.1074/JBC.M107935200

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31 July 2017

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