Characterization of the mitochondrial inner membrane translocase complex: the Tim23p hydrophobic domain interacts with Tim17p but not with other Tim23p molecules (Q39631205)

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scientific article published on January 1998

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English	Characterization of the mitochondrial inner membrane translocase complex: the Tim23p hydrophobic domain interacts with Tim17p but not with other Tim23p molecules	scientific article published on January 1998

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

13 September 2017

Characterization of the mitochondrial inner membrane translocase complex: the Tim23p hydrophobic domain interacts with Tim17p but not with other Tim23p molecules (English)

1 reference

Europe PubMed Central

PMC publication ID

13 September 2017

1 reference

based on heuristic

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author name string

K R Ryan

1

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Europe PubMed Central

PMC publication ID

13 September 2017

R S Leung

2

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Europe PubMed Central

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13 September 2017

R E Jensen

3

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Europe PubMed Central

PMC publication ID

13 September 2017

language of work or name

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publication date

1 January 1998

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Europe PubMed Central

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13 September 2017

Molecular and Cellular Biology

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Europe PubMed Central

PMC publication ID

13 September 2017

18

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Europe PubMed Central

PMC publication ID

13 September 2017

1

1 reference

Europe PubMed Central

PMC publication ID

13 September 2017

178-187

1 reference

Europe PubMed Central

PMC publication ID

13 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=121472

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Tim23, a protein import component of the mitochondrial inner membrane, is required for normal activity of the multiple conductance channel, MCC.

1 reference

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Role of Tim23 as voltage sensor and presequence receptor in protein import into mitochondria

1 reference

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The YTA10-12 complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria

1 reference

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Common principles of protein translocation across membranes

1 reference

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Acidic receptor domains on both sides of the outer membrane mediate translocation of precursor proteins into yeast mitochondria

1 reference

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Specific recognition of mitochondrial preproteins by the cytosolic domain of the import receptor MOM72.

1 reference

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Mitochondrial Hsp70/MIM44 complex facilitates protein import

1 reference

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SMS1, a high-copy suppressor of the yeast mas6 mutant, encodes an essential inner membrane protein required for mitochondrial protein import

1 reference

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

1 reference

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Dynamic interaction of the protein translocation systems in the inner and outer membranes of yeast mitochondria.

1 reference

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

1 reference

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Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria

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Two nuclear mutations that block mitochondrial protein import in yeast

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Disruption of the outer membrane restores protein import to trypsin-treated yeast mitochondria.

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1 reference

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MAS1, a gene essential for yeast mitochondrial assembly, encodes a subunit of the mitochondrial processing protease

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Import of proteins into yeast mitochondria: the purified matrix processing protease contains two subunits which are encoded by the nuclear MAS1 and MAS2 genes

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Disrupted yeast mitochondria can import precursor proteins directly through their inner membrane

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Protein import into yeast mitochondria is accelerated by the outer membrane protein MAS70.

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The protein import machinery of the mitochondrial inner membrane

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1 reference

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1 reference

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Identification of a mitochondrial receptor complex required for recognition and membrane insertion of precursor proteins

1 reference

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1 reference

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1 reference

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1 reference

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Mitochondrial protein import: reversible binding of the presequence at the trans side of the outer membrane drives partial translocation and unfolding

1 reference

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inferred from PubMed ID database lookup

Functional and physical interactions of components of the yeast mitochondrial inner-membrane import machinery (MIM)

1 reference

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based on heuristic

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Mitochondrial precursor proteins are imported through a hydrophilic membrane environment

1 reference

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based on heuristic

inferred from PubMed ID database lookup

13 Immunochemical identification of membrane proteins after sodium dodecyl sulfate—polyacrylamide gel electrophoresis

1 reference

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based on heuristic

inferred from PubMed ID database lookup

The cleavable prepiece of an imported mitochondrial protein is sufficient to direct cytosolic dihydrofolate reductase into the mitochondrial matrix

1 reference

https://pubmed.ncbi.nlm.nih.gov/9418865

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based on heuristic

inferred from PubMed ID database lookup

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1 reference

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inferred from PubMed ID database lookup

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10.1128/MCB.18.1.178

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Europe PubMed Central

PMC publication ID

13 September 2017

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24 November 2022

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Europe PubMed Central

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13 September 2017

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Europe PubMed Central

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13 September 2017

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