Adriamycin, a drug interacting with acidic phospholipids, blocks import of precursor proteins by isolated yeast mitochondria.

No abstract is available for this paper.

• Publication year

  1989

• Venue

  Journal of Biological Chemistry

• Publication date

  1989-02-15

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  PMID 2644274
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Binding of a tightly folded artificial mitochondrial precursor protein to the mitochondrial outer membrane involves a lipid-mediated conformational change.

  1989cited by this paper
• Protein translocation across membranes.

  1988cited by this paper
• Unfolding and refolding of a purified precursor protein during import into isolated mitochondria.

  1988cited by this paper
• A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides

  1988cited by this paper
• Point mutations destabilizing a precursor protein enhance its post‐translational import into mitochondria.

  1988cited by this paper
• Protein unfolding and the energetics of protein translocation across biological membranes.

  1988cited by this paper
• Specific binding of mitochondrial protein precursors to liposomes containing cardiolipin.

  1988cited by this paper
• Biogenesis of mitochondria.

  1988cited by this paper
• Latent membrane perturbation activity of a mitochondrial precursor protein is exposed by unfolding.

  1988cited by this paper
• Both ATP and an energized inner membrane are required to import a purified precursor protein into mitochondria.

  1987cited by this paper
• Disruption of the outer membrane restores protein import to trypsin‐treated yeast mitochondria.

  1987cited by this paper
• Mitochondrial protein import: nucleoside triphosphates are involved in conferring import-competence to precursors.

  1987cited by this paper
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  1987cited by this paper
• A chemically synthesized pre‐sequence of an imported mitochondrial protein can form an amphiphilic helix and perturb natural and artificial phospholipid bilayers.

  1986cited by this paper
• Targeting proteins into mitochondria.

  1986cited by this paper
• Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria

  1986cited by this paper
• The first twelve amino acids (less than half of the pre‐sequence) of an imported mitochondrial protein can direct mouse cytosolic dihydrofolate reductase into the yeast mitochondrial matrix.

  1985cited by this paper
• Adriamycin as a probe for the transversal distribution of cardiolipin in the inner mitochondrial membrane.

  1985cited by this paper
• The cleavable prepiece of an imported mitochondrial protein is sufficient to direct cytosolic dihydrofolate reductase into the mitochondrial matrix

  1984cited by this paper
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  1984cited by this paper
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  1982cited by this paper
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  1982cited by this paper
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  1982cited by this paper
• Evidence of a specific complex between adriamycin and negatively-charged phospholipids.

  1980cited by this paper
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