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Binding of a tightly folded artificial mitochondrial precursor protein to the mitochondrial outer membrane involves a lipid-mediated conformational change.
Endo T, Eilers M, Schatz G. Endo T, et al. Among authors: schatz g. J Biol Chem. 1989 Feb 15;264(5):2951-6. J Biol Chem. 1989. PMID: 2536727 Free article.
These results, and those reported in the accompanying paper (Eilers, M., Endo, T., and Schatz, G. (1989) J. Biol. Chem. 264, 2945-2950) suggest that import of this fusion protein into isolated mitochondria involves at least partial unfolding by acidic phospholipids …
These results, and those reported in the accompanying paper (Eilers, M., Endo, T., and Schatz, G. (1989) J. Biol. Chem. 264, 2 …
Adriamycin, a drug interacting with acidic phospholipids, blocks import of precursor proteins by isolated yeast mitochondria.
Eilers M, Endo T, Schatz G. Eilers M, et al. Among authors: schatz g. J Biol Chem. 1989 Feb 15;264(5):2945-50. J Biol Chem. 1989. PMID: 2644274 Free article.
Acidic phospholipids such as cardiolipin partially unfold an artificial precursor protein which consists of a mitochondrial presequence fused to mouse dihydrofolate reductase (Endo, T., and Schatz, G. (1988) EMBO J. 7, 1153-1158). We now show that import of this pre …
Acidic phospholipids such as cardiolipin partially unfold an artificial precursor protein which consists of a mitochondrial presequence fuse …
909 results