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Journal Abstract Search

89 related items for PubMed ID: 6319139

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  • 4. Topological and functional aspects of the proton conductor, F0, of the Escherichia coli ATP-synthase.
    Schairer HU, Hoppe J, Sebald W, Friedl P.
    Biosci Rep; 1982 Aug; 2(8):631-9. PubMed ID: 6291669
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  • 5. Modification of subunit b of the F0 complex from Escherichia coli ATP synthase by a hydrophobic maleimide and its effects on F0 functions.
    Schneider E, Altendorf K.
    Eur J Biochem; 1985 Nov 15; 153(1):105-9. PubMed ID: 2866095
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  • 6. Cross-linking and labeling of the Escherichia coli F1F0-ATP synthase reveal a compact hydrophilic portion of F0 close to an F1 catalytic subunit.
    Aris JP, Simoni RD.
    J Biol Chem; 1983 Dec 10; 258(23):14599-609. PubMed ID: 6315730
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  • 7. The dicyclohexylcarbodiimide-binding protein c of ATP synthase from Escherichia coli is not sufficient to express an efficient H+ conduction.
    Friedl P, Bienhaus G, Hoppe J, Schairer HU.
    Proc Natl Acad Sci U S A; 1981 Nov 10; 78(11):6643-6. PubMed ID: 6273880
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  • 8. Reconstitution of mitochondrial oligomycin and dicyclohexylcarbodiimide-sensitive ATPase.
    Glaser E, Norling B, Ernster L.
    Eur J Biochem; 1980 Sep 10; 110(1):225-35. PubMed ID: 6108210
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  • 9. F0 of Escherichia coli ATP-synthase containing mutant and wild-type carbodiimide-binging proteins is impaired in H+ -conduction.
    Friedl P, Friedl C, Schairer HU.
    FEBS Lett; 1980 Oct 06; 119(2):254-6. PubMed ID: 6253323
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  • 10. A mutant ATP synthetase of Escherichia coli with an altered sensitivity to N,N' -dicyclohexylcarbodiimide: characterization in native membranes and reconstituted proteoliposomes.
    Friedl P, Schmid BI, Schairer HU.
    Eur J Biochem; 1977 Mar 01; 73(2):461-8. PubMed ID: 14831
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  • 12. The isolated F0 of Escherichia coli aTP-synthase is reconstitutively active in H+-conduction and ATP-dependent energy-transduction.
    Friedl P, Schairer HU.
    FEBS Lett; 1981 Jun 15; 128(2):261-4. PubMed ID: 6266871
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  • 13. F0 complex of the Escherichia coli ATP synthase. Not all monomers of the subunit c oligomer are involved in F1 interaction.
    Birkenhäger R, Greie JC, Altendorf K, Deckers-Hebestreit G.
    Eur J Biochem; 1999 Sep 15; 264(2):385-96. PubMed ID: 10491083
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  • 14. Modification of the F0 portion of the H+-translocating adenosinetriphosphatase complex of Escherichia coli by the water-soluble carbodiimide 1-ethyl-3-[3-(dimethylamino)propyl]carbodiimide and effect on the proton channeling function.
    Lötscher HR, deJong C, Capaldi RA.
    Biochemistry; 1984 Aug 28; 23(18):4128-34. PubMed ID: 6237682
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  • 15. The b and delta subunits of the Escherichia coli ATP synthase interact via residues in their C-terminal regions.
    McLachlin DT, Bestard JA, Dunn SD.
    J Biol Chem; 1998 Jun 12; 273(24):15162-8. PubMed ID: 9614129
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  • 19. Oligomycin sensitivity conferring protein of mitochondrial ATP synthase: deletions in the N-terminal end cause defects in interactions with F1, while deletions in the C-terminal end cause defects in interactions with F0.
    Joshi S, Cao GJ, Nath C, Shah J.
    Biochemistry; 1996 Sep 17; 35(37):12094-103. PubMed ID: 8810915
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