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PUBMED FOR HANDHELDS

Journal Abstract Search


126 related items for PubMed ID: 2872219

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  • 2. Regulation of the synthesis and hydrolysis of ATP by mitochondrial ATPase. Role of the natural ATPase inhibitor protein.
    Tuena de Gómez-Puyou MT, Muller U, Dreyfus G, Ayala G, Gómez-Puyou A.
    J Biol Chem; 1983 Nov 25; 258(22):13680-4. PubMed ID: 6227615
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  • 7. Catalytic hydrolysis and synthesis of adenosine 5'-triphosphate by stereoisomers of covalently labeled F1-adenosinetriphosphatase and reconstituted submitochondrial particles.
    Wang JH, Cesana J, Wu JC.
    Biochemistry; 1987 Aug 25; 26(17):5527-33. PubMed ID: 2890376
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  • 8. Inhibitory chemical modifications of F1-ATPase: effects on the kinetics of adenosine 5'-triphosphate synthesis and hydrolysis in reconstituted systems.
    Matsuno-Yagi A, Hatefi Y.
    Biochemistry; 1984 Jul 17; 23(15):3508-14. PubMed ID: 6235851
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  • 9. Structural and functional differences in H+-ATPases with native and reconstituted inhibitor protein.
    Valdés AM, Dreyfus G.
    Biochem Int; 1987 Aug 17; 15(2):459-66. PubMed ID: 2893614
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  • 16. Fate of nucleotides bound to reconstituted Fo-F1 during adenosine 5'-triphosphate synthesis activation or hydrolysis: role of protein inhibitor and hysteretic inhibition.
    Penin F, Di Pietro A, Godinot C, Gautheron DC.
    Biochemistry; 1988 Dec 13; 27(25):8969-74. PubMed ID: 2906804
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  • 17. Cation requirement for the reconstitution of oligomycin-sensitive ATPase by means of soluble F1-ATPase and F1-depleted submitochondrial particles.
    Sandri G, Suranyi E, Eriksson LE, Westman J, Ernster L.
    Biochim Biophys Acta; 1983 Apr 22; 723(1):1-6. PubMed ID: 6219697
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  • 19. Regulation of the synthesis and hydrolysis of ATP by mitochondrial ATPase. Role of Mg2+.
    Gómez-Puyou A, Ayala G, Muller U, Tuena de Gómez-Puyou M.
    J Biol Chem; 1983 Nov 25; 258(22):13673-9. PubMed ID: 6227614
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  • 20. Kinetic analysis of proton translocation catalyzed by F0F1 ATPase.
    Muneyuki E, Hirata H.
    FEBS Lett; 1988 Jul 18; 234(2):455-8. PubMed ID: 2899034
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