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212 related items for PubMed ID: 1457596
1. [Membrane ATPase of Vibrio alginolyticus. Ion transport activity and homology with F0F1-ATPase from E. coli]. Dmitriev OIu, Dann S, Krasnosel'skaia IA, Papa S, Skulachev VP. Biokhimiia; 1992 Oct; 57(10):1499-507. PubMed ID: 1457596 [Abstract] [Full Text] [Related]
2. F0F1-ATPase from Vibrio alginolyticus. Subunit composition and proton pumping activity. Dmitriev OYu, Krasnoselskaya IA, Papa S, Skulachev VP. FEBS Lett; 1991 Jun 24; 284(2):273-6. PubMed ID: 1647986 [Abstract] [Full Text] [Related]
3. Mode of interaction of the single a subunit with the multimeric c subunits during the translocation of the coupling ions by F1F0 ATPases. Kaim G, Matthey U, Dimroth P. EMBO J; 1998 Feb 02; 17(3):688-95. PubMed ID: 9450994 [Abstract] [Full Text] [Related]
4. The effect of F0 inhibitors on the Vibrio alginolyticus membrane ATPase. Capozza G, Dmitriev OYu, Krasnoselskaya IA, Papa S, Skulachev VP. FEBS Lett; 1991 Mar 25; 280(2):274-6. PubMed ID: 1826482 [Abstract] [Full Text] [Related]
5. A double mutation in subunit c of the Na(+)-specific F1F0-ATPase of Propionigenium modestum results in a switch from Na+ to H(+)-coupled ATP synthesis in the Escherichia coli host cells. Kaim G, Dimroth P. J Mol Biol; 1995 Nov 10; 253(5):726-38. PubMed ID: 7473747 [Abstract] [Full Text] [Related]
8. [Nature of membrane ATPase inactivation in an Escherichia coli mutant with genetically impaired ATPase]. Chetkauskaĭte AV, Planutis DL, Zimkus AZ, Akimenko VK, Grinius LL. Biokhimiia; 1980 Jul 10; 45(7):1274-83. PubMed ID: 6452179 [Abstract] [Full Text] [Related]
9. Structure and function of the Na(+)-translocating ATPase of Propionigenium modestum. Dimroth P. Acta Physiol Scand Suppl; 1992 Jul 10; 607():97-103. PubMed ID: 1449075 [Abstract] [Full Text] [Related]
11. Purification and reconstitution of the F1F0-ATP synthase from alkaliphilic Bacillus firmus OF4. Evidence that the enzyme translocates H+ but not Na+. Hicks DB, Krulwich TA. J Biol Chem; 1990 Nov 25; 265(33):20547-54. PubMed ID: 2173711 [Abstract] [Full Text] [Related]