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Journal Abstract Search


198 related items for PubMed ID: 2858408

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  • 4. Changes in the adenine nucleotide content of beef-heart mitochondrial F1 ATPase during ATP synthesis in dimethyl sulfoxide.
    Beharry S, Bragg PD.
    Biochem Biophys Res Commun; 1992 Jan 31; 182(2):697-702. PubMed ID: 1531174
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  • 5. Significant quantities of endogenous GDP and ADP are present on catalytic sites of the F1-ATPase isolated from M. lysodeikticus in the absence of added nucleotides.
    Mileykovskaya EI, Kormer SS, Allison WS.
    Biochim Biophys Acta; 1992 Mar 13; 1099(3):219-25. PubMed ID: 1532327
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  • 6. Dissociation of phosphate from beef heart mitochondrial F1-ATPase. Effect of adenine nucleotides.
    Beharry S, Gresser MJ.
    J Biol Chem; 1987 Aug 05; 262(22):10630-7. PubMed ID: 2886500
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  • 7. Catalytic properties of the Escherichia coli proton adenosinetriphosphatase: evidence that nucleotide bound at noncatalytic sites is not involved in regulation of oxidative phosphorylation.
    Wise JG, Senior AE.
    Biochemistry; 1985 Nov 19; 24(24):6949-54. PubMed ID: 2866799
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  • 8. Further investigations on the inorganic phosphate binding site of beef heart mitochondrial F1-ATPase.
    Pougeois R, Lauquin GJ.
    Biochemistry; 1985 Feb 12; 24(4):1020-4. PubMed ID: 2859884
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  • 9. Bound adenosine 5'-triphosphate formation, bound adenosine 5'-diphosphate and inorganic phosphate retention, and inorganic phosphate oxygen exchange by chloroplast adenosinetriphosphatase in the presence of Ca2+ or Mg2+.
    Wu D, Boyer PD.
    Biochemistry; 1986 Jun 03; 25(11):3390-6. PubMed ID: 2873834
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  • 10. Adenine nucleotide binding at a noncatalytic site of mitochondrial F1-ATPase accelerates a Mg(2+)- and ADP-dependent inactivation during ATP hydrolysis.
    Murataliev MB.
    Biochemistry; 1992 Dec 29; 31(51):12885-92. PubMed ID: 1463756
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  • 11. The effect of depletion of nucleotide and of delta and epsilon subunits on ATP synthesis in dimethyl sulfoxide by F1-ATPase of Escherichia coli.
    Beharry S, Bragg PD.
    Biochem Biophys Res Commun; 1993 Jul 15; 194(1):483-9. PubMed ID: 8333861
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  • 12. Effect of the natural ATPase inhibitor on the binding of adenine nucleotides and inorganic phosphate to mitochondrial F1-ATPase.
    Klein G, Lunardi J, Vignais PV.
    Biochim Biophys Acta; 1981 Jul 15; 636(2):185-92. PubMed ID: 6456765
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  • 13. The mechanism of stimulation of MgATPase activity of chloroplast F1-ATPase by non-catalytic adenine-nucleotide binding. Acceleration of the ATP-dependent release of inhibitory ADP from a catalytic site.
    Murataliev MB, Boyer PD.
    Eur J Biochem; 1992 Oct 15; 209(2):681-7. PubMed ID: 1425675
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  • 14. Changes in chemical properties of mitochondrial adenosinetriphosphatase upon removal of tightly bound nucleotides.
    Tamura JK, Wang JH.
    Biochemistry; 1983 Apr 12; 22(8):1947-54. PubMed ID: 6221755
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  • 15. The bound adenine nucleotides of purified bovine mitochondrial ATP synthase.
    Beharry S, Bragg PD.
    Eur J Biochem; 1996 Aug 15; 240(1):165-72. PubMed ID: 8797850
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  • 16. Trinitrophenyl-ATP and -ADP bind to a single nucleotide site on isolated beta-subunit of Escherichia coli F1-ATPase. In vitro assembly of F1-subunits requires occupancy of the nucleotide-binding site on beta-subunit by nucleoside triphosphate.
    Rao R, Al-Shawi MK, Senior AE.
    J Biol Chem; 1988 Apr 25; 263(12):5569-73. PubMed ID: 2895769
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  • 17. Identification of the nucleotide-binding site for ATP synthesis and hydrolysis in mitochondrial soluble F1-ATPase.
    Sakamoto J.
    J Biochem; 1984 Aug 25; 96(2):475-81. PubMed ID: 6238951
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  • 18. 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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  • 19. Does pyrophosphate bind to the catalytic sites of mitochondrial F1-ATPase?
    Peinnequin A, Issartel JP, Lunardi J, Vignais PV.
    Biochemistry; 1992 Feb 25; 31(7):2088-92. PubMed ID: 1311204
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  • 20. Isolated noncatalytic and catalytic subunits of F1-ATPase exhibit similar, albeit not identical, energetic strategies for recognizing adenosine nucleotides.
    Salcedo G, Cano-Sánchez P, de Gómez-Puyou MT, Velázquez-Campoy A, García-Hernández E.
    Biochim Biophys Acta; 2014 Jan 25; 1837(1):44-50. PubMed ID: 23994287
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