These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Journal Abstract Search

126 related items for PubMed ID: 2904148

  • 1. Inhibition of H+-transporting ATPase by formation of a tight nucleoside diphosphate-fluoroaluminate complex at the catalytic site.
    Lunardi J, Dupuis A, Garin J, Issartel JP, Michel L, Chabre M, Vignais PV.
    Proc Natl Acad Sci U S A; 1988 Dec; 85(23):8958-62. PubMed ID: 2904148
    [Abstract] [Full Text] [Related]

  • 2. Photolabeling of mitochondrial F1-H+ATPase by 2-azido[3H]ADP and 8-azido[3H]ADP entrapped as fluorometal complexes into the catalytic sites of the enzyme.
    Garin J, Vinçon M, Gagnon J, Vignais P.
    Biochemistry; 1994 Mar 29; 33(12):3772-7. PubMed ID: 8142378
    [Abstract] [Full Text] [Related]

  • 3. Fluoroaluminate complexes are bifunctional analogues of phosphate in sarcoplasmic reticulum Ca(2+)-ATPase.
    Troullier A, Girardet JL, Dupont Y.
    J Biol Chem; 1992 Nov 15; 267(32):22821-9. PubMed ID: 1429630
    [Abstract] [Full Text] [Related]

  • 4.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 5. Fluoroaluminum and fluoroberyllium nucleoside diphosphate complexes as probes of the enzymatic mechanism of the mitochondrial F1-ATPase.
    Issartel JP, Dupuis A, Lunardi J, Vignais PV.
    Biochemistry; 1991 May 14; 30(19):4726-33. PubMed ID: 1827593
    [Abstract] [Full Text] [Related]

  • 6.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 7. ADP-fluoroaluminate complexes are formed cooperatively at two catalytic sites of wild-type and mutant alpha3beta3gamma subcomplexes of the F1-ATPase from the thermophilic Bacillus PS3.
    Dou C, Grodsky NB, Matsui T, Yoshida M, Allison WS.
    Biochemistry; 1997 Mar 25; 36(12):3719-27. PubMed ID: 9132025
    [Abstract] [Full Text] [Related]

  • 8. Use of ADP analogs for functional and structural analysis of F1-ATPase.
    Schäfer G, Lücken U, Lübben M.
    Methods Enzymol; 1986 Mar 25; 126():682-712. PubMed ID: 2908477
    [No Abstract] [Full Text] [Related]

  • 9. Mutations in the nucleotide binding domain of the alpha subunits of the F1-ATPase from thermophilic Bacillus PS3 that affect cross-talk between nucleotide binding sites.
    Grodsky NB, Dou C, Allison WS.
    Biochemistry; 1998 Jan 27; 37(4):1007-14. PubMed ID: 9454591
    [Abstract] [Full Text] [Related]

  • 10. Interaction of Mg2+ with F0.F1 mitochondrial ATPase as related to its slow active/inactive transition.
    Bulygin VV, Vinogradov AD.
    Biochem J; 1991 May 15; 276 ( Pt 1)(Pt 1):149-56. PubMed ID: 1828147
    [Abstract] [Full Text] [Related]

  • 11. Kinetic mechanism of mitochondrial adenosine triphosphatase. Inhibition by azide and activation by sulphite.
    Vasilyeva EA, Minkov IB, Fitin AF, Vinogradov AD.
    Biochem J; 1982 Jan 15; 202(1):15-23. PubMed ID: 6211171
    [Abstract] [Full Text] [Related]

  • 12. Kinetic mechanism of ATP synthesis catalyzed by mitochondrial Fo x F1-ATPase.
    Galkin MA, Syroeshkin AV.
    Biochemistry (Mosc); 1999 Oct 15; 64(10):1176-85. PubMed ID: 10561566
    [Abstract] [Full Text] [Related]

  • 13.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 14. Kinetic mechanism of Fo x F1 mitochondrial ATPase: Mg2+ requirement for Mg x ATP hydrolysis.
    Syroeshkin AV, Galkin MA, Sedlov AV, Vinogradov AD.
    Biochemistry (Mosc); 1999 Oct 15; 64(10):1128-37. PubMed ID: 10561559
    [Abstract] [Full Text] [Related]

  • 15.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 16. The ADP that binds tightly to nucleotide-depleted mitochondrial F1-ATPase and inhibits catalysis is bound at a catalytic site.
    Milgrom YM, Boyer PD.
    Biochim Biophys Acta; 1990 Oct 24; 1020(1):43-8. PubMed ID: 2145975
    [Abstract] [Full Text] [Related]

  • 17. Inhibitory effect of NaN3 on the F0F1 ATPase of submitochondrial particles as related to nucleotide binding.
    Muneyuki E, Makino M, Kamata H, Kagawa Y, Yoshida M, Hirata H.
    Biochim Biophys Acta; 1993 Aug 16; 1144(1):62-8. PubMed ID: 8347662
    [Abstract] [Full Text] [Related]

  • 18. Kinetic mechanism of mitochondrial adenosine triphosphatase. ADP-specific inhibition as revealed by the steady-state kinetics.
    Vasilyeva EA, Minkov IB, Fitin AF, Vinogradov AD.
    Biochem J; 1982 Jan 15; 202(1):9-14. PubMed ID: 6211173
    [Abstract] [Full Text] [Related]

  • 19. Pre-steady-state studies of the adenosine triphosphatase activity of coupled submitochondrial particles. Regulation by ADP.
    Martins OB, Tuena de Gómez-Puyou M, Gómez-Puyou A.
    Biochemistry; 1988 Sep 20; 27(19):7552-8. PubMed ID: 2974725
    [Abstract] [Full Text] [Related]

  • 20.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

    Page: [Next] [New Search]
    of 7.