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PUBMED FOR HANDHELDS

Journal Abstract Search

329 related items for PubMed ID: 10506126

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  • 4. Mitochondrial ATP synthase catalytic mechanism: a novel visual comparative structural approach emphasizes pivotal roles for Mg²⁺ and P-loop residues in making ATP.
    Blum DJ, Ko YH, Pedersen PL.
    Biochemistry; 2012 Feb 21; 51(7):1532-46. PubMed ID: 22243519
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  • 5. The transition-like state and Pi entrance into the catalytic a subunit of the biological engine A-ATP synthase.
    Manimekalai MS, Kumar A, Jeyakanthan J, Grüber G.
    J Mol Biol; 2011 May 13; 408(4):736-54. PubMed ID: 21396943
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  • 6. Catalytic site forms and controls in ATP synthase catalysis.
    Boyer PD.
    Biochim Biophys Acta; 2000 May 31; 1458(2-3):252-62. PubMed ID: 10838041
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  • 7. ATP synthase: a tentative structural model.
    Engelbrecht S, Junge W.
    FEBS Lett; 1997 Sep 15; 414(3):485-91. PubMed ID: 9323021
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  • 8. X-ray structure of the magnesium(II).ADP.vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 A resolution.
    Smith CA, Rayment I.
    Biochemistry; 1996 Apr 30; 35(17):5404-17. PubMed ID: 8611530
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  • 11. Crystallographic and enzymatic insights into the mechanisms of Mg-ADP inhibition in the A1 complex of the A1AO ATP synthase.
    Singh D, Grüber G.
    J Struct Biol; 2018 Jan 30; 201(1):26-35. PubMed ID: 29074108
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  • 13. Inhibitory Mg-ADP-fluoroaluminate complexes bound to catalytic sites of F(1)-ATPases: are they ground-state or transition-state analogs?
    Allison WS, Ren H, Dou C.
    J Bioenerg Biomembr; 2000 Oct 30; 32(5):531-8. PubMed ID: 15254389
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  • 15. The rotary binding change mechanism of ATP synthases.
    Cross RL.
    Biochim Biophys Acta; 2000 May 31; 1458(2-3):270-5. PubMed ID: 10838043
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  • 17. Amino Acid Residues β139, β189, and β319 Modulate ADP-Inhibition in Escherichia coli H+-FOF1-ATP Synthase.
    Lapashina AS, Shugaeva TE, Berezina KM, Kholina TD, Feniouk BA.
    Biochemistry (Mosc); 2019 Apr 31; 84(4):407-415. PubMed ID: 31228932
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