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Journal Abstract Search

209 related items for PubMed ID: 15710614

  • 1. Role of a conserved glutamate residue in the Escherichia coli SecA ATPase mechanism.
    Zito CR, Antony E, Hunt JF, Oliver DB, Hingorani MM.
    J Biol Chem; 2005 Apr 15; 280(15):14611-9. PubMed ID: 15710614
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  • 4. Bacillus subtilis SecA ATPase exists as an antiparallel dimer in solution.
    Ding H, Hunt JF, Mukerji I, Oliver D.
    Biochemistry; 2003 Jul 29; 42(29):8729-38. PubMed ID: 12873133
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  • 5. Lysine 106 of the putative catalytic ATP-binding site of the Bacillus subtilis SecA protein is required for functional complementation of Escherichia coli secA mutants in vivo.
    Klose M, Schimz KL, van der Wolk J, Driessen AJ, Freudl R.
    J Biol Chem; 1993 Feb 25; 268(6):4504-10. PubMed ID: 8440733
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  • 7. Nucleotide and phospholipid-dependent control of PPXD and C-domain association for SecA ATPase.
    Ding H, Mukerji I, Oliver D.
    Biochemistry; 2003 Nov 25; 42(46):13468-75. PubMed ID: 14621992
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  • 10. Using a low denaturant model to explore the conformational features of translocation-active SecA.
    Maki JL, Krishnan B, Gierasch LM.
    Biochemistry; 2012 Feb 21; 51(7):1369-79. PubMed ID: 22304380
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  • 11. SecA proteins of Bacillus subtilis and Escherichia coli possess homologous amino-terminal ATP-binding domains regulating integration into the plasma membrane.
    McNicholas P, Rajapandi T, Oliver D.
    J Bacteriol; 1995 Dec 21; 177(24):7231-7. PubMed ID: 8522532
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  • 12. A large conformational change couples the ATP binding site of SecA to the SecY protein channel.
    Robson A, Booth AE, Gold VA, Clarke AR, Collinson I.
    J Mol Biol; 2007 Dec 07; 374(4):965-76. PubMed ID: 17964601
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  • 14. Cross-talk between catalytic and regulatory elements in a DEAD motor domain is essential for SecA function.
    Sianidis G, Karamanou S, Vrontou E, Boulias K, Repanas K, Kyrpides N, Politou AS, Economou A.
    EMBO J; 2001 Mar 01; 20(5):961-70. PubMed ID: 11230120
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  • 15. Nucleotide exchange from the high-affinity ATP-binding site in SecA is the rate-limiting step in the ATPase cycle of the soluble enzyme and occurs through a specialized conformational state.
    Fak JJ, Itkin A, Ciobanu DD, Lin EC, Song XJ, Chou YT, Gierasch LM, Hunt JF.
    Biochemistry; 2004 Jun 15; 43(23):7307-27. PubMed ID: 15182175
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  • 16. The bacterial ATPase SecA functions as a monomer in protein translocation.
    Or E, Boyd D, Gon S, Beckwith J, Rapoport T.
    J Biol Chem; 2005 Mar 11; 280(10):9097-105. PubMed ID: 15618215
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  • 17. In vivo studies of the role of SecA during protein export in Escherichia coli.
    Chun SY, Randall LL.
    J Bacteriol; 1994 Jul 11; 176(14):4197-203. PubMed ID: 8021205
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  • 18. Mechanism of conformational coupling in SecA: Key role of hydrogen-bonding networks and water interactions.
    Milenkovic S, Bondar AN.
    Biochim Biophys Acta; 2016 Feb 11; 1858(2):374-85. PubMed ID: 26607006
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