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Journal Abstract Search

256 related items for PubMed ID: 19923224

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  • 4. Functional and structural interactions of the transmembrane domain X of NhaA, Na+/H+ antiporter of Escherichia coli, at physiological pH.
    Kozachkov L, Herz K, Padan E.
    Biochemistry; 2007 Mar 06; 46(9):2419-30. PubMed ID: 17284054
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  • 6. The fourth transmembrane domain of the Helicobacter pylori Na+/H+ antiporter NhaA faces a water-filled channel required for ion transport.
    Kuwabara N, Inoue H, Tsuboi Y, Nakamura N, Kanazawa H.
    J Biol Chem; 2004 Sep 24; 279(39):40567-75. PubMed ID: 15263004
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  • 7. Revealing the ligand binding site of NhaA Na+/H+ antiporter and its pH dependence.
    Maes M, Rimon A, Kozachkov-Magrisso L, Friedler A, Padan E.
    J Biol Chem; 2012 Nov 02; 287(45):38150-7. PubMed ID: 22915592
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  • 8. Trans membrane domain IV is involved in ion transport activity and pH regulation of the NhaA-Na(+)/H(+) antiporter of Escherichia coli.
    Galili L, Rothman A, Kozachkov L, Rimon A, Padan E.
    Biochemistry; 2002 Jan 15; 41(2):609-17. PubMed ID: 11781101
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  • 13. NhaA Na+/H+ antiporter mutants that hardly react to the membrane potential.
    Alkoby D, Rimon A, Budak M, Patino-Ruiz M, Călinescu O, Fendler K, Padan E.
    PLoS One; 2014 Jan 15; 9(4):e93200. PubMed ID: 24699187
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  • 15. Replacements of histidine 226 of NhaA-Na+/H+ antiporter of Escherichia coli. Cysteine (H226C) or serine (H226S) retain both normal activity and pH sensitivity, aspartate (H226D) shifts the pH profile toward basic pH, and alanine (H226A) inactivates the carrier at all pH values.
    Rimon A, Gerchman Y, Olami Y, Schuldiner S, Padan E.
    J Biol Chem; 1995 Nov 10; 270(45):26813-7. PubMed ID: 7592922
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  • 16. A point mutation (G338S) and its suppressor mutations affect both the pH response of the NhaA-Na+/H+ antiporter as well as the growth phenotype of Escherichia coli.
    Rimon A, Gerchman Y, Kariv Z, Padan E.
    J Biol Chem; 1998 Oct 09; 273(41):26470-6. PubMed ID: 9756882
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  • 17. Essential aspartic acid residues, Asp-133, Asp-163 and Asp-164, in the transmembrane helices of a Na+/H+ antiporter (NhaA) from Escherichia coli.
    Inoue H, Noumi T, Tsuchiya T, Kanazawa H.
    FEBS Lett; 1995 Apr 24; 363(3):264-8. PubMed ID: 7737413
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