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2. Replacement of Lys-300 with a glutamine in the NhaA Na+/H+ antiporter of Escherichia coli yields a functional electrogenic transporter. Patiño-Ruiz M, Dwivedi M, Călinescu O, Karabel M, Padan E, Fendler K. J Biol Chem; 2019 Jan 04; 294(1):246-256. PubMed ID: 30409911 [Abstract] [Full Text] [Related]
3. Identification of membrane domains of the Na+/H+ antiporter (NhaA) protein from Helicobacter pylori required for ion transport and pH sensing. Tsuboi Y, Inoue H, Nakamura N, Kanazawa H. J Biol Chem; 2003 Jun 13; 278(24):21467-73. PubMed ID: 12670937 [Abstract] [Full Text] [Related]
5. Differential effects of mutations on the transport properties of the Na+/H+ antiporter NhaA from Escherichia coli. Mager T, Braner M, Kubsch B, Hatahet L, Alkoby D, Rimon A, Padan E, Fendler K. J Biol Chem; 2013 Aug 23; 288(34):24666-75. PubMed ID: 23836890 [Abstract] [Full Text] [Related]
6. Site-directed mutagenesis at the Glu78 in Ec-NhaA transporter impacting ion exchange: a biophysical study. Yadav A, Kumar D, Dwivedi M. Eur Biophys J; 2024 May 23; 53(4):193-203. PubMed ID: 38647543 [Abstract] [Full Text] [Related]
8. Structure-based functional study reveals multiple roles of transmembrane segment IX and loop VIII-IX in NhaA Na+/H+ antiporter of Escherichia coli at physiological pH. Tzubery T, Rimon A, Padan E. J Biol Chem; 2008 Jun 06; 283(23):15975-87. PubMed ID: 18387952 [Abstract] [Full Text] [Related]
9. 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 Jun 06; 9(4):e93200. PubMed ID: 24699187 [Abstract] [Full Text] [Related]
10. 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 [Abstract] [Full Text] [Related]
11. Transmembrane segment II of NhaA Na+/H+ antiporter lines the cation passage, and Asp65 is critical for pH activation of the antiporter. Herz K, Rimon A, Olkhova E, Kozachkov L, Padan E. J Biol Chem; 2010 Jan 15; 285(3):2211-20. PubMed ID: 19923224 [Abstract] [Full Text] [Related]
12. Functional role of polar amino acid residues in Na+/H+ exchangers. Wiebe CA, Dibattista ER, Fliegel L. Biochem J; 2001 Jul 01; 357(Pt 1):1-10. PubMed ID: 11415429 [Abstract] [Full Text] [Related]
13. Site-directed tryptophan fluorescence reveals two essential conformational changes in the Na+/H+ antiporter NhaA. Kozachkov L, Padan E. Proc Natl Acad Sci U S A; 2011 Sep 20; 108(38):15769-74. PubMed ID: 21873214 [Abstract] [Full Text] [Related]
14. Site-directed mutations reflecting functional and structural properties of Ec-NhaA. Dwivedi M. Biochimie; 2021 Jan 20; 180():79-89. PubMed ID: 33129932 [Abstract] [Full Text] [Related]
15. 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 [Abstract] [Full Text] [Related]
16. Crystal structure of the Na+/H+ antiporter NhaA at active pH reveals the mechanistic basis for pH sensing. Winkelmann I, Uzdavinys P, Kenney IM, Brock J, Meier PF, Wagner LM, Gabriel F, Jung S, Matsuoka R, von Ballmoos C, Beckstein O, Drew D. Nat Commun; 2022 Oct 26; 13(1):6383. PubMed ID: 36289233 [Abstract] [Full Text] [Related]
17. The crossing of two unwound transmembrane regions that is the hallmark of the NhaA structural fold is critical for antiporter activity. Rimon A, Amartely H, Padan E. Sci Rep; 2024 Mar 11; 14(1):5915. PubMed ID: 38467695 [Abstract] [Full Text] [Related]
18. 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 [Abstract] [Full Text] [Related]
19. Towards Molecular Understanding of the pH Dependence Characterizing NhaA of Which Structural Fold is Shared by Other Transporters. Mondal R, Rimon A, Masrati G, Ben-Tal N, Friedler A, Padan E. J Mol Biol; 2021 Sep 17; 433(19):167156. PubMed ID: 34273399 [Abstract] [Full Text] [Related]
20. 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 [Abstract] [Full Text] [Related] Page: [Next] [New Search]