Site-directed tryptophan fluorescence reveals two essential conformational changes in the Na⁺ /H⁺ antiporter NhaA von Kozachkov, Lena, Padan, Etana

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NhaA crystal structure: functional-structural insights von Padan, Etana, Kozachkov, Lena, Herz, Katia, Rimon, Abraham

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Transmembrane Segment II of NhaA Na+/H+ Antiporter Lines the Cation Passage, and Asp65 Is Critical for pH Activation of the Antiporter von Herz, Katia, Rimon, Abraham, Olkhova, Elena, Kozachkov, Lena, Padan, Etana

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Trans Membrane Domain IV Is Involved in Ion Transport Activity and pH Regulation of the NhaA-Na+/H+ Antiporter of Escherichia coli von Galili, Livnat, Rothman, Andrea, Kozachkov, Lena, Rimon, Abraham, Padan, Etana

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Conformational changes in NhaA Na+/H+ antiporter von Kozachkov, Lena, Padan, Etana

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Functional and Structural Interactions of the Transmembrane Domain X of NhaA, Na+/H+ Antiporter of Escherichia coli, at Physiological pH von Kozachkov, Lena, Herz, Katia, Padan, Etana

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Combined computational and biochemical study reveals the importance of electrostatic interactions between the "pH sensor" and the cation binding site of the sodium/proton antiporte... von Olkhova, Elena, Kozachkov, Lena, Padan, Etana, Michel, Hartmut

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The Unwound Portion Dividing Helix IV of NhaA Undergoes a Conformational Change at Physiological pH and Lines the Cation Passage von Rimon, Abraham, Kozachkov-Magrisso, Lena, Padan, Etana

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Revealing the Ligand Binding Site of NhaA Na+/H+ Antiporter and Its pH Dependence von Maes, Michal, Rimon, Abraham, Kozachkov-Magrisso, Lena, Friedler, Assaf, Padan, Etana

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