The crossing of two unwound transmembrane regions that is the hallmark of the NhaA structural fold is critical for antiporter activity von Rimon, Abraham, Amartely, Hadar, Padan, Etana

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Cardiolipin is an Optimal Phospholipid for the Assembly, Stability, and Proper Functionality of the Dimeric Form of NhaA Na+/H+ Antiporter von Rimon, Abraham, Mondal, Ramakanta, Friedler, Assaf, Padan, Etana

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Broad phylogenetic analysis of cation/proton antiporters reveals transport determinants von Masrati, Gal, Dwivedi, Manish, Rimon, Abraham, Gluck-Margolin, Yael, Kessel, Amit, Ashkenazy, Haim, Mayrose, Itay, Padan, Etana, Ben-Tal, Nir

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Structure of a Na + /H + antiporter and insights into mechanism of action and regulation by pH von Hunte, Carola, Venturi, Miro, Rimon, Abraham, Michel, Hartmut, Padan, Etana, Screpanti, Emanuela

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

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Monomers of the NhaA Na+/H+ Antiporter of Escherichia coli Are Fully Functional yet Dimers Are Beneficial under Extreme Stress Conditions at Alkaline pH in the Presence of Na+ or L... von Rimon, Abraham, Tzubery, Tzvi, Padan, Etana

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NhaA antiporter functions using 10 helices, and an additional 2 contribute to assembly/stability von Padan, Etana, Danieli, Tsafi, Keren, Yael, Alkoby, Dudu, Masrati, Gal, Haliloglu, Turkan, Ben-Tal, Nir, Rimon, Abraham

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NhaA Na+/H+ antiporter mutants that hardly react to the membrane potential von Alkoby, Dudu, Rimon, Abraham, Budak, Maral, Burdak, Maral, Patino-Ruiz, Miyer, Călinescu, Octavian, Fendler, Klaus, Padan, Etana

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Transport Mechanism and pH Regulation of the Na+/H+ Antiporter NhaA from Escherichia coli von Mager, Thomas, Rimon, Abraham, Padan, Etana, Fendler, Klaus

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Mutation E252C Increases Drastically the Km Value for Na+ and Causes an Alkaline Shift of the pH Dependence of NhaA Na+/H+ Antiporter of Escherichia coli von Tzubery, Tzvi, Rimon, Abraham, Padan, Etana

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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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Transport mechanism and pH regulation of the Na+/H+ antiporter NhaA from Escherichia coli: an electrophysiological study von Mager, Thomas, Rimon, Abraham, Padan, Etana, Fendler, Klaus

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Asp133 Residue in NhaA Na+/H+ Antiporter Is Required for Stability Cation Binding and Transport von Rimon, Abraham, Dwivedi, Manish, Friedler, Assaf, 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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An angular motion of a conserved four-helix bundle facilitates alternating access transport in the TtNapA and EcNhaA transporters von Masrati, Gal, Mondal, Ramakanta, Rimon, Abraham, Kessel, Amit, Padan, Etana, Lindahl, Erik, Ben-Tal, Nir

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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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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 von Rimon, Abraham, Gerchman, Yoram, Kariv, Zehavit, Padan, Etana

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Using Phylogeny to Decipher Electrogenicity in Cation/Proton Antiporters von Masrati, Gal, Dwivedi, Manish, Rimon, Abraham, Gluck-Margolin, Yael, Kessel, Amit, Ashkenazy, Haim, Mayrose, Itay, Padan, Etana, Ben-Tal, Nir

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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 von Tzubery, Tzvi, Rimon, Abraham, Padan, Etana

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β-Sheet-dependent Dimerization Is Essential for the Stability of NhaA Na+/H+ Antiporter von Herz, Katia, Rimon, Abraham, Jeschke, Gunnar, Padan, Etana

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