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Molecular Membrane Biology|June 15, 2012
Conformational changes in NhaA Na+/H+ antiporterLena Kozachkov, Etana PadanProceedings of the National Academy of Sciences of the United States of America|August 30, 2011
Site-directed tryptophan fluorescence reveals two essential conformational changes in the Na+/H+ antiporter NhaALena Kozachkov, Etana PadanBiochemistry|February 8, 2007
Functional and structural interactions of the transmembrane domain X of NhaA, Na+/H+ antiporter of Escherichia coli, at physiological pHLena Kozachkov, Katia Herz, Etana PadanBiochemistry|November 8, 2012
The unwound portion dividing helix IV of NhaA undergoes a conformational change at physiological pH and lines the cation passageAbraham Rimon, Lena Kozachkov-Magrisso, Etana PadanThe Journal of Experimental Biology|May 19, 2009
NhaA crystal structure: functional-structural insightsEtana Padan, Lena Kozachkov, Katia Herz, et al.The Journal of Biological Chemistry|November 20, 2009
Transmembrane segment II of NhaA Na+/H+ antiporter lines the cation passage, and Asp65 is critical for pH activation of the antiporterKatia Herz, Abraham Rimon, Elena Olkhova, et al.Proteins|March 11, 2009
Combined computational and biochemical study reveals the importance of electrostatic interactions between the "pH sensor" and the cation binding site of the sodium/proton antiporter NhaA of Escherichia coliElena Olkhova, Lena Kozachkov, Etana Padan, et al.Biochemistry|January 10, 2002
Trans membrane domain IV is involved in ion transport activity and pH regulation of the NhaA-Na(+)/H(+) antiporter of Escherichia coliLivnat Galili, Andrea Rothman, Lena Kozachkov, et al.The Journal of Biological Chemistry|August 24, 2012
Revealing the ligand binding site of NhaA Na+/H+ antiporter and its pH dependenceMichal Maes, Abraham Rimon, Lena Kozachkov-Magrisso, et al.Pageof 1