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E Padan

Showing results (61-70 of 98) with videos related to

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The Journal of Biological Chemistry|July 25, 1988
Sequencing of the gene ant which affects the Na+/H+ antiporter activity in Escherichia coliR Karpel, Y Olami, D Taglicht, et al.
Journal of Bacteriology|June 11, 1998
Altered Na+ and Li+ homeostasis in Saccharomyces cerevisiae cells expressing the bacterial cation antiporter NhaAR Ros, C Montesinos, A Rimon, et al.
The Journal of Biological Chemistry|January 17, 1997
Histidine 225, a residue of the NhaA-Na+/H+ antiporter of Escherichia coli is exposed and faces the cell exteriorY Olami, A Rimon, Y Gerchman, et al.
The Journal of Biological Chemistry|February 25, 1994
Purification and characterization of sulfide-quinone reductase, a novel enzyme driving anoxygenic photosynthesis in Oscillatoria limneticaB Arieli, Y Shahak, D Taglicht, et al.
Journal of Bacteriology|June 15, 2000
Cyanobacterial sulfide-quinone reductase: cloning and heterologous expressionM Bronstein, M Schütz, G Hauska, et al.
Biochemistry|November 9, 1982
Mechanism of lactose transport in Escherichia coli membrane vesicles: evidence for the involvement of histidine residue(s) in the response of the lac carrier to the proton electrochemical gradientM L Garcia, L Patel, E Padan, et al.
The Journal of Biological Chemistry|November 15, 1991
Expression of a sodium proton antiporter (NhaA) in Escherichia coli is induced by Na+ and Li+ ionsR Karpel, T Alon, G Glaser, et al.
Biophysical Journal|August 21, 2007
High-resolution structure of a Na+/H+ antiporter dimer obtained by pulsed electron paramagnetic resonance distance measurementsD Hilger, Y Polyhach, E Padan, et al.
The Journal of Biological Chemistry|November 10, 1995
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 valuesA Rimon, Y Gerchman, Y Olami, et al.
Biochimica Et Biophysica Acta|May 2, 1998
Topological study of Vibrio alginolyticus NhaB Na+/H+ antiporter using gene fusions in Escherichia coli cellsH Enomoto, T Unemoto, M Nishibuchi, et al.
Pageof 10

Showing results (61-70 of 98) with videos related to

Sort By:
Pageof 10
The Journal of Biological Chemistry|July 25, 1988
Sequencing of the gene ant which affects the Na+/H+ antiporter activity in Escherichia coliR Karpel, Y Olami, D Taglicht, et al.
Journal of Bacteriology|June 11, 1998
Altered Na+ and Li+ homeostasis in Saccharomyces cerevisiae cells expressing the bacterial cation antiporter NhaAR Ros, C Montesinos, A Rimon, et al.
The Journal of Biological Chemistry|January 17, 1997
Histidine 225, a residue of the NhaA-Na+/H+ antiporter of Escherichia coli is exposed and faces the cell exteriorY Olami, A Rimon, Y Gerchman, et al.
The Journal of Biological Chemistry|February 25, 1994
Purification and characterization of sulfide-quinone reductase, a novel enzyme driving anoxygenic photosynthesis in Oscillatoria limneticaB Arieli, Y Shahak, D Taglicht, et al.
Journal of Bacteriology|June 15, 2000
Cyanobacterial sulfide-quinone reductase: cloning and heterologous expressionM Bronstein, M Schütz, G Hauska, et al.
Biochemistry|November 9, 1982
Mechanism of lactose transport in Escherichia coli membrane vesicles: evidence for the involvement of histidine residue(s) in the response of the lac carrier to the proton electrochemical gradientM L Garcia, L Patel, E Padan, et al.
The Journal of Biological Chemistry|November 15, 1991
Expression of a sodium proton antiporter (NhaA) in Escherichia coli is induced by Na+ and Li+ ionsR Karpel, T Alon, G Glaser, et al.
Biophysical Journal|August 21, 2007
High-resolution structure of a Na+/H+ antiporter dimer obtained by pulsed electron paramagnetic resonance distance measurementsD Hilger, Y Polyhach, E Padan, et al.
The Journal of Biological Chemistry|November 10, 1995
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 valuesA Rimon, Y Gerchman, Y Olami, et al.
Biochimica Et Biophysica Acta|May 2, 1998
Topological study of Vibrio alginolyticus NhaB Na+/H+ antiporter using gene fusions in Escherichia coli cellsH Enomoto, T Unemoto, M Nishibuchi, et al.
Pageof 10