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Y Gerchman

Showing results (1-10 of 12) with videos related to

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The Journal of Biological Chemistry|August 24, 1999
A pH-dependent conformational change of NhaA Na(+)/H(+) antiporter of Escherichia coli involves loop VIII-IX, plays a role in the pH response of the protein, and is maintained by the pure protein in dodecyl maltosideY Gerchman, A Rimon, E Padan
Microbial Ecology|September 24, 2018
High-Throughput Quantitative Measurement of Bacterial Attachment Kinetics on Seconds Time ScaleN Shteindel, D Yankelev, Y Gerchman
The Journal of Biological Chemistry|October 3, 1998
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 coliA Rimon, Y Gerchman, Z Kariv, et al.
Biochemistry|December 16, 1997
Probing the conformation of NhaA, a Na+/H+ antiporter from Escherichia coli, with trypsinA Rothman, Y Gerchman, E Padan, et al.
Biochemistry|March 22, 2001
Oligomerization of NhaA, the Na+/H+ antiporter of Escherichia coli in the membrane and its functional and structural consequencesY Gerchman, A Rimon, M Venturi, et al.
Biochimica Et Biophysica Acta|March 15, 2001
Na(+)/H(+) antiportersE Padan, M Venturi, Y Gerchman, 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.
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.
Proceedings of the National Academy of Sciences of the United States of America|February 15, 1993
Histidine-226 is part of the pH sensor of NhaA, a Na+/H+ antiporter in Escherichia coliY Gerchman, Y Olami, A Rimon, et al.
The Journal of Biological Chemistry|February 15, 2000
The monoclonal antibody 1F6 identifies a pH-dependent conformational change in the hydrophilic NH(2) terminus of NhaA Na(+)/H(+) antiporter of Escherichia coliM Venturi, A Rimon, Y Gerchman, et al.
Pageof 2

Showing results (1-10 of 12) with videos related to

Sort By:
Pageof 2
The Journal of Biological Chemistry|August 24, 1999
A pH-dependent conformational change of NhaA Na(+)/H(+) antiporter of Escherichia coli involves loop VIII-IX, plays a role in the pH response of the protein, and is maintained by the pure protein in dodecyl maltosideY Gerchman, A Rimon, E Padan
Microbial Ecology|September 24, 2018
High-Throughput Quantitative Measurement of Bacterial Attachment Kinetics on Seconds Time ScaleN Shteindel, D Yankelev, Y Gerchman
The Journal of Biological Chemistry|October 3, 1998
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 coliA Rimon, Y Gerchman, Z Kariv, et al.
Biochemistry|December 16, 1997
Probing the conformation of NhaA, a Na+/H+ antiporter from Escherichia coli, with trypsinA Rothman, Y Gerchman, E Padan, et al.
Biochemistry|March 22, 2001
Oligomerization of NhaA, the Na+/H+ antiporter of Escherichia coli in the membrane and its functional and structural consequencesY Gerchman, A Rimon, M Venturi, et al.
Biochimica Et Biophysica Acta|March 15, 2001
Na(+)/H(+) antiportersE Padan, M Venturi, Y Gerchman, 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.
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.
Proceedings of the National Academy of Sciences of the United States of America|February 15, 1993
Histidine-226 is part of the pH sensor of NhaA, a Na+/H+ antiporter in Escherichia coliY Gerchman, Y Olami, A Rimon, et al.
The Journal of Biological Chemistry|February 15, 2000
The monoclonal antibody 1F6 identifies a pH-dependent conformational change in the hydrophilic NH(2) terminus of NhaA Na(+)/H(+) antiporter of Escherichia coliM Venturi, A Rimon, Y Gerchman, et al.
Pageof 2