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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.
American Journal of Perinatology|December 8, 2000
Continuous measurement of core body temperature in preterm infantsS Dollberg, A Rimon, H D Atherton, et al.
Blood|August 1, 1976
Factor XI activity and factor XI antigen in homozygous and heterozygous factor XI deficiencyA Rimon, S Schiffman, D I Feinstein, et al.
Bone|October 1, 1995
Quantitative ultrasound of the tibia: a novel approach for assessment of bone statusA J Foldes, A Rimon, D D Keinan, et al.
Arteriosclerosis, Thrombosis, and Vascular Biology|February 1, 1997
The effect of immunodepletion of antithrombin III on the response of rabbits to Russell's viper venom-induced activation of factor XS I Rapaport, T Toneff, A Rimon, et al.
Biochemistry|November 20, 1984
Sequence variation in heparin octasaccharides with high affinity for antithrombin IIID H Atha, A W Stephens, A Rimon, et al.
Biochimica Et Biophysica Acta|July 30, 2004
NhaA of Escherichia coli, as a model of a pH-regulated Na+/H+antiporterE Padan, T Tzubery, K Herz, 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.
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