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Molecular Clock of Neutral Mutations in a Fitness-Increasing Evolutionary Process.
Kishimoto T, Ying BW, Tsuru S, Iijima L, Suzuki S, Hashimoto T, Oyake A, Kobayashi H, Someya Y, Narisawa D, Yomo T. Kishimoto T, et al. Among authors: someya y. PLoS Genet. 2015 Jul 15;11(7):e1005392. doi: 10.1371/journal.pgen.1005392. eCollection 2015 Jul. PLoS Genet. 2015. PMID: 26177190 Free PMC article.
Second-site mutation of Ala-220 to Glu or Asp suppresses the mutation of Asp-285 to Asn in the transposon Tn10-encoded metal-tetracycline/H+ antiporter of Escherichia coli.
Yamaguchi A, O'yauchi R, Someya Y, Akasaka T, Sawai T. Yamaguchi A, et al. Among authors: someya y. J Biol Chem. 1993 Dec 25;268(36):26990-5. J Biol Chem. 1993. PMID: 7903301 Free article.
A carboxyl group of Asp-285 is essential for tetracycline/H+ antiport mediated by the transposon Tn10-encoded metal-tetracycline/H+ antiporter (TetA) of Escherichia coli (Yamaguchi, A., Akasaka, T., Ono, N., Someya, Y., Nakatani, M., and Sawai, T. (1992) J. Biol. Ch …
A carboxyl group of Asp-285 is essential for tetracycline/H+ antiport mediated by the transposon Tn10-encoded metal-tetracycline/H+ antiport …
Site-specificity of the second-site suppressor mutation of the Asp-285-->Asn mutant of metal-tetracycline/H+ antiporter of Escherichia coli and the effects of amino acid substitutions at the first and second sites.
Someya Y, Niwa A, Sawai T, Yamaguchi A. Someya Y, et al. Biochemistry. 1995 Jan 10;34(1):7-12. doi: 10.1021/bi00001a002. Biochemistry. 1995. PMID: 7819225
The deleterious effect of the mutation of Asp-285 to Asn of the metal-tetracycline/H+ antiporter (TetA) of Escherichia coli is suppressed by the second-site mutation of Ala-220 to an acidic amino acid residue (Yamaguchi, A., O'yauchi, R., Someya, Y., & Sawai, T. …
The deleterious effect of the mutation of Asp-285 to Asn of the metal-tetracycline/H+ antiporter (TetA) of Escherichia coli is suppressed by …
Metal-tetracycline/H+ antiporter of Escherichia coli encoded by transposon Tn10. The structural resemblance and functional difference in the role of the duplicated sequence motif between hydrophobic segments 2 and 3 and segments 8 and 9.
Yamaguchi A, Kimura T, Someya Y, Sawai T. Yamaguchi A, et al. Among authors: someya y. J Biol Chem. 1993 Mar 25;268(9):6496-504. J Biol Chem. 1993. PMID: 8384213 Free article.
The properties of site-directed mutants as to the putative hydrophilic loop region between hydrophobic segments 2 and 3 in the transposon Tn10-encoded metal-tetracycline/H+ antiporter (TET) were reported in our previous paper (Yamaguchi, A., Someya, Y., and Sawai, T …
The properties of site-directed mutants as to the putative hydrophilic loop region between hydrophobic segments 2 and 3 in the transposon Tn …
Second-site suppressor mutations for the Arg70 substitution mutants of the Tn10-encoded metal-tetracycline/H+ antiporter of Escherichia coli.
Someya Y, Yamaguchi A. Someya Y, et al. Biochim Biophys Acta. 1997 Dec 15;1322(2-3):230-6. doi: 10.1016/s0005-2728(97)00088-1. Biochim Biophys Acta. 1997. PMID: 9452769 Free article.
The positive charge of the Arg70 residue in the cytoplasmic loop of the Tn10-encoded metal-tetracycline/H+ antiporter (Tet(B)) of Escherichia coli is essential for the tetracycline transport function (Y. Someya and A. Yamaguchi, Biochemistry 35, 9385-9391 (1996)). . …
The positive charge of the Arg70 residue in the cytoplasmic loop of the Tn10-encoded metal-tetracycline/H+ antiporter (Tet(B)) of Escherichi …
227 results