Kenji Kamata

Summary

Affiliation: Merck Research Laboratories
Country: USA

Publications

  1. ncbi Structures of the PKC-iota kinase domain in its ATP-bound and apo forms reveal defined structures of residues 533-551 in the C-terminal tail and their roles in ATP binding
    Tetsuo Takimura
    Tsukuba Research Institute, Merck Research Laboratories, Banyu Pharmaceutical Co Ltd, Okubo 3, Tsukuba, 300 2611 Ibaraki, Japan
    Acta Crystallogr D Biol Crystallogr 66:577-83. 2010
  2. ncbi Structural basis for allosteric regulation of the monomeric allosteric enzyme human glucokinase
    Kenji Kamata
    Banyu Tsukuba Research Institute in collaboration with Merck Research Laboratories, Okubo 3, Tsukuba, Ibaraki 300 2611, Japan
    Structure 12:429-38. 2004
  3. ncbi Discovery of potent and orally active 3-alkoxy-5-phenoxy-N-thiazolyl benzamides as novel allosteric glucokinase activators
    Tomoharu Iino
    Banyu Tsukuba Research Institute, Banyu Pharmaceutical Co Ltd, Okubo 3, Tsukuba 300 2611, Ibaraki, Japan
    Bioorg Med Chem 17:2733-43. 2009
  4. ncbi Discovery of novel 3,6-disubstituted 2-pyridinecarboxamide derivatives as GK activators
    Morihiro Mitsuya
    Banyu Tsukuba Research Institute, Banyu Pharmaceutical Co Ltd, Okubo, Tsukuba, Ibaraki, Japan
    Bioorg Med Chem Lett 19:2718-21. 2009
  5. ncbi The design and optimization of a series of 2-(pyridin-2-yl)-1H-benzimidazole compounds as allosteric glucokinase activators
    Keiji Takahashi
    Banyu Tsukuba Research Institute, Banyu Pharmaceutical Co, Ltd, 3 Okubo, Tsukuba, Ibaraki 300 2611, Japan
    Bioorg Med Chem 17:7042-51. 2009
  6. ncbi Identification of novel and potent 2-amino benzamide derivatives as allosteric glucokinase activators
    Teruyuki Nishimura
    Banyu Tsukuba Research Institute, Banyu Pharmaceutical Co Ltd, Okubo 3, Tsukuba, 300 2611 Ibaraki, Japan
    Bioorg Med Chem Lett 19:1357-60. 2009
  7. ncbi Discovery and structure-activity relationships of a novel class of quinazoline glucokinase activators
    Tomoharu Iino
    Banyu Tsukuba Research Institute, Banyu Pharmaceutical Co Ltd, Okubo 3, Tsukuba 300 2611, Ibaraki, Japan
    Bioorg Med Chem Lett 19:5531-8. 2009
  8. ncbi Structural snapshots of the KMSKS loop rearrangement for amino acid activation by bacterial tyrosyl-tRNA synthetase
    Takatsugu Kobayashi
    Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, 7 3 1 Hongo, Bunkyo ku, Tokyo 113 0033, Japan
    J Mol Biol 346:105-17. 2005

Collaborators

Detail Information

Publications8

  1. ncbi Structures of the PKC-iota kinase domain in its ATP-bound and apo forms reveal defined structures of residues 533-551 in the C-terminal tail and their roles in ATP binding
    Tetsuo Takimura
    Tsukuba Research Institute, Merck Research Laboratories, Banyu Pharmaceutical Co Ltd, Okubo 3, Tsukuba, 300 2611 Ibaraki, Japan
    Acta Crystallogr D Biol Crystallogr 66:577-83. 2010
    ..These results indicate that the protein structure is pre-organized before substrate binding to PKC-iota, which is different from the case of the prototypical AGC-branch kinase PKA...
  2. ncbi Structural basis for allosteric regulation of the monomeric allosteric enzyme human glucokinase
    Kenji Kamata
    Banyu Tsukuba Research Institute in collaboration with Merck Research Laboratories, Okubo 3, Tsukuba, Ibaraki 300 2611, Japan
    Structure 12:429-38. 2004
    ..This finding provided the mechanistic basis for activation of glucokinase as a potential therapeutic approach for treating type 2 diabetes mellitus...
  3. ncbi Discovery of potent and orally active 3-alkoxy-5-phenoxy-N-thiazolyl benzamides as novel allosteric glucokinase activators
    Tomoharu Iino
    Banyu Tsukuba Research Institute, Banyu Pharmaceutical Co Ltd, Okubo 3, Tsukuba 300 2611, Ibaraki, Japan
    Bioorg Med Chem 17:2733-43. 2009
    ..Rat oral glucose tolerance test indicated that 27e exhibited a glucose-lowering effect after 10 mg/kg oral administration...
  4. ncbi Discovery of novel 3,6-disubstituted 2-pyridinecarboxamide derivatives as GK activators
    Morihiro Mitsuya
    Banyu Tsukuba Research Institute, Banyu Pharmaceutical Co Ltd, Okubo, Tsukuba, Ibaraki, Japan
    Bioorg Med Chem Lett 19:2718-21. 2009
    ..Compound 7 demonstrated glucose lowering effect in a rat OGTT model...
  5. ncbi The design and optimization of a series of 2-(pyridin-2-yl)-1H-benzimidazole compounds as allosteric glucokinase activators
    Keiji Takahashi
    Banyu Tsukuba Research Institute, Banyu Pharmaceutical Co, Ltd, 3 Okubo, Tsukuba, Ibaraki 300 2611, Japan
    Bioorg Med Chem 17:7042-51. 2009
    ..The binding site and binding mode of the benzimidazole class of GKA with GK protein was confirmed by X-ray crystallographic analysis...
  6. ncbi Identification of novel and potent 2-amino benzamide derivatives as allosteric glucokinase activators
    Teruyuki Nishimura
    Banyu Tsukuba Research Institute, Banyu Pharmaceutical Co Ltd, Okubo 3, Tsukuba, 300 2611 Ibaraki, Japan
    Bioorg Med Chem Lett 19:1357-60. 2009
    ..In vivo pharmacokinetic and acute in vivo efficacy studies of compound 18 are also described...
  7. ncbi Discovery and structure-activity relationships of a novel class of quinazoline glucokinase activators
    Tomoharu Iino
    Banyu Tsukuba Research Institute, Banyu Pharmaceutical Co Ltd, Okubo 3, Tsukuba 300 2611, Ibaraki, Japan
    Bioorg Med Chem Lett 19:5531-8. 2009
    ..Prototype quinazoline leads (4 and 5) were designed based on the X-ray analyses of the previous 2-aminobenzamide lead classes. Modifications of the quinazoline leads led to the identification of a potent GK activator (21d)...
  8. ncbi Structural snapshots of the KMSKS loop rearrangement for amino acid activation by bacterial tyrosyl-tRNA synthetase
    Takatsugu Kobayashi
    Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, 7 3 1 Hongo, Bunkyo ku, Tokyo 113 0033, Japan
    J Mol Biol 346:105-17. 2005
    ..After the amino acid activation, the KMSKS loop adopts the semi-open form again to accept the CCA end of tRNA for the aminoacyl transfer reaction...