Miki H Maeda

Summary

Affiliation: National Institute of Agrobiological Sciences
Country: Japan

Publications

  1. ncbi request reprint The conserved residues of the ligand-binding domains of steroid receptors are located in the core of the molecules
    M Maeda
    Biochemistry Department, National Institute of Agrobiological Sciences, Kannondai 2 1 2, Tsukuba, Ibaraki 305 8602, Japan
    J Mol Graph Model 19:543-51, 601-6. 2001
  2. ncbi request reprint Cloning and sequence analysis of D-erythrulose reductase from chicken: its close structural relation to tetrameric carbonyl reductases
    Miki Maeda
    National Institute of Agrobiological Sciences, Kannondai 2 1 2, Tsukuba, Ibaraki 305 8602, Japan
    Protein Eng 15:611-7. 2002
  3. doi request reprint Development of new indices to evaluate protein-protein interfaces: assembling space volume, assembling space distance, and global shape descriptor
    Miki H Maeda
    Bioinformatics Research Unit, National Institute of Agrobiological Sciences, Kannondai 2 1 2, Tsukuba, Ibaraki 305 8602, Japan
    J Mol Graph Model 27:706-11. 2009
  4. ncbi request reprint Effect of salt and osmotic stresses on the expression of genes for the vacuolar H+-pyrophosphatase, H+-ATPase subunit A, and Na+/H+ antiporter from barley
    Atsunori Fukuda
    National Institute of Agrobiological Sciences, Kannondai 2 1 2, Tsukuba, Ibaraki 305 8602, Japan
    J Exp Bot 55:585-94. 2004

Detail Information

Publications4

  1. ncbi request reprint The conserved residues of the ligand-binding domains of steroid receptors are located in the core of the molecules
    M Maeda
    Biochemistry Department, National Institute of Agrobiological Sciences, Kannondai 2 1 2, Tsukuba, Ibaraki 305 8602, Japan
    J Mol Graph Model 19:543-51, 601-6. 2001
    ..These conserved residues may be essential for conformational change in the ligand-binding domain from its inactive to active form...
  2. ncbi request reprint Cloning and sequence analysis of D-erythrulose reductase from chicken: its close structural relation to tetrameric carbonyl reductases
    Miki Maeda
    National Institute of Agrobiological Sciences, Kannondai 2 1 2, Tsukuba, Ibaraki 305 8602, Japan
    Protein Eng 15:611-7. 2002
    ..The phylogenic analysis of D-erythrulose reductase and the other related proteins suggests that the protein described as a carbonyl reductase D-erythrulose reductase...
  3. doi request reprint Development of new indices to evaluate protein-protein interfaces: assembling space volume, assembling space distance, and global shape descriptor
    Miki H Maeda
    Bioinformatics Research Unit, National Institute of Agrobiological Sciences, Kannondai 2 1 2, Tsukuba, Ibaraki 305 8602, Japan
    J Mol Graph Model 27:706-11. 2009
    ..As a result, our indices behave differently from the existing ones, and shed light on new features of protein-protein interfaces, as general trends of AS-distances for all protein interfaces...
  4. ncbi request reprint Effect of salt and osmotic stresses on the expression of genes for the vacuolar H+-pyrophosphatase, H+-ATPase subunit A, and Na+/H+ antiporter from barley
    Atsunori Fukuda
    National Institute of Agrobiological Sciences, Kannondai 2 1 2, Tsukuba, Ibaraki 305 8602, Japan
    J Exp Bot 55:585-94. 2004
    ..In addition, the HVP1 expression changed in a pattern similar to that of HvNHX1 expression. These results indicate that the expression of HVP1 is co-ordinated with that of HvNHX1 in barley roots in response to salt and osmotic stresses...