Yoko Hayashi‐Iwasaki
Kyowa-kako (Japan)(JP)
Publications by Year
Research Areas
Enzyme Structure and Function, Protein Structure and Dynamics, Hemoglobin structure and function, Biochemical and Molecular Research, Photosynthetic Processes and Mechanisms
Most-Cited Works
- → The initial step of the thermal unfolding of 3-isopropylmalate dehydrogenase detected by the temperature-jump Laue method(2000)21 cited
- → Spectroscopic Investigation of Selective Cluster Conversion of Archaeal Zinc-containing Ferredoxin fromSulfolobus sp. Strain 7(2000)21 cited
- → Thermostabilization of a chimeric enzyme by residue substitutions: four amino acid residues in loop regions are responsible for the thermostability of Thermus thermophilus isopropylmalate dehydrogenase(2001)21 cited
- → A stable intermediate in the thermal unfolding process of a chimeric 3‐isopropylmalate dehydrogenase between a thermophilic and a mesophilic enzymes(1996)19 cited
- → Purification and Characterization of Recombinant 3-Isopropylmalate Dehydrogenases from Thermus thermophilus Other Microorganisms(2000)13 cited
- → Crystallization and preliminary X-ray diffraction studies of the prototypal homologue of mitoNEET (Tth-NEET0026) from the extreme thermophileThermus thermophilusHB8(2008)10 cited
- → Studies on interdomain interaction of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus , by constructing chimeric enzymes(1999)4 cited
- → Molecular dynamics simulation of the thermal denaturation of 3-isopropylmalate dehydrogenase(2000)
- → 2P069 Thermodynamic evaluation of the highly stabilized cold shock protein homologue by introducing a disulfide bond(Proteins-stability, folding, and other physicochemical properties,Oral Presentations)(2007)
- → Electrostatic interaction between two domains of isocitrate dehydrogenase from Thermus thermophilus is important for the catalytic function and protein stability(1996)