Isao Morishima undertakes multidisciplinary investigations into Horseradish peroxidase and Peroxidase in his work. His study on Peroxidase is mostly dedicated to connecting different topics, such as Nuclear magnetic resonance. His Nuclear magnetic resonance study frequently intersects with other fields, such as Horseradish peroxidase. He performs multidisciplinary study on Enzyme and Photochemistry in his works. In his research, he undertakes multidisciplinary study on Photochemistry and Organic chemistry. Many of his studies involve connections with topics such as Divalent and Organic chemistry. He combines Divalent and Calcium in his studies. In his study, Isao Morishima carries out multidisciplinary Calcium and Ionophore research. His research on Biochemistry frequently connects to adjacent areas such as Guaiacol.
His work on Atomic physics as part of general Resonance (particle physics) research is frequently linked to Nuclear magnetic resonance, thereby connecting diverse disciplines of science. His research on Atomic physics often connects related areas such as Resonance (particle physics). Isao Morishima combines topics linked to Hemeprotein with his work on Nuclear magnetic resonance. He has begun a study into Gene, looking into Mutant, Protein subunit and Escherichia coli. Isao Morishima performs integrative Biochemistry and Biophysics research in his work. Isao Morishima merges Biophysics with Biochemistry in his research. His Organic chemistry study frequently intersects with other fields, such as Calcium. He integrates many fields, such as Enzyme and Photochemistry, in his works. He merges Photochemistry with Enzyme in his study.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Roles of proximal ligand in heme proteins: replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase.
Shin Ichi Adachi;Shingo Nagano;Koichiro Ishimori;Yoshihito Watanabe.
Conformational landscape of cytochrome c folding studied by microsecond-resolved small-angle x-ray scattering.
Shuji Akiyama;Satoshi Takahashi;Tetsunari Kimura;Koichiro Ishimori.
Proceedings of the National Academy of Sciences of the United States of America (2002)
Oxidized Human Neuroglobin Acts as a Heterotrimeric Gα Protein Guanine Nucleotide Dissociation Inhibitor
Keisuke Wakasugi;Keisuke Wakasugi;Tomomi Nakano;Isao Morishima.
Journal of Biological Chemistry (2003)
Identification of the ubiquitin-protein ligase that recognizes oxidized IRP2.
Koji Yamanaka;Haruto Ishikawa;Haruto Ishikawa;Yuzuru Megumi;Fuminori Tokunaga.
Nature Cell Biology (2003)
Stepwise formation of alpha-helices during cytochrome c folding.
Shuji Akiyama;Satoshi Takahashi;Koichiro Ishimori;Isao Morishima.
Nature Structural & Molecular Biology (2000)
Collapse and search dynamics of apomyoglobin folding revealed by submillisecond observations of α-helical content and compactness
Takanori Uzawa;Shuji Akiyama;Tetsunari Kimura;Satoshi Takahashi.
Proceedings of the National Academy of Sciences of the United States of America (2004)
Acylperoxo-Iron(III) Porphyrin Complexes: A New Entry of Potent Oxidants for the Alkene Epoxidation
Kenji Machii;Yoshihito Watanabe;Isao Morishima.
Journal of the American Chemical Society (1995)
Direct observation of the push effect on the oxygen-oxygen bond cleavage of acylperoxoiron(III) porphyrin complexes
Kazuya Yamaguchi;Yoshihito Watanabe;Isao Morishima.
Journal of the American Chemical Society (1993)
Intra- and intermolecular beta-pleated sheet formation in glutamine-repeat inserted myoglobin as a model for polyglutamine diseases
Motomasa Tanaka;Isao Morishima;Takumi Akagi;Tsutomu Hashikawa.
Journal of Biological Chemistry (2001)
Presence of endogenous calcium ion and its functional and structural regulation in horseradish peroxidase.
Y Shiro;M Kurono;I Morishima.
Journal of Biological Chemistry (1986)
If you think any of the details on this page are incorrect, let us know.
We appreciate your kind effort to assist us to improve this page, it would be helpful providing us with as much detail as possible in the text box below: