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Masao Ikeda-Saito

Masao Ikeda-Saito

D-Index & Metrics

Chemistry

D-Index
67
Citations
11295
World Ranking
7131
National Ranking
462

Research.com Recognitions

  • 2000 - Fellow of the American Association for the Advancement of Science (AAAS)

Overview

Masao Ikeda-Saito is affiliated with Tohoku University in Japan and conducts research primarily in the fields of biochemistry, genetics and molecular biology, medicine, and chemistry. Their work spans several subfields including molecular biology, pediatrics, perinatology and child health, cell biology, electrochemistry, and oncology.

Their recent scholarly output features studies published in venues such as Biochemistry and Chemical Biology & Drug Design. Notable papers include "Unique Electronic Structures of the Highly Ruffled Hemes in Heme-Degrading Enzymes of Staphylococcus aureus, IsdG and IsdI, by Resonance Raman and Electron Paramagnetic Resonance Spectroscopies" published in 2020 in Biochemistry, as well as "Spectroscopic study of in situ-formed metallocomplexes of proton pump inhibitors in water," also from 2020, published in Chemical Biology & Drug Design.

Their research addresses topics such as:

  • Heme Oxygenase-1 and Carbon Monoxide
  • Neonatal Health and Biochemistry
  • Hemoglobin structure and function
  • Electrochemical Analysis and Applications
  • Drug Transport and Resistance Mechanisms
  • Molecular Sensors and Ion Detection

Frequent co-authors collaborating with Masao Ikeda-Saito include:

  • Satoshi Takahashi
  • Shusuke Nambu
  • Toshitaka Matsui
  • Hiroshi Fujii
  • Haruto Ishikawa

Prominent publication venues for their work are:

  • Biochemistry
  • Chemical Biology & Drug Design

Masao Ikeda-Saito has contributed consistently to expanding knowledge in biochemical and medical research contexts, focusing on areas like heme degradation, proton pump inhibitors, and advanced spectroscopic methods.

In recognition of their contributions, Masao Ikeda-Saito was named a Fellow of the American Association for the Advancement of Science (AAAS) in 2000.

Best Publications

  • Frataxin Acts as an Iron Chaperone Protein to Modulate Mitochondrial Aconitase Activity

    Anne Laure Bulteau;Heather A. O'Neill;Mary Claire Kennedy;Masao Ikeda-Saito

  • Nature of the Fe-O2 bonding in oxy-myoglobin: effect of the protein.

    Hui Chen;Masao Ikeda-Saito;Sason Shaik

  • Redox-Dependent Modulation of Aconitase Activity in Intact Mitochondria

    Anne Laure Bulteau;Masao Ikeda-Saito;Luke I. Szweda

  • Heme regulates gene expression by triggering Crm1‐dependent nuclear export of Bach1

    Hiroshi Suzuki;Satoshi Tashiro;Shusuke Hira;Jiying Sun

  • Catalytic mechanism of heme oxygenase through EPR and ENDOR of cryoreduced oxy-heme oxygenase and its Asp 140 mutants.

    Roman Davydov;Viktoria Kofman;Hiroshi Fujii;Tadashi Yoshida

  • Structural and Functional Effects of Apolar Mutations of the Distal Valine in Myoglobin

    Michael L. Quillin;Tiansheng Li;John S. Olson;George N. Phillips

  • Stability of myoglobin: a model for the folding of heme proteins.

    Mark S. Hargrove;Szymon Krzywda;Anthony J. Wilkinson;Yi Dou

  • Ischemic injury to mitochondrial electron transport in the aging heart: damage to the iron-sulfur protein subunit of electron transport complex III.

    Edward J. Lesnefsky;Tatyana I. Gudz;Catharina T. Migita;Masao Ikeda-Saito

  • Coordination structure of the ferric heme iron in engineered distal histidine myoglobin mutants

    M Ikeda-Saito;H Hori;L.A. Andersson;R.C. Prince

  • Aging decreases electron transport complex III activity in heart interfibrillar mitochondria by alteration of the cytochrome c binding site.

    Edward J. Lesnefsky;Edward J. Lesnefsky;Tatyana I. Gudz;Shadi Moghaddas;Catharina T. Migita

  • Reversible redox-dependent modulation of mitochondrial aconitase and proteolytic activity during in vivo cardiac ischemia/reperfusion

    Anne Laure Bulteau;Kathleen C. Lundberg;Masao Ikeda-Saito;Grazia Isaya

  • Structure and catalytic mechanism of heme oxygenase

    Masaki Unno;Toshitaka Matsui;Masao Ikeda-Saito

  • Heme oxygenase reveals its strategy for catalyzing three successive oxygenation reactions.

    Toshitaka Matsui;Masaki Unno;Masao Ikeda-Saito

  • Hydroperoxy-Heme Oxygenase Generated by Cryoreduction Catalyzes the Formation of α-meso-Hydroxyheme as Detected by EPR and ENDOR

    Roman M. Davydov;Tadashi Yoshida;Masao Ikeda-Saito;Brian M. Hoffman

  • Nitric oxide myoglobin: Crystal structure and analysis of ligand geometry

    Eric Allen Brucker;John S. Olson;Masao Ikeda-Saito;George N. Phillips

  • Heme-heme oxygenase complex. Structure of the catalytic site and its implication for oxygen activation.

    S. Takahashi;Jianling Wang;D. L. Rousseau;K. Ishikawa

  • Bach1, a heme-dependent transcription factor, reveals presence of multiple heme binding sites with distinct coordination structure.

    Shusuke Hira;Takeshi Tomita;Toshitaka Matsui;Kazuhiko Igarashi

  • A role for highly conserved carboxylate, aspartate-140, in oxygen activation and heme degradation by heme oxygenase-1.

    Hiroshi Fujii;Xuhong Zhang;Takeshi Tomita;Masao Ikeda-Saito

  • Heme coordination and structure of the catalytic site in nitric oxide synthase.

    Jianling Wang;D. J. Stuehr;M. Ikeda-Saito;D. L. Rousseau

  • Confirmation of the assignment of the iron-histidine stretching mode in myoglobin

    Pramod V. Argade;Massimo Sassaroli;Denis L. Rousseau;Toshiro Inubushi

Frequent Co-Authors

Takashi Yonetani
Takashi Yonetani University of Pennsylvania
John S. Olson
John S. Olson Rice University
Satoshi Takahashi
Satoshi Takahashi Tohoku University
Denis L. Rousseau
Denis L. Rousseau Albert Einstein College of Medicine
Kazuhiko Igarashi
Kazuhiko Igarashi Tohoku University
Teizo Kitagawa
Teizo Kitagawa University of Hyogo
Brian M. Hoffman
Brian M. Hoffman Northwestern University
Koichiro Ishimori
Koichiro Ishimori Hokkaido University
Dennis J. Stuehr
Dennis J. Stuehr Cleveland Clinic Lerner College of Medicine
Luke I. Szweda
Luke I. Szweda The University of Texas Southwestern Medical Center

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