Hiroaki Kodama
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Hiroaki Kodama has a total of 72 co-authors. Here are the top co-authors by number of shared publications:
- Motomichi Fujita
Department of Molecular Patho-Physiology, Faculty of Pharmaceutical Sciences, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan
13 shared publications - Takuya Iyoda
Department of Pharmacy, Faculty of Pharmaceutical Sciences, Sanyo-Onoda City University, 1-1-1 Daigaku-Doori, Sanyo-Onoda, Yamaguchi 756-0884, Japan
13 shared publications Chikako Kudo
10 shared publicationsReo Nagai
10 shared publicationsFumio Fukai
9 shared publicationsKazuki Otsuka
9 shared publications
Latest Publications
- Open Access
- 23 September 2026
- Published by Wiley in ChemistrySelect
- Vol. 11 (37) , e74572
Pyridin‐2‐ylsulfinylfluoroacetate Reagent for the Stereoselective Synthesis of Z ‑Monofluoroalkenes
We report a practical modification of the classical Allmendinger‐type reagent for the stereoselective synthesis of Z ‑monofluoroalkenes. Replacement of the phenylsulfinyl group with a pyridin‐2‐ylsulfinyl moiety provides a reagent that affords cleaner reaction mixtures and facilitates product isolation. This difference translates into improved isolated yields and enhanced compatibility with acid‐sensitive substrates while maintaining the overall efficiency of the reaction. The utility of this method was demonstrated for representative alkyl halides as well as structurally complex substrates derived from amino acids and carbohydrates, including the synthesis of a Z ‑fluoroalkene analogue of acetylated lysine. This study emphasizes practical reliability rather than exhaustive substrate scope, and highlights the advantage of the pyridyl sulfoxide framework as a useful alternative for the preparation of Z ‑fluoroalkenes.
- 23 September 2026
- Published by Wiley in ChemistrySelect
- Vol. 11 (37) , e74572
Open AccessPyridin‐2‐ylsulfinylfluoroacetate Reagent for the Stereoselective Synthesis of Z ‑Monofluoroalkenes
We report a practical modification of the classical Allmendinger‐type reagent for the stereoselective synthesis of Z ‑monofluoroalkenes. Replacement of the phenylsulfinyl group with a pyridin‐2‐ylsulfinyl moiety provides a reagent that affords cleaner reaction mixtures and facilitates product isolation. This difference translates into improved isolated yields and enhanced compatibility with acid‐sensitive substrates while maintaining the overall efficiency of the reaction. The utility of this method was demonstrated for representative alkyl halides as well as structurally complex substrates derived from amino acids and carbohydrates, including the synthesis of a Z ‑fluoroalkene analogue of acetylated lysine. This study emphasizes practical reliability rather than exhaustive substrate scope, and highlights the advantage of the pyridyl sulfoxide framework as a useful alternative for the preparation of Z ‑fluoroalkenes.
- Open Access
- 3 April 2023
- Published by American Association for Cancer Research (AACR)
Supplementary Movie S3 from Aggressive Progression in Glioblastoma Cells through Potentiated Activation of Integrin α5β1 by the Tenascin-C–Derived Peptide TNIIIA2
Time lapse evaluation of cell scattering (TNIIIA2 + FNIII14)
- 3 April 2023
- Published by American Association for Cancer Research (AACR)
Open AccessSupplementary Movie S3 from Aggressive Progression in Glioblastoma Cells through Potentiated Activation of Integrin α5β1 by the Tenascin-C–Derived Peptide TNIIIA2
Time lapse evaluation of cell scattering (TNIIIA2 + FNIII14)
- Open Access
- 3 April 2023
- Published by American Association for Cancer Research (AACR)
Supplementary Movie S1 from Aggressive Progression in Glioblastoma Cells through Potentiated Activation of Integrin α5β1 by the Tenascin-C–Derived Peptide TNIIIA2
Time lapse evaluation of cell scattering (control)
- 3 April 2023
- Published by American Association for Cancer Research (AACR)
Open AccessSupplementary Movie S1 from Aggressive Progression in Glioblastoma Cells through Potentiated Activation of Integrin α5β1 by the Tenascin-C–Derived Peptide TNIIIA2
Time lapse evaluation of cell scattering (control)