High-affinity binding of Clostridium perfringens epsilon-toxin to rat brain.

Por Nagahama, M, Sakurai, J
Publicado em 1992

Tryptophan content of Clostridium perfringens epsilon toxin.

Por Sakurai, J, Nagahama, M
Publicado em 1985

Effect of Clostridium perfringens epsilon toxin on the cardiovascular system of rats.

Por Sakurai, J, Nagahama, M, Fujii, Y
Publicado em 1983

Phospholipid metabolism induced by Clostridium perfringens alpha-toxin elicits a hot-cold type of hemolysis in rabbit erythrocytes.

Por Ochi, S, Hashimoto, K, Nagahama, M, Sakurai, J
Publicado em 1996

Site-specific mutagenesis of Clostridium perfringens alpha-toxin: replacement of Asp-56, Asp-130, or Glu-152 causes loss of enzymatic and hemolytic activities.

Por Nagahama, M, Nakayama, T, Michiue, K, Sakurai, J
Publicado em 1997

Site-directed mutagenesis of histidine residues in Clostridium perfringens alpha-toxin.

Por Nagahama, M, Okagawa, Y, Nakayama, T, Nishioka, E, Sakurai, J
Publicado em 1995

Involvement of tumour necrosis factor-α in Clostridium perfringens β-toxin-induced plasma extravasation in mice

Por Nagahama, M, Kihara, A, Kintoh, H, Oda, M, Sakurai, J
Publicado em 2008

Irreversible hyperoxidation of peroxiredoxin 2 is caused by tert-butyl hydroperoxide in human red blood cells

Por Ishida, Y.I., Takikawa, M., Suzuki, T., Nagahama, M., Ogasawara, Y.
Publicado em 2014

Identity of hemolysins produced by Vibrio cholerae non-O1 and V. cholerae O1, biotype El Tor.

Por Yamamoto, K, Ichinose, Y, Nakasone, N, Tanabe, M, Nagahama, M, Sakurai, J, Iwanaga, M
Publicado em 1986