M. Maejima

Porcine aminopeptidase N is not a cellular receptor of porcine epidemic diarrhea virus, but promotes its infectivity via aminopeptidase activity.

F. Taguchi, K. Shirato, S. Matsuyama, 2016, The Journal of general virology.

Enhanced cell fusion activity in porcine epidemic diarrhea virus adapted to suckling mice

T. Nunoya, F. Taguchi, K. Shirato, 2010, Archives of Virology.

Classification of Omicron BA.1, BA.1.1, and BA.2 sublineages by TaqMan assay consistent with whole genome analysis data

M. Maejima, Y. Hirotsu, H. Mochizuki, 2022, International Journal of Infectious Diseases.

Similar viral loads in Omicron infections regardless of vaccination status

Y. Hirotsu, H. Mochizuki, M. Shibusawa, 2022, medRxiv.

Mutation in the cytoplasmic retrieval signal of porcine epidemic diarrhea virus spike (S) protein is responsible for enhanced fusion activity

F. Taguchi, K. Shirato, S. Matsuyama, 2011, Virus Research.

Heparin-binding activity of feline herpesvirus type 1 glycoproteins.

T. Mikami, K. Maeda, K. Fujita, 1997, Virus research.

Mutation in the cytoplasmic retrieval signal of porcine epidemic diarrhea virus spike (S) protein is responsible for enhanced fusion activity

F. Taguchi, K. Shirato, S. Matsuyama, 2011, Virus Research.

Porcine aminopeptidase N is not a cellular receptor of porcine epidemic diarrhea virus, but promotes its infectivity via aminopeptidase activity.

F. Taguchi, K. Shirato, S. Matsuyama, 2016, The Journal of general virology.