The binding of Vibrio parahaemolyticus 125I-labeled thermostable direct hemolysin to erythrocytes
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Structure, function and regulation of the thermostable direct hemolysin (TDH) in pandemic Vibrio parahaemolyticus
2018, Microbial PathogenesisCitation Excerpt :The imbalance of ions inside and outside of the cells causes membrane permeabilization and erythrocytes to swell, leading to lysis [34,35]. GT1 ganglioside was thought to be the receptor sites for TDH on erythrocyte membranes [36,37], however other studies reported contradictory results [38–40]. TDH has been observed to exhibit cytotoxicity in a variety of cell lines [41–44].
A mutant cell line resistant to Vibrio parahaemolyticus thermostable direct hemolysin (TDH): Its potential in identification of putative receptor for TDH
1997, Biochimica et Biophysica Acta - Molecular Basis of DiseasePhosphorylation of a 25 kDa protein is induced by thermostable direct hemolysin of Vibrio parahaemolyticus
1996, International Journal of Biochemistry and Cell BiologyNature of the cation leak induced in erythrocyte membranes by Kanagawa haemolysin of Vibrio parahaemolyticus
1996, Biochimica et Biophysica Acta - Biomembranes
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