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• W2022382087 endingPage "6054" @default.
• W2022382087 startingPage "6047" @default.
• W2022382087 abstract "Previous work has identified sphingosine kinase-1 (SK1) as a substrate for the cysteine protease cathepsin B in vitro. In this study, the mechanism of SK1 cleavage by cathepsin B was investigated. We identified two initial cleavage sites for the protease, the first at histidine 122 and the second at arginine 199. Mutation analysis showed that replacement of histidine 122 with a tyrosine maintained the activity of SK1 while significantly reducing cleavage by cathepsin B at the initial cleavage site. The efficacy of cleavage of SK1 at arginine 199, however, was not affected. These studies demonstrate that SK1 is cleaved by cathepsin B in a sequential manner after basic amino acids, and that the initial cleavages at the two identified sites occur independently of each other." @default.
• W2022382087 created "2016-06-24" @default.
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• W2022382087 creator A5023831938 @default.
• W2022382087 creator A5042150655 @default.
• W2022382087 creator A5090422329 @default.
• W2022382087 date "2006-10-12" @default.
• W2022382087 modified "2023-09-26" @default.
• W2022382087 title "Sphingosine kinase-1 is cleaved by cathepsin B in vitro: Identification of the initial cleavage sites for the protease" @default.
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• W2022382087 doi "https://doi.org/10.1016/j.febslet.2006.09.070" @default.
• W2022382087 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1732625" @default.
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