HIGHLIGHTS
SUMMARY
Glycosylation modification is one of such post-translational modifications and has been implicated in the development of various cancer types by affecting protein conformation and protein-protein interaction (Lemjabbar-Alaoui et_al, 2015; Takahashi et_al, 2016; Yang et_al, 2021b). In mammalian cells, the ST3GAL family, which consists of six family members, is responsible for the specific catalysis of the transfer of sialic acid in the α2,3- junction (Harduin-Lepers et_al, 1995; Harduin-Lepers et_al, 2001). A highly abnormal sialylation on the glycosyl-terminal surface of tumor cells facilitates signal_transduction and cell-to-cell interaction . . .
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