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Fig. 1 | Journal of Translational Medicine

Fig. 1

From: Stathmin-dependent molecular targeting therapy for malignant tumor: the latest 5 years’ discoveries and developments

Fig. 1

Structure diagram of stathmin and related signal patterns. Stathmin has a highly conserved stathmin-like domain (α-helical structure) and has four positions of serine phosphorylation sites (S16, S25, S38 and S63). The N- and C-terminal of stathmin exert different functions when stathmin participate the molecular actions. Some downstream target and/or partner proteins participate the modulation process of stathmin and interact each other to exert biological actions through phosphorylation of stathmin

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