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Gao L, Du X, Li J, Xiao-Feng Qin F. Evolving roles of CD38 metabolism in solid tumour microenvironment. Br J Cancer. 2022. https://doi.org/10.1038/s41416-022-02052-6.
Zocchi E, Franco L, Guida L, Calder L, De Flora A. Self-aggregation of purified and membrane-bound erythrocyte CD38 induces extensive decrease of its ADP-ribosyl cyclase activity. FEBS Lett. 1995;359:35–40.
Takasawa S, Tohgo A, Noguchi N, Koguma T, Nata K, Sugimoto T, et al. Synthesis and hydrolysis of cyclic ADP-ribose by human leukocyte antigen CD38 and inhibition of the hydrolysis by ATP. J Biol Chem. 1993;268:26052–4.
Tohgo A, Munakata H, Takasawa S, Nata K, Akiyama T, Hayashi N, et al. Lysine 129 of CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase) participates in the binding of ATP to inhibit the cyclic ADP-ribose hydrolase. J Biol Chem. 1997;272:3879–82.
Okamoto H, Takasawa S. Recent advances in the Okamoto model: the CD38-cyclic ADP-ribose signal system and the regenerating gene protein (Reg)-Reg receptor system in β-cells. Diabetes. 2002;51:S462–73.
Takasawa S. CD38–cyclic ADP-ribose signal system in physiology, biochemistry, and pathophysiology. Int J Mol Sci. 2022;23:4306.
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Nesmiyanov, P. Comment on: “Evolving roles of CD38 metabolism in solid tumour microenvironment”. Br J Cancer 128, 491 (2023). https://doi.org/10.1038/s41416-022-02113-w