Abstract
Metallothioneins (MTs) are low molecular weight (2–7 kDa), cysteine-rich proteins which bind with high affinity to metal ions, such as Zn(II), Cd(II), Cu(I) and Ag(I), in unusual metal-thiolate clusters [1-3]. MT biosynthesis is induced by a wide range of factors, including metal ions, oxidative stress, glucocorticoid hormones and cytokines, leading to their implication in many diverse cellular processes. However, the primary function of MTs under normal physiological conditions is in the transport and storage of the essential metals: zinc and copper.
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© 1999 Springer Basel AG
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Öz, G., Pountney, D.L., Armitage, I.M. (1999). Metallothionein structure update. In: Klaassen, C.D. (eds) Metallothionein IV. Advances in Life Sciences. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-8847-9_5
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DOI: https://doi.org/10.1007/978-3-0348-8847-9_5
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