The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
The Functions of Metallothionein and ZIP and ZnT Transporters: An Overview and Perspective
Open accessAbstract
Around 3000 proteins are thought to bind zinc in vivo, which corresponds to ~10% of the human proteome. Zinc plays a pivotal role as a structural, catalytic, and signaling component that functions in numerous physiological processes. It is more widely used as a structural element in proteins than any other transition metal ion, is a catalytic component of many enzymes, and acts as a cellular signaling mediator. Thus, it is expected that zinc metabolism and homeostasis have sophisticated regulation, and elucidating the underlying molecular basis of this is essential to understanding zinc functions in cellular physiology and pathogenesis. In recent decades, an increasing amount of evidence has uncovered critical roles of a number of proteins in zinc metabolism and homeostasis through influxing, chelating, sequestrating, coordinating, releasing, and effluxing zinc. Metallothioneins (MT) and Zrt- and Irt-like proteins (ZIP) and Zn transporters (ZnT) are the proteins primarily involved in these processes, and their malfunction has been implicated in a number of inherited diseases such as acrodermatitis enteropathica. The present review updates our current understanding of the biological functions of MTs and ZIP and ZnT transporters from several new perspectives.
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Cited by
The role of zinc, copper, manganese and iron in neurodegenerative diseases
Mezzaroba, L., Alfieri, D. F., Colado Simão, A. N., & Vissoci Reiche, E. M. (2019) · NeuroToxicology · doi:10.1016/j.neuro.2019.07.007 · Cited by 524
Critical Role of Zinc as Either an Antioxidant or a Prooxidant in Cellular Systems
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Nutrient Zinc at the Host–Pathogen Interface
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Metadata
- Authors
- Kimura, T., & Kambe, T.
- Venue
- International Journal of Molecular Sciences
- Publisher
- MDPI AG
- Published
- 2016-03-04
- Volume
- 17
- Issue
- 3
- Pages
- 336
- ISSN
- 1422-0067 (ISSN-L)
- OpenAlex
- W2288699132
- Cited by
- 409
- References
- 14
- FWCI
- 33.92
- Type
- journal article
- Language
- en
- Open access
- gold
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