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Metallothionein in Platelets

International Archives of Allergy and Immunology, 2009
The zinc content in platelets from rabbits, humans and horses was determined, and the levels of zinc were found to be significantly higher (3 μg/1010 cells) than those in other peripheral blood cells. About 70% of the zinc in the supernatants of platelet lysates could be detected.
T, Sugiura, H, Nakamura
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Cadmium in Metallothioneins

2012
Metallothioneins (MTs) are low-molecular-mass cysteine-rich proteins with the ability to bind mono- and divalent metal ions with the electron configuration d ( 10 ) in form of metal-thiolate clusters. MTs are thought, among others, to play a role in the homeostasis of essential Zn(II) and Cu(I) ions.
Freisinger, Eva, Vasak, Milan
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Metallothioneins and Cancer

Current Protein & Peptide Science, 2009
Metallothioneins (MTs) are low molecular, cysteine-rich proteins that have naturally-occurring Zn(2+) in both clusters. They may serve as a reservoir of metals for synthesis of apoenzymes and zinc-finger transcription regulators. MTs are also involved with several important proteins e.g. p53, NF-kappaB, PKCl, and GTPase Rab3A.
Tomas, Eckschlager   +4 more
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Mammalian metallothionein

Biological Trace Element Research, 1989
Chemical, spectroscopic, and structural studies have established the metallothioneins (MTs) to be a widely occurring family of polypeptidic bioinorganic structures. They are distinguished by an extremely high metal (Zn, Cd, Cu) and Cys content and by the arrangement of these components in metal-thiolate clusters.
Kägi JH, Hunziker P
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Cadmium and Metallothionein

2013
The role of cadmium in inducing hepatotoxicity and nephrotoxicity, as well as the role of metallothionein as a cadmium-induced intracellular protector of toxicity has been described.
Breljak, Davorka   +3 more
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Metalation of metallothioneins

IUBMB Life, 2009
AbstractEnergy‐minimized molecular models of Cd7‐βαhMT: space filling. See Metalation of Metallothioneins by Ngu and Stillman, pp. 438–446.
Thanh T, Ngu, Martin J, Stillman
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Microbial metallothioneins

2001
Bacterial metallothioneins bind, sequester and buffer excess intracellular zinc. At present, the vast majority of the available experimental data relate to cyanobacterial metallothionein, SmtA, from Synechococcus PCC 7942. SmtA is required for normal resistance to zinc and smtA-mediated zinc resistance has been used as a selectable marker.
Robinson NJ, Whitehall SK, Cavet JS
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Nomenclature of Metallothionein

1987
The original recommendations concerning the nomenclature of metallothionein were made by the plenum of the First International Meeting on Metallothionein and Other Low Molecular Weight Metal-binding Proteins in 1978 (Nordberg and Kojima, 1979). The present revised version includes amendments to these recommendations as adopted by the Committee on the ...
B A, Fowler   +3 more
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The function of metallothionein

Neurochemistry International, 1995
Since its discovery in 1957 metallothionein (MT) has remained a protein in search of a function. After 40 years of frustrating efforts, three areas of research point to its zinc cluster structure as the basis of its functional potential: (1) the regulation of MT gene expression by zinc-dependent transcription factors, (2) neuronal growth inhibition in ...
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Metallothioneins in Plants

2009
The earliest perception restricted the occurrence of metallothioneins to animals, fungi, and certain bacteria and assigned the corresponding functions in plants to the enzymatically synthesized phytochelatins. This picture has now clearly changed, and the existence of plant metallothioneins is generally accepted. Compared to the vertebrate forms, plant
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