Results 141 to 150 of about 34,151 (189)
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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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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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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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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, 2009AbstractEnergy‐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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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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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
1987The 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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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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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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The function of metallothionein
Neurochemistry International, 1995Since 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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Metallothionein in Antarctic Fish
1998Zinc occupies a prominent position among transition and d10 elements because of the role played in many biological processes [1,2], including catalysis [3], transcription and translation [4]. The functional role of zinc depends on the large variety of metallorganic complexes produced by this element as a result of its interaction with different protein
V Carginale +8 more
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2014
Metallothioneins (MTs) are small cysteine-rich proteins that bind multiple metal ions in characteristic metal-thiolate clusters. They have been identified and studied in both prokaryotes, where they seem to be limited to a relatively small number of genera, and eukaryotes, where they are nearly ubiquitous. These are the archetypal cytosolic binders and
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Metallothioneins (MTs) are small cysteine-rich proteins that bind multiple metal ions in characteristic metal-thiolate clusters. They have been identified and studied in both prokaryotes, where they seem to be limited to a relatively small number of genera, and eukaryotes, where they are nearly ubiquitous. These are the archetypal cytosolic binders and
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