Results 171 to 180 of about 63,819 (225)
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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.
J H, Kägi, P, Hunziker
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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.
J H, Kägi, P, Hunziker
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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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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 (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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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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International Archives of Allergy and Immunology, 1994
The zinc content in platelets from rabbits, humans and horses was determined, and the levels of zinc were found to be significantly higher (3 micrograms/10(10) 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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The zinc content in platelets from rabbits, humans and horses was determined, and the levels of zinc were found to be significantly higher (3 micrograms/10(10) 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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Mini-Reviews in Medicinal Chemistry, 2007
Diabetes is a widespread disease, and its development and toxic effects on various organs have been attributed to increased oxidative stress. Metallothionein (MT) is a group of intracellular metal-binding and cysteine-rich proteins, being highly inducible in many tissues.
null Xiaokun Li +5 more
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Diabetes is a widespread disease, and its development and toxic effects on various organs have been attributed to increased oxidative stress. Metallothionein (MT) is a group of intracellular metal-binding and cysteine-rich proteins, being highly inducible in many tissues.
null Xiaokun Li +5 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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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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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
openaire +2 more sources