Results 201 to 210 of about 30,614 (220)
Some of the next articles are maybe not open access.

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
openaire   +1 more source

Metallothionein and brain inflammation

JBIC Journal of Biological Inorganic Chemistry, 2011
Since the seminal discoveries of Bert Vallee regarding zinc and metallothioneins (MTs) more than 50 years ago, thousands of studies have been published concerning this fascinating story. One of the most active areas of research is the involvement of these proteins in the inflammatory response in general, and in neuroinflammation in particular.
Manso, Y   +4 more
openaire   +4 more sources

Molecular splicing of metallothionein — study on domains of metallothionein [PDF]

open access: possible, 1999
Mammalian metallothioneins (MTs) are a class of low-molecular weight proteins containing 20 cysteine residues out of a total of 61 amino acid residues. MTs fold into two separate domains in the presence of certain metal ions [1,2]. Each domain binds metal ions in a polynuclear metalthiolate cluster with ligation through thiolates of the 20 cysteines ...
Yan-Jiao Zhou   +3 more
openaire   +1 more source

Metallothionein in Antarctic Fish

1998
Zinc 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
openaire   +4 more sources

Metallothionein and anticancer agents: the role of metallothionein in cancer chemotherapy

Journal of Neuro-Oncology, 1993
Metallothioneins (MTs) are intracellular proteins containing the highest amount of thiol groups within the cytoplasm. These thiol groups are able to bind several cytotoxic agents, such as platinum compounds and alkylating agents. Increased levels of MT are one mechanism of resistance to these anticancer drugs, as intracytoplasmic binding of MT prevents
Norbert Roosen   +2 more
openaire   +2 more sources

Bacterial Metallothioneins

2009
The bacterial metallothioneins (MT), BmtAs, constitute a well defined sub-family, sharing a number of characteristics with eukaryotic metallothioneins. They are small, cysteine-rich proteins, are inducible by metal ion stress, and contain metal-thiolate clusters with topologies similar to those of mammalian MTs. They also have a number of features that
openaire   +2 more sources

Metallothioneins

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
openaire   +2 more sources

Metallothionein and Metallothionein-Like Proteins: Physiological Importance

1989
Since the initial demonstration of a low-molecular weight cadmium-binding protein in mammals, the research on the function of these proteins, which also can bind Cu, Zn, and Hg, has been focused primarily on their detoxifying properties. Such a direction is understandable, since the synthesis of the proteins can be induced by these potentially toxic ...
Marius Brouwer, David W. Engel
openaire   +2 more sources

Functions of metallothionein

Biochemical Pharmacology, 1982
K. Cain, M. Webb
openaire   +3 more sources

Metallothionein

Annual Review of Biochemistry, 1986
openaire   +2 more sources

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