Results 11 to 20 of about 30,614 (220)
IUBMB Life, 2017 AbstractMetallothioneins (MTs) are a class of low molecular weight and cysteine‐rich metal binding proteins present in all the branches of the tree of life. MTs efficiently bind with high affinity several essential and toxic divalent and monovalent transition metals by forming characteristic polynuclear metal‐thiolate clusters within their structure ...
Jenifer S. Calvo +2 more
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Anti-metallothionein IgG and levels of metallothionein in autistic families [PDF]
Swiss Medical Weekly, 2008 Metallothioneins (MTs) are a family of small proteins containing 61-68 amino acids with an unusually high concentration of cysteine. MT-1, the most functional and active MT in humans, has the ability to react with and enhance the detoxification of a number of metals including zinc, mercury, copper and cadmium.
A Russo
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Hepatology, EarlyView., 2022 CHIN117 is a dual cysteinyl leukotriene receptor 1 (CYSLTR1) antagonist and G‐protein‐coupled bile acid receptor 1 (GPBAR1) agonist. In the liver, GPBAR1 and CYSLTR1 are coexpressed by liver sinusoidal endothelial cells (LSECs), HSCs, circulating monocytes/macrophages, and liver resident macrophages (Kupffer cells).
Michele Biagioli +13 more
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Experimental Biology and Medicine, 1987 Early research on metallothionein centered on aspects related to a detoxification role. As our understanding of the complex endocrine control that regulates metallothionein gene expression increases, a wider appreciation of a functional role(s) is emerging.
M A, Dunn, T L, Blalock, R J, Cousins
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Structure of mammalian metallothionein. [PDF]
Environmental Health Perspectives, 1984 All mammalian metallothioneins characterized contain a single polypeptide chain of 61 amino acid residues, among them 20 cysteines providing the ligands for seven metal-binding sites. Native metallothioneins are usually heterogeneous in metal composition, with Zn, Cd, and Cu occurring in varying proportions.
Jeremias H.R. Kägi +6 more
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Metallothionein: An overview [PDF]
World Journal of Gastroenterology, 2007 Metallothioneins (MTs) were discovered in 1957 by Margoshes and Vallee and identified as low-molecular weight and sulphydryl rich proteins. It is not surprising that most mammalian tissues contain age related basal levels of MTs since they are involved in metalloregulatory processes that include cell growth and multiplication.
KT Manisenthil Kumar +4 more
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BioTechniques, 2002 We investigated the potential utility of a recombinant E. coli that expresses the human metallothionein II gene as a fusion protein with β-galactosidase as a heavy metal biosorbent. E.
N. Yoshida +5 more
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Journal of Education, Health and Sport, 2018 In an experiment on white wild-type laboratory rats, it was shown that 90 minutes after intraperitoneal administration of cisplatin at a dose of 4 mg / kg as a solution heated to 43 °C, the integral level of metallothionein significantly increased in the
E. D. Pykhtieieva +2 more
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Scientia Marina, 2010 The metallothionein levels and metal concentrations in whole body, digestive gland and gills of Crassostrea angulata were analyzed in field samples collected from the River Guadalquivir estuary over several years following a mining waste spill upstream ...
Chiara Trombini +2 more
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Antigenicity of metallothionein. [PDF]
Proceedings of the National Academy of Sciences, 1983 The antigenic determinants of vertebrate metallothionein have been determined by a competitive-binding double-antibody radioimmunoassay to consist of two immunologically dominant regions in the NH2-terminal domain (residues 1-29). The COOH-terminal domain (residues 30-61) exhibited trivial immunoreactivity in competitive binding assays.
Justine S. Garvey, Dennis R. Winge
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