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The Atx1-Ccc2 complex is a metal-mediated protein-protein interaction
Cellular systems allow transition-metal ions to reach or leave the cell or intracellular locations through metal transfer between proteins. By coupling mutagenesis and advanced NMR experiments, weExpand
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An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal‐binding domains of the Menkes protein
The interaction between the human copper(I) chaperone, HAH1, and one of its two physiological partners, the Menkes disease protein (ATP7A), was investigated in solution using heteronuclear NMR. TheExpand
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Synthesis, structural characterization and in vitro cytotoxicity of new Au(III) and Au(I) complexes with thioamides.
The reactions of tetrachloroauric(III) acid (HAuCl4) with the thioamides; 2-mercapto-benzothiazole (mbztH) and 5-ethoxy-2-mercapto-benzimidazole (EtmbzimH) lead to the desulfuration of the ligandsExpand
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Antitumour and toxic effects on Wistar rats of two new platinum complexes
Background Cancer chemotherapy in humans based on metal complexes started at the clinical level in the late 1970s with the use of cisplatin, which forms intra‐strand cross‐links with DNA.
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A NMR Study of the Interaction of a Three-domain Construct of ATP7A with Copper(I) and Copper(I)-HAH1
ATP7A is a P-type ATPase involved in copper(I) homeostasis in humans. It possesses a long N-terminal tail protruding into the cytosol and containing six copper(I)-binding domains, which areExpand
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Cytotoxic, mutagenic, and carcinogenic potential of heavy metals related to human environment
Metal Carcinogenesis. Metallothioneins. Biological Role of Aluminium. Bioinorganic Chemistry (General). Metal Transport. Heavy Metals in the Environment. Antitumor Metal Complexes. Metal InteractionsExpand
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Tetrameric 1:1 and monomeric 1:3 complexes of silver(I) halides with tri( p -tolyl)-phosphine: A structural and biological study
Silver(I) halides react with tri(p-tolyl)phosphine (tptp, C21H21P) in MeOH/MeCN solutions in 1:1 or 1:3 molar ratios to give complexes of formulae {[AgCl(tptp)]4} (1) or [AgX(tptp)3] (X = Cl (2), BrExpand
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On the mechanism of action of thiamin enzymes, Crystal structure of 2-(α-hydroxyethyl)thiamin pyrophosphate (HETPP). Complexes of HETPP with zinc(II) and cadmium(II)
Abstract The crystal structure of the 2-(α-hydroxethyl) thiamin pyrophosphate (LH2) was solved by X-ray diffraction. Crystallographic data: space group F2dd, a=7.922(4) Å, b=33.11(2) Å, c=36.232(10)Expand
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Copper(II) and zinc(II) complexes of the peptides Ac-HisValHis-NH2 and Ac-HisValGlyAsp-NH2 related to the active site of the enzyme CuZnSOD.
Copper(II) and zinc(II) complexes of the peptides Ac-HisValHis-NH2 and Ac-HisValGlyAsp-NH2 related to the active site of the enzyme CuZnSOD were studied by potentiometric and spectroscopic (UV-Vis,Expand
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Metal Complex–DNA Interactions
A Basic Structural and Kinetic Aspects 1. Sequence-Selective Binding of Transition Metal Complexes to DNA 2. Thermodynamic Models of Metal Ion -DNA.Interactions 3. Metal Ion Coordination inExpand
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