XAS Investigation of Silver(I) Coordination in Copper(I) Biological Binding Sites.
Grenoble, France. In Inorg Chem, Jan 2016
By making use of X-ray absorption spectroscopy (XAS), we characterized the Ag(I) binding sites in proteins related to copper homeostasis, such as the chaperone Atox1 and metallothioneins (MTs), as well as in bioinspired thiolate Cu(I) chelators mimicking these proteins, in solution and at physiological pH.
Role of metal in folding and stability of copper proteins in vitro.
Umeå, Sweden. In Biochim Biophys Acta, 2012
Examples of proteins discussed are: a blue-copper protein (Pseudomonas aeruginosa azurin), members of copper-transport systems (bacterial CopZ, human Atox1 and ATP7B domains) and multi-copper ferroxidases (yeast Fet3p and human ceruloplasmin).
Spinocerebellar ataxia type 1.
Milano, Italy. In Handb Clin Neurol, 2011
SCA1, the first autosomal dominant cerebellar ataxia (ADCA) to be genetically characterized, is caused by the expansion of a CAG triplet repeat located in the N-terminal coding region of the disease-causing gene ATX1 located on chromosome 6p23: the mutation results in the production of a mutant protein, dubbed ataxin-1, with a longer-than-normal polyglutamine stretch.