3 results match your criteria: "CNRS UPR 8241 (associated with University Toulouse III)[Affiliation]"
Thioflavin derivatives as markers for amyloid-beta fibrils: insights into structural features important for high-affinity binding.
ChemMedChem
January 2008
Laboratoire de Chimie de Coordination, CNRS UPR 8241 associated with University Toulouse III, 205 route de Narbonne, 31077 Toulouse Cedex 4, France.
Structural and thermodynamical properties of CuII amyloid-beta16/28 complexes associated with Alzheimer's disease.
J Biol Inorg Chem
November 2006
Laboratoire de Chimie de Coordination, CNRS UPR 8241 (associated with University Toulouse III), 205 route de Narbonne, 31077, Toulouse Cedex 4, France.
The aggregation of the peptide amyloid-beta (Abeta) to form amyloid plaques is a key event in Alzheimer's disease. It has been shown that CuII can bind to soluble Abeta and influence its aggregation properties. Three histidines and the N-terminal amine have been proposed to be involved in its coordination.
View Article and Find Full Text PDFMetal-binding properties of the peptide APP170-188: a model of the ZnII-binding site of amyloid precursor protein (APP).
Chemistry
January 2005
Laboratoire de Chimie de Coordination, CNRS UPR 8241 (associated with University Toulouse III), 205 route de Narbonne, 31077 Toulouse Cedex, France.
Amyloid precursor protein (APP) plays a key role in Alzheimer's disease (AD), although the function of this membrane protein is still unclear. Metal ions are implicated in AD and they also interact with APP. APP possesses a strong ZnII binding site, which is evolutionary conserved.
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