Common molecular mechanism of amyloid pore formation by Alzheimer’s β-amyloid peptide and α-synuclein

Autor: Di Scala, Coralie, Yahi, Nouara, Boutemeur, Sonia, Flores, Alessandra, Rodriguez, Léa, Chahinian, Henri, Fantini, Jacques

Publikováno v: Scientific Reports

Calcium-permeable pores formed by small oligomers of amyloid proteins are the primary pathologic species in Alzheimer's and Parkinson's diseases. However, the molecular mechanisms underlying the assembly of these toxic oligomers in the plasma membran

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::5a39d32089a994134359c44243254c99

Comparison of the amyloid pore forming properties of rat and human Alzheimer’s beta-amyloid peptide 1-42: Calcium imaging data

Autor: Scala, Coralie, Yahi, Nouara, Flores, Alessandra, Boutemeur, Sonia, Kourdougli, Nazim, Chahinian, Henri, Fantini, Jacques

Publikováno v: Data in Brief
Data in Brief, Elsevier, 2014, 6, pp.640-643. ⟨10.1016/j.dib.2016.01.019⟩
Data in Brief, Vol 6, Iss, Pp 640-643 (2016)
Data in Brief, Elsevier, 2014, 6, pp.640-643. 〈10.1016/j.dib.2016.01.019〉

International audience; The data here consists of calcium imaging of human neuro-blastoma SH-SY5Y cells treated with the calcium-sensitive dye Fluo-4AM and then incubated with nanomolar concentrations of either human or rat Alzheimer's β-amyloid pep

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::e669798eff77fcb184b3ec11d5170d8d
https://hal-amu.archives-ouvertes.fr/hal-01768262

Comparison of the amyloid pore forming properties of rat and human Alzheimer’s beta-amyloid peptide 1-42: Calcium imaging data

Autor: Di Scala, Coralie, Yahi, Nouara, Flores, Alessandra, Boutemeur, Sonia, Kourdougli, Nazim, Chahinian, Henri, Fantini, Jacques

Publikováno v: In Data in Brief March 2016 6:640-643