Comparison of the amyloid pore forming properties of rat and human Alzheimer's beta-amyloid peptide 1-42: Calcium imaging data.
Identifieur interne : 000323 ( Main/Exploration ); précédent : 000322; suivant : 000324Comparison of the amyloid pore forming properties of rat and human Alzheimer's beta-amyloid peptide 1-42: Calcium imaging data.
Auteurs : Coralie Di Scala [France] ; Nouara Yahi [France] ; Alessandra Flores [France] ; Sonia Boutemeur [France] ; Nazim Kourdougli [France] ; Henri Chahinian [France] ; Jacques Fantini [France]Source :
- Data in brief ; 2016.
Abstract
The data here consists of calcium imaging of human neuroblastoma 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 peptide Aβ1-42. These data are both of a qualitative (fluorescence micrographs) and semi-quantitative nature (estimation of intracellular calcium concentrations of cells probed by Aβ1-42 peptides vs. control untreated cells). Since rat Aβ1-42 differs from its human counterpart at only three amino acid positions, this comparative study is a good assessment of the specificity of the amyloid pore forming assay. The interpretation of this dataset is presented in the accompanying study "Broad neutralization of calcium-permeable amyloid pore channels with a chimeric Alzheimer/Parkinson peptide targeting brain gangliosides" [1].
DOI: 10.1016/j.dib.2016.01.019
PubMed: 26909380
Affiliations:
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type="city">Marseille</settlement></placeName><orgName type="university">Université d'Aix-Marseille</orgName></affiliation></author></analytic><series><title level="j">Data in brief</title><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The data here consists of calcium imaging of human neuroblastoma 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 peptide Aβ1-42. These data are both of a qualitative (fluorescence micrographs) and semi-quantitative nature (estimation of intracellular calcium concentrations of cells probed by Aβ1-42 peptides vs. control untreated cells). Since rat Aβ1-42 differs from its human counterpart at only three amino acid positions, this comparative study is a good assessment of the specificity of the amyloid pore forming assay. The interpretation of this dataset is presented in the accompanying study "Broad neutralization of calcium-permeable amyloid pore channels with a chimeric Alzheimer/Parkinson peptide targeting brain gangliosides" [1].</div></front></TEI><affiliations><list><country><li>France</li></country><region><li>Provence-Alpes-Côte d'Azur</li></region><settlement><li>Marseille</li></settlement><orgName><li>Université d'Aix-Marseille</li></orgName></list><tree><country name="France"><region name="Provence-Alpes-Côte d'Azur"><name sortKey="Di Scala, Coralie" sort="Di Scala, Coralie" uniqKey="Di Scala C" first="Coralie" last="Di Scala">Coralie Di Scala</name></region><name sortKey="Boutemeur, Sonia" sort="Boutemeur, Sonia" uniqKey="Boutemeur S" first="Sonia" last="Boutemeur">Sonia Boutemeur</name><name sortKey="Chahinian, Henri" sort="Chahinian, Henri" uniqKey="Chahinian H" first="Henri" last="Chahinian">Henri Chahinian</name><name sortKey="Fantini, Jacques" sort="Fantini, Jacques" uniqKey="Fantini J" first="Jacques" last="Fantini">Jacques Fantini</name><name sortKey="Flores, Alessandra" sort="Flores, Alessandra" uniqKey="Flores A" first="Alessandra" last="Flores">Alessandra Flores</name><name sortKey="Kourdougli, Nazim" sort="Kourdougli, Nazim" uniqKey="Kourdougli N" first="Nazim" last="Kourdougli">Nazim Kourdougli</name><name sortKey="Yahi, Nouara" sort="Yahi, Nouara" uniqKey="Yahi N" first="Nouara" last="Yahi">Nouara Yahi</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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