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Piero Valenti

Researcher at University of Bologna

Publications -  92
Citations -  1675

Piero Valenti is an academic researcher from University of Bologna. The author has contributed to research in topics: Xanthone & Chronotropic. The author has an hindex of 20, co-authored 92 publications receiving 1591 citations.

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3-(4-{[Benzyl(methyl)amino]methyl}phenyl)-6,7-dimethoxy-2H-2-chromenone (AP2238) Inhibits Both Acetylcholinesterase and Acetylcholinesterase-Induced β-Amyloid Aggregation: A Dual Function Lead for Alzheimer's Disease Therapy§

TL;DR: For the first time, a direct evidence of the Abeta antiaggregating action of an AChE inhibitor (AP2238) purposely designed to bind at both the catalytic and the peripheral sites of the human enzyme is presented.
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SAR of 9-Amino-1,2,3,4-tetrahydroacridine-Based Acetylcholinesterase Inhibitors: Synthesis, Enzyme Inhibitory Activity, QSAR, and Structure-Based CoMFA of Tacrine Analogues

TL;DR: This study attempted to derive a comprehensive SAR picture for the class of acetylcholinesterase (AChE) inhibitors related to tacrine, a drug currently in use for the treatment of the Alzheimer's disease.
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Nonsteroidal aromatase inhibitors: recent advances.

TL;DR: A survey of the compounds that have been recently reported as nonsteroidal aromatase inhibitors to provide a broad view on the general structure–activity relationships of the class and some aspects regarding the possible future development of the field are considered.
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In vitro evaluation of newly developed chalcone analogues in human cancer cells.

TL;DR: Morphological analysis of apoptosis showed that chalcone analogues induced apoptosis to a higher extent than quercetin, and S1 and S2 chalcones could be considered as potential new anticancer drugs.
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Acetylcholinesterase inhibitors for potential use in Alzheimer's disease: molecular modeling, synthesis and kinetic evaluation of 11H-indeno-[1,2-b]-quinolin-10-ylamine derivatives.

TL;DR: It is derived that the indenoquinoline nucleus probably represents the maximum allowable molecular size for rigid compounds binding to AChE, and seems particularly important in the context of Alzheimer's disease research in the light of recent observations showing that peripheral A ChE inhibitors might decrease the aggregating effects of the enzyme on the beta-amyloid peptide (betaA).