L
Luisa Diomede
Researcher at Mario Negri Institute for Pharmacological Research
Publications - 118
Citations - 4077
Luisa Diomede is an academic researcher from Mario Negri Institute for Pharmacological Research. The author has contributed to research in topics: Chemistry & Amyloidosis. The author has an hindex of 31, co-authored 108 publications receiving 3617 citations.
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Journal ArticleDOI
Inhibition of monocyte chemotactic protein-1 synthesis by statins.
Maria Romano,Luisa Diomede,Marina Sironi,Lucia Massimiliano,Marcello Sottocorno,Nadia Polentarutti,Angelo Guglielmotti,Diego Albani,Alessandra Bruno,Paolo Fruscella,Mario Salmona,Annunciata Vecchi,Mario Pinza,Alberto Mantovani,Alberto Mantovani +14 more
TL;DR: In this article, Lovastatin and pravastatin were administered to mice according to a treatment schedule that significantly inhibited the hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase activity without affecting total blood cholesterol.
Journal ArticleDOI
In vivo anti-inflammatory effect of statins is mediated by nonsterol mevalonate products.
Luisa Diomede,Diego Albani,Marcello Sottocorno,Maria Benedetta Donati,M. Bianchi,Paolo Fruscella,Mario Salmona +6 more
TL;DR: The inhibition of sterol synthesis by squalestatin did not have any anti-inflammatory effect, indicating that the biosynthesis of nonsterol compounds arising from mevalonate is crucial for the in vivo regulation of cytokine and chemokine production by statins.
Journal ArticleDOI
Molecular Characteristics of a Protease-Resistant, Amyloidogenic and Neurotoxic Peptide Homologous to Residues 106-126 of the Prion Protein
C. Selvaggini,L. De Gioia,Laura Cantù,Elena Maria Ghibaudi,Luisa Diomede,F Passerini,Gianluigi Forloni,O. Bugiani,Fabrizio Tagliavini,Mario Salmona +9 more
TL;DR: This work has investigated the conformational properties, aggregation behaviour and sensitivity to protease digestion of a synthetic peptide homologous to residues 106-126 of human PrP, which was previously found to form amyloid-like fibrils in vitro and displayed neurotoxic activity toward primary cultures of rat hippocampal neurons.
Journal ArticleDOI
Conformational polymorphism of the amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein.
L. De Gioia,C. Selvaggini,Elena Maria Ghibaudi,Luisa Diomede,Orso Bugiani,Gianluigi Forloni,Fabrizio Tagliavini,Mario Salmona +7 more
TL;DR: The environment-dependent conformational polymorphism of PrP 106-126 and its marked tendency to form stablebeta-sheet structures at acidic pH could account for the shift from alpha-helix to beta-sheet associated with the conversion of PrPC to PrPSc, which occurs most likely in the endosomal-lysosomal compartment.
Journal ArticleDOI
An N-terminal Fragment of the Prion Protein Binds to Amyloid-β Oligomers and Inhibits Their Neurotoxicity in Vivo
Brian R. Fluharty,Emiliano Biasini,Matteo Stravalaci,Alessandra Sclip,Luisa Diomede,Claudia Balducci,Pietro La Vitola,Massimo Messa,Laura Colombo,Gianluigi Forloni,Tiziana Borsello,Marco Gobbi,David A. Harris +12 more
TL;DR: N1, the main physiological cleavage fragment of the cellular prion protein, is necessary and sufficient for binding early oligomeric intermediates during Aβ polymerization into amyloid fibrils and strongly suppresses Aβ oligomer toxicity in cultured murine hippocampal neurons, in a Caenorhabditis elegans-based assay, and in vivo in a mouse model of Aβ-induced memory dysfunction.