Francesco Lipari

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OBJECTIVE Cerebral accumulation of amyloid β (Aβ) is a pathological hallmark of Alzheimer's disease (AD). Proteolytic processing of amyloid precursor protein (APP) by α- or β-secretase results in two soluble metabolites, sAPPα and sAPPβ, respectively. However, previous data have shown that both α- and β-secretase have multiple cleavage sites. The aim of(More)
Cerebrospinal fluid (CSF) biomarkers for Alzheimer’s disease (AD) reflect brain biochemistry. Using combined immunoprecipitation and mass spectrometry, we have shown that amyloid beta 1-15 (Aβ1-15) is produced by concerted β- and α-secretase cleavage of amyloid precursor protein (APP) and that the relative levels of Aβ1-16 in AD compared to controls are(More)
Out of the 90 human protein tyrosine kinases, 81 were assayed with short peptides derived from well-characterized [CDK1(Tyr15), IRS1(Tyr983), and JAK1(Tyr1023)] or generic [polyGlu:Tyr(4:1) and poly-Glu:Ala:Tyr(1:1:1)] substrates. As expected, the CDK1 peptide is a substrate for all Src family kinases. On the other hand, some of the activities are novel and(More)
Fig. 1. TLC overlay assay of ganghoside XQ with CSLEX1 and Lewis* specific CD 15 monoclonal antibodies. Gangliosides were chromatographed in solvent 1 Whole ganghoside fraction from human granulocytes (a, 20 u.g) and purified ganglioside XQ (b, 1 u,g) were stained with resorcinol Ganglioside XQ was immunostained with sialyl Lewis" specific CSLEX1 (c, 1 jig)(More)
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