Synthetic amyloid-β oligomers impair long-term memory independently of cellular prion protein
- C. Balducci, M. Beeg, G. Forloni
- Biology, PsychologyProceedings of the National Academy of Sciences
- 19 January 2010
It is reported that, in mice, acute intracerebroventricular injections of synthetic Aβ1–42 oligomers impaired consolidation of the long-term recognition memory, whereas mature Aβ 1–42 fibrils and freshly dissolved peptide did not, and it was confirmed that A β1– 42 oligomers interact with PrPC, with nanomolar affinity.
An N-terminal Fragment of the Prion Protein Binds to Amyloid-β Oligomers and Inhibits Their Neurotoxicity in Vivo*
- Brian R. Fluharty, E. Biasini, D. Harris
- Biology, ChemistryJournal of Biological Chemistry
- 28 January 2013
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.
A Recessive Mutation in the APP Gene with Dominant-Negative Effect on Amyloidogenesis
- G. Di Fede, M. Catania, F. Tagliavini
- BiologyScience
- 13 March 2009
An APP mutation that causes disease only in the homozygous state, whereas heterozygous carriers were unaffected, consistent with a recessive Mendelian trait of inheritance is found, with implications for genetic screening and the potential treatment of Alzheimer's disease.
The SIRT1 activator resveratrol protects SK‐N‐BE cells from oxidative stress and against toxicity caused by α‐synuclein or amyloid‐β (1‐42) peptide
- D. Albani, L. Polito, G. Forloni
- Biology, ChemistryJournal of Neurochemistry
- 1 September 2009
SIRT1 activation by RES can prevent in the neuroblastoma model the deleterious effects triggered by oxidative stress or α‐syn(A30P) aggregation, while RES displayed a SIRT1‐independent protective action against Aβ42.
Tetracyclines affect prion infectivity
- G. Forloni, S. Iussich, F. Tagliavini
- BiologyProceedings of the National Academy of Sciences…
- 29 July 2002
The data suggest that these well characterized antibiotics reduce prion infectivity through a direct interaction with PrPSc and are potentially useful for inactivation of BSE- or vCJD-contaminated products and prevention strategies.
Regulation and Biochemistry of Mouse Molybdo-flavoenzymes
- R. Vilà, M. Kurosaki, E. Garattini
- Biology, ChemistryJournal of Biological Chemistry
- 5 March 2004
It is demonstrated that CD-1, C57BL/6, 129/Sv, and other mouse strains synthesize high levels of AOH1 in the liver and AOH2 in the skin, and that neither enzyme is involved in the in vivo biotransformation of acetaldehyde.
Calcitonin Gene-Related Peptide-Mediated Enhancement of Purinergic Neuron/Glia Communication by the Algogenic Factor Bradykinin in Mouse Trigeminal Ganglia from Wild-Type and R192Q Cav2.1 Knock-In…
- S. Ceruti, G. Villa, M. Abbracchio
- BiologyJournal of Neuroscience
- 9 March 2011
The findings suggest that P2Y receptors on glial cells might be considered as novel players in the cellular processes underlying migraine pathophysiology and might represent new targets for the development of innovative therapeutic agents against migraine pain.
P3-357 Structural properties of gerstmann-Sträussler-Scheinker disease amyloid protein
- F. Tagliavini, M. Morbin, M. Salmona
- Biology, ChemistryNeurobiology of Aging
- 28 November 2003
Data indicate that the intrinsic properties of PrP-(82-146) are dependent upon the integrity of the C-terminal region and account for the massive deposition ofPrP amyloid in GSS.
The neurotoxicity of prion protein (PrP) peptide 106–126 is independent of the expression level of PrP and is not mediated by abnormal PrP species
- L. Fioriti, E. Quaglio, R. Chiesa
- BiologyMolecular and Cellular Neuroscience
- 31 January 2005
Organ Distribution and Bone Tropism of Cellulose Nanocrystals in Living Mice.
- L. Colombo, L. Zoia, B. La Ferla
- BiologyBiomacromolecules
- 7 August 2015
The results strongly suggest that the peculiar tropism to the bones is due to the chemical interaction between the Ca(2+) of the bone matrix and the active surface of negatively-charged CNCs, which makes C NCs a potential nanodevice for theranostics in bone tumors.
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