Search

Your search keyword '"Pozzi, D."' showing total 13 results
Start Over Author "Pozzi, D." Publisher springer science and business media llc
13 results on '"Pozzi, D."'

1. Correction: Brain mapping across 16 autism mouse models reveals a spectrum of functional connectivity subtypes

Author

Zerbi, V., primary, Pagani, M., additional, Markicevic, M., additional, Matteoli, M., additional, Pozzi, D., additional, Fagiolini, M., additional, Bozzi, Y., additional, Galbusera, A., additional, Scattoni, M. L., additional, Provenzano, G., additional, Banerjee, A., additional, Helmchen, F., additional, Basson, M. A., additional, Ellegood, J., additional, Lerch, J. P., additional, Rudin, M., additional, Gozzi, A., additional, and Wenderoth, N., additional

Published
2022
Full Text
View/download PDF

2. Brain mapping across 16 autism mouse models reveals a spectrum of functional connectivity subtypes

Author

Zerbi, V., primary, Pagani, M., additional, Markicevic, M., additional, Matteoli, M., additional, Pozzi, D., additional, Fagiolini, M., additional, Bozzi, Y., additional, Galbusera, A., additional, Scattoni, M. L., additional, Provenzano, G., additional, Banerjee, A., additional, Helmchen, F., additional, Basson, M. A., additional, Ellegood, J., additional, Lerch, J. P., additional, Rudin, M., additional, Gozzi, A., additional, and Wenderoth, N., additional

Published
2021
Full Text
View/download PDF

4. Reduced SNAP-25 increases PSD-95 mobility and impairs spine morphogenesis

Author

Fossati, G, primary, Morini, R, additional, Corradini, I, additional, Antonucci, F, additional, Trepte, P, additional, Edry, E, additional, Sharma, V, additional, Papale, A, additional, Pozzi, D, additional, Defilippi, P, additional, Meier, J C, additional, Brambilla, R, additional, Turco, E, additional, Rosenblum, K, additional, Wanker, E E, additional, Ziv, N E, additional, Menna, E, additional, and Matteoli, M, additional

Published
2015
Full Text
View/download PDF

6. Role of temperature-independent lipoplex–cell membrane interactions in the efficiency boost of multicomponent lipoplexes

Author

Marchini, C, primary, Pozzi, D, additional, Montani, M, additional, Alfonsi, C, additional, Amici, A, additional, Candeloro De Sanctis, S, additional, Digman, M A, additional, Sanchez, S, additional, Gratton, E, additional, Amenitsch, H, additional, Fabbretti, A, additional, Gualerzi, C O, additional, and Caracciolo, G, additional

Published
2011
Full Text
View/download PDF

13. Amyloid-β 1–24 C-terminal truncated fragment promotes amyloid-β 1–42 aggregate formation in the healthy brain

Author

Antonino Natalello, Marco Rasile, Eliana Lauranzano, Sonia Mazzitelli, Davide Pozzi, Isabella Barajon, Matteo Tamborini, Chiara Starvaggi-Cucuzza, Fabia Filipello, Michela Matteoli, Toni Giorgino, Mazzitelli, S, Filipello, F, Rasile, M, Lauranzano, E, Starvaggi Cucuzza, C, Tamborini, M, Pozzi, D, Barajon, I, Giorgino, T, Natalello, A, and Matteoli, M

Subjects
0301 basic medicine, Protein Folding, Amyloid β, Plaque, Amyloid, Peptide, metabolism [Microglia], pathology [Alzheimer Disease], Mice, 0302 clinical medicine, pathology [Brain], metabolism [Peptide Fragments], Cytotoxic T cell, Senile plaques, genetics [Matrix Metalloproteinase 9], Mice, Knockout, chemistry.chemical_classification, Mice, Inbred BALB C, Learning Disabilities, administration & dosage [Amyloid beta-Peptides], P3 peptide, Brain, metabolism [Memory Disorders], pathology [Microglia], Alzheimer's disease, administration & dosage [Peptide Fragments], amyloid beta-protein (1-42), Phenotype, amyloid beta-peptide (1-24), Cell biology, metabolism [Matrix Metalloproteinase 9], physiology [Motor Activity], medicine.anatomical_structure, Matrix Metalloproteinase 9, Microglia, Alzheimer’s disease, metabolism [Alzheimer Disease], FIS/07 - FISICA APPLICATA (A BENI CULTURALI, AMBIENTALI, BIOLOGIA E MEDICINA), metabolism [Amyloid beta-Peptides], Mice, Transgenic, Amyloid-?, Motor Activity, Biology, Blood–brain barrier, Cleavage (embryo), Pathology and Forensic Medicine, 03 medical and health sciences, Cellular and Molecular Neuroscience, Alzheimer Disease, medicine, Animals, Humans, A?24, Amyloid-β, pathology [Memory Disorders], ddc:610, pathology [Plaque, Amyloid], Social Behavior, Memory Disorders, Aβ24, metabolism [Learning Disabilities], Amyloid beta-Peptides, Research, pathology [Learning Disabilities], Proteolytic activity, metabolism [Plaque, Amyloid], Peptide Fragments, Mice, Inbred C57BL, Mmp9 protein, mouse, Disease Models, Animal, 030104 developmental biology, chemistry, metabolism [Brain], Immunology, Neurology (clinical), Protein Multimerization, 030217 neurology & neurosurgery
Abstract

Substantial data indicate that amyloid-? (A?), the major component of senile plaques, plays a central role in Alzheimer's Disease and indeed the assembly of naturally occurring amyloid peptides into cytotoxic aggregates is linked to the disease pathogenesis. Although A?42 is a highly aggregating form of A?, the co-occurrence of shorter A? peptides might affect the aggregation potential of the A? pool. In this study we aimed to assess whether the structural behavior of human A?42 peptide inside the brain is influenced by the concomitant presence of N-terminal fragments produced by the proteolytic activity of glial cells. We show that the occurrence of the human C-terminal truncated 1-24 A? fragment impairs A?42 clearance through blood brain barrier and promotes the formation of A?42 aggregates even in the healthy brain. By showing that A?1-24 has seeding properties for aggregate formation in intracranially injected wild type mice, our study provide the proof-of-concept that peptides produced upon A?42 cleavage by activated glial cells may cause phenotypic defects even in the absence of genetic mutations associated with Alzheimer's Disease, possibly contributing to the development of the sporadic form of the pathology.

Published
2016

Catalog

Books, media, physical & digital resources
See catalog results