F
Fabrizio Tagliavini
Researcher at Carlo Besta Neurological Institute
Publications - 422
Citations - 21532
Fabrizio Tagliavini is an academic researcher from Carlo Besta Neurological Institute. The author has contributed to research in topics: Frontotemporal dementia & Amyloid. The author has an hindex of 73, co-authored 380 publications receiving 18785 citations. Previous affiliations of Fabrizio Tagliavini include University of Parma & Laval University.
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Journal ArticleDOI
Staging of Neurofibrillary Pathology in Alzheimer's Disease: A Study of the BrainNet Europe Consortium
Irina Alafuzoff,Thomas Arzberger,Safa Al-Sarraj,Istvan Bodi,Nenad Bogdanovic,Heiko Braak,Orso Bugiani,Kelly Del-Tredici,Isidro Ferrer,Ellen Gelpi,Giorgio Giaccone,Manuel B. Graeber,Paul G. Ince,Wouter Kamphorst,Andrew T. King,Penelope Korkolopoulou,Gabor G. Kovacs,Sergey Larionov,David Meyronet,Camelia M. Monoranu,Piero Parchi,Efstratios Patsouris,Wolfgang Roggendorf,Danielle Seilhean,Fabrizio Tagliavini,Christine Stadelmann,Nathalie Streichenberger,Dietmar Rudolf Thal,Dietmar Rudolf Thal,Stephen B. Wharton,Hans A. Kretzschmar +30 more
TL;DR: The results indicate that good agreement can be reached when the lesions are substantial, i.e., the lesions have reached isocortical structures, whereas when only mild subtle lesions were present the agreement was poorer, and it is strongly recommended that the assessment of lesions should be carried out by at least two independent observers.
Journal ArticleDOI
Apoptosis mediated neurotoxicity induced by chronic application of β amyloid fragment 25–35
Gianluigi Forloni,Roberto Chiesa,S. Smiroldo,Laura Verga,Mario Salmona,Fabrizio Tagliavini,Nadia Angeretti +6 more
TL;DR: The results confirm the potential pathogenic role of A beta in AD, and indicate that amyloid fibrils may induce neuronal death through a specific programmed process.
Journal ArticleDOI
Aging-related tau astrogliopathy (ARTAG): harmonized evaluation strategy
Gabor G. Kovacs,Isidro Ferrer,Lea T. Grinberg,Lea T. Grinberg,Irina Alafuzoff,Johannes Attems,Herbert Budka,Nigel J. Cairns,John F. Crary,Charles Duyckaerts,Bernardino Ghetti,Glenda M. Halliday,James W. Ironside,Seth Love,Ian R. A. Mackenzie,David G. Munoz,Melissa E. Murray,Peter T. Nelson,Hitoshi Takahashi,John Q. Trojanowski,Olaf Ansorge,Thomas Arzberger,Atik Baborie,Thomas G. Beach,Kevin F. Bieniek,Eileen H. Bigio,Istvan Bodi,Brittany N. Dugger,Mel B. Feany,Ellen Gelpi,Stephen M. Gentleman,Giorgio Giaccone,Kimmo J. Hatanpaa,Richard Heale,Patrick R. Hof,Monika Hofer,Tibor Hortobágyi,Kurt A. Jellinger,Gregory A. Jicha,Paul G. Ince,Julia Kofler,Eniko Veronika Kovari,Jillian J. Kril,David M. A. Mann,Radoslav Matej,Ann C. McKee,Catriona McLean,Ivan Milenkovic,Thomas J. Montine,Shigeo Murayama,Edward B. Lee,Jasmin Rahimi,Roberta Diehl Rodriguez,Annemieke J.M. Rozemuller,Julie A. Schneider,Christian Schultz,William W. Seeley,Danielle Seilhean,Colin Smith,Fabrizio Tagliavini,Masaki Takao,Dietmar Rudolf Thal,Dietmar Rudolf Thal,Jon B. Toledo,Markus Tolnay,Juan C. Troncoso,Harry V. Vinters,Serge Weis,Stephen B. Wharton,Charles L. White,Thomas Wisniewski,John Woulfe,Masahito Yamada,Dennis W. Dickson +73 more
Abstract: Pathological accumulation of abnormally phosphorylated tau protein in astrocytes is a frequent, but poorly characterized feature of the aging brain. Its etiology is uncertain, but its presence is sufficiently ubiquitous to merit further characterization and classification, which may stimulate clinicopathological studies and research into its pathobiology. This paper aims to harmonize evaluation and nomenclature of aging-related tau astrogliopathy (ARTAG), a term that refers to a morphological spectrum of astroglial pathology detected by tau immunohistochemistry, especially with phosphorylation-dependent and 4R isoform-specific antibodies. ARTAG occurs mainly, but not exclusively, in individuals over 60 years of age. Tau-immunoreactive astrocytes in ARTAG include thorn-shaped astrocytes at the glia limitans and in white matter, as well as solitary or clustered astrocytes with perinuclear cytoplasmic tau immunoreactivity that extends into the astroglial processes as fine fibrillar or granular immunopositivity, typically in gray matter. Various forms of ARTAG may coexist in the same brain and might reflect different pathogenic processes. Based on morphology and anatomical distribution, ARTAG can be distinguished from primary tauopathies, but may be concurrent with primary tauopathies or other disorders. We recommend four steps for evaluation of ARTAG: (1) identification of five types based on the location of either morphologies of tau astrogliopathy: subpial, subependymal, perivascular, white matter, gray matter; (2) documentation of the regional involvement: medial temporal lobe, lobar (frontal, parietal, occipital, lateral temporal), subcortical, brainstem; (3) documentation of the severity of tau astrogliopathy; and (4) description of subregional involvement. Some types of ARTAG may underlie neurological symptoms; however, the clinical significance of ARTAG is currently uncertain and awaits further studies. The goal of this proposal is to raise awareness of astroglial tau pathology in the aged brain, facilitating communication among neuropathologists and researchers, and informing interpretation of clinical biomarkers and imaging studies that focus on tau-related indicators.
Journal ArticleDOI
Sporadic human prion diseases: molecular insights and diagnosis
Gianfranco Puoti,Alberto Bizzi,Gianluigi Forloni,Jiri G. Safar,Fabrizio Tagliavini,Pierluigi Gambetti +5 more
TL;DR: An accurate and timely diagnosis depends on careful clinical examination and early performance and interpretation of diagnostic tests, including electroencephalography, quantitative assessment of the surrogate markers 14-3-3, tau, and of the prion protein in the CSF, and neuroimaging.
Journal ArticleDOI
Reversion of prion protein conformational changes by synthetic b-sheet breaker peptides
Claudio Soto,Richard J. Kascsak,Gabriela P. Saborio,Pierre Aucouturier,Thomas Wisniewski,Frances Prelli,Regina Kascsak,Enrique Méndez,David A. Harris,James W. Ironside,Fabrizio Tagliavini,Richard I. Carp,Blas Frangione +12 more
TL;DR: Beta-sheet breaker peptides reverse PrP conformational changes implicated in the pathogenesis of spongiform encephalopathies and might represent a novel therapeutic approach for prion-related disorders.