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21 results on '"Scialò, Carlo"'

3. Clinical epidemiology of amyotrophic lateral sclerosis in Liguria, Italy: a ten year follow up study.

Author

Cabona, Corrado, Ferraro, Pilar Maria, Scialò, Carlo, Bandettini Di Poggio, Monica, Novi, Giovanni, Gemelli, Chiara, Vignolo, Manuela, Rao, Fabrizio, Capovilla, Marina, Marogna, Maura, Mandich, Paola, Origone, Paola, Schenone, Angelo, and Caponnetto, Claudia

Subjects
AMYOTROPHIC lateral sclerosis, CLINICAL epidemiology, FOLLOW-up studies (Medicine), PERCUTANEOUS endoscopic gastrostomy, DELAYED diagnosis
Abstract

This article presents an updated analysis of the LIGALS register, a prospective study conducted over a ten-year period (2009-2018) in Liguria, Italy, aimed at evaluating the incidence, prevalence, clinical presentation, and management of amyotrophic lateral sclerosis (ALS). We calculated the mean annual crude incidence rate of ALS, assessed the point prevalence of ALS on January 1, 2018, and analyzed demographic factors, clinical characteristics, and clinical management strategies. Data analysis included Cox regression analysis to identify predictors of survival. The mean annual crude incidence rate of ALS was 3.16/100,000 per year (CI 95%) while the point prevalence of ALS on January 1, 2018, was 9.31/100,000 population (CI 95%). Among the patients, 6.5% were familial ALS, while 93.5% were sporadic cases. Clinical management strategies, including percutaneous endoscopic gastrostomy (PEG) and noninvasive ventilation (NIV), were employed. The study observed a stable frequency of NIV initiation and PEG placement over time, with a growing trend toward earlier PEG positioning. The mean survival from symptom onset was 39 months, whereas from diagnosis, it was 26 months. Cox regression analysis identified several predictors of survival, including gender, age at onset and diagnosis, site of onset, diagnostic category, phenotype, and diagnostic delay. This comprehensive analysis provides valuable insights into the long-term trends in ALS epidemiology and clinical management in Liguria, Italy. It underscores the importance of continued research efforts in understanding and addressing the challenges posed by ALS, particularly in terms of early diagnosis and optimizing clinical interventions to improve patient outcomes. [ABSTRACT FROM AUTHOR]

Published
2024
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4. Comorbidity of dementia with amyotrophic lateral sclerosis (ALS): insights from a large multicenter Italian cohort

Author

Trojsi, Francesca, Siciliano, Mattia, Femiano, Cinzia, Santangelo, Gabriella, Lunetta, Christian, Calvo, Andrea, Moglia, Cristina, Marinou, Kalliopi, Ticozzi, Nicola, Drago Ferrante, Gianluca, Scialò, Carlo, Sorarù, Gianni, Conte, Amelia, Falzone, Yuri M., Tortelli, Rosanna, Russo, Massimo, Sansone, Valeria Ada, Chiò, Adriano, Mora, Gabriele, Poletti, Barbara, Volanti, Paolo, Caponnetto, Claudia, Querin, Giorgia, Sabatelli, Mario, Riva, Nilo, Logroscino, Giancarlo, Messina, Sonia, Fasano, Antonio, Monsurrò, Maria Rosaria, Tedeschi, Gioacchino, and Mandrioli, Jessica

Published
2017
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6. A PET/CT approach to spinal cord metabolism in amyotrophic lateral sclerosis

Author

Marini, Cecilia, Cistaro, Angelina, Campi, Cristina, Calvo, Andrea, Caponnetto, Claudia, Nobili, Flavio Mariano, Fania, Piercarlo, Beltrametti, Mauro C., Moglia, Cristina, Novi, Giovanni, Buschiazzo, Ambra, Perasso, Annalisa, Canosa, Antonio, Scialò, Carlo, Pomposelli, Elena, Massone, Anna Maria, Bagnara, Maria Caludia, Cammarosano, Stefania, Bruzzi, Paolo, Morbelli, Silvia, Sambuceti, Gianmario, Mancardi, Gianluigi, Piana, Michele, and Chiò, Adriano

Published
2016
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8. Erythropoietin in amyotrophic lateral sclerosis: a multicentre, randomised, double blind, placebo controlled, phase III study

Author

Lauria, Giuseppe, Dalla Bella, Eleonora, Antonini, Giovanni, Borghero, Giuseppe, Capasso, Margherita, Caponnetto, Claudia, Chiò, Adriano, Corbo, Massimo, Eleopra, Roberto, Fazio, Raffaella, Filosto, Massimiliano, Giannini, Fabio, Granieri, Enrico, La Bella, Vincenzo, Logroscino, Giancarlo, Mandrioli, Jessica, Mazzini, Letizia, Monsurrò, Maria Rosaria, Mora, Gabriele, Pietrini, Vladimiro, Quatrale, Rocco, Rizzi, Romana, Salvi, Fabrizio, Siciliano, Gabriele, Sorarù, Gianni, Volanti, Paolo, Tramacere, Irene, Filippini, Graziella, Cazzato, Daniele, Cesnik, Edward, Groppo, Elisabetta, Sette, Elisabetta, Pani, Carla, Costantino, Emanuela, Orlandini, Francesco, Boi, Daniela, Querin, Giorgia, DʼAscenzo, Carla, Sagnelli, Anna, Piccirillo, Giovanni, Aiello, Marina, Chetta, Alfredo, Grassi, Andrea, Lunetta, Christian, Maestri, Eleonora, Padovani, Alessandro, Cotelli, Mariasofia, Todeschini, Alice, Morino, Stefania, Di Pasquale, Antonella, Latino, Pamela, Casali, Stefania, Battistini, Stefania, Pirrelli, Marilena, Cantello, Roberto, Nasuelli, Nicola, Servo, Serena, De Gennaro, Riccardo, Gastaldo, Ernesto, Georgoulopoulou, Eleni, Fini, Nicola, Taiello, Alfonsa C., Colletti, Tiziana, Calvo, Andrea, Moglia, Cristina, Fuda, Giuseppe, Marinou, Kalliopi, Riva, Nilo, Cerri, Federica, Lopez, Ignazio D., De Cicco, Domenico, Battaglia, Gianluca, Marcello, Norina, Rinaldi, Manuela, Scialò, Carlo, Mantero, Vittorio, Mascolo, Maria, Carlesi, Cecilia, Caldarazzo Ienco, Elena, Di Muzio, Antonio, Verriello, Lorenzo, DʼAmico, Delia, Simone, Isabella L., Tortelli, Rosanna, Cortese, Rosa, and Bartolomei, Ilaria

Published
2015
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11. TDP-43 real-time quaking induced conversion reaction optimization and detection of seeding activity in CSF of amyotrophic lateral sclerosis and frontotemporal dementia patients

Author

Scialò, Carlo, primary, Tran, Thanh Hoa, additional, Salzano, Giulia, additional, Novi, Giovanni, additional, Caponnetto, Claudia, additional, Chiò, Adriano, additional, Calvo, Andrea, additional, Canosa, Antonio, additional, Moda, Fabio, additional, Caroppo, Paola, additional, Silani, Vincenzo, additional, Ticozzi, Nicola, additional, Ratti, Antonia, additional, Borroni, Barbara, additional, Benussi, Luisa, additional, Ghidoni, Roberta, additional, Furlanis, Giovanni, additional, Manganotti, Paolo, additional, Senigagliesi, Beatrice, additional, Parisse, Pietro, additional, Brasselet, Romain, additional, Buratti, Emanuele, additional, and Legname, Giuseppe, additional

Published
2020
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14. Comparative Analysis of C9orf72 and Sporadic Disease in a Large Multicenter ALS Population: The Effect of Male Sex on Survival of C9orf72 Positive Patients

Author

Trojsi, Francesca, primary, Siciliano, Mattia, additional, Femiano, Cinzia, additional, Santangelo, Gabriella, additional, Lunetta, Christian, additional, Calvo, Andrea, additional, Moglia, Cristina, additional, Marinou, Kalliopi, additional, Ticozzi, Nicola, additional, Ferro, Christian, additional, Scialò, Carlo, additional, Sorarù, Gianni, additional, Conte, Amelia, additional, Falzone, Yuri M., additional, Tortelli, Rosanna, additional, Russo, Massimo, additional, Sansone, Valeria Ada, additional, Chiò, Adriano, additional, Mora, Gabriele, additional, Silani, Vincenzo, additional, Volanti, Paolo, additional, Caponnetto, Claudia, additional, Querin, Giorgia, additional, Sabatelli, Mario, additional, Riva, Nilo, additional, Logroscino, Giancarlo, additional, Messina, Sonia, additional, Fasano, Antonio, additional, Monsurrò, Maria Rosaria, additional, Tedeschi, Gioacchino, additional, and Mandrioli, Jessica, additional

Published
2019
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18. Agomelatine Improves Apathy in Frontotemporal Dementia

Author

Callegari, Ilaria, primary, Mattei, Chiara, additional, Benassi, Francesca, additional, Krueger, Frank, additional, Grafman, Jordan, additional, Yaldizli, Özgür, additional, Sassos, Davide, additional, Massucco, Davide, additional, Scialò, Carlo, additional, Nobili, Flavio, additional, Serrati, Carlo, additional, Amore, Mario, additional, Cocito, Leonardo, additional, Emberti Gialloreti, Leonardo, additional, and Pardini, Matteo, additional

Published
2016
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20. Prion and Prion-Like Protein Strains: Deciphering the Molecular Basis of Heterogeneity in Neurodegeneration

Author

Paolo Manganotti, Carlo Scialò, Giuseppe Legname, Elena De Cecco, Scialò, Carlo, De Cecco, Elena, Manganotti, Paolo, and Legname, Giuseppe

Subjects
0301 basic medicine, Protein Folding, Amyloid beta-Peptide, animal diseases, lcsh:QR1-502, Review, lcsh:Microbiology, Strain, prion-like proteins, Mice, 0302 clinical medicine, Settore BIO/10 - Biochimica, Infectivity, Genetics, education.field_of_study, Neurodegeneration, neurodegeneration, Neurodegenerative Diseases, DNA-Binding Proteins, Infectious Diseases, Prion, Protein folding, Human, Prions, DNA-Binding Protein, Population, Prion-like proteins, Strains, Amyloid beta-Peptides, Animals, Disease Models, Animal, Humans, Prion Proteins, tau Proteins, Context (language use), Biology, Prion Protein, DNA-binding protein, prion, strains, 03 medical and health sciences, Virology, medicine, education, Neurodegenerative Disease, Mechanism (biology), Animal, Prion-like protein, medicine.disease, nervous system diseases, 030104 developmental biology, Disease Models, Adaptation, 030217 neurology & neurosurgery
Abstract

Increasing evidence suggests that neurodegenerative disorders share a common pathogenic feature: the presence of deposits of misfolded proteins with altered physicochemical properties in the Central Nervous System. Despite a lack of infectivity, experimental data show that the replication and propagation of neurodegenerative disease-related proteins including amyloid-β (Aβ), tau, α-synuclein and the transactive response DNA-binding protein of 43 kDa (TDP-43) share a similar pathological mechanism with prions. These observations have led to the terminology of “prion-like” to distinguish between conditions with noninfectious characteristics but similarities with the prion replication and propagation process. Prions are considered to adapt their conformation to changes in the context of the environment of replication. This process is known as either prion selection or adaptation, where a distinct conformer present in the initial prion population with higher propensity to propagate in the new environment is able to prevail over the others during the replication process. In the last years, many studies have shown that prion-like proteins share not only the prion replication paradigm but also the specific ability to aggregate in different conformations, i.e., strains, with relevant clinical, diagnostic and therapeutic implications. This review focuses on the molecular basis of the strain phenomenon in prion and prion-like proteins.

Published
2019

21. The role of the cellular prion protein in the uptake and toxic signaling of pathological neurodegenerative aggregates.

Author

Scialò C and Legname G

Subjects
Amyloid beta-Peptides toxicity, Animals, Humans, Prion Proteins chemistry, Prion Proteins toxicity, alpha-Synuclein toxicity, Neurodegenerative Diseases pathology, Prion Proteins metabolism, Protein Aggregates, Signal Transduction
Abstract

Neurodegenerative disorders are invariably associated with intra- or extra-cellular deposition of aggregates composed of misfolded insoluble proteins. These deposits composed of tau, amyloid-β or α-synuclein spread from cell to cell, in a prion-like manner. Emerging evidence suggests that the circulating soluble species of these misfolded proteins (usually referred as oligomers) could play a major role in pathology, while insoluble aggregates would represent their protective less toxic counterparts. Convincing data support the hypothesis that the cellular prion protein, PrP C , act as a toxicity-transducing receptor for amyloid-β oligomers. As a consequence, several studies extended investigations to the role played by PrP C in binding aggregates of proteins other than Aβ, such as tau and α-synuclein, for its possible common role in mediating toxic signaling. A better characterization of the biological relevance of PrP C as key ligand and potential mediator of toxicity for multiple proteinaceous aggregated species, prions or PrP Sc included, would bring relevant therapeutic implications. Here we will first describe the structure of the prion protein and the hypothesized interplay with its pathological counterpart PrP Sc and then we will recapitulate the most relevant discoveries regarding the role of PrP C in the interaction with aggregated forms of other neurodegeneration-associated proteins., (© 2020 Elsevier Inc. All rights reserved.)

Published
2020
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