Zobrazeno 1 - 10
of 72
pro vyhledávání: '"Roberta Cascella"'
Autor:
Alessandra Bigi, Giulia Fani, Valentina Bessi, Liliana Napolitano, Silvia Bagnoli, Assunta Ingannato, Lorenzo Neri, Roberta Cascella, Paolo Matteini, Sandro Sorbi, Benedetta Nacmias, Cristina Cecchi, Fabrizio Chiti
Publikováno v:
Translational Neurodegeneration, Vol 13, Iss 1, Pp 1-5 (2024)
Externí odkaz:
https://doaj.org/article/47ee1919563b4474a43a02c85f006f48
Autor:
Panagis Polykretis, Cristiano D’Andrea, Martina Banchelli, Liliana Napolitano, Roberta Cascella, Marella de Angelis, Paolo Matteini
Publikováno v:
Frontiers in Molecular Biosciences, Vol 11 (2024)
Introduction: Alzheimer’s disease (AD) is a progressive debilitating neurological disorder representing the most common neurodegenerative disease worldwide. Although the exact pathogenic mechanisms of AD remain unresolved, the presence of extracell
Externí odkaz:
https://doaj.org/article/dce15d66ff4e4beb8d050cb8c9361eb1
A single-domain antibody detects and neutralises toxic Aβ42 oligomers in the Alzheimer’s disease CSF
Autor:
Alessandra Bigi, Liliana Napolitano, Devkee M. Vadukul, Fabrizio Chiti, Cristina Cecchi, Francesco A. Aprile, Roberta Cascella
Publikováno v:
Alzheimer’s Research & Therapy, Vol 16, Iss 1, Pp 1-19 (2024)
Abstract Background Amyloid-β42 (Aβ42) aggregation consists of a complex chain of nucleation events producing soluble oligomeric intermediates, which are considered the major neurotoxic agents in Alzheimer’s disease (AD). Cerebral lesions in the
Externí odkaz:
https://doaj.org/article/e31cb433d4c24d6992d739c228d88a50
Autor:
Roberta Cascella, Martina Banchelli, Seyyed Abolghasem Ghadami, Diletta Ami, Maria Cristina Gagliani, Alessandra Bigi, Tommaso Staderini, Davide Tampellini, Katia Cortese, Cristina Cecchi, Antonino Natalello, Hadi Adibi, Paolo Matteini, Fabrizio Chiti
Publikováno v:
Annals of Medicine, Vol 55, Iss 1, Pp 72-88 (2023)
AbstractIntroduction: Several neurodegenerative conditions are associated with a common histopathology within neurons of the central nervous system, consisting of the deposition of cytoplasmic inclusions of TAR DNA-binding protein 43 (TDP-43). Such i
Externí odkaz:
https://doaj.org/article/7e364bb09819442fa3a62e822f0fa695
Publikováno v:
Neural Regeneration Research, Vol 18, Iss 11, Pp 2332-2342 (2023)
The misfolding and aggregation of α-synuclein is the general hallmark of a group of devastating neurodegenerative pathologies referred to as synucleinopathies, such as Parkinson’s disease, dementia with Lewy bodies, and multiple system atrophy. In
Externí odkaz:
https://doaj.org/article/f9aec9d61e1f481d9eaab50c51f933cf
Autor:
Claudia Capitini, Alessandra Bigi, Niccolò Parenti, Marco Emanuele, Niccolò Bianchi, Roberta Cascella, Cristina Cecchi, Laura Maggi, Francesco Annunziato, Francesco Saverio Pavone, Martino Calamai
Publikováno v:
iScience, Vol 26, Iss 5, Pp 106611- (2023)
Summary: High cholesterol levels are a risk factor for the development of Alzheimer’s disease. Experiments investigating the influence of cholesterol on the proteolytic processing of the amyloid precursor protein (APP) by the β-secretase Bace1 and
Externí odkaz:
https://doaj.org/article/e5cdfea39b1f486bb26e475a39847fc9
Autor:
Roberta Cascella, Serene W. Chen, Alessandra Bigi, José D. Camino, Catherine K. Xu, Christopher M. Dobson, Fabrizio Chiti, Nunilo Cremades, Cristina Cecchi
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
The self-assembly of α-synuclein (αS) is a pathological feature of Parkinson’s disease. The αS species responsible for neuronal damage are not well characterized. Here, the authors show that αS fibrils release soluble prefibrillar oligomeric sp
Externí odkaz:
https://doaj.org/article/c2f2c92ceab748c787667121d9608d0b
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 9, p 7974 (2023)
The aberrant aggregation of specific peptides and proteins is the common feature of a range of more than 50 human pathologies, collectively referred to as protein misfolding diseases [...]
Externí odkaz:
https://doaj.org/article/da726f11b51c41229c96aac97accb1fe
Autor:
Ryan Limbocker, Roxine Staats, Sean Chia, Francesco S. Ruggeri, Benedetta Mannini, Catherine K. Xu, Michele Perni, Roberta Cascella, Alessandra Bigi, Liam R. Sasser, Natalie R. Block, Aidan K. Wright, Ryan P. Kreiser, Edward T. Custy, Georg Meisl, Silvia Errico, Johnny Habchi, Patrick Flagmeier, Tadas Kartanas, Jared E. Hollows, Lam T. Nguyen, Kathleen LeForte, Denise Barbut, Janet R. Kumita, Cristina Cecchi, Michael Zasloff, Tuomas P. J. Knowles, Christopher M. Dobson, Fabrizio Chiti, Michele Vendruscolo
Publikováno v:
Frontiers in Neuroscience, Vol 15 (2021)
The aberrant aggregation of proteins is a key molecular event in the development and progression of a wide range of neurodegenerative disorders. We have shown previously that squalamine and trodusquemine, two natural products in the aminosterol class
Externí odkaz:
https://doaj.org/article/dd03b8d056964d40bab6c08d74df6acb
Autor:
Ryan Limbocker, Sean Chia, Francesco S. Ruggeri, Michele Perni, Roberta Cascella, Gabriella T. Heller, Georg Meisl, Benedetta Mannini, Johnny Habchi, Thomas C. T. Michaels, Pavan K. Challa, Minkoo Ahn, Samuel T. Casford, Nilumi Fernando, Catherine K. Xu, Nina D. Kloss, Samuel I. A. Cohen, Janet R. Kumita, Cristina Cecchi, Michael Zasloff, Sara Linse, Tuomas P. J. Knowles, Fabrizio Chiti, Michele Vendruscolo, Christopher M. Dobson
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
Transient oligomeric species of the amyloid-β peptide (Aβ42) have been identified as key pathogenic agents in Alzheimer’s disease. Here the authors find that the aminosterol trodusquemine enhances Aβ42 aggregation and suppresses Aβ42-induced to
Externí odkaz:
https://doaj.org/article/e4aca3eea6e44315b03de5b6488da79d