Zobrazeno 1 - 10
of 54
pro vyhledávání: '"Ersilia De Lorenzi"'
Autor:
Ersilia De Lorenzi, Davide Franceschini, Cecilia Contardi, Rita Maria Concetta Di Martino, Francesca Seghetti, Massimo Serra, Federica Bisceglia, Andrea Pagetta, Morena Zusso, Federica Belluti
Publikováno v:
International Journal of Molecular Sciences, Vol 23, Iss 8, p 4381 (2022)
Alzheimer’s disease (AD) is a progressive neurodegenerative disorder that is not restricted to the neuronal compartment but includes important interactions with immune cells, including microglia. Protein aggregates, common pathological hallmarks of
Externí odkaz:
https://doaj.org/article/2a8a2ea6d106484f8995e35f52ae06e4
Autor:
Ersilia De Lorenzi, Francesca Seghetti, Andrea Tarozzi, Letizia Pruccoli, Cecilia Contardi, Massimo Serra, Alessandra Bisi, Silvia Gobbi, Giulio Vistoli, Silvia Gervasoni, Carla Argentini, Giulia Ghirardo, Giulia Guarato, Genny Orso, Federica Belluti, Rita Maria Concetta Di Martino, Morena Zusso
Publikováno v:
European Journal of Medicinal Chemistry. 252:115297
Publikováno v:
European Journal of Organic Chemistry. 2020:3568-3575
Publikováno v:
European Journal of Organic Chemistry. 2019:732-741
Autor:
Antonino Natalello, Raffaella Colombo, Federica Bisceglia, Laura Verga, Cristina Lanni, Ersilia De Lorenzi, Melania Maria Serafini
Publikováno v:
Talanta. 188:17-26
Despite great efforts, it is not known which oligomeric population of amyloid beta (Aß) peptides is the main neurotoxic mediator in Alzheimer's disease. In vitro and in vivo experiments are challenging, mainly because of the high aggregation tendenc
Publikováno v:
The Journal of organic chemistry. 84(23)
Azabicyclo[4.3.0]- and [5.3.0]alkanone amino acid derivatives were easily prepared by submitting the same starting dipeptide to a direct ring-closing enyne metathesis or an ethylene-mediated cross-enyne metathesis/ring-closing metathesis, respectivel
Autor:
Simone Brogi, Stefania Butini, Samuele Maramai, Raffaella Colombo, Laura Verga, Cristina Lanni, Ersilia De Lorenzi, Stefania Lamponi, Marco Andreassi, Manuela Bartolini, Vincenza Andrisano, Giuseppe Campiani, Margherita Brindisi, Sandra Gemma, BRINDISI, MARGHERITA, NOVELLINO, ETTORE
Publikováno v:
CNS Neuroscience & Therapeutics. 20:624-632
Summary Aims We recently described multifunctional tools (2a–c) as potent inhibitors of human Cholinesterases (ChEs) also able to modulate events correlated with Aβ aggregation. We herein propose a thorough biological and computational analysis ai
Autor:
Laura Sola, Ersilia De Lorenzi, Jennifer Lin, Annelise E. Barron, Carlo Morasso, Marcella Chiari, Raffaella Colombo, Marina Cretich, Patrick L. McGeer, Paola Gagni, Renzo Vanna, Federica Bisceglia, Moonhee Lee
Publikováno v:
Journal of Alzheimer's disease 59 (2017): 1213–1226. doi:10.3233/JAD-170223
info:cnr-pdr/source/autori:De Lorenzi E.; Chiari M.; Colombo R.; Cretich M.; Sola L.; Vanna R.; Gagni P.; Bisceglia F.; Morasso C.; Lin J.S.; Lee M.; Mcgeer P.L.; Barron A.E./titolo:Evidence that the human innate immune peptide LL-37 may be a binding partner of amyloid-? and inhibitor of fibril assembly/doi:10.3233%2FJAD-170223/rivista:Journal of Alzheimer's disease/anno:2017/pagina_da:1213/pagina_a:1226/intervallo_pagine:1213–1226/volume:59
Journal of Alzheimer's Disease
info:cnr-pdr/source/autori:De Lorenzi E.; Chiari M.; Colombo R.; Cretich M.; Sola L.; Vanna R.; Gagni P.; Bisceglia F.; Morasso C.; Lin J.S.; Lee M.; Mcgeer P.L.; Barron A.E./titolo:Evidence that the human innate immune peptide LL-37 may be a binding partner of amyloid-? and inhibitor of fibril assembly/doi:10.3233%2FJAD-170223/rivista:Journal of Alzheimer's disease/anno:2017/pagina_da:1213/pagina_a:1226/intervallo_pagine:1213–1226/volume:59
Journal of Alzheimer's Disease
Background Identifying physiologically relevant binding partners of amyloid-β (Aβ) that modulate in vivo fibril formation may yield new insights into Alzheimer's disease (AD) etiology. Human cathelicidin peptide, LL-37, is an innate immune effector
Autor:
Giulio Vistoli, Ersilia De Lorenzi, Laura Verga, Cristina Lanni, Morena Zusso, Federica Bisceglia, Francesca Seghetti, Massimo Serra, Silvia Gervasoni, Federica Belluti, Michele Catanzaro
Alzheimer's disease is likely to be caused by copathogenic factors including aggregation of Aβ peptides into oligomers and fibrils, neuroinflammation, and oxidative stress. To date, no effective treatments are available, and because of the multifact
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14b5560ac3a9ed8dffe75e0e68b86dd2
http://hdl.handle.net/11585/724713
http://hdl.handle.net/11585/724713
Autor:
Elena Domínguez-Vega, Julie Schappler, Laura Bertoletti, Raffaella Colombo, Serge Rudaz, Ersilia De Lorenzi, Sara Raimondi, Govert W. Somsen, Rob Haselberg
Publikováno v:
Bertoletti, L, Schappler, J, Colombo, R, Rudaz, S, Haselberg, R, Dominguez Vega, E, Raimondi, S, Somsen, G W & De Lorenzi, E 2016, ' Evaluation of capillary electrophoresis-mass spectrometry for the analysis of the conformational heterogeneity of intact proteins using beta2-microglobulin as model compound. ', Analytica Chimica Acta, vol. 945, pp. 102-109 . https://doi.org/10.1016/j.aca.2016.10.010
Analytica Chimica Acta, 945, 102-109. Elsevier
Analytica Chimica Acta, 945, 102-109. Elsevier
In this work we explored the feasibility of different CE-ESI-MS set-ups for the analysis of conformational states of an intact protein. By using the same background electrolyte at quasi physiological conditions (50 mM ammonium bicarbonate, pH 7.4) a