Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Sean M. DeGuire"'
Autor:
Hilal A. Lashuel, Anne-Laure Mahul-Mellier, Salvatore Novello, Ramanath Narayana Hegde, Yllza Jasiqi, Melek Firat Altay, Sonia Donzelli, Sean M. DeGuire, Ritwik Burai, Pedro Magalhães, Anass Chiki, Jonathan Ricci, Manel Boussouf, Ahmed Sadek, Erik Stoops, Christian Iseli, Nicolas Guex
Publikováno v:
npj Parkinson's Disease, Vol 8, Iss 1, Pp 1-19 (2022)
Abstract Antibodies against phosphorylated alpha-synuclein (aSyn) at S129 have emerged as the primary tools to investigate, monitor, and quantify aSyn pathology in the brain and peripheral tissues of patients with Parkinson’s disease and other neur
Externí odkaz:
https://doaj.org/article/ccd4a55ef8a5402e84ee4c5adc02d9d4
Autor:
Manuel Daldin, Valentina Fodale, Cristina Cariulo, Lucia Azzollini, Margherita Verani, Paola Martufi, Maria Carolina Spiezia, Sean M. Deguire, Marta Cherubini, Douglas Macdonald, Andreas Weiss, Alberto Bresciani, Jean-Paul Gerard Vonsattel, Lara Petricca, J. Lawrence Marsh, Silvia Gines, Iolanda Santimone, Massimo Marano, Hilal A. Lashuel, Ferdinando Squitieri, Andrea Caricasole
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-15 (2017)
Abstract Conformational changes in disease-associated or mutant proteins represent a key pathological aspect of Huntington’s disease (HD) and other protein misfolding diseases. Using immunoassays and biophysical approaches, we and others have recen
Externí odkaz:
https://doaj.org/article/28a4ca589dda4cb5b33f36313fe3c9c6
Autor:
Cristina Cariulo, Paola Martufi, Margherita Verani, Lucia Azzollini, Giordana Bruni, Andreas Weiss, Sean M. Deguire, Hilal A. Lashuel, Eugenia Scaricamazza, Giulia Maria Sancesario, Tommaso Schirinzi, Nicola Biagio Mercuri, Giuseppe Sancesario, Andrea Caricasole, Lara Petricca
Publikováno v:
Frontiers in Neuroscience, Vol 13 (2019)
Accumulation and aggregation of misfolded alpha-synuclein is believed to be a cause of Parkinson’s disease (PD). Phosphorylation of alpha-synuclein at S129 is known to be associated with the pathological misfolding process, but efforts to investiga
Externí odkaz:
https://doaj.org/article/1fd0919526c9414b8d75d8867779eee4
Autor:
Hilal A. Lashuel, Anne-Laure Mahul-Mellier, Salvatore Novello, Ramanath Narayana Hegde, Yllza Jasiqi, Melek Firat Altay, Sonia Donzelli, Sean M. DeGuire, Ritwik Burai, Pedro Magalhães, Anass Chiki, Jonathan Ricci, Manel Boussouf, Ahmed Sadek, Erik Stoops, Christian Iseli, Nicolas Guex
Alpha-synuclein (aSyn) within Lewy bodies, Lewy neurites, and other pathological hallmarks of Parkinson’s disease and synucleinopathies have consistently been shown to accumulate in aggregated and phosphorylated forms of the protein, predominantly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ece1a363e47d9f98b078b7ec801c4b5b
https://doi.org/10.1101/2022.03.30.486322
https://doi.org/10.1101/2022.03.30.486322
Autor:
Margherita Verani, Paola Martufi, Celia Dominguez, Ramee Lee, Lara Petricca, Raffaele Ingenito, Cristina Cariulo, Daniel J. Lavery, Marco Finotto, Leticia Toledo-Sherman, Sean M. DeGuire, Andrea Caricasole, Thomas F. Vogt, Elizabeth M. Doherty, Hilal A. Lashuel
Publikováno v:
Biochemical and Biophysical Research Communications. 521:549-554
Huntington's disease (HD) is a progressive neurodegenerative disorder caused by an expansion of a CAG triplet repeat (encoding for a polyglutamine tract) within the first exon of the huntingtin gene. Expression of the mutant huntingtin (mHTT) protein
Autor:
Hilal A. Lashuel, Giovanni Dietler, Urszula Cendrowska, Anass Chiki, Sean M. DeGuire, Nathan Riguet, Francesco S. Ruggeri, Anne-Laure Mahul-Mellier, Sophie Vieweg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9f0613b886a2e99d7ccb78bc654fc96f
https://doi.org/10.15252/rc.2022402060
https://doi.org/10.15252/rc.2022402060
Autor:
Mohamed Bilal Fares, Francesco Simone Ruggeri, Urszula Cendrowska, Hilal A. Lashuel, Giovanni Dietler, Anass Chiki, Sean M. DeGuire
Publikováno v:
Journal of Biological Chemistry 293 (2018) 48
Journal of Biological Chemistry, 293(48), 18540-18558
The Journal of Biological Chemistry
Journal of Biological Chemistry, 293(48), 18540-18558
The Journal of Biological Chemistry
Huntington's disease is a fatal neurodegenerative disorder resulting from a CAG repeat expansion in the first exon of the gene encoding the Huntingtin protein (Htt). Phosphorylation of this protein region (Httex1) has been shown to play important rol
Autor:
Urszula Cendrowska, Mohamed Bilal Fares, Giovanni Dietler, Francesco Simone Ruggeri, Hilal A. Lashuel, Sean M. DeGuire, Anass Chiki
Phosphorylation of exon1 of the Huntingtin protein (Httex1) has been shown to play important roles in regulating the structure, toxicity and cellular properties of N-terminal fragments and the full-length Huntingtin protein. Here, we investigated and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7d3e935c44564395d9dc9ae9b74d965
https://doi.org/10.1101/358234
https://doi.org/10.1101/358234
Autor:
Sean M. DeGuire, Margherita Verani, Andrea Caricasole, Iolanda Santimone, Paola Martufi, Silvia Ginés, Lara Petricca, Elena Cattaneo, Anass Chiki, Roberto Boggio, Marta Cherubini, Lucia Azzollini, Cristina Cariulo, Ferdinando Squitieri, Paola Conforti, Hilal A. Lashuel, J. Lawrence Marsh
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance The findings in this manuscript report on the identification of a posttranslational modification in the huntingtin protein (phosphorylation on residue T3 in the N17 region of the protein), which can revert the conformational effects of t
Autor:
Brian O. Bachmann, David W. Piston, Alessandro Ustione, David C. Earl, Aaron T. Jacobs, Sean M. DeGuire, Brenda A. Crews, Lawrence J. Marnett, Katherine M. Chong, Gary A. Sulikowski, Yu Du, Cristina Daniel
Publikováno v:
Angewandte Chemie International Edition. 54:961-964
Apoptolidin A has been described as among the top 0.1% most cell selective cytotoxic agents to be evaluated in the NCI 60 cell line panel. The molecular structure of apoptolidin A consists of a 20-membered macrolide with mono- and disaccharide moieti