Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Stefania Santarelli"'
Autor:
Stefania Santarelli, Chiara Londero, Alessia Soldano, Carlotta Candelaresi, Leonardo Todeschini, Luisa Vernizzi, Paola Bellosta
Publikováno v:
Frontiers in Neuroscience, Vol 17 (2023)
Proteinopathies are a large group of neurodegenerative diseases caused by both genetic and sporadic mutations in particular genes which can lead to alterations of the protein structure and to the formation of aggregates, especially toxic for neurons.
Externí odkaz:
https://doaj.org/article/0ca74545f77645b299efe7a2110cd2b4
Autor:
Luisa Vernizzi, Chiara Paiardi, Giusimaria Licata, Teresa Vitali, Stefania Santarelli, Martino Raneli, Vera Manelli, Manuela Rizzetto, Mariarosa Gioria, Maria E. Pasini, Daniela Grifoni, Maria A. Vanoni, Cinzia Gellera, Franco Taroni, Paola Bellosta
Publikováno v:
Cells, Vol 9, Iss 1, p 196 (2020)
Glutamine Synthetase 1 (GS1) is a key enzyme that catalyzes the ATP-dependent synthesis of l-glutamine from l-glutamate and is also member of the Glutamate Glutamine Cycle, a complex physiological process between glia and neurons that controls glutam
Externí odkaz:
https://doaj.org/article/b0c23f7ef2ed4f918a4713db0e37249d
Autor:
Francesca Destefanis, Valeria Manara, Stefania Santarelli, Sheri Zola, Marco Brambilla, Giacomo Viola, Paola Maragno, Ilaria Signoria, Gabriella Viero, Maria Enrica Pasini, Marianna Penzo, Paola Bellosta
Publikováno v:
Journal of Cell Science. 135
NOC1 is a nucleolar protein necessary in yeast for both transport and maturation of ribosomal subunits. Here, we show that Drosophila NOC1 (annotated CG7839) is necessary for rRNAs maturation and for a correct animal development. Its ubiquitous downr
Autor:
Stefania Santarelli, Carlotta Candelaresi, Leonardo Todeschini, Chiara Londero, Paola Bellosta
Publikováno v:
I: Experimental therapeutics – preclinical.
Publikováno v:
I: Experimental therapeutics – preclinical.
Autophagy is a fundamental cellular pathway involved in the clearance of protein aggregates, and it is particularly important in neurons. The toxic aggregates derived from the mutated Huntingtin have been shown to interfere with the physiological aut
Autor:
Martino Raneli, Stefania Santarelli, Paola Bellosta, G. Licata, Maria A. Vanoni, Chiara Paiardi, Cinzia Gellera, Daniela Grifoni, Maria Enrica Pasini, Luisa Vernizzi, Mariarosa Gioria, Vera Manelli, Manuela Rizzetto, Teresa Vitali, Franco Taroni
Publikováno v:
Cells
Volume 9
Issue 1
Cells, Vol 9, Iss 1, p 196 (2020)
Volume 9
Issue 1
Cells, Vol 9, Iss 1, p 196 (2020)
Glutamine Synthetase 1 (GS1) is a key enzyme that catalyzes the ATP-dependent synthesis of l-glutamine from l-glutamate and is also member of the Glutamate Glutamine Cycle, a complex physiological process between glia and neurons that controls glutam
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b5eee7ae8eea859b611655067a904b6
http://hdl.handle.net/11572/248388
http://hdl.handle.net/11572/248388
Autor:
Luisa, Vernizzi, Chiara, Paiardi, Giusimaria, Licata, Teresa, Vitali, Stefania, Santarelli, Martino, Raneli, Vera, Manelli, Manuela, Rizzetto, Mariarosa, Gioria, Maria E, Pasini, Daniela, Grifoni, Maria A, Vanoni, Cinzia, Gellera, Franco, Taroni, Paola, Bellosta
Publikováno v:
Cells
Glutamine Synthetase 1 (GS1) is a key enzyme that catalyzes the ATP-dependent synthesis of l-glutamine from l-glutamate and is also member of the Glutamate Glutamine Cycle, a complex physiological process between glia and neurons that controls glutam
Autor:
L. Vernizzi, Franco Taroni, Stefania Santarelli, Paola Bellosta, Martino Raneli, G. Licata, Manuela Rizzetto, Cinzia Gellera, Mariarosa Gioria, Manelli, Marco Vanoni, Maria Enrica Pasini, Daniela Grifoni, T. Vitali, Chiara Paiardi
Glutamine Synthetase1 (GS1) is an enzyme that catalyzes the ATP-dependent synthesis of L-glutamine from L-glutamate and ammonia as a key element of the glutamate glutamine cycle, a complex physiological process occurring between glia and neurons, nec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e0caf7cd095e733aa6ff742861f2ef1e