Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Eva Milanesi"'
Autor:
Paola Costantini, Raffaele Colonna, Anna Cabrelle, Cesura Andrea, Paolo Bernardi, Gianpietro Semenzato, Valeria Petronilli, Alberto Gambalunga, Emmanuel Pinard, Eva Milanesi
Publikováno v:
Journal of Biological Chemistry. 281:10066-10072
We have investigated the mitochondrial effects of BH3I-2', Chelerythrine, and HA14-1, small organic molecules that share the ability to bind the BH3 domain of BCL-2. All compounds displayed a biphasic effect on mitochondrial respiration with uncoupli
Autor:
Julius Liobikas, Paola Costantini, Ove Eriksson, Maria Panagiotaki, Lucedio Greci, Milena Johans, Marina Franck, Paolo Bernardi, Giovanni Principato, Christoffer Johans, Eva Milanesi, Paavo K.J. Kinnunen
Publikováno v:
Journal of Biological Chemistry. 280:12130-12136
Methylglyoxal and synthetic glyoxal derivatives react covalently with arginine residue(s) on the mitochondrial permeability transition pore (PTP). In this study, we have investigated how the binding of a panel of synthetic phenylglyoxal derivatives i
Autor:
Vera Bianchi, Chiara Rampazzo, Peter Reichard, Katia Crovatto, Giovanna Pontarin, Eva Milanesi, Paola Ferraro, Lisa Gallinaro
Publikováno v:
Journal of Biological Chemistry. 277:35080-35087
Deoxynucleoside triphosphates (dNTPs) used for mitochondrial DNA replication are mainly formed by phosphorylation of deoxynucleosides imported into mitochondria from the cytosol. We earlier obtained evidence for a mitochondrial 5′-nucleotidase (dNT
Autor:
Saverio Minucci, Giacomo Carenzi, Agnese Abate, Manuela Villa, Andrea Colombo, Fabio Di Lisa, Mario Varasi, Alessandra Saccani, Stefania Gagliardi, Anna Cappa, Marco Ballarini, Raffaella Amici, Cristina Contursi, Pier Giuseppe Pelicci, Paolo Bernardi, Simon Plyte, Daniele Fancelli, Mariangela Storto, Gilles Pain, Eva Milanesi, Florian Thaler, Giulio Dondio
In this account, we report the development of a series of substituted cinnamic anilides that represents a novel class of mitochondrial permeability transition pore (mPTP) inhibitors. Initial class expansion led to the establishment of the basic struc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c77e620ef49425f74f43740fb325e475
http://hdl.handle.net/11577/3228236
http://hdl.handle.net/11577/3228236
Autor:
Cesare Montecucco, Marco Paoli, Paolo Bernardi, Paola Caccin, Michela Rigoni, Andrea Rasola, Eva Milanesi
Snake presynaptic neurotoxins with phospholipase A2 activity are potent inducers of paralysis through inhibition of the neuromuscular junction. These neurotoxins were recently shown to induce exocytosis of synaptic vesicles following the production o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afece18d45312b1b864174959dd3e05a
http://hdl.handle.net/11577/2506110
http://hdl.handle.net/11577/2506110
Autor:
Eva, Milanesi, Paola, Costantini, Alberto, Gambalunga, Raffaele, Colonna, Valeria, Petronilli, Anna, Cabrelle, Gianpietro, Semenzato, Andrea M, Cesura, Emmanuel, Pinard, Paolo, Bernardi
Publikováno v:
The Journal of biological chemistry. 281(15)
We have investigated the mitochondrial effects of BH3I-2', Chelerythrine, and HA14-1, small organic molecules that share the ability to bind the BH3 domain of BCL-2. All compounds displayed a biphasic effect on mitochondrial respiration with uncoupli
Autor:
Milena, Johans, Eva, Milanesi, Marina, Franck, Christoffer, Johans, Julius, Liobikas, Maria, Panagiotaki, Lucedio, Greci, Giovanni, Principato, Paavo K J, Kinnunen, Paolo, Bernardi, Paola, Costantini, Ove, Eriksson
Publikováno v:
The Journal of biological chemistry. 280(13)
Methylglyoxal and synthetic glyoxal derivatives react covalently with arginine residue(s) on the mitochondrial permeability transition pore (PTP). In this study, we have investigated how the binding of a panel of synthetic phenylglyoxal derivatives i
Autor:
Peter Reichard, Elisabetta Frigimelica, Vera Bianchi, Chiara Rampazzo, Eva Milanesi, Lisa Gallinaro
Three cytosolic and one plasma membrane-bound 5′-nucleotidases have been cloned and characterized. Their various substrate specificities suggest widely different functions in nucleotide metabolism. We now describe a 5′-nucleotidase in mitochondri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e362c9edd3cd78bf7888e6cd5b2d8f69
https://europepmc.org/articles/PMC26931/
https://europepmc.org/articles/PMC26931/