Zobrazeno 1 - 10
of 944
pro vyhledávání: '"G. Rotilio"'
Autor:
G. Rotilio
Publikováno v:
Structure and Functions of Amine Oxidases ISBN: 9781351076951
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e4e08eb94129b1a5ffa4e2f20fec4a10
https://doi.org/10.1201/9781351076951-12
https://doi.org/10.1201/9781351076951-12
This study aims to elucidate the processes underlying neuroprotection of kaempferol in models of rotenone-induced acute toxicity. We demonstrate that kaempferol, but not quercetin, myricetin or resveratrol, protects SH-SY5Y cells and primary neurons
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______4034::eedf6c4565ea7a56f2ccb0c3b0094120
https://hdl.handle.net/11587/344451
https://hdl.handle.net/11587/344451
Autor:
G Rotilio, Katia Aquilano, Maria Rosa Ciriolo, Sara Baldelli, D Lettieri Barbato, Stefano Cannata, Sergio Bernardini
The nutrient-sensing lipolytic enzyme adipose triglyceride lipase (ATGL) has a key role in adipose tissue function, and alterations in its activity have been implicated in many age-related metabolic disorders. In adipose tissue reduced blood vessel d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b8617c4df96d079a7e0f36141a1f614
http://hdl.handle.net/2108/97227
http://hdl.handle.net/2108/97227
Publikováno v:
IUBMB Life. 50:309-314
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fa1dbce1e04a0c9cd79c6404f1fdc6e9
https://doi.org/10.1080/15216540051081074
https://doi.org/10.1080/15216540051081074
Autor:
G. Rotilio, Alessandro Desideri, Angelo Merli, Martino Bolognesi, Gian Luigi Rossi, Kristina Djinović-Carugo
Publikováno v:
Biochemical and Biophysical Research Communications. 210:1040-1044
The polarized absorption spectra of the cobalt chromophore in orthorhombic crystals of bovine Cu,Co superoxide dismutase (SOD), bearing the copper ion in both the oxidized and the reduced states, are reported together with the calculated isotropic sp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::135d19801aa21854dbd9a578aea97531
https://doi.org/10.1006/bbrc.1995.1761
https://doi.org/10.1006/bbrc.1995.1761
Publikováno v:
Journal of Magnetic Resonance, Series B. 105:91-94
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::913dc405fd29e31f32e25806146d23f4
https://doi.org/10.1006/jmrb.1994.1107
https://doi.org/10.1006/jmrb.1994.1107
Autor:
Alessandro Desideri, Amalia Lania, G. Rotilio, Antonio Galtieri, Mattia Falconi, Fabio Polticelli, Peter O'Neill, R Petruzelli, L Calabrese
Publikováno v:
Archives of Biochemistry and Biophysics. 312:22-30
The three-dimensional structure of Cu,Zn superoxide dismutase (SOD) from the shark Prionace glauca was homology modeled on the structure of the bovine enzyme used as a template. Shark SOD displays the conservative substitution of one of the residues
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0dae04f5655fe9ff2c7a01a6324ab014
https://doi.org/10.1006/abbi.1994.1275
https://doi.org/10.1006/abbi.1994.1275
Autor:
Franco Marmocchi, G. Rotilio, Giorgio Pelosi, Martino Bolognesi, Mattia Falconi, Alessandro Coda, Giuseppina Gatti, K. Djinovic, L. Antolini, Alessandro Desideri
Publikováno v:
Journal of Molecular Biology. 225:791-809
The structure of Cu,Zn yeast superoxide dismutase has been determined to 2.5 A resolution. The enzyme crystallizes in the P21212 space group with two dimeric enzyme molecules per asymmetric unit. The structure has been solved by molecular replacement
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c2fc8dd622535a56ce470b49dd0c9466
https://doi.org/10.1016/0022-2836(92)90401-5
https://doi.org/10.1016/0022-2836(92)90401-5
Publikováno v:
Protoplasma. 169:1-8
Immunogold labeling and transmission electron microscopy were used to localize iron-superoxide dismutase (Fe-SOD) in the different cells of nitrogen-fixing cyanobacterial symbiont present within different leaf cavity groups ofAzolla filiculoides Lam.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9c3e95f1f114c83ed5e449601b6ba636
https://doi.org/10.1007/bf01343364
https://doi.org/10.1007/bf01343364
Publikováno v:
FEMS Microbiology Letters. 80:161-165
• Superoxide dismutase (SOD) activity was assayed in vegetative cells, heterocysts and akinetes of Anabaena cylindrica Lemm. The iron-containing isoenzyme (Fe-SOD) was in all cases predominant over the manganese-containing isoenzyme (Mn-SOD). Diffe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::da767d8c582a0b16c267f172d60dfe3a
https://doi.org/10.1111/j.1574-6968.1991.tb04654.x
https://doi.org/10.1111/j.1574-6968.1991.tb04654.x