Zobrazeno 1 - 10
of 88
pro vyhledávání: '"Vittoria Ventrella"'
Autor:
Fabiana Trombetti, Paola Minardi, Attilio Luigi Mordenti, Anna Badiani, Vittoria Ventrella, Sabrina Albonetti
Publikováno v:
Foods, Vol 11, Iss 13, p 1911 (2022)
The effects and specificity of dietary supplementation of EconomasETM (EcoE), mainly consisting of organic selenium (0.15 or 0.30 mg/kg feed; Se) or of vitamin E (100 or 200 mg/kg feed; VE), on lipid oxidation were evaluated in rabbit hamburgers duri
Externí odkaz:
https://doaj.org/article/bdeb2482d9954883a71504f5ef0c0b11
Autor:
Salvatore Nesci, Fabiana Trombetti, Alessandra Pagliarani, Vittoria Ventrella, Cristina Algieri, Gaia Tioli, Giorgio Lenaz
Publikováno v:
Life, Vol 11, Iss 3, p 242 (2021)
Under aerobic conditions, mitochondrial oxidative phosphorylation (OXPHOS) converts the energy released by nutrient oxidation into ATP, the currency of living organisms. The whole biochemical machinery is hosted by the inner mitochondrial membrane (m
Externí odkaz:
https://doaj.org/article/1313825b099e46a79deabb214be4078f
Autor:
Rosamaria Fiorini, Alessandra Pagliarani, Salvatore Nesci, Micaela Fabbri, Vittoria Ventrella, Fabiana Trombetti
Publikováno v:
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology. 227:12-20
The mitochondrial F1FO-ATPase, the key enzyme in cell bioenergetics, apparently works in the same way in mollusks and in mammals. We previously pointed out a raft-like arrangement in mussel gill mitochondrial membranes, which apparently distinguishes
Autor:
Cristina, Algieri, Fabiana, Trombetti, Alessandra, Pagliarani, Vittoria, Ventrella, Salvatore, Nesci
Publikováno v:
Archives of biochemistry and biophysics. 712
The dithiol reagents phenylarsine oxide (PAO) and dibromobimane (DBrB) have opposite effects on the F
Autor:
Fabiana Trombetti, Alessandra Pagliarani, Vittoria Ventrella, Chiara Bernardini, Salvatore Nesci, Cristina Algieri, Monica Forni, Micaela Fabbri
Publikováno v:
Annals of the New York Academy of Sciences. 1457:142-157
The properties of the mitochondrial F1 FO -ATPase catalytic site, which can bind Mg2+ , Mn2+ , or Ca2+ and hydrolyze ATP, were explored by inhibition kinetic analyses to cast light on the Ca2+ -activated F1 FO -ATPase connection with the permeability
Autor:
Vittoria Ventrella, Cristina Algieri, Alessandra Pagliarani, Salvatore Nesci, Fabiana Trombetti
Publikováno v:
Amino Acids. 51:579-587
The eukaryotic F 1 F O -ATP synthase/hydrolase activity is coupled to H + translocation through the inner mitochondrial membrane. According to a recent model, two asymmetric H + half-channels in the a subunit translate a transmembrane vertical H + fl
Autor:
Vittoria Ventrella, Cristina Algieri, Giorgio Lenaz, Fabiana Trombetti, Alessandra Pagliarani, Gaia Tioli, Salvatore Nesci
Publikováno v:
Life, Vol 11, Iss 242, p 242 (2021)
Life
Life
Under aerobic conditions, mitochondrial oxidative phosphorylation (OXPHOS) converts the energy released by nutrient oxidation into ATP, the currency of living organisms. The whole biochemical machinery is hosted by the inner mitochondrial membrane (m
Autor:
Fabiana Trombetti, Vittoria Ventrella, Cristina Algieri, Micaela Fabbri, Alessandra Pagliarani, Salvatore Nesci
open 6 no The molecular mechanisms which rule the formation and opening of the mitochondrial permeability transition pore (mPTP), the lethal mechanism which permeabilizes mitochondria to water and solutes and drives the cell to death, are still uncle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb9072daa95560acb4c2e1843b32016a
http://hdl.handle.net/11585/783596
http://hdl.handle.net/11585/783596
Autor:
Salvatore, Nesci, Cristina, Algieri, Fabiana, Trombetti, Vittoria, Ventrella, Micaela, Fabbri, Alessandra, Pagliarani
Publikováno v:
Pharmacological research. 166
In mammalian cells enzymatic and non-enzymatic pathways produce H
Autor:
Cristina, Algieri, Salvatore, Nesci, Fabiana, Trombetti, Micaela, Fabbri, Vittoria, Ventrella, Alessandra, Pagliarani
Publikováno v:
Biochimie. 180
The molecular mechanisms which rule the formation and opening of the mitochondrial permeability transition pore (mPTP), the lethal mechanism which permeabilizes mitochondria to water and solutes and drives the cell to death, are still unclear and par