Zobrazeno 1 - 10
of 47
pro vyhledávání: '"Gabriella Rosi"'
Autor:
Rita Romani, Gianna Evelina De Medio, Simona di Tullio, Rosa Lapalombella, Irene Pirisinu, Vittoria Margonato, Arsenio Veicsteinas, Marina Marini, Gabriella Rosi
Publikováno v:
Journal of Lipid Research, Vol 50, Iss 10, Pp 2036-2045 (2009)
Paraoxonases (PONs) are a small family of antioxidant enzymes whose antiatherogenic activity is well known. The aim of the present study was the evaluation of the effects of moderate aerobic training on their expression using a rat model. In order to
Externí odkaz:
https://doaj.org/article/baa4a1ea1078410dbc3046ff753a82b5
Autor:
Francesca Fallarino, Maria Teresa Pallotta, Alessandro Di Michele, Paolo Prontera, Rita Romani, Davide Matino, Irene Pirisinu, Mario Calvitti, Vincenzo Nicola Talesa, Ciriana Orabona, Gabriella Rosi, Jessica Rosati, Stefano Giovagnoli, Carmine Vacca, Paolo Puccetti, Matteo Pirro, Ursula Grohmann, Marco Gargaro, Giovanni Bistoni, Emilio Donti
Publikováno v:
Journal of Cellular and Molecular Medicine
Although human amniotic fluid does contain different populations of foetal-derived stem cells, scanty information is available on the stemness and the potential immunomodulatory activity of in vitro expanded, amniotic fluid stem cells. By means of a
Publikováno v:
Environmental Toxicology and Chemistry. 21:102-108
The benthic mollusk Scapharca inaequivalvis was collected in spring 1999 from three areas of the northern Adriatic Sea. From the mollusk, molecular forms of acetylcholinesterase (AChE), consisting of two prevailing spontaneously soluble (SS) forms pr
Publikováno v:
Journal of Medicinal Chemistry. 40:3009-3013
Fourteen alkyl and aryl thiocarbonate derivatives of choline were synthesized and studied as potential inhibitors of acetylcholinesterase (AChE). Twelve of the compounds inhibited AChEs derived from calf forebrain, human red blood cells, and octopus
Publikováno v:
The Journal of Experimental Zoology. 276:102-111
Publikováno v:
Biochemical Journal
Biochemical Journal, Portland Press, 1995, 306, pp.687-692
Biochemical Journal, Portland Press, 1995, 306, pp.687-692
Two acetylcholinesterases (AChE) differing in substrate and inhibitor specificities have been characterized in the medical leech (Hirudo medicinalis). A ‘spontaneously-soluble’ portion of AChE activity (SS-AChE) was recovered from haemolymph and
Autor:
Marta Grauso, Giovanni B. Principato, Gabriella Rosi, Elvio Giovannini, Vincenzo Nicola Talesa
Publikováno v:
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology. 110:649-656
Two forms of cholinesterase (ChE) were detected in the gastropod mollusc Helix pomatia : a fully soluble (FS) ChE in the hemolymph, representing about 90% of total activity, and a detergent-soluble (DS) membrane-bound enzyme. The FS enzyme seems to b
Autor:
Marta Grauso, Elvio Giovannini, Scott J. Norton, Giovanni B. Principato, Vincenzo Nicola Talesa, Gabriella Rosi
Publikováno v:
Journal of Experimental Zoology. 270:233-244
In the marine snail Murex brandaris about 80% of cholinesterase (ChE) activity lies in the blood. It can be recovered as a fully soluble (FS) form by mincing the whole animal. Two more ChE forms, detergent (DS) and high-salt soluble (HSS) (18 and 2%
Autor:
Scott J. Norton, A. Concetta Elia, Gabriella Rosi, Elvio Giovannini, Giovanni Principato, Ming K. Chyan
Publikováno v:
Enzyme and Protein. 48:164-173
Inhibitors having high specificity toward mammalian glyoxalase II, but not glyoxalase I, were sought as part of a program to study glyoxalase enzyme function in mammalian cells. The compound, S-fluorenylmethoxycarbonyl glutathione (FMOC-G), was synth
Autor:
Giovanna Zolese, Rosamaria Fiorini, Rita Romani, Roberta Galeazzi, Irene Pirisinu, Gabriella Rosi, Annarina Ambrosini
Butyrylcholinesterase (BChE), a serine hydrolase biochemically related to the cholinergic enzyme Acetylcholinesterase (AChE), is found in many mammalian tissues, such as serum and central nervous system, but its physiological role is still unclear. B
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c4f0759311a481192f43f3542ae709b6
http://hdl.handle.net/11391/414295
http://hdl.handle.net/11391/414295