Zobrazeno 1 - 10
of 51
pro vyhledávání: '"Paolo Natalini"'
Autor:
G. De Sanctis, Stefania Pucciarelli, Pierluigi Mariani, B. Quadrini, Silvia Vincenzetti, Valeria Polzonetti, Natalina Cammertoni, Alberto Vita, Paolo Natalini
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 70:144-156
An investigation was made of the role exerted by some residues supposed to be involved in the intersubunit interaction and also in the catalytic site of homotetrameric human cytidine deaminase (T-CDA). Attention was focused on Y33, Y60, R68, and F137
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4954c2159460dbaef4ef611d18921843
https://doi.org/10.1002/prot.21533
https://doi.org/10.1002/prot.21533
Publikováno v:
Food Chemistry. 88:11-15
Olive oil is the principal source of fats in the Mediterranean diet and it has been postulated that the components in olive oil can contribute to a lower incidence of coronary heart disease and cancers (prostate, colon, breast, and skin). The positiv
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31b51dd5cc7baf780ad5f5cdb2418331
https://doi.org/10.1016/j.foodchem.2004.01.029
https://doi.org/10.1016/j.foodchem.2004.01.029
Autor:
Paolo Natalini, Valeria Polzonetti, Iris Meiri, Gilberto Mosconi, Oliana Carnevali, Marco Cardinali
Publikováno v:
Molecular Reproduction and Development. 61:213-217
The cell egg is in a state of quiescence and only after its fusion with the sperm, a series of pre-programmed metabolic processes will be activated, culminating with embryonic development. The egg/sperm fusion induces a transitory increase of Ca2+ in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b0cbad88e8a6a92ec264cfba87d68e5
https://doi.org/10.1002/mrd.1150
https://doi.org/10.1002/mrd.1150
Autor:
Daniela Salvatori, Jan Neuhard, Silvia Vincenzetti, G. Gaubert, F. Bertorelle, Georges Maury, G. De Sanctis, Alberto Vita, Paolo Natalini, Alessandra Cambi
Publikováno v:
Scopus-Elsevier
Site-directed mutagenesis on human cytidine deaminase (CDA) was employed to mutate specifically two highly conserved phenylalanine residues, F36 and F137, to tryptophan; at the same time, the unique tryptophan residue present in the sequence at posit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78e642dd51c4b558d97cbdccabf3ad82
https://doi.org/10.1093/protein/13.11.791
https://doi.org/10.1093/protein/13.11.791
Autor:
Silvia Vincenzetti, Jan Neuhard, Paolo Natalini, Alberto Vita, Alessandra Cambi, Stefano Costanzi
Publikováno v:
Scopus-Elsevier
By site-directed mutagenesis on human cytidine deaminase (CDA), five mutant proteins were obtained: C65A, C99A, C102A, E67D and E67Q. The three cysteine mutants were completely inactive, whereas E67D and E67Q showed a specific activity about 200- and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae4fe0fedd1b521c4fd485c8420c0bf8
https://doi.org/10.1093/protein/11.1.59
https://doi.org/10.1093/protein/11.1.59
Autor:
Alberto Vita, Francesco M. Carpi, I. Santarelli, Valeria Polzonetti, Stefania Pucciarelli, Daniela Micozzi, Paolo Natalini, Paolo Polidori, Silvia Vincenzetti
Cytidine deaminase (CDA), is one of the enzymes involved in the pyrimidine salvage pathways, which catalyzes the formation of uridine and deoxyuridine by the hydrolytic deamination of cytidine and deoxycytidine, respectively. Human CDA is a tetrameri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ad59e24c75dadd65fa880a402fdc564
http://hdl.handle.net/11581/264592
http://hdl.handle.net/11581/264592
Autor:
Giuseppe Orsomando, Alberto Vita, Paolo Natalini, Valeria Polzonetti, Silverio Ruggieri, Enrico Balducci, M. Emanuelli, Giulio Magni, Nadia Raffaelli
Publikováno v:
Scopus-Elsevier
The purification procedure of NMN adenylyltransferase from bull testis presented here consists of a heat step and an acidic precipitation followed by four chromatographic steps, including dye ligand, adsorption and hydrophobic chromatography. The fin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe87f56e4549585621ad6e6ac887c693
https://doi.org/10.1042/bj3100395
https://doi.org/10.1042/bj3100395
Autor:
Silveri Ruggieri, Adolfo Amici, Giulio Magni, Nadia Raffaelli, Enrico Balducci, M. Emanuelli, Paolo Natalini
Publikováno v:
Biochemical Pharmacology. 49:575-579
Nicotinamide mononucleotide (NMN) adenylyltransferase (EC 2.7.7.1) from human placenta is rapidly inactivated by 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU). A similar inactivation is observed with other C- and N-nitroso compounds. The inactivation b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6edbdb2193e914dfbfb8e5a7eacbb03e
https://doi.org/10.1016/0006-2952(94)00478-5
https://doi.org/10.1016/0006-2952(94)00478-5
Autor:
Stefania Pucciarelli, Paolo Natalini, Daniela Micozzi, Francesco M. Carpi, Valeria Polzonetti, Alberto Vita, Paolo Polidori, Silvia Vincenzetti, Adolfo Amici
Publikováno v:
Biochemistry & Analytical Biochemistry. 1
In children with Cow Milk Protein Allergy (CMPA), when it is not possible to breast feed or to use cow milk, the clinical use of donkey milk is considered since several studies have demonstrated the high similarity of donkey milk compared to human mi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f289a719b0b8c5d018db6b11ed0cea6
https://doi.org/10.4172/2161-1009.1000109
https://doi.org/10.4172/2161-1009.1000109
Autor:
Giusi Serena De Fronzo, Stefania Pucciarelli, Giovanni Filippo Palmieri, Franco Bernabucci, Giulia Bonacucina, Giovanna Mencarelli, Paolo Natalini, Marco Cespi
Yeast alcohol dehydrogenase (ADH) is an enzyme widely studied for biotechnological applications due to its involvement in fermentation industry, and various attempts to improve its catalytic properties and its thermal stability have been carried out.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fceff8b72619289ad225b68a6c37720d
http://hdl.handle.net/11581/239549
http://hdl.handle.net/11581/239549