Zobrazeno 1 - 10
of 35
pro vyhledávání: '"Romano Felicioli"'
Autor:
Anna Gloria Sabatini, Donatella Fortunato, Elena Donadio, Romano Felicioli, Antonio Felicioli, Maria Gabriella Giuffrida, Roberta Scarselli, Ettore Balestreri, Amedeo Conti, M Pinzauti
Publikováno v:
Proteomics (Weinh., Print) 5 (2005): 769–776. doi:10.1002/pmic.200401149
info:cnr-pdr/source/autori:Scarselli R., Donadio E., Giuffrida M.G., Fortunato D., Conti A., Balestreri E., Felicioli R., Pinzauti M., Sabatini A.G., Felicioli A./titolo:Towards royal jelly proteome/doi:10.1002%2Fpmic.200401149/rivista:Proteomics (Weinh., Print)/anno:2005/pagina_da:769/pagina_a:776/intervallo_pagine:769–776/volume:5
info:cnr-pdr/source/autori:Scarselli R., Donadio E., Giuffrida M.G., Fortunato D., Conti A., Balestreri E., Felicioli R., Pinzauti M., Sabatini A.G., Felicioli A./titolo:Towards royal jelly proteome/doi:10.1002%2Fpmic.200401149/rivista:Proteomics (Weinh., Print)/anno:2005/pagina_da:769/pagina_a:776/intervallo_pagine:769–776/volume:5
The recent availability of the honey-bee Apis mellifera genome and trascriptome of both the female castes, has stimulated new efforts in investigating the protein composition of royal jelly (RJ), its role in caste differentiation and its quality and
Publikováno v:
Scopus-Elsevier
A novel protease has been identified, purified and partially characterised from complete medium grown Spirulina platensis, which could be responsible for the selective proteolysis of phycobiliproteins. It is an 80 kDa homodimeric enzyme; its N-termin
Publikováno v:
Plant Physiology and Biochemistry. 36:427-432
A novel proteinase has been evidenced in spinach (Spinacia oleracea L.) leaves. Substrate and inhibitor specificities of the purified enzyme indicate that this proteinase is different from the previously described proteinase which displays a peculiar
Publikováno v:
LWT - Food Science and Technology. 30:616-619
Optimization of protein extraction for food use by wet fractionation procedure requires knowledge of the possible degradation processes which usually accompany the purification procedures and of the basic molecular features of the particular protein.
Autor:
Adriano Podestà, Cristina Amato, Lucia Vaccari, Romano Felicioli, Simone Giannecchini, Ettore Balestreri
Publikováno v:
Letters in Peptide Science. 2:333-338
One Lys/Phe copolymer and two series of copolymers of lysine with either alanine or tyrosine have been used as inhibitors of a plant proteinase that is known to be inhibited by polycationic inhibitors. The copolymers differ in the hydrophobicity of t
Publikováno v:
LWT - Food Science and Technology. 29:465-469
A time-dependent loss of ribulose-1,5-bisphosphate carboxylase (RuBPcase) activity and partial proteolysis were observed in squeezed juices of Jerusalem artichoke (Helianthus tuberosusL.) obtained by the typical wet green crop fractionation procedure
Autor:
Ettore Balestreri, Cristina Amato, Lucia Vaccari, Paolo Rovero, Romano Felicioli, Stefania Viganò, S. Pegoraro
Publikováno v:
Letters in Peptide Science. 2:27-32
The synthesis and biological activity of a photochromic compound, in which two Lys2 dipeptides are linked through their N-terminal amino groups by an azobenzene moiety, are reported. The synthesis was achieved by a novel solid-phase dimerization stra
Publikováno v:
Journal of Plant Physiology. 143:274-278
Summary The role of the degree of polymerization and of interlinked positively charged groups in the mechanism of inhibition of a proteinase purified from alfalfa ( Medicago sativa ) leaf by polycations has been investigated using L-lysine oligomers
Autor:
Ettore Balestreri, Elena Donadio, Romano Felicioli, Antonio Felicioli, Carlo Donadio, Alessandro Armini, Veronica Dimuccio, Riccardo Cianti, Francesco Piccolomini, Luca Bini
Publikováno v:
Clinical chemistry and laboratory medicine 47 (2009): 1373–1378. doi:10.1515/CCLM.2009.303
info:cnr-pdr/source/autori:Donadio E.; Piccolomini F., Dimuccio V.; Felicioli A.; Balestreri E.; Cianti R.; Armini A., Bini L.; Felicioli R.; Donadio C./titolo:Serum albumin fragmentation in end-stage renal disease patients a pilot study./doi:10.1515%2FCCLM.2009.303/rivista:Clinical chemistry and laboratory medicine/anno:2009/pagina_da:1373/pagina_a:1378/intervallo_pagine:1373–1378/volume:47
info:cnr-pdr/source/autori:Donadio E.; Piccolomini F., Dimuccio V.; Felicioli A.; Balestreri E.; Cianti R.; Armini A., Bini L.; Felicioli R.; Donadio C./titolo:Serum albumin fragmentation in end-stage renal disease patients a pilot study./doi:10.1515%2FCCLM.2009.303/rivista:Clinical chemistry and laboratory medicine/anno:2009/pagina_da:1373/pagina_a:1378/intervallo_pagine:1373–1378/volume:47
Background: The goal of this study was to detect modification in the expression of plasma proteins and/or post-translational modifications of their structure in patients with end stage renal disease. Methods: Serum samples from 19 adult patients trea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::91aaa9a400577b9d8e67d016c2c09451
http://hdl.handle.net/11365/36404
http://hdl.handle.net/11365/36404
Autor:
Francesco, Piccolomini, Elena, Donadio, Felicioli, Antonio, Luca, Bini, Sabrina, Liberatori, Vitagliano, Pallini, Ettore, Balestreri, Arduini, M., Romano, Felicioli, Donadio, Carlo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______3728::ac9abb9546f6bbd23a030a32377ad92f
http://hdl.handle.net/11568/98183
http://hdl.handle.net/11568/98183