Guido Sello

Guido Sello

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Guido Sello

Department of Chemistry, University of Milano, Via Golgi 19, 20133 Milan, Italy

Research Focus & Metrics

Academic Career Length

43Years (1984-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 January 2010 in Current Medicinal Chemistry
Verified
Journal Article
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FOF. Orsini
F. Orsini
GSG. Sello
G. Sello
MSM. Sisti
M. Sisti
In recent years, phosphonic acids and their derivatives have received increasing attention as analogues of a series of naturally occurring phosphates and as “bio-isosteric phosphorus analogues” of aminoacids. Unlike a phosphate group, the phosphonate moiety is not readily hydrolyzed, in a biological environment, by the enzymes involved in the phosphate cleavage. This feature makes these compounds extremely useful in several applications, in metabolic regulation, in enhancement or inhibition studies, in the development of potential drugs against several metabolic disorders. The great potential of these compounds in biological applications resulted in an intense effort directed to the development of efficient synthetic methods for their preparation, with particular attention to stereoselective synthesis. The purpose of this review is to give an up-to-date account of the chemistry, the synthesis and the biological activity of aminophosphonic acids and their derivatives.

1 July 2001 in Electrochimica Acta
Verified
Journal Article
Closed access
Sandra RondininiSandra Rondinini
Sandra Rondinini
PMPatrizia Mussini
Patrizia Mussini
PMPaolo Muttini
Paolo Muttini
GSGuido Sello
Guido Sello

1 July 2001 in Applied and Environmental Microbiology
Verified
Journal Article
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FAFabio L. G. Arenghi
Fabio L. G. Arenghi
DBDavide Berlanda
Davide Berlanda
EGEnrica Galli
Enrica Galli
GSGuido Sello
Guido Sello
PBPaola Barbieri
Paola Barbieri
Pseudomonas stutzeri OX1 meta pathway genes for toluene and o -xylene catabolism were analyzed, and loci encoding phenol hydroxylase, catechol 2,3-dioxygenase, 2-hydroxymuconate semialdehyde dehydrogenase, and 2-hydroxymuconate semialdehyde hydrolase were mapped. Phenol hydroxylase converted a broad range of substrates, as it was also able to transform the nongrowth substrates 2,4-dimethylphenol and 2,5-dimethylphenol into 3,5-dimethylcatechol and 3,6-dimethylcatechol, respectively, which, however, were not cleaved by catechol 2,3-dioxygenase. The identified gene cluster displayed a gene order similar to that of the Pseudomonas sp. strain CF600 dmp operon for phenol catabolism and was found to be coregulated by the tou operon activator TouR. A hypothesis about the evolution of the toluene and o -xylene catabolic pathway in P. stutzeri OX1 is discussed.

17 June 2019 in AMB Express
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Journal Article
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AGAlessandra De Giani
Alessandra De Giani
FBFederica Bovio
Federica Bovio
MFMatilde Forcella
Matilde Forcella
Paola FusiPaola Fusi
Paola Fusi
GSGuido Sello
Guido Sello
PGPatrizia Di Gennaro
Patrizia Di Gennaro
In this paper, we demonstrate that the antimicrobial activity of L. plantarum PBS067 strain against antagonist microorganisms was mediated by the production of a bacteriocin-like compound secreted at the stationary phase of the growth. The novel bacteriocin-like compound, designed plantaricin P1053, was identified by using sorption–desorption method, butanol extraction and SEC-HPLC. The molecular mass of plantaricin P1053 was shown to be 1053 Da by ESI-MS analysis. Plantaricin P1053 exhibited a broad-spectrum antimicrobial activity against Gram-positive bacteria as S. aureus and Gram-negative bacteria as E. coli. In addition to the antimicrobial activity, the isolated bacteriocin-like compound showed effects on normal and cancerogenic epithelial intestinal cell lines through an enhancing of viability of healthy cells and a proliferation reduction of cancer cells. Moreover, in this paper we demonstrate that the isolated bacteriocin-like compound acts on healthy cells through the epidermal growth factor receptor (EGFR) pathways. In conclusion, plantaricin P1053 isolated from L. plantarum PBS067 strain could represent one of the first multifunctional bacteriocin-like compound acting on human epithelial intestinal cells.

1 September 2001 in Research in Microbiology
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Journal Article
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PGPatrizia Di Gennaro
Patrizia Di Gennaro
EREmanuela Rescalli
Emanuela Rescalli
EGEnrica Galli
Enrica Galli
GSGuido Sello
Guido Sello
GBGiuseppina Bestetti
Giuseppina Bestetti

1 April 2005 in Journal of Applied Electrochemistry
Verified
Journal Article
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GFGiorgio Fiori
Giorgio Fiori
Sandra RondininiSandra Rondinini
Sandra Rondinini
GSGuido Sello
Guido Sello
Alberto VertovaAlberto Vertova
Alberto Vertova
MCMagdalena Cirja
Magdalena Cirja
LCLuca Conti
Luca Conti