Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Teresa Maria, Carusone"'
Autor:
Teresa Maria Carusone, Giuseppe Manco
Publikováno v:
Symmetry, Vol 14, Iss 2, p 212 (2022)
Paraoxonase 2 (PON2) is a member of a small family of human lactonases. Recently, post-translational modifications (PTMs) of PON2 were highlighted, one of which involved the modulation of the enzyme activity. Furthermore, two important single nucleot
Externí odkaz:
https://doaj.org/article/f23fd7e194364f3f8b7a6e5a2c239931
Publikováno v:
Antioxidants, Vol 10, Iss 2, p 256 (2021)
PON1, PON2, and PON3 belong to a family of lactone hydrolyzing enzymes endowed with various substrate specificities. Among PONs, PON2 shows the highest hydrolytic activity toward many acyl-homoserine lactones (acyl-HL) involved in bacterial quorum-se
Externí odkaz:
https://doaj.org/article/5bfef073ee264d159006b7b3861eb6bc
Autor:
Valentina De Luca, Piero Porcaro, Elena Porzio, Franz Worek, Ilaria Palchetti, Antonio Pisanti, Giuseppe Manco, Teresa Maria Carusone, Immacolata Del Giudice, Mario De Rosa, Odile F. Restaino, Maria Giovanna Borzacchiello, Chiara Schiraldi, Serena Laschi, Francesca Bettazzi, Luigi Mandrich, Ferdinando Febbraio
Publikováno v:
13th International Meeting on Cholinesterases-7th International Conference on Paraoxonases", 9-14/9/2018.
info:cnr-pdr/source/autori:Elena Porzio1*, Francesca Bettazzi2*, Luigi Mandrich1, Immacolata Del Giudice1, Odile F. Restaino3, Serena Laschi4, Ferdinando Febbraio1, Valentina De Luca1, Maria G. Borzacchiello3, Teresa M. Carusone1, Franz Worek5, Antonio Pisanti6, Piero Porcaro6, Chiara Schiraldi3, Mario De Rosa3, Ilaria Palchetti2, Giuseppe Manco1#/congresso_nome:13th International Meeting on Cholinesterases-7th International Conference on Paraoxonases"/congresso_luogo:/congresso_data:9-14%2F9%2F2018./anno:2018/pagina_da:/pagina_a:/intervallo_pagine
Scientific Reports
Scientific Reports, Vol 8, Iss 1, Pp 1-13 (2018)
Scientific reports (Nature Publishing Group) 8 (2018). doi:10.1038/s41598-018-31751-5
info:cnr-pdr/source/autori:Porzio, Elena; Bettazzi, Francesca; Mandrich, Luigi; Del Giudice, Immacolata; Restaino, Odile F.; Laschi, Serena; Febbraio, Ferdinando; De Luca, Valentina; Borzacchiello, Maria G.; Carusone, Teresa M.; Worek, Franz; Pisanti, Antonio; Porcaro, Piero; Schiraldi, Chiara; De Rosa, Mario; Palchetti, Ilaria; Manco, Giuseppe/titolo:Innovative Biocatalysts as Tools to Detect and Inactivate Nerve Agents/doi:10.1038%2Fs41598-018-31751-5/rivista:Scientific reports (Nature Publishing Group)/anno:2018/pagina_da:/pagina_a:/intervallo_pagine:/volume:8
info:cnr-pdr/source/autori:Elena Porzio1*, Francesca Bettazzi2*, Luigi Mandrich1, Immacolata Del Giudice1, Odile F. Restaino3, Serena Laschi4, Ferdinando Febbraio1, Valentina De Luca1, Maria G. Borzacchiello3, Teresa M. Carusone1, Franz Worek5, Antonio Pisanti6, Piero Porcaro6, Chiara Schiraldi3, Mario De Rosa3, Ilaria Palchetti2, Giuseppe Manco1#/congresso_nome:13th International Meeting on Cholinesterases-7th International Conference on Paraoxonases"/congresso_luogo:/congresso_data:9-14%2F9%2F2018./anno:2018/pagina_da:/pagina_a:/intervallo_pagine
Scientific Reports
Scientific Reports, Vol 8, Iss 1, Pp 1-13 (2018)
Scientific reports (Nature Publishing Group) 8 (2018). doi:10.1038/s41598-018-31751-5
info:cnr-pdr/source/autori:Porzio, Elena; Bettazzi, Francesca; Mandrich, Luigi; Del Giudice, Immacolata; Restaino, Odile F.; Laschi, Serena; Febbraio, Ferdinando; De Luca, Valentina; Borzacchiello, Maria G.; Carusone, Teresa M.; Worek, Franz; Pisanti, Antonio; Porcaro, Piero; Schiraldi, Chiara; De Rosa, Mario; Palchetti, Ilaria; Manco, Giuseppe/titolo:Innovative Biocatalysts as Tools to Detect and Inactivate Nerve Agents/doi:10.1038%2Fs41598-018-31751-5/rivista:Scientific reports (Nature Publishing Group)/anno:2018/pagina_da:/pagina_a:/intervallo_pagine:/volume:8
Pesticides and warfare nerve agents are frequently organophosphates (OPs) or related compounds. Their acute toxicity highlighted more than ever the need to explore applicable strategies for the sensing, decontamination and/or detoxification of these
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf3fcd48f5d1f1f0d577df6710f040cc
http://www.cnr.it/prodotto/i/393478
http://www.cnr.it/prodotto/i/393478
An efficient thermostable organophosphate hydrolase and its application in pesticide decontamination
Autor:
Luigia Merone, Elena Porzio, Immacolata Del Giudice, Giuseppe Manco, Teresa Maria Carusone, Franz Worek, Luigi Mandrich, Rossella Coppolecchia
Publikováno v:
Biotechnology and Bioengineering. 113:724-734
In vitro evolution of enzymes represents a powerful device to evolve new or to improve weak enzymatic functions. In the present work a semi-rational engineering approach has been used to design an efficient and thermostable organophosphate hydrolase,
An efficient thermostable organophosphate hydrolase and its application in pesticide decontamination
Autor:
Immacolata, Del Giudice, Rossella, Coppolecchia, Luigia, Merone, Elena, Porzio, Teresa Maria, Carusone, Luigi, Mandrich, Franz, Worek, Giuseppe, Manco
Publikováno v:
Biotechnology and bioengineering. 113(4)
In vitro evolution of enzymes represents a powerful device to evolve new or to improve weak enzymatic functions. In the present work a semi-rational engineering approach has been used to design an efficient and thermostable organophosphate hydrolase,
Autor:
Paola Sabrina Barbato, BARRA, LUCIA, CARUSONE, TERESA MARIA, Andrea Causa, Carmen Cioffi, Anna De Fenzo, Vincenza Faraco, Carlo Fasano, GIACOMELLI, STEFANO, Ettore Guerrera, IANNUCCI, PIERPAOLO, INVERSO, MICHELA, Mario Malinconico, Alberto Pascale, Guido Ranieri, SALVATORE, Adele, SOLA, MARIA ELENA, Guglielmo Trupiano, VELLA, FILOMENA MONICA, VESTITO, COSIMO, VITALE, LAURA
Il percorso formativo “ESPERTO NELLA GESTIONE DI BIORAFFINERIE: ALLESTIMENTO DI SISTEMI COLTURALI SOSTENIBILI, BIOCONVERSIONE DI BIOMASSE IN BIOCHEMICALS, LORO POLIMERIZZAZIONE E SUCCESSIVA TRASFORMAZIONE DEI POLIMERI IN MATERIALI PER L’INDUSTRIA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______3730::a2ca36af1f10fa2bfbc8414f80c19131
http://hdl.handle.net/11588/695594
http://hdl.handle.net/11588/695594