Zobrazeno 1 - 10
of 39
pro vyhledávání: '"Mosé Rossi"'
A MILP algorithm for the optimal sizing of an off-grid hybrid renewable energy system in South Tyrol
Publikováno v:
Energy Reports, Vol 6, Iss , Pp 21-26 (2020)
The exploitation of renewable energy sources through sustainable energy technologies are taking the field to decrease the pollutions’ emissions into the Earth’s environment. To offset the limitations of such resources, hybrid energy systems are b
Externí odkaz:
https://doaj.org/article/f0ecee0b7ddf47dcb4519ce39f36fed1
Autor:
Andrea Strazzulli, Giuseppe Perugino, Marialuisa Mazzone, Mosè Rossi, Stephen G. Withers, Marco Moracci
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 34, Iss 1, Pp 973-980 (2019)
The reaction mechanism of glycoside hydrolases belonging to family 1 (GH1) of carbohydrate-active enzymes classification, hydrolysing β-O-glycosidic bonds, is well characterised. This family includes several thousands of enzymes with more than 20 di
Externí odkaz:
https://doaj.org/article/0530f2b6eba446bd9eb035a48b6d9df8
Autor:
Sonia Del Prete, Rosa Merlo, Anna Valenti, Rosanna Mattossovich, Mosè Rossi, Vincenzo Carginale, Claudiu T. Supuran, Giuseppe Perugino, Clemente Capasso
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 34, Iss 1, Pp 946-954 (2019)
Carbonic anhydrases (CAs, EC 4.2.1.1) are a superfamily of ubiquitous metalloenzymes present in all living organisms on the planet. They are classified into seven genetically distinct families and catalyse the hydration reaction of carbon dioxide to
Externí odkaz:
https://doaj.org/article/65113c1a6f1b4516b7abd372a652a5f3
Autor:
Rosa Perfetto, Sonia Del Prete, Daniela Vullo, Giovanni Sansone, Carmela Barone, Mosè Rossi, Claudiu T. Supuran, Clemente Capasso
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 32, Iss 1, Pp 632-639 (2017)
A α-carbonic anhydrase (CA, EC 4.2.1.1) has been purified and characterized biochemically from the mollusk Mytilus galloprovincialis. As in most mollusks, this α-CA is involved in the biomineralization processes leading to the precipitation of calc
Externí odkaz:
https://doaj.org/article/4f780020a1bd45a69dfe5b154c088972
Autor:
Rosa Perfetto, Sonia Del Prete, Daniela Vullo, Vincenzo Carginale, Giovanni Sansone, Carmela M. A. Barone, Mosè Rossi, Fatmah A. S. Alasmary, Sameh M. Osman, Zeid AlOthman, Claudiu T. Supuran, Clemente Capasso
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 32, Iss 1, Pp 1029-1035 (2017)
We cloned, expressed, purified, and determined the kinetic constants of the recombinant α-carbonic anhydrase (rec-MgaCA) identified in the mantle tissue of the bivalve Mediterranean mussel, Mytilus galloprovincialis. In metazoans, the α-CA family i
Externí odkaz:
https://doaj.org/article/fff9f1a1da964a998d406da9e156831c
Autor:
Rosa Perfetto, Sonia Del Prete, Daniela Vullo, Giovanni Sansone, Carmela M.A. Barone, Mosè Rossi, Claudiu T. Supuran, Clemente Capasso
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 32, Iss 1, Pp 759-766 (2017)
Carbonic anhydrases (CAs; EC 4.2.1.1) are metalloenzymes with a pivotal potential role in the biomimetic CO2 capture process (CCP) because these biocatalysts catalyse the simple but physiologically crucial reaction of carbon dioxide hydration to bica
Externí odkaz:
https://doaj.org/article/9a444733d3e2425aa633d1d3c207b1be
Autor:
Sonia Del Prete, Rosa Perfetto, Mosè Rossi, Fatmah A. S. Alasmary, Sameh M. Osman, Zeid AlOthman, Claudiu T. Supuran, Clemente Capasso
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 32, Iss 1, Pp 1120-1128 (2017)
The carbonic anhydrase superfamily (CA, EC 4.2.1.1) of metalloenzymes is present in all three domains of life (Eubacteria, Archaea, and Eukarya), being an interesting example of convergent/divergent evolution, with its seven families (α-, β-, γ-,
Externí odkaz:
https://doaj.org/article/14c41e31204f4d57aa25c4d12f1bbf08
Autor:
Valeria Visone, Wenyuan Han, Giuseppe Perugino, Giovanni Del Monaco, Qunxin She, Mosè Rossi, Anna Valenti, Maria Ciaramella
Publikováno v:
PLoS ONE, Vol 12, Iss 10, p e0185791 (2017)
Protein imaging, allowing a wide variety of biological studies both in vitro and in vivo, is of great importance in modern biology. Protein and peptide tags fused to proteins of interest provide the opportunity to elucidate protein location and funct
Externí odkaz:
https://doaj.org/article/e404c1ac4bf44ab69be0098405853b77
Autor:
Alessia Riccio, Marta Gogliettino, Gianna Palmieri, Marco Balestrieri, Angelo Facchiano, Mosè Rossi, Stefania Palumbo, Giuseppe Monti, Ennio Cocca
Publikováno v:
PLoS ONE, Vol 10, Iss 5, p e0125594 (2015)
Acylpeptide hydrolase (APEH) is a ubiquitous cytosolic protease that plays an important role in the detoxification of oxidised proteins. In this work, to further explore the physiological role of this enzyme, two apeh cDNAs were isolated from the Chi
Externí odkaz:
https://doaj.org/article/a4ce8022459e4dd0a4583d6160c49b12
Publikováno v:
PLoS ONE, Vol 10, Iss 11, p e0142345 (2015)
The nuclease NurA and the ATPase HerA are present in all known thermophilic archaea and cooperate with the highly conserved MRE11/RAD50 proteins to facilitate efficient DNA double-strand break end processing during homologous recombinational repair.
Externí odkaz:
https://doaj.org/article/ff0e1a16c3314b17b1e595f61ca52a74