Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Alessandro Paradisi"'
Autor:
Badri S. Rajagopal, Nick Yates, Jake Smith, Alessandro Paradisi, Catherine Tétard-Jones, William G. T. Willats, Susan Marcus, J. Paul Knox, Mohd Firdaus-Raih, Bernard Henrissat, Gideon J. Davies, Paul H. Walton, Alison Parkin, Glyn R. Hemsworth
Publikováno v:
IUCrJ, Vol 11, Iss 2, Pp 260-274 (2024)
The discovery of lytic polysaccharide monooxygenases (LPMOs), a family of copper-dependent enzymes that play a major role in polysaccharide degradation, has revealed the importance of oxidoreductases in the biological utilization of biomass. In fungi
Externí odkaz:
https://doaj.org/article/5416359705ac4bb7868e9c0558924d6d
Autor:
João Paulo L. Franco Cairo, Fernanda Mandelli, Robson Tramontina, David Cannella, Alessandro Paradisi, Luisa Ciano, Marcel R. Ferreira, Marcelo V. Liberato, Lívia B. Brenelli, Thiago A. Gonçalves, Gisele N. Rodrigues, Thabata M. Alvarez, Luciana S. Mofatto, Marcelo F. Carazzolle, José G. C. Pradella, Adriana F. Paes Leme, Ana M. Costa-Leonardo, Mário Oliveira-Neto, André Damasio, Gideon J. Davies, Claus Felby, Paul H. Walton, Fabio M. Squina
Publikováno v:
Franco Cairo, J P L, Mandelli, F, Tramontina, R, Cannella, D, Paradisi, A, Ciano, L, Ferreira, M R, Liberato, M V, Brenelli, L B, Goncalves, T A, Rodrigues, G N, Alvarez, T M, Mofatto, L S, Carazzolle, M F, Pradella, J G C, Leme, A F P, Costa-Leonardo, A M, Oliveira-Neto, M, Damasio, A, Davies, G J, Felby, C, Walton, P H & Squina, F M 2022, ' Oxidative cleavage of polysaccharides by a termite-derived superoxide dismutase boosts the degradation of biomass by glycoside hydrolases ', Green Chemistry, vol. 24, no. 12, pp. 4845-4858 . https://doi.org/10.1039/d1gc04519a
Wood-feeding termites effectively degrade plant biomass through enzymatic degradation. Despite their high efficiencies, however, individual glycoside hydrolases isolated from termites and their symbionts exhibit anomalously low effectiveness in ligno
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6bec8f2b4a169d8b8859cf96836695d
https://doi.org/10.1039/d1gc04519a
https://doi.org/10.1039/d1gc04519a
Autor:
Alessandro Paradisi, Finn Lillelund Aachmann, Gaston Courtade, Zarah Forsberg, Gideon J. Davies, Peter J. Lindley, Reinhard Wimmer, Luisa Ciano, Paul H. Walton, Vincent G. H. Eijsink, Morten Sørlie
Publikováno v:
Proceedings of the National Academy of Sciences
Courtade, G, Ciano, L, Paradisi, A, Lindley, P J, Forsberg, Z, Sørlie, M, Wimmer, R, Davies, G J, Eijsink, V G H, Walton, P H & Aachmann, F L 2020, ' Mechanistic basis of substrate-O 2 coupling within a chitin-active lytic polysaccharide monooxygenase : An integrated NMR/EPR study ', Proceedings of the National Academy of Sciences of the United States of America, vol. 117, no. 32, pp. 19178-19189 . https://doi.org/10.1073/pnas.2004277117
Proceedings of the National Academy of Sciences of the United States of America
Courtade, G, Ciano, L, Paradisi, A, Lindley, P J, Forsberg, Z, Sørlie, M, Wimmer, R, Davies, G J, Eijsink, V G H, Walton, P H & Aachmann, F L 2020, ' Mechanistic basis of substrate-O 2 coupling within a chitin-active lytic polysaccharide monooxygenase : An integrated NMR/EPR study ', Proceedings of the National Academy of Sciences of the United States of America, vol. 117, no. 32, pp. 19178-19189 . https://doi.org/10.1073/pnas.2004277117
Proceedings of the National Academy of Sciences of the United States of America
Significance Lytic polysaccharide monooxygenases (LPMOs) have unique catalytic centers, at which a single copper catalyzes the oxidative cleavage of a glycosidic bond. The mechanism by which LPMOs activate molecular oxygen is key to understanding cop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::997aace39de2f1747828cf638cb4cedb
https://doi.org/10.1073/pnas.2004277117
https://doi.org/10.1073/pnas.2004277117
Autor:
Morten Tovborg, Luisa Ciano, Alessandro Paradisi, Paul H. Walton, Gideon J. Davies, Glyn R. Hemsworth
Publikováno v:
Dalton Transactions. 49:3413-3422
Probing the detailed interaction between lytic polysaccharide monooxygenases (LPMOs) and their polysaccharide substrates is key to revealing further insights into the mechanism of action of this class of enzymes on recalcitrant biomass. This investig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::506f258e903dd544edbd18331761cc92
https://doi.org/10.1039/c9dt04065j
https://doi.org/10.1039/c9dt04065j
Autor:
Marco Sola, Lidia Lancellotti, Marzia Bellei, Carlo Augusto Bortolotti, Alessandro Paradisi, Gianantonio Battistuzzi, Giulia Di Rocco, Antonio Ranieri, Marco Borsari
Publikováno v:
RSC Chemical Biology. 1:421-435
Urea-induced denaturation of the Met80Ala and Met80Ala/Tyr67Ala variants of S. cerevisiae iso-1 cytochrome c (ycc) was studied through variable temperature diffusive cyclic voltammetry and electronic absorption, CD and MCD spectroscopies. The suscept
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6491d2e797f3af6468622d501675bb59
https://doi.org/10.1039/d0cb00115e
https://doi.org/10.1039/d0cb00115e
Autor:
Ambili Ramanthrikkovil Variyam, Yuval Agam, Alessandro Paradisi, Carlo Augusto Bortolotti, Nadav Amdursky
A proton conducting protein-based biopolymer is modified with naphthalenediimide (NDI) monomers to specific amino acids resulting in an oriented organization of the NDI moieties exhibiting electronic conductivity of 40 mS cm−1 upon reduction.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c0b8662e851f68c0ce23f8b49afc84ab
https://hdl.handle.net/11380/1288061
https://hdl.handle.net/11380/1288061
Autor:
João Paulo L, Franco Cairo, Fernanda, Mandelli, Robson, Tramontina, David, Cannella, Alessandro, Paradisi, Luisa, Ciano, Marcel R, Ferreira, Marcelo V, Liberato, Lívia B, Brenelli, Thiago A, Gonçalves, Gisele N, Rodrigues, Thabata M, Alvarez, Luciana S, Mofatto, Marcelo F, Carazzolle, José G C, Pradella, Adriana F, Paes Leme, Ana M, Costa-Leonardo, Mário, Oliveira-Neto, André, Damasio, Gideon J, Davies, Claus, Felby, Paul H, Walton, Fabio M, Squina
Publikováno v:
Green chemistry : an international journal and green chemistry resource : GC. 24(12)
Wood-feeding termites effectively degrade plant biomass through enzymatic degradation. Despite their high efficiencies, however, individual glycoside hydrolases isolated from termites and their symbionts exhibit anomalously low effectiveness in ligno
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a947b2a36cb90298fc84880de67afafb
https://pubmed.ncbi.nlm.nih.gov/35813357
https://pubmed.ncbi.nlm.nih.gov/35813357
Autor:
Gideon J. Davies, Jonathan McMaster, Esther M. Johnston, Morten Tovborg, Luisa Ciano, Y. Hancock, Paul H. Walton, Adam Dowle, Callum R. Nicoll, Alessandro Paradisi
Publikováno v:
Journal of the American Chemical Society. 141:18585-18599
Hydrogen peroxide is a cosubstrate for the oxidative cleavage of saccharidic substrates by copper-containing lytic polysaccharide monooxygenases (LPMOs). The rate of reaction of LPMOs with hydrogen...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6f33584cdcb5016098ad44a9c0f3e3ee
https://doi.org/10.1021/jacs.9b09833
https://doi.org/10.1021/jacs.9b09833
Publikováno v:
Comprehensive Coordination Chemistry III ISBN: 9780081026892
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::62cdb8a1c47e1554897328401c173657
https://doi.org/10.1016/b978-0-12-409547-2.14928-5
https://doi.org/10.1016/b978-0-12-409547-2.14928-5
Autor:
Alessandro Paradisi, Giulia Di Rocco, Antonio Ranieri, Carlo Augusto Bortolotti, Marco Borsari, Gianantonio Battistuzzi, Marco Sola, Licia Paltrinieri, Marzia Bellei
Publikováno v:
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry. 25(3)
The interaction of cytochrome c with cardiolipin (CL) is a critical step in the initial stages of apoptosis and is mediated by a positively charged region on the protein surface comprising several lysine residues (site A). Here, the interaction of wt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27cc289684fe8436e52b9cfc25b4ddcf
https://pubmed.ncbi.nlm.nih.gov/32189145
https://pubmed.ncbi.nlm.nih.gov/32189145