Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Emanuela Truppo"'
Autor:
Giuseppina De Simone, Anna Di Fiore, Emanuela Truppo, Emma Langella, Daniela Vullo, Claudiu T. Supuran, Simona Maria Monti
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 34, Iss 1, Pp 1506-1510 (2019)
Carbonic anhydrases (CAs) are ubiquitous metallo-enzymes that catalyse the reversible hydration of carbon dioxide to bicarbonate and proton. In humans there are 15 isoforms among which only 12 are catalytically active. Since active human (h) CAs show
Externí odkaz:
https://doaj.org/article/9f170bbeb47743aa83686eb06fe82839
Autor:
Annamaria Sandomenico, Silvia Scaramuzza, Fabio Selis, Emanuela Iaccarino, Luisa Calvanese, Andrea Esperti, Emanuela Truppo, Paolo Dell'Omo, Maria Cantile, Sandro De Falco, Lucia Falcigno, Menotti Ruvo, Andrea Caporale, Riccardo Sanna, Giancarlo Tonon, Annalia Focà
Publikováno v:
International journal of biological macromolecules 164 (2020): 4516–4531. doi:10.1016/j.ijbiomac.2020.09.050
info:cnr-pdr/source/autori:Selis F.; Sandomenico A.; Cantile M.; Sanna R.; Calvanese L.; Falcigno L.; Dell'Omo P.; Esperti A.; De Falco S.; Foca A.; Caporale A.; Iaccarino E.; Truppo E.; Scaramuzza S.; Tonon G.; Ruvo M./titolo:Generation and testing of engineered multimeric Fabs of trastuzumab/doi:10.1016%2Fj.ijbiomac.2020.09.050/rivista:International journal of biological macromolecules/anno:2020/pagina_da:4516/pagina_a:4531/intervallo_pagine:4516–4531/volume:164
info:cnr-pdr/source/autori:Selis F.; Sandomenico A.; Cantile M.; Sanna R.; Calvanese L.; Falcigno L.; Dell'Omo P.; Esperti A.; De Falco S.; Foca A.; Caporale A.; Iaccarino E.; Truppo E.; Scaramuzza S.; Tonon G.; Ruvo M./titolo:Generation and testing of engineered multimeric Fabs of trastuzumab/doi:10.1016%2Fj.ijbiomac.2020.09.050/rivista:International journal of biological macromolecules/anno:2020/pagina_da:4516/pagina_a:4531/intervallo_pagine:4516–4531/volume:164
Recombinant antibodies fragments in several new formats are routinely investigated and used in diagnostic and therapeutic applications as anti-cancers molecules. New antibody formats are generated to compensate the need for multispecificity and site-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27c83f8eb5924b3f47cced55512ce8ab
http://hdl.handle.net/11588/825466
http://hdl.handle.net/11588/825466
Autor:
Vincenzo Alterio, Alessio Innocenti, Claudiu T. Supuran, Simona Maria Monti, Emanuela Truppo, Anna Di Fiore, Giuseppina De Simone, Annamaria Sandomenico, Daniela Vullo
Publikováno v:
Bioorganic & Medicinal Chemistry Letters
Bioorganic & medicinal chemistry letters
22 (2012): 1560–1564. doi:10.1016/j.bmcl.2011.12.134
info:cnr-pdr/source/autori:Truppo E, Supuran CT, Sandomenico A, Vullo D, Innocenti A, Di Fiore A, Alterio V, De Simone G, Monti SM./titolo:Carbonic anhydrase VII is S-glutathionylated without loss of catalytic activity and affinity for sulfonamide inhibitors/doi:10.1016%2Fj.bmcl.2011.12.134/rivista:Bioorganic & medicinal chemistry letters (Print)/anno:2012/pagina_da:1560/pagina_a:1564/intervallo_pagine:1560–1564/volume:22
Bioorganic & Medicinal Chemistry Letters; Vol 22
Bioorganic & medicinal chemistry letters
22 (2012): 1560–1564. doi:10.1016/j.bmcl.2011.12.134
info:cnr-pdr/source/autori:Truppo E, Supuran CT, Sandomenico A, Vullo D, Innocenti A, Di Fiore A, Alterio V, De Simone G, Monti SM./titolo:Carbonic anhydrase VII is S-glutathionylated without loss of catalytic activity and affinity for sulfonamide inhibitors/doi:10.1016%2Fj.bmcl.2011.12.134/rivista:Bioorganic & medicinal chemistry letters (Print)/anno:2012/pagina_da:1560/pagina_a:1564/intervallo_pagine:1560–1564/volume:22
Bioorganic & Medicinal Chemistry Letters; Vol 22
Human carbonic anhydrase (CA, EC 4.2.1.1) VII is a cytosolic enzyme with high carbon dioxide hydration activity. Here we report an unexpected S-glutathionylation of hCA VII which has also been observed earlier in vivo for hCA III, another cytosolic i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0b14b4e55dd42f334c37d331ceaadc8
Autor:
Angela Arciello, Rita Del Giudice, Emanuela Truppo, Daria Maria Monti, Claudiu T. Supuran, Simona Maria Monti, Giuseppina De Simone
Publikováno v:
Biological chemistry
394 (2013): 1343–1348. doi:10.1515/hsz-2013-0204
info:cnr-pdr/source/autori:Del Giudice, Rita; Monti, Daria M.; Truppo, Emanuela; Arciello, Angela; Supuran, Claudiu T.; De Simone, Giuseppina; Monti, Simona M./titolo:Human carbonic anhydrase VII protects cells from oxidative damage/doi:10.1515%2Fhsz-2013-0204/rivista:Biological chemistry (Print)/anno:2013/pagina_da:1343/pagina_a:1348/intervallo_pagine:1343–1348/volume:394
394 (2013): 1343–1348. doi:10.1515/hsz-2013-0204
info:cnr-pdr/source/autori:Del Giudice, Rita; Monti, Daria M.; Truppo, Emanuela; Arciello, Angela; Supuran, Claudiu T.; De Simone, Giuseppina; Monti, Simona M./titolo:Human carbonic anhydrase VII protects cells from oxidative damage/doi:10.1515%2Fhsz-2013-0204/rivista:Biological chemistry (Print)/anno:2013/pagina_da:1343/pagina_a:1348/intervallo_pagine:1343–1348/volume:394
Human carbonic anhydrase (hCA) VII is a cytosolic enzyme with high carbon dioxide hydration activity. Recently, S-glutathionylation of two cysteine residues from the enzyme was revealed, suggesting a new role as oxygen radical scavenger. We analyzed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d433be0b7b66992b284e828f8afeed8
http://hdl.handle.net/11588/564037
http://hdl.handle.net/11588/564037
Autor:
Emanuela Truppo, Fatemeh Bootorabi, Simona Maria Monti, Giuseppina De Simone, Claudiu T. Supuran, Vincenzo Alterio, Seppo Parkkila, Anna Di Fiore, Nina A. Dathan
Publikováno v:
Bioorganic & medicinal chemistry letters
20 (2010): 5023–5026. doi:10.1016/j.bmcl.2010.07.051
info:cnr-pdr/source/autori:Di Fiore A; Truppo E; Supuran CT; Alterio V; Dathan NA; Bootorabi F; Parkkila S; Monti SM; De Simone G./titolo:Crystal structure of the C183S%2FC217S mutant of human CA VII in complex with acetazolamide./doi:10.1016%2Fj.bmcl.2010.07.051/rivista:Bioorganic & medicinal chemistry letters (Print)/anno:2010/pagina_da:5023/pagina_a:5026/intervallo_pagine:5023–5026/volume:20
20 (2010): 5023–5026. doi:10.1016/j.bmcl.2010.07.051
info:cnr-pdr/source/autori:Di Fiore A; Truppo E; Supuran CT; Alterio V; Dathan NA; Bootorabi F; Parkkila S; Monti SM; De Simone G./titolo:Crystal structure of the C183S%2FC217S mutant of human CA VII in complex with acetazolamide./doi:10.1016%2Fj.bmcl.2010.07.051/rivista:Bioorganic & medicinal chemistry letters (Print)/anno:2010/pagina_da:5023/pagina_a:5026/intervallo_pagine:5023–5026/volume:20
Human carbonic anhydrase VII (hCA VII) is a cytosolic member of the alpha-CA family. This enzyme is mainly localized in a number of brain tissues such as the cortex, hippocampus and thalamus and has been noted for its contribution in generating neuro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9dac1699d372ce23f8c825f96db956f
Autor:
Carlo Pedone, Simona Maria Monti, Vincenzo Alterio, Emanuela Truppo, Giuseppina De Simone, Claudiu T. Supuran
Publikováno v:
Organic & biomolecular chemistry 8 (2010): 3528–3533. doi:10.1039/b926832d
info:cnr-pdr/source/autori:Alterio V; Monti SM; Truppo E; Pedone C; Supuran CT; De Simone G./titolo:The first example of a significant active site conformational rearrangement in a carbonic anhydrase-inhibitor adduct: the carbonic anhydrase I-topiramate complex./doi:10.1039%2Fb926832d/rivista:Organic & biomolecular chemistry/anno:2010/pagina_da:3528/pagina_a:3533/intervallo_pagine:3528–3533/volume:8
info:cnr-pdr/source/autori:Alterio V; Monti SM; Truppo E; Pedone C; Supuran CT; De Simone G./titolo:The first example of a significant active site conformational rearrangement in a carbonic anhydrase-inhibitor adduct: the carbonic anhydrase I-topiramate complex./doi:10.1039%2Fb926832d/rivista:Organic & biomolecular chemistry/anno:2010/pagina_da:3528/pagina_a:3533/intervallo_pagine:3528–3533/volume:8
Topiramate is a widely used antiepileptic drug, which has been demonstrated to act as an efficient weight loss agent. Since several studies have pointed out that TPM is a potent in vitro inhibitor of several Carbonic anhydrase (CA) isozymes, it has b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d930c17c76f2670de4c2ea13ce4b626
http://www.cnr.it/prodotto/i/14196
http://www.cnr.it/prodotto/i/14196