Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Eleonora Margheritis"'
Autor:
Arianna Lanza, Eleonora Margheritis, Enrico Mugnaioli, Valentina Cappello, Gianpiero Garau, Mauro Gemmi
Publikováno v:
IUCrJ, Vol 6, Iss 2, Pp 178-188 (2019)
Recent advances in 3D electron diffraction have allowed the structure determination of several model proteins from submicrometric crystals, the unit-cell parameters and structures of which could be immediately validated by known models previously obt
Externí odkaz:
https://doaj.org/article/38fd381db7aa474f9859ee1507544fe1
Autor:
Simona Sestito, Sara Chiarugi, Eleonora Margheritis, Massimiliano Runfola, Simone Bertini, Gianpiero Garau, Simona Rapposelli
Publikováno v:
Proceedings, Vol 22, Iss 1, p 45 (2019)
The struggle to find novel efficacious pharmacological approaches for cancer treatment has ledto the identification of several kinases involved in neoplastic genesis and cell development. [...]
Externí odkaz:
https://doaj.org/article/4349d8e50fcf404384e002458cc3c699
Autor:
Filippo Begarani, Domenico Cassano, Eleonora Margheritis, Roberto Marotta, Francesco Cardarelli, Valerio Voliani
Publikováno v:
Nanomaterials, Vol 8, Iss 11, p 886 (2018)
Although conceptually obvious, the effective delivery of proteins in therapeutic applications is far from being a routine practice. The major limitation is the conservation of protein physicochemical identity during the transport to the target site.
Externí odkaz:
https://doaj.org/article/ed9d91150afc49b0b50ebb92e3e2c11e
Publikováno v:
International Journal of Molecular Sciences. 24:4528
Pore-forming proteins (PFPs) play a central role in many biological processes related to infection, immunity, cancer, and neurodegeneration. A common feature of PFPs is their ability to form pores that disrupt the membrane permeability barrier and io
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2af75c84f74f0e23217f907fc9275e88
https://doi.org/10.3390/ijms24054528
https://doi.org/10.3390/ijms24054528
Autor:
Massimiliano Runfola, Francesca Gado, Eleonora Margheritis, Andrea Bacci, Sara Chiarugi, Gianpiero Garau, Maria E. Riveiro, Clementina Manera, Ramiro Vázquez, Simona Sestito, Simona Rapposelli, Sheraz Gul, Keyvan Rezai, Samuel Huguet
Publikováno v:
European journal of medicinal chemistry. 226
We report the synthesis of novel first-in-class 2-oxindole-based derivatives as dual PDK1-AurA kinase inhibitors as a novel strategy to treat Ewing sarcoma. The most potent compound 12 is suitable for progression to in vivo studies. The specific attr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d22e5a71354dcbc682f269856d613e27
https://pubmed.ncbi.nlm.nih.gov/34624821
https://pubmed.ncbi.nlm.nih.gov/34624821
Autor:
Eleonora Margheritis, Simona Sestito, Sara Chiarugi, Simone Bertini, Simona Rapposelli, Massimiliano Runfola, Gianpiero Garau
Publikováno v:
Proceedings, Vol 22, Iss 1, p 45 (2019)
The struggle to find novel efficacious pharmacological approaches for cancer treatment has ledto the identification of several kinases involved in neoplastic genesis and cell development. [...]
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4dc875d86619e586b311fa13bcb0ddd8
https://doi.org/10.3390/proceedings2019022045
https://doi.org/10.3390/proceedings2019022045
Autor:
Gianpiero Garau, Francesca Natali, Sara Peruzzi, Antimo Gioiello, Serena Mostarda, Daniele Piomelli, Elisa Romeo, Eleonora Margheritis, Beatrice Castellani, Paola Magotti
Publikováno v:
Margheritis, E; Castellani, B; Magotti, P; Peruzzi, S; Romeo, E; Natali, F; et al.(2016). Bile Acid Recognition by NAPE-PLD. ACS CHEMICAL BIOLOGY, 11(10), 2908-2914. doi: 10.1021/acschembio.6b00624. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/6721134h
ACS chemical biology 11 (2016): 2908–2914. doi:10.1021/acschembio.6b00624
info:cnr-pdr/source/autori:Margheritis, Eleonora; Castellani, Beatrice; Magotti, Paola; Peruzzi, Sara; Romeo, Elisa; Natali, Francesca; Mostarda, Serena; Gioiello, Antimo; Piomelli, Daniele; Garau, Gianpiero/titolo:Bile Acid Recognition by NAPE-PLD/doi:10.1021%2Facschembio.6b00624/rivista:ACS chemical biology/anno:2016/pagina_da:2908/pagina_a:2914/intervallo_pagine:2908–2914/volume:11
ACS chemical biology 11 (2016): 2908–2914. doi:10.1021/acschembio.6b00624
info:cnr-pdr/source/autori:Margheritis, Eleonora; Castellani, Beatrice; Magotti, Paola; Peruzzi, Sara; Romeo, Elisa; Natali, Francesca; Mostarda, Serena; Gioiello, Antimo; Piomelli, Daniele; Garau, Gianpiero/titolo:Bile Acid Recognition by NAPE-PLD/doi:10.1021%2Facschembio.6b00624/rivista:ACS chemical biology/anno:2016/pagina_da:2908/pagina_a:2914/intervallo_pagine:2908–2914/volume:11
The membrane-associated enzyme NAPE-PLD (N-acyl phosphatidylethanolamine specific-phospholipase D) generates the endogenous cannabinoid arachidonylethanolamide and other lipid signaling amides, including oleoylethanolamide and palmitoylethanolamide.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72e123a8cdb22d3277f3d642f947e0d3
https://doi.org/10.1021/acschembio.6b00624
https://doi.org/10.1021/acschembio.6b00624
Autor:
Francesco Cardarelli, Filippo Begarani, Eleonora Margheritis, Domenico Cassano, Valerio Voliani, Roberto Marotta
Publikováno v:
Nanomaterials
Volume 8
Issue 11
Nanomaterials (Basel) 8 (2018): 886. doi:10.3390/nano8110886
info:cnr-pdr/source/autori:Begarani F.; Cassano D.; Margheritis E.; Marotta R.; Cardarelli F.; Voliani V./titolo:Silica-based nanoparticles for protein encapsulation and delivery/doi:10.3390%2Fnano8110886/rivista:Nanomaterials (Basel)/anno:2018/pagina_da:886/pagina_a:/intervallo_pagine:886/volume:8
Nanomaterials, Vol 8, Iss 11, p 886 (2018)
Volume 8
Issue 11
Nanomaterials (Basel) 8 (2018): 886. doi:10.3390/nano8110886
info:cnr-pdr/source/autori:Begarani F.; Cassano D.; Margheritis E.; Marotta R.; Cardarelli F.; Voliani V./titolo:Silica-based nanoparticles for protein encapsulation and delivery/doi:10.3390%2Fnano8110886/rivista:Nanomaterials (Basel)/anno:2018/pagina_da:886/pagina_a:/intervallo_pagine:886/volume:8
Nanomaterials, Vol 8, Iss 11, p 886 (2018)
Although conceptually obvious, the effective delivery of proteins in therapeutic applications is far from being a routine practice. The major limitation is the conservation of protein physicochemical identity during the transport to the target site.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25932ce6b8c872386425c5ff0b7c5a20
https://pubmed.ncbi.nlm.nih.gov/30388755
https://pubmed.ncbi.nlm.nih.gov/30388755
Autor:
Gerardo Abbandonato, Ilaria Testa, Gianpiero Garau, Riccardo Nifosì, Giorgio Domenichini, Eleonora Margheritis, Barbara Storti, Ranieri Bizzarri, Jes Dreier
Publikováno v:
ACS chemical biology (Online) 13 (2018): 2082–2093. doi:10.1021/acschembio.8b00267
info:cnr-pdr/source/autori:Storti B.; Margheritis E.; Abbandonato G.; Domenichini G.; Dreier J.; Testa I.; Garau G.; Nifosi R.; Bizzarri R./titolo:Role of Gln222 in Photoswitching of Aequorea Fluorescent Proteins: A Twisting and H-Bonding Affair?/doi:10.1021%2Facschembio.8b00267/rivista:ACS chemical biology (Online)/anno:2018/pagina_da:2082/pagina_a:2093/intervallo_pagine:2082–2093/volume:13
info:cnr-pdr/source/autori:Storti B.; Margheritis E.; Abbandonato G.; Domenichini G.; Dreier J.; Testa I.; Garau G.; Nifosi R.; Bizzarri R./titolo:Role of Gln222 in Photoswitching of Aequorea Fluorescent Proteins: A Twisting and H-Bonding Affair?/doi:10.1021%2Facschembio.8b00267/rivista:ACS chemical biology (Online)/anno:2018/pagina_da:2082/pagina_a:2093/intervallo_pagine:2082–2093/volume:13
Reversibly photoswitchable fluorescent proteins (RSFPs) admirably combine the genetic encoding of fluorescence with the ability to repeatedly toggle between a bright and dark state, adding a new temporal dimension to the fluorescence signal. Accordin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d3cd842e9a092e09fe9903c399f9a02
https://pubmed.ncbi.nlm.nih.gov/29878744
https://pubmed.ncbi.nlm.nih.gov/29878744
Autor:
Gary Rudnick, Lucy R. Forrest, Elizabeth Rhoades, Edwin Rosado, Sotiria Tavoulari, Silvia Ravera, Anu Nagarajan, Yuan-Wei Zhang, David C. DeWitt, Eleonora Margheritis
Publikováno v:
The Journal of biological chemistry. 291(3)
In LeuT, a prokaryotic homolog of neurotransmitter transporters, Na(+) stabilizes outward-open conformational states. We examined how each of the two LeuT Na(+) binding sites contributes to Na(+)-dependent closure of the cytoplasmic pathway using bio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c37229e1d378e351bd70e9ae758a1293
https://pubmed.ncbi.nlm.nih.gov/26582198
https://pubmed.ncbi.nlm.nih.gov/26582198