Zobrazeno 1 - 10
of 52
pro vyhledávání: '"Antonio Magrì"'
Autor:
Antonio Magrì, Barbara Tomasello, Irina Naletova, Giovanni Tabbì, Warren R. L. Cairns, Valentina Greco, Sebastiano Sciuto, Diego La Mendola, Enrico Rizzarelli
Publikováno v:
Biomolecules, Vol 14, Iss 9, p 1104 (2024)
A low level of Neurotrophins (NTs), their Tyrosine Kinase Receptors (Trks), Vascular Endothelial Growth Factors (VEGFs) and their receptors, mainly VEGFR1 and VEGFR2, characterizes AD brains. The use of NTs and VEGFs as drugs presents different issue
Externí odkaz:
https://doaj.org/article/c00511307d7247e288aaa9fd96d62597
Autor:
Patrizia Di Pietro, Nunzia Caporarello, Carmelina D. Anfuso, Gabriella Lupo, Antonio Magrì, Diego La Mendola, Cristina Satriano
Publikováno v:
ACS Omega, Vol 2, Iss 8, Pp 4071-4079 (2017)
Externí odkaz:
https://doaj.org/article/063836f7d90b4195a54d82a6f82740d0
Autor:
Carla Isernia, Diego La Mendola, Gaetano Malgieri, Giuseppe Pappalardo, Roberto Fattorusso, Antonio Magrì, Luigi Russo, Maria Anna Campitiello, Luca Raiola
Publikováno v:
Molecules, Vol 18, Iss 9, Pp 11467-11484 (2013)
Many proteins perform essential biological functions by means of regions that lacking specific organized structure exist as an ensemble of interconverting transient conformers. The characterization of such regions, including the description of their
Externí odkaz:
https://doaj.org/article/91454a39419c4e4f8f90e688d2392b0d
Autor:
Antonio, Magrì, Giovanni, Tabbì, Irina, Naletova, Francesco, Attanasio, Giuseppe, Arena, Enrico, Rizzarelli
Publikováno v:
International journal of molecular sciences. 23(6)
Ctr1 regulates copper uptake and its intracellular distribution. The first 14 amino acid sequence of the Ctr1 ectodomain Ctr1
Autor:
Antonio Magrì, Giovanni Tabbì, Irina Naletova, Francesco Attanasio, Giuseppe Arena, Enrico Rizzarelli
Publikováno v:
International journal of molecular sciences (Online) (2022): 2929–2947. doi:10.3390/ijms23062929
info:cnr-pdr/source/autori:Antonio Magrì, Giovanni Tabbì, Irina Naletova, Francesco Attanasio*, Giuseppe Arena and Enrico Rizzarelli/titolo:A Deeper Insight in Metal Binding to the hCtr1 N-terminus Fragment: Affinity, Speciation and Binding Mode of Binuclear Cu2+ and Mononuclear Ag+ Complex Species./doi:10.3390%2Fijms23062929/rivista:International journal of molecular sciences (Online)/anno:2022/pagina_da:2929/pagina_a:2947/intervallo_pagine:2929–2947/volume
International Journal of Molecular Sciences; Volume 23; Issue 6; Pages: 2929
info:cnr-pdr/source/autori:Antonio Magrì, Giovanni Tabbì, Irina Naletova, Francesco Attanasio*, Giuseppe Arena and Enrico Rizzarelli/titolo:A Deeper Insight in Metal Binding to the hCtr1 N-terminus Fragment: Affinity, Speciation and Binding Mode of Binuclear Cu2+ and Mononuclear Ag+ Complex Species./doi:10.3390%2Fijms23062929/rivista:International journal of molecular sciences (Online)/anno:2022/pagina_da:2929/pagina_a:2947/intervallo_pagine:2929–2947/volume
International Journal of Molecular Sciences; Volume 23; Issue 6; Pages: 2929
Ctr1 regulates copper uptake and its intracellular distribution. The first 14 amino acid sequence of the Ctr1 ectodomain Ctr1(1-14) encompasses the characteristic Amino Terminal Cu2+ and Ni2+ binding motif (ATCUN) as well as the bis-His binding motif
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b2594b5b1175be8c912f279e55fdb36
http://www.cnr.it/prodotto/i/465035
http://www.cnr.it/prodotto/i/465035
Autor:
Lara Russo, Chiara Giacomelli, Mariagrazia Fortino, Tiziano Marzo, Gianmarco Ferri, Mariantonietta Calvello, Alessandro Viegi, Antonio Magrì, Alessandro Pratesi, Adriana Pietropaolo, Francesco Cardarelli, Claudia Martini, Enrico Rizzarelli, Laura Marchetti, Diego La Mendola, Maria Letizia Trincavelli
Brain-derived neurotrophic factor (BDNF) is a neurotrophin (NT) essential for neuronal development and synaptic plasticity. Dysregulation of BDNF signaling is implicated in different neurological disorders. The direct NT administration as therapeutic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ec7524565244c503983178e1505c6da
https://hdl.handle.net/11384/125262
https://hdl.handle.net/11384/125262
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 9343, p 9343 (2020)
International Journal of Molecular Sciences
Volume 21
Issue 24
International journal of molecular sciences
21 (2020). doi:10.3390/ijms21249343
info:cnr-pdr/source/autori:Santoro, Anna Maria; Zimbone, Stefania; Magri, Antonio; La Mendola, Diego; Grasso, Giulia/titolo:The Role of Copper (II) on Kininogen Binding to Tropomyosin in the Presence of a Histidine-Proline-Rich Peptide/doi:10.3390%2Fijms21249343/rivista:International journal of molecular sciences (Print)/anno:2020/pagina_da:/pagina_a:/intervallo_pagine:/volume:21
International Journal of Molecular Sciences
Volume 21
Issue 24
International journal of molecular sciences
21 (2020). doi:10.3390/ijms21249343
info:cnr-pdr/source/autori:Santoro, Anna Maria; Zimbone, Stefania; Magri, Antonio; La Mendola, Diego; Grasso, Giulia/titolo:The Role of Copper (II) on Kininogen Binding to Tropomyosin in the Presence of a Histidine-Proline-Rich Peptide/doi:10.3390%2Fijms21249343/rivista:International journal of molecular sciences (Print)/anno:2020/pagina_da:/pagina_a:/intervallo_pagine:/volume:21
The antiangiogenic activity of the H/P domain of histidine&ndash
proline-rich glycoprotein is mediated by its binding with tropomyosin, a protein exposed on endothelial cell-surface during the angiogenic switch, in presence of zinc ions. Althoug
proline-rich glycoprotein is mediated by its binding with tropomyosin, a protein exposed on endothelial cell-surface during the angiogenic switch, in presence of zinc ions. Althoug
Autor:
Giuseppe Di Natale, Giovanni Tabbì, Diego La Mendola, Antonio Magrì, Massimiliano Francesco Peana, Enrico Rizzarelli, Maria Antonietta Zoroddu, Adriana Pietropaolo
Publikováno v:
Chemistry (Weinh., Print) 26 (2020): 13072–13084. doi:10.1002/chem.202002114
info:cnr-pdr/source/autori:Magri A.; Tabbi G.; Di Natale G.; La Mendola D.; Pietropaolo A.; Zoroddu M.A.; Peana M.; Rizzarelli E./titolo:Zinc Interactions with a Soluble Mutated Rat Amylin to Mimic Whole Human Amylin: An Experimental and Simulation Approach to Understand Stoichiometry, Speciation and Coordination of the Metal Complexes/doi:10.1002%2Fchem.202002114/rivista:Chemistry (Weinh., Print)/anno:2020/pagina_da:13072/pagina_a:13084/intervallo_pagine:13072–13084/volume:26
info:cnr-pdr/source/autori:Magri A.; Tabbi G.; Di Natale G.; La Mendola D.; Pietropaolo A.; Zoroddu M.A.; Peana M.; Rizzarelli E./titolo:Zinc Interactions with a Soluble Mutated Rat Amylin to Mimic Whole Human Amylin: An Experimental and Simulation Approach to Understand Stoichiometry, Speciation and Coordination of the Metal Complexes/doi:10.1002%2Fchem.202002114/rivista:Chemistry (Weinh., Print)/anno:2020/pagina_da:13072/pagina_a:13084/intervallo_pagine:13072–13084/volume:26
Islet amyloid polypeptide (IAPP) is a hormone co-secreted with insulin and zinc from pancreatic β-cells. To overcome the low solubility of human IAPP, we characterized zinc complexes species formed with 1) a mutated form of rat-IAPP(1-37; R18 H) abl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2fb85b4ec6f8489780b62d3ecf192d1
http://www.scopus.com/record/display.url?eid=2-s2.0-85091145213&origin=inward
http://www.scopus.com/record/display.url?eid=2-s2.0-85091145213&origin=inward
Autor:
Gabriella Lupo, Carmelina Daniela Anfuso, Lorena Maria Cucci, Antonio Magrì, Cristina Satriano, Vanessa Sanfilippo, Anna Longo, Diego La Mendola, Valeria Verde
Publikováno v:
International Journal of Molecular Sciences
Volume 21
Issue 15
International journal of molecular sciences
21 (2020): 1–23. doi:10.3390/ijms21155571
info:cnr-pdr/source/autori:Verde, Valeria; Longo, Anna; Cucci, Lorena Maria; Sanfilippo, Vanessa; Magrì, Antonio; Satriano, Cristina; Anfuso, Carmelina Daniela; Lupo, Gabriella; La Mendola, Diego/titolo:Anti-angiogenic and anti-proliferative graphene oxide nanosheets for tumor cell therapy/doi:10.3390%2Fijms21155571/rivista:International journal of molecular sciences (Print)/anno:2020/pagina_da:1/pagina_a:23/intervallo_pagine:1–23/volume:21
International Journal of Molecular Sciences, Vol 21, Iss 5571, p 5571 (2020)
Volume 21
Issue 15
International journal of molecular sciences
21 (2020): 1–23. doi:10.3390/ijms21155571
info:cnr-pdr/source/autori:Verde, Valeria; Longo, Anna; Cucci, Lorena Maria; Sanfilippo, Vanessa; Magrì, Antonio; Satriano, Cristina; Anfuso, Carmelina Daniela; Lupo, Gabriella; La Mendola, Diego/titolo:Anti-angiogenic and anti-proliferative graphene oxide nanosheets for tumor cell therapy/doi:10.3390%2Fijms21155571/rivista:International journal of molecular sciences (Print)/anno:2020/pagina_da:1/pagina_a:23/intervallo_pagine:1–23/volume:21
International Journal of Molecular Sciences, Vol 21, Iss 5571, p 5571 (2020)
Graphene oxide (GO) is a bidimensional novel material that exhibits high biocompatibility and angiogenic properties, mostly related to the intracellular formation of reactive oxygen species (ROS). In this work, we set up an experimental methodology f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2588bfdd14f211133ad9827514a2847
http://hdl.handle.net/11568/1053099
http://hdl.handle.net/11568/1053099
Publikováno v:
Inorganica Chimica Acta (Testo stamp.) 472 (2018): 93–102. doi:10.1016/j.ica.2017.10.032
info:cnr-pdr/source/autori:Magri A.; Di Natale G.; Rizzarelli E./titolo:Copper-assisted interaction between amyloid-? and prion: Ternary metal complexes with A? N-terminus and octarepeat/doi:10.1016%2Fj.ica.2017.10.032/rivista:Inorganica Chimica Acta (Testo stamp.)/anno:2018/pagina_da:93/pagina_a:102/intervallo_pagine:93–102/volume:472
info:cnr-pdr/source/autori:Magri A.; Di Natale G.; Rizzarelli E./titolo:Copper-assisted interaction between amyloid-? and prion: Ternary metal complexes with A? N-terminus and octarepeat/doi:10.1016%2Fj.ica.2017.10.032/rivista:Inorganica Chimica Acta (Testo stamp.)/anno:2018/pagina_da:93/pagina_a:102/intervallo_pagine:93–102/volume:472
Alzheimer and prion diseases are neurodegenerative disorders in which amyloid-beta (Aβ) and prion protein (PrP), respectively, failed their normal functions inducing cellular apoptosis. Histidine-based high-affinity metal-binding sites in the N-term