Zobrazeno 1 - 10
of 50
pro vyhledávání: '"V G, Nicoletti"'
Autor:
Giuseppe Grasso, Roberto Fattorusso, Luciano Pirone, Calcagno D, Francesco Bellia, Massimo Coletta, Sara García-Viñuales, Ahmed Imm, Emilia Pedone, Grazia R. Tundo, Danilo Milardi, Diego Sbardella, Claudio Iacobucci, Lanza, V. G. Nicoletti, Gaetano Malgieri, Gianluca D'Abrosca, Adriana Pietropaolo
Publikováno v:
Chemical science (Online) Chem. Sci., 2019, 10, 2732 (2019). doi:10.1039/c8sc03394c
info:cnr-pdr/source/autori:F. Bellia, V. Lanza, S. Garcia-Vinuales, I. M. M. Ahmed, A. Pietropaolo, C. Iacobucci, G. Malgieri, G. D'Abrosca, R. Fattorusso, V. G. Nicoletti, D. Sbardella, G. R. Tundo, M. Coletta,L. Pirone,E. Pedone, D. Calcagno,G. Grasso and D. Milardi/titolo:Ubiquitin binds the amyloid b peptide and interferes with its clearance pathways/doi:10.1039%2Fc8sc03394c/rivista:Chemical science (Online)/anno:2019/pagina_da:/pagina_a:/intervallo_pagine:/volume:Chem. Sci., 2019, 10, 2732
Chemical Science
info:cnr-pdr/source/autori:F. Bellia, V. Lanza, S. Garcia-Vinuales, I. M. M. Ahmed, A. Pietropaolo, C. Iacobucci, G. Malgieri, G. D'Abrosca, R. Fattorusso, V. G. Nicoletti, D. Sbardella, G. R. Tundo, M. Coletta,L. Pirone,E. Pedone, D. Calcagno,G. Grasso and D. Milardi/titolo:Ubiquitin binds the amyloid b peptide and interferes with its clearance pathways/doi:10.1039%2Fc8sc03394c/rivista:Chemical science (Online)/anno:2019/pagina_da:/pagina_a:/intervallo_pagine:/volume:Chem. Sci., 2019, 10, 2732
Chemical Science
Appetite for ubiquitin: a gushy travel companion in the intracellular journey of the amyloid β peptide.
Several lines of evidence point to a compromised proteostasis associated with a reduction of the Ubiquitin Proteasome System (UPS) activity
Several lines of evidence point to a compromised proteostasis associated with a reduction of the Ubiquitin Proteasome System (UPS) activity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::792f03f6255646de6b9b235d01b3180d
Autor:
Ikhlas Mohamed Mohamud Ahmed, Grazia R. Tundo, Giosuè Costa, V. G. Nicoletti, Anna Santoro, Danilo Milardi, Gianluca D'Abrosca, Diego Sbardella, Alessandra Cannizzo, Francesco Bellia, Gaetano Malgieri, Adriana Pietropaolo, Sara García-Viñuales, Massimiliano Coletta, Stefano Alcaro, Roberto Fattorusso, Valeria Lanza, Mariaconcetta Arizzi, Giuseppe Grasso
Publikováno v:
ChemMedChem
15 (2020): 302–316. doi:10.1002/cmdc.201900612
info:cnr-pdr/source/autori:Santoro A.M.; Lanza V.; Bellia F.; Sbardella D.; Tundo G.R.; Cannizzo A.; Grasso G.; Arizzi M.; Nicoletti V.G.; Alcaro S.; Costa G.; Pietropaolo A.; Malgieri G.; D'Abrosca G.; Fattorusso R.; Garcia-Vinuales S.; Ahmed I.M.M.; Coletta M.; Milardi D./titolo:Pyrazolones Activate the Proteasome by Gating Mechanisms and Protect Neuronal Cells from ?-Amyloid Toxicity/doi:10.1002%2Fcmdc.201900612/rivista:ChemMedChem (Print)/anno:2020/pagina_da:302/pagina_a:316/intervallo_pagine:302–316/volume:15
15 (2020): 302–316. doi:10.1002/cmdc.201900612
info:cnr-pdr/source/autori:Santoro A.M.; Lanza V.; Bellia F.; Sbardella D.; Tundo G.R.; Cannizzo A.; Grasso G.; Arizzi M.; Nicoletti V.G.; Alcaro S.; Costa G.; Pietropaolo A.; Malgieri G.; D'Abrosca G.; Fattorusso R.; Garcia-Vinuales S.; Ahmed I.M.M.; Coletta M.; Milardi D./titolo:Pyrazolones Activate the Proteasome by Gating Mechanisms and Protect Neuronal Cells from ?-Amyloid Toxicity/doi:10.1002%2Fcmdc.201900612/rivista:ChemMedChem (Print)/anno:2020/pagina_da:302/pagina_a:316/intervallo_pagine:302–316/volume:15
Proteasome malfunction parallels abnormal amyloid accumulation in Alzheimer's Disease (AD). Here we scrutinize a small library of pyrazolones by assaying their ability to enhance proteasome activity and protect neuronal cells from amyloid toxicity. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b05aae170c72e9441febd8137a4cb1fa
http://hdl.handle.net/11591/424097
http://hdl.handle.net/11591/424097
Publikováno v:
Chemistry (Weinh., Print) 22 (2016): 13287–13300. doi:10.1002/chem.201602816
info:cnr-pdr/source/autori:Magri, Antonio; La Mendola, Diego; Nicoletti, Vincenzo Giuseppe; Pappalardo, Giuseppe; Rizzarelli, Enrico/titolo:New Insight in Copper-Ion Binding to Human Islet Amyloid: The Contribution of Metal-Complex Speciation To Reveal the Polypeptide Toxicity/doi:10.1002%2Fchem.201602816/rivista:Chemistry (Weinh., Print)/anno:2016/pagina_da:13287/pagina_a:13300/intervallo_pagine:13287–13300/volume:22
info:cnr-pdr/source/autori:Magri, Antonio; La Mendola, Diego; Nicoletti, Vincenzo Giuseppe; Pappalardo, Giuseppe; Rizzarelli, Enrico/titolo:New Insight in Copper-Ion Binding to Human Islet Amyloid: The Contribution of Metal-Complex Speciation To Reveal the Polypeptide Toxicity/doi:10.1002%2Fchem.201602816/rivista:Chemistry (Weinh., Print)/anno:2016/pagina_da:13287/pagina_a:13300/intervallo_pagine:13287–13300/volume:22
Type-2 diabetes (T2D) is considered to be a potential threat on a global level. Recently, T2D has been listed as a misfolding disease, such as Alzheimer's and Parkinson's diseases. Human islet amyloid polypeptide (hIAPP) is a molecule cosecreted in p
Autor:
Giuseppe Arena, Nicola Margiotta, Irina Naletova, Alessandra Curci, Giovanni Natile, Diego La Mendola, Cristina Satriano, V. G. Nicoletti, Enrico Rizzarelli
Publikováno v:
Oncotarget
Copper homeostasis is generally investigated focusing on a single component of the metallostasis network. Here we address several of the factors controlling the metallostasis for neuroblastoma cells (SH-SY5Y) upon treatment with 2,9-dimethyl-1,10-phe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c23edd0db3e25b1e0ac04359af45671
http://hdl.handle.net/20.500.11769/360441
http://hdl.handle.net/20.500.11769/360441
Autor:
V. G. Nicoletti, Giuseppe Caruso, Susan M. Lunte, Donatella A. Distefano, Claudia G. Fresta, Giuseppe Lazzarino, Paolo Parlascino
Human amylin (hA1-37) is a polypeptide hormone secreted in conjunction with insulin from the pancreatic β-cells involved in the pathogenesis of type 2 diabetes mellitus (T2DM). The shorter fragment hA17-29 than full-length peptide is capable to form
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::91f4d5881227d666fab2d1a03a6ceddf
http://hdl.handle.net/20.500.11769/43681
http://hdl.handle.net/20.500.11769/43681
Autor:
V. G. Nicoletti, Bruno Pignataro, Claudia Cascio, Francesco Attanasio, Anna Savarino, Enrico Rizzarelli, Salvatore Fisichella
Publikováno v:
Biochemical and biophysical research communications
354 (2007): 899–905. doi:10.1016/j.bbrc.2007.01.061
info:cnr-pdr/source/autori:Attanasio F., C. Cascio, S. Fisichella, V. G. Nicoletti, B. Pignataro, A. Savarino and E. Rizzarelli/titolo:Trehalose effects on alpha-crystallin aggregates/doi:10.1016%2Fj.bbrc.2007.01.061/rivista:Biochemical and biophysical research communications (Print)/anno:2007/pagina_da:899/pagina_a:905/intervallo_pagine:899–905/volume:354
354 (2007): 899–905. doi:10.1016/j.bbrc.2007.01.061
info:cnr-pdr/source/autori:Attanasio F., C. Cascio, S. Fisichella, V. G. Nicoletti, B. Pignataro, A. Savarino and E. Rizzarelli/titolo:Trehalose effects on alpha-crystallin aggregates/doi:10.1016%2Fj.bbrc.2007.01.061/rivista:Biochemical and biophysical research communications (Print)/anno:2007/pagina_da:899/pagina_a:905/intervallo_pagine:899–905/volume:354
alpha-Crystallin in its native state is a large, heterogeneous, low-molecular weight (LMW) aggregate that under certain conditions may progressively became part of insoluble high-molecular weight (HMW) systems. These systems are supposed to play a re
Autor:
V. G. Nicoletti, Giuseppe Pandini, Enrico Rizzarelli, Cristina Satriano, Diego La Mendola, Fiorenza Gianì, Adriana Pietropaolo, Alessio Travaglia
Publikováno v:
Frontiers in Neuroscience
The nerve growth factor (NGF) N-terminus peptide, NGF(1-14), and its acetylated form, Ac-NGF(1-14), were investigated to scrutinise the ability of this neurotrophin domain to mimic the whole protein. Theoretical calculations demonstrated that non-cov
Autor:
Antonio Magrì, Irina Naletova, Alessandro Giuffrida, Giovanni Tabbì, Cristina Satriano, Giuseppe Pappalardo, Francesco Attanasio, V. G. Nicoletti
Publikováno v:
Journal of inorganic biochemistry 164 (2016): 59–69. doi:10.1016/j.jinorgbio.2016.08.013
info:cnr-pdr/source/autori:Magri, Antonio; Tabbi, Giovanni; Giuffrida, Alessandro; Pappalardo, Giuseppe; Satriano, Cristina; Naletova, Irina; Nicoletti, Vincenzo G.; Attanasio, Francesco/titolo:Influence of the N-terminus acetylation of Semax, a synthetic analog of ACTH(4-10), on copper(II) and zinc(II) coordination and biological properties/doi:10.1016%2Fj.jinorgbio.2016.08.013/rivista:Journal of inorganic biochemistry/anno:2016/pagina_da:59/pagina_a:69/intervallo_pagine:59–69/volume:164
info:cnr-pdr/source/autori:Magri, Antonio; Tabbi, Giovanni; Giuffrida, Alessandro; Pappalardo, Giuseppe; Satriano, Cristina; Naletova, Irina; Nicoletti, Vincenzo G.; Attanasio, Francesco/titolo:Influence of the N-terminus acetylation of Semax, a synthetic analog of ACTH(4-10), on copper(II) and zinc(II) coordination and biological properties/doi:10.1016%2Fj.jinorgbio.2016.08.013/rivista:Journal of inorganic biochemistry/anno:2016/pagina_da:59/pagina_a:69/intervallo_pagine:59–69/volume:164
Semax is a heptapeptide (Met-Glu-His-Phe-Pro-Gly-Pro) that encompasses the sequence 4-7 of N-terminal domain of the adrenocorticotropic hormone and a C-terminal Pro-Gly-Pro tripeptide. N-terminal amino group acetylation (Ac-Semax) modulates the chemi
Publikováno v:
Metallomics (Online) 8 (2016): 750–761. doi:10.1039/c6mt00067c
info:cnr-pdr/source/autori:Naletova, Irina; Nicoletti, Vincenzo G; Milardi, Danilo; Pietropaolo, Adriana; Grasso, Giuseppe/titolo:Copper, differently from zinc, affects the conformation, oligomerization state and activity of bradykinin./doi:10.1039%2Fc6mt00067c/rivista:Metallomics (Online)/anno:2016/pagina_da:750/pagina_a:761/intervallo_pagine:750–761/volume:8
info:cnr-pdr/source/autori:Naletova, Irina; Nicoletti, Vincenzo G; Milardi, Danilo; Pietropaolo, Adriana; Grasso, Giuseppe/titolo:Copper, differently from zinc, affects the conformation, oligomerization state and activity of bradykinin./doi:10.1039%2Fc6mt00067c/rivista:Metallomics (Online)/anno:2016/pagina_da:750/pagina_a:761/intervallo_pagine:750–761/volume:8
The sole role of bradykinin (BK) as an inflammatory mediator is controversial, as recent data also support an anti-inflammatory role for BK in Alzheimer's disease (AD). The involvement of two different receptors (B1R and B2R) could be a key to unders
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9fbf81240893d5dc6731072203044bf2
http://hdl.handle.net/20.500.11769/19002
http://hdl.handle.net/20.500.11769/19002
Wound healing is a complex biological process that aims to repair damaged tissue. Even though many biological and biochemical mechanisms associated with the steps of physiological wound healing are known, there is still significant morbidity and mort
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d19457c90ca2f7621c047e978869a6b
http://hdl.handle.net/20.500.11769/19003
http://hdl.handle.net/20.500.11769/19003