Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Maria Grazia Santangelo"'
Autor:
Elena Zanni, Erika Bruni, Chandrakanth Reddy Chandraiahgari, Giovanni De Bellis, Maria Grazia Santangelo, Maurizio Leone, Agnese Bregnocchi, Patrizia Mancini, Maria Sabrina Sarto, Daniela Uccelletti
Publikováno v:
Journal of Nanobiotechnology, Vol 15, Iss 1, Pp 1-12 (2017)
Abstract Background Nanotechnologies are currently revolutionizing the world around us, improving the quality of our lives thanks to a multitude of applications in several areas including the environmental preservation, with the biodeterioration phen
Externí odkaz:
https://doaj.org/article/82a5997612bd4075a5b2caa66f66d460
Autor:
Rosina Noto, Maria Grazia Santangelo, Stefano Ricagno, Maria Rosalia Mangione, Matteo Levantino, Margherita Pezzullo, Vincenzo Martorana, Antonio Cupane, Martino Bolognesi, Mauro Manno
Publikováno v:
PLoS ONE, Vol 7, Iss 3, p e32444 (2012)
Neuroserpin, a member of the serpin protein superfamily, is an inhibitor of proteolytic activity that is involved in pathologies such as ischemia, Alzheimer's disease, and Familial Encephalopathy with Neuroserpin Inclusion Bodies (FENIB). The latter
Externí odkaz:
https://doaj.org/article/006e9ff63bbb424697374b674fb907f4
Autor:
Bernhard Spingler, Chiara Da Pieve, Alfredo Medina-Molner, Philipp M. Antoni, Maria Grazia Santangelo
Publikováno v:
CHIMIA, Vol 63, Iss 3 (2009)
Metal ions bind to nucleic acids at various positions. This binding can be modulated by using metal complexes with appropriate ligands. Novel mono- and especially dinuclear metal complexes could be a powerful tool to detect rare, but still physiologi
Externí odkaz:
https://doaj.org/article/c073233622bd48aab6d79c17f3a10340
Publikováno v:
RSC Advances. 6:75082-75091
The subtle interplay between long range electrostatic forces, hydrophobic interactions and short range protein-protein interactions regulates the onset/evolution of protein aggregation processes as well as the stability of protein supramolecular stru
Autor:
Matteo Levantino, Maria Rosalia Mangione, Antonio Cupane, Martino Bolognesi, Stefano Ricagno, Vincenzo Martorana, Rosina Noto, Maria Grazia Santangelo, Mauro Manno, Daniele Parisi
Publikováno v:
Biochimica et Biophysica Acta
Biochimica et biophysica acta. Proteins and proteomics 1854 (2015): 110–117. doi:10.1016/j.bbapap.2014.10.002
info:cnr-pdr/source/autori:Noto, Rosina; Santangelo, Maria Grazia; Levantino, Matteo; Cupane, Antonio; Mangione, Maria Rosalia; Parisi, Daniele; Ricagno, Stéfano; Bolognesi, Martino; Manno, Mauro; Martorana, Vincenzo/titolo:Functional and dysfunctional conformers of human neuroserpin characterized by optical spectroscopies and Molecular Dynamics/doi:10.1016%2Fj.bbapap.2014.10.002/rivista:Biochimica et biophysica acta. Proteins and proteomics/anno:2015/pagina_da:110/pagina_a:117/intervallo_pagine:110–117/volume:1854
Biochimica et biophysica acta. Proteins and proteomics 1854 (2015): 110–117. doi:10.1016/j.bbapap.2014.10.002
info:cnr-pdr/source/autori:Noto, Rosina; Santangelo, Maria Grazia; Levantino, Matteo; Cupane, Antonio; Mangione, Maria Rosalia; Parisi, Daniele; Ricagno, Stéfano; Bolognesi, Martino; Manno, Mauro; Martorana, Vincenzo/titolo:Functional and dysfunctional conformers of human neuroserpin characterized by optical spectroscopies and Molecular Dynamics/doi:10.1016%2Fj.bbapap.2014.10.002/rivista:Biochimica et biophysica acta. Proteins and proteomics/anno:2015/pagina_da:110/pagina_a:117/intervallo_pagine:110–117/volume:1854
Neuroserpin (NS) is a serine protease inhibitor (SERPIN) involved in different neurological pathologies, including the Familial Encephalopathy with Neuroserpin Inclusion Bodies (FENIB), related to the aberrant polymerization of NS mutants. Here we pr
Autor:
Maria Sabrina Sarto, Chandrakanth Reddy Chandraiahgari, Maria Grazia Santangelo, Patrizia Mancini, Giovanni De Bellis, Daniela Uccelletti, Maurizio Leone, Elena Zanni, Erika Bruni, Agnese Bregnocchi
Publikováno v:
Journal of Nanobiotechnology, Vol 15, Iss 1, Pp 1-12 (2017)
Journal of Nanobiotechnology
Journal of Nanobiotechnology
Background Nanotechnologies are currently revolutionizing the world around us, improving the quality of our lives thanks to a multitude of applications in several areas including the environmental preservation, with the biodeterioration phenomenon re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95cc55b12f6aa7506adc060dbfe86533
http://www.jnanobiotechnology.com/start.asp
http://www.jnanobiotechnology.com/start.asp
Autor:
Alberto Barbiroli, Margherita Pezzullo, Martino Bolognesi, Maria Grazia Santangelo, Mauro Manno, Francesco Bonomi, Stefano Ricagno, Matteo Levantino
Publikováno v:
Biophysical journal
99 (2010): 3402–3411. doi:10.1016/j.bpj.2010.09.021
info:cnr-pdr/source/autori:Ricagno S.; Pezzullo M.; Barbiroli A.; Manno M.; Levantino M.; Santangelo M.G.; Bonomi F.; Bolognesi M./titolo:Two latent and two hyperstable polymeric forms of human neuroserpin/doi:10.1016%2Fj.bpj.2010.09.021/rivista:Biophysical journal (Print)/anno:2010/pagina_da:3402/pagina_a:3411/intervallo_pagine:3402–3411/volume:99
99 (2010): 3402–3411. doi:10.1016/j.bpj.2010.09.021
info:cnr-pdr/source/autori:Ricagno S.; Pezzullo M.; Barbiroli A.; Manno M.; Levantino M.; Santangelo M.G.; Bonomi F.; Bolognesi M./titolo:Two latent and two hyperstable polymeric forms of human neuroserpin/doi:10.1016%2Fj.bpj.2010.09.021/rivista:Biophysical journal (Print)/anno:2010/pagina_da:3402/pagina_a:3411/intervallo_pagine:3402–3411/volume:99
Human neuroserpin (hNS) is a serine protease inhibitor that belongs to the serpin superfamily and is expressed in nervous tissues. The serpin fold is generally characterized by a long exposed loop, termed the reactive center loop, that acts as bait f
Publikováno v:
The Journal of Physical Chemistry B. 106:11323-11328
We have used a sol−gel technique to obtain optically transparent hydrogels in which water is trapped within a tridimensional disordered silica matrix. A suitable aging of these hydrogels enables to have transparent noncracking samples down to cryog
Autor:
Matteo Levantino, Margherita Pezzullo, Stefano Ricagno, Maria Grazia Santangelo, Maria Rosalia Mangione, Antonio Cupane, Martino Bolognesi, Rosina Noto, Vincenzo Martorana, Mauro Manno
Publikováno v:
Proteins
80 (2012): 8–13. doi:10.1002/prot.23197
info:cnr-pdr/source/autori:Santangelo MG; Noto R; Levantino M; Cupane A; Ricagno S, Pezzullo M, Bolognesi M, Mangione MR, Martorana V, Manno M/titolo:On the molecular structure of human neuroserpin polymers/doi:10.1002%2Fprot.23197/rivista:Proteins (Print)/anno:2012/pagina_da:8/pagina_a:13/intervallo_pagine:8–13/volume:80
80 (2012): 8–13. doi:10.1002/prot.23197
info:cnr-pdr/source/autori:Santangelo MG; Noto R; Levantino M; Cupane A; Ricagno S, Pezzullo M, Bolognesi M, Mangione MR, Martorana V, Manno M/titolo:On the molecular structure of human neuroserpin polymers/doi:10.1002%2Fprot.23197/rivista:Proteins (Print)/anno:2012/pagina_da:8/pagina_a:13/intervallo_pagine:8–13/volume:80
The polymerization of serpins is at the root of a large class of diseases; the molecular structure of serpin polymers has been recently debated. In this work, we study the polymerization kinetics of human neuroserpin by Fourier Transform Infra Red sp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fdf86da2e01772b09fa88ab63d8b30ad
http://hdl.handle.net/10447/60941
http://hdl.handle.net/10447/60941
Publikováno v:
ChemInform. 33