Zobrazeno 1 - 4
of 4
pro vyhledávání: '"chemistry [Imidazoles]"'
Publikováno v:
Journal of chemical theory and computation 11(10), 4911-4922 (2015). doi:10.1021/acs.jctc.5b00208
Huntington's disease is a fatal and devastating neurodegenerative genetic disorder for which there is currently no cure. It is characterized by Huntingtin protein's mRNA transcripts with 36 or more CAG repeats. Inhibiting the formation of pathologica
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9747a4ce15b50440ec6afb29faee8fa2
https://pubmed.ncbi.nlm.nih.gov/26574279
https://pubmed.ncbi.nlm.nih.gov/26574279
Autor:
Karl Jansen, Giovanni La Penna, Giancarlo Rossi, Velia Minicozzi, Silvia Morante, Francesco Stellato, Paolo Giannozzi
Publikováno v:
Metallomics
4 (2012): 156–165. doi:10.1039/c2mt00148a
info:cnr-pdr/source/autori:Giannozzi, Paolo; Jansen, Karl; La Penna, Giovanni; Minicozzi, Velia; Morante, Silvia; Rossi, Giancarlo; Stellato, Francesco/titolo:Zn induced structural aggregation patterns of beta-amyloid peptides by first-principle simulations and XAS measurements/doi:10.1039%2Fc2mt00148a/rivista:Metallomics (Print)/anno:2012/pagina_da:156/pagina_a:165/intervallo_pagine:156–165/volume:4
Metallomics 4, 156-165 (2012). doi:10.1039/c2mt00148a
4 (2012): 156–165. doi:10.1039/c2mt00148a
info:cnr-pdr/source/autori:Giannozzi, Paolo; Jansen, Karl; La Penna, Giovanni; Minicozzi, Velia; Morante, Silvia; Rossi, Giancarlo; Stellato, Francesco/titolo:Zn induced structural aggregation patterns of beta-amyloid peptides by first-principle simulations and XAS measurements/doi:10.1039%2Fc2mt00148a/rivista:Metallomics (Print)/anno:2012/pagina_da:156/pagina_a:165/intervallo_pagine:156–165/volume:4
Metallomics 4, 156-165 (2012). doi:10.1039/c2mt00148a
We show in this paper that in the presence of Zn ions a peculiar structural aggregation pattern of beta-amyloid peptides in which metal ions are sequentially coordinated to either three or four histidines of nearby peptides is favored. To stabilize t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef9c4dd8f751640d58a609d54c032371
Autor:
Gianfranco Menestrina, Silvia Morante, Wolfram Meyer-Klaucke, Francesco Stellato, Rossella Tomazzolli, Mauro Dalla Serra, Cristina Potrich
Publikováno v:
European biophysics journal 35, 12 (2006). doi:10.1007/s00249-005-0041-7
European biophysics journal 35 (2006): 340–351. doi:10.1007/s00249-005-0041-7
info:cnr-pdr/source/autori:Stellato F., Menestrina G., Dalla Serra M., Potrich C., Tomazzolli R., Meyer-Klaucke W., Morante S./titolo:Metal binding in amyloid beta-peptides shows intra-and inter-peptide coordination modes/doi:10.1007%2Fs00249-005-0041-7/rivista:European biophysics journal/anno:2006/pagina_da:340/pagina_a:351/intervallo_pagine:340–351/volume:35
European biophysics journal 35 (2006): 340–351. doi:10.1007/s00249-005-0041-7
info:cnr-pdr/source/autori:Stellato F., Menestrina G., Dalla Serra M., Potrich C., Tomazzolli R., Meyer-Klaucke W., Morante S./titolo:Metal binding in amyloid beta-peptides shows intra-and inter-peptide coordination modes/doi:10.1007%2Fs00249-005-0041-7/rivista:European biophysics journal/anno:2006/pagina_da:340/pagina_a:351/intervallo_pagine:340–351/volume:35
X-ray absorption spectroscopy data show different metal binding site structures in beta-amyloid peptides according to whether they are complexed with Cu(2+) or Zn(2+) ions. While the geometry around copper is stably consistent with an intra-peptide b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4e03be362a0c676d7545b97a93696c6
https://bib-pubdb1.desy.de/record/80585
https://bib-pubdb1.desy.de/record/80585
Autor:
Alessandro Triolo, Miguel Angel Gonzalez, Olga Russina, Christopher Hardacre, Mark Nieuwenhuyzen, Hans Grimm
Publikováno v:
The journal of physical chemistry. B 109 (2005): 22061–22066. doi:10.1021/jp053355j
info:cnr-pdr/source/autori:A. Triolo1; O. Russina2; C. Hardacre3; M. Nieuwenhuyzen3; M. A. Gonzalez4; and H. Grimm5/titolo:Relaxation processes in room temperature ionic liquids: the case of 1-butyl-3-methyl imidazolium hexafluorophosphate/doi:10.1021%2Fjp053355j/rivista:The journal of physical chemistry. B/anno:2005/pagina_da:22061/pagina_a:22066/intervallo_pagine:22061–22066/volume:109
The journal of physical chemistry / B 109, 22061-22066 (2005). doi:10.1021/jp053355j
info:cnr-pdr/source/autori:A. Triolo1; O. Russina2; C. Hardacre3; M. Nieuwenhuyzen3; M. A. Gonzalez4; and H. Grimm5/titolo:Relaxation processes in room temperature ionic liquids: the case of 1-butyl-3-methyl imidazolium hexafluorophosphate/doi:10.1021%2Fjp053355j/rivista:The journal of physical chemistry. B/anno:2005/pagina_da:22061/pagina_a:22066/intervallo_pagine:22061–22066/volume:109
The journal of physical chemistry
A detailed investigation on the nature of the relaxation processes occurring in a typical room temperature ionic liquid (RTIL), namely, 1-butyl-3-methyl imidazolium hexafluorophosphate ([bmim][PF(6)]), is reported. The study was conducted using both
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a487f00c47d3a3fd84ec443b01ffa255
https://publications.cnr.it/doc/39727
https://publications.cnr.it/doc/39727