S.I.C.A.M.O.R. Sviluppo di indagini chimiche applicate al mantenimento delle opere e al restauro

Autor: Marchettini, N, Atrei, A, Benetti, F, Carretti, E, Dei, L, Gaggelli, E, Giambi, F, Gliozzo, E, Guerranti, C, Migliorini, C, Papini, Am, Perra, G, Potenza, M, Rosi, L, Sabatino, G, Turbanti Memmi, I, Uva, M, Valensin, D, Valensin, G

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3674::ee9b96943f1811c136707d66728aac2e
https://hdl.handle.net/11380/1303965

Structural features of Apramycin bound at the bacterial ribosome A site as detected by NMR and CD spectroscopy

Autor: Balenci D., D'Amelio N., Gaggelli N., Cellai L., Molteni E., Valensin G.

Publikováno v: ChemBioChem
11 (2010): 166–169.
info:cnr-pdr/source/autori:Balenci D., D'Amelio N., Gaggelli N., Cellai L., Molteni E., Valensin G./titolo:Structural features of Apramycin bound at the bacterial ribosome A site as detected by NMR and CD spectroscopy./doi:/rivista:ChemBioChem (Print)/anno:2010/pagina_da:166/pagina_a:169/intervallo_pagine:166–169/volume:11

Transferred-NOE and CD techniques were found to provide a very convenient method for investigating the solution structure of kanamycin A interacting with a ribosomal A-site fragment.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=cnr_________::9ffc6ab47ae79055edac339cfb929d3c
https://publications.cnr.it/doc/19855

The Interaction of Kanamycin A with the Bacterial Ribosomal A-Site: Effect of Cu(II) on the Adduct

Autor: Balenci D, Bernardi F, Cellai L, D'Amelio N, Gaggelli E, Gaggelli N, Molteni E, Valensin G.

Publikováno v: ChemBioChem
9 (2008): 114–123.
info:cnr-pdr/source/autori:Balenci D, Bernardi F, Cellai L, D'Amelio N, Gaggelli E, Gaggelli N, Molteni E, Valensin G./titolo:The Interaction of Kanamycin A with the Bacterial Ribosomal A-Site: Effect of Cu(II) on the Adduct/doi:/rivista:ChemBioChem (Print)/anno:2008/pagina_da:114/pagina_a:123/intervallo_pagine:114–123/volume:9

The solution structure of kanamycin A interacting with a ribosomal A-site fragment was solved by transferred-NOE techniques and found to agree with the structure of the complex observed in the crystal. Despite the fast exchange conditions found for t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=cnr_________::74ac4eb5ac8da0e5c2083862f3aa3431
https://publications.cnr.it/doc/19641

Potentiometric and spectroscopic studies of the neurotoxic peptide fragments of prion protein: hPrP92-100, hPrP100-106 and hPrP91-114 with CuII ions

Autor: Janicka, A., Valensin, D., Migliorini, C., Valensin, G., Guerrini, Remo, Remelli, Maurizio, Miecznikowska, H., Rolka, K., Kozlowski, H.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3709::ae5d36363ae84d087d27edfd4c700210
http://hdl.handle.net/11392/521901

Specific interaction of copper(II) ions with fragments of prion and related proteins

Autor: Kozlowski, H., Janicka, A., Luczkowski, M., Stanczak, P., Gaggelli, E., Valensin, D., Valensin, G., Grzonka, Z., Juszcyk, P., Remelli, Maurizio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3709::f367f4ae339a12164b34cef0d1053a74
http://hdl.handle.net/11392/521994