Zobrazeno 1 - 10
of 640
pro vyhledávání: '"Chiancone E."'
Autor:
Cambria, V, Buffi, F, Attorre, F, De Sanctis, M, Fanelli, G, Massimi, M, Testolin, R, Del Vico, E, Sitzia, T, Campagnaro, T, Perfetti, M, Semenzato, P, Rizzi, A, Michielon, B, Iacopino, S, Piazzi, C, Quetri, T, Pirovano, C, Rossi, K, Cesaroni, D, Sbordoni, V, De Felici, S, Trimani, G, Chiancone, E, Luise, D, Rinzafri, C, Minicuci, M, Martellos, S
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::5d4dd640889124ef7e01a3a1b71e6c7f
http://hdl.handle.net/11577/3276966
http://hdl.handle.net/11577/3276966
Akademický článek
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Publikováno v:
The FEBS journal
277 (2010): 903–917. doi:10.1111/j.1742-4658.2009.07532.x
info:cnr-pdr/source/autori:Alaleona F, Franceschini S, Ceci P, Ilari A, Chiancone E./titolo:Thermosynechococcus elongatus DpsA binds Zn(II) at a unique three histidine-containing ferroxidase center and utilizes O2 as iron oxidant with very high efficiency, unlike the typical Dps proteins/doi:10.1111%2Fj.1742-4658.2009.07532.x/rivista:The FEBS journal (Print)/anno:2010/pagina_da:903/pagina_a:917/intervallo_pagine:903–917/volume:277
277 (2010): 903–917. doi:10.1111/j.1742-4658.2009.07532.x
info:cnr-pdr/source/autori:Alaleona F, Franceschini S, Ceci P, Ilari A, Chiancone E./titolo:Thermosynechococcus elongatus DpsA binds Zn(II) at a unique three histidine-containing ferroxidase center and utilizes O2 as iron oxidant with very high efficiency, unlike the typical Dps proteins/doi:10.1111%2Fj.1742-4658.2009.07532.x/rivista:The FEBS journal (Print)/anno:2010/pagina_da:903/pagina_a:917/intervallo_pagine:903–917/volume:277
The cyanobacterium Thermosynechococcus elongatus is one the few bacteria to possess two Dps proteins, DpsA-Te and Dps-Te. The present characterization of DpsA-Te reveals unusual structural and functional features that differentiate it from Dps-Te and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=cnr_________::9c09e07787067697497486f3535c4954
Publikováno v:
(2009).
info:cnr-pdr/source/autori:Bellapadrona G, Stefanini S, Zamparelli C, Theil EC, Chiancone E./titolo:Iron translocation into and out of Listeria innocua Dps and size distribution of the protein-enclosed nanomineral are modulated by the electrostatic gradient at the 3-fold/doi:/rivista:/anno:2009/pagina_da:/pagina_a:/intervallo_pagine:/volume
info:cnr-pdr/source/autori:Bellapadrona G, Stefanini S, Zamparelli C, Theil EC, Chiancone E./titolo:Iron translocation into and out of Listeria innocua Dps and size distribution of the protein-enclosed nanomineral are modulated by the electrostatic gradient at the 3-fold/doi:/rivista:/anno:2009/pagina_da:/pagina_a:/intervallo_pagine:/volume
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=cnr_________::9f732a354fee7beec4b7d824c1172db0
https://publications.cnr.it/doc/11749
https://publications.cnr.it/doc/11749
Publikováno v:
Gene (Amst.) 410 (2008): 113–121.
info:cnr-pdr/source/autori:Fiorini F, Stefanini S, Valenti P, Chiancone E, De Biase D./titolo:Transcription of the Listeria monocytogenes fri gene is growth-phase dependent and is repressed directly by Fur, the ferric uptake regulator./doi:/rivista:Gene (Amst.)/anno:2008/pagina_da:113/pagina_a:121/intervallo_pagine:113–121/volume:410
info:cnr-pdr/source/autori:Fiorini F, Stefanini S, Valenti P, Chiancone E, De Biase D./titolo:Transcription of the Listeria monocytogenes fri gene is growth-phase dependent and is repressed directly by Fur, the ferric uptake regulator./doi:/rivista:Gene (Amst.)/anno:2008/pagina_da:113/pagina_a:121/intervallo_pagine:113–121/volume:410
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=cnr_________::c28ec9dec450961c280db4aec49e62a9
https://publications.cnr.it/doc/11571
https://publications.cnr.it/doc/11571
Publikováno v:
Dioxygen Binding and Sensing Proteins, pp. 107–119. Milano: Springer-Verlag Italia, 2008
info:cnr-pdr/source/autori:Colotti G, Boffi A, Chiancone E/titolo:Cooperativity and Ligand-linked Polymerisation in Scapharca Tetrameric Haemoglobin./titolo_volume:Dioxygen Binding and Sensing Proteins/curatori_volume:/editore: /anno:2008
info:cnr-pdr/source/autori:Colotti G, Boffi A, Chiancone E/titolo:Cooperativity and Ligand-linked Polymerisation in Scapharca Tetrameric Haemoglobin./titolo_volume:Dioxygen Binding and Sensing Proteins/curatori_volume:/editore: /anno:2008
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=cnr_________::128225a3e303b915a71378c6d5ca63d5
https://publications.cnr.it/doc/260114
https://publications.cnr.it/doc/260114
Autor:
Giorgi A, Mignogna G, Bellapadrona G, Gattoni M, Chiaraluce R, Consalvi V, Chiancone E, Stefanini S.
Publikováno v:
Archives of biochemistry and biophysics
478 (2008): 69–74.
info:cnr-pdr/source/autori:Giorgi A, Mignogna G, Bellapadrona G, Gattoni M, Chiaraluce R, Consalvi V,Chiancone E, Stefanini S./titolo:The unusual co-assembly of H-and M-chains in the ferritin molecule from the Antarctic teleosts Trematomus bernacchii and Trematomus newnesi./doi:/rivista:Archives of biochemistry and biophysics (Print)/anno:2008/pagina_da:69/pagina_a:74/intervallo_pagine:69–74/volume:478
478 (2008): 69–74.
info:cnr-pdr/source/autori:Giorgi A, Mignogna G, Bellapadrona G, Gattoni M, Chiaraluce R, Consalvi V,Chiancone E, Stefanini S./titolo:The unusual co-assembly of H-and M-chains in the ferritin molecule from the Antarctic teleosts Trematomus bernacchii and Trematomus newnesi./doi:/rivista:Archives of biochemistry and biophysics (Print)/anno:2008/pagina_da:69/pagina_a:74/intervallo_pagine:69–74/volume:478
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=cnr_________::6bd11ccf52506492bb9412a4eae6a4b3
https://publications.cnr.it/doc/11570
https://publications.cnr.it/doc/11570
Publikováno v:
Experimental physiology
93 (2008): 1233–1238. doi:10.1113/expphysiol.2008.043497
info:cnr-pdr/source/autori:Fowler MR; Colotti G; Chiancone E; Smith GL; Fearon M/titolo:Sorcin modulates cardiac L-type Ca(2+) current by functional interaction with the alpha(1C) subunit in rabbits/doi:10.1113%2Fexpphysiol.2008.043497/rivista:Experimental physiology (Print)/anno:2008/pagina_da:1233/pagina_a:1238/intervallo_pagine:1233–1238/volume:93
93 (2008): 1233–1238. doi:10.1113/expphysiol.2008.043497
info:cnr-pdr/source/autori:Fowler MR; Colotti G; Chiancone E; Smith GL; Fearon M/titolo:Sorcin modulates cardiac L-type Ca(2+) current by functional interaction with the alpha(1C) subunit in rabbits/doi:10.1113%2Fexpphysiol.2008.043497/rivista:Experimental physiology (Print)/anno:2008/pagina_da:1233/pagina_a:1238/intervallo_pagine:1233–1238/volume:93
We examined the modulation of the cardiac L-type Ca(2+) channel (LTCC) by the regulatory protein sorcin and tested the hypothesis that modulation occurred by direct interaction. Whole-cell patch-clamp recordings were made on native rabbit ventricular
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=cnr_________::76166b4a337f2df34c69221284bd60c0