Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Ilari A (1)"'
Autor:
Ilari A (1), Johnson KA (2), Nastopoulos V (3), Verzili D (1), Zamparelli C (2), Colotti G (1), Tsernoglou D (2), Chiancone E. (1
Publikováno v:
Journal of Molecular Biology 29 (2002): 447–458.
info:cnr-pdr/source/autori:Ilari A (1), Johnson KA (2), Nastopoulos V (3), Verzili D (1), Zamparelli C (2), Colotti G (1), Tsernoglou D (2), Chiancone E. (1,2)/titolo:The crystal structure of the sorcin calcium binding domain provides a model of Ca2+-dependent processes in the full-length protein/doi:/rivista:Journal of Molecular Biology/anno:2002/pagina_da:447/pagina_a:458/intervallo_pagine:447–458/volume:29
info:cnr-pdr/source/autori:Ilari A (1), Johnson KA (2), Nastopoulos V (3), Verzili D (1), Zamparelli C (2), Colotti G (1), Tsernoglou D (2), Chiancone E. (1,2)/titolo:The crystal structure of the sorcin calcium binding domain provides a model of Ca2+-dependent processes in the full-length protein/doi:/rivista:Journal of Molecular Biology/anno:2002/pagina_da:447/pagina_a:458/intervallo_pagine:447–458/volume:29
Sorcin is a 21.6 kDa calcium binding protein, expressed in a number of mammalian tissues that belongs to the small, recently identified penta-EF-hand (PEF) family. Like all members of this family, sorcin undergoes a Ca2+-dependent translocation from
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=cnr_________::9b0e25a61313ab71e004899ac1346db2
https://publications.cnr.it/doc/11344
https://publications.cnr.it/doc/11344
Publikováno v:
277 (2002): 23725–23732.
info:cnr-pdr/source/autori:Ilari A. 1, Bonamore A. 2, Farina A. 2, Johnson K. A. 2, Boffi A.2/titolo:The X-ray structure of ferric Escherichia coli flavohemoglobin reveals an unexpected geometry of the distal heme pocket/doi:/rivista:/anno:2002/pagina_da:23725/pagina_a:23732/intervallo_pagine:23725–23732/volume:277
info:cnr-pdr/source/autori:Ilari A. 1, Bonamore A. 2, Farina A. 2, Johnson K. A. 2, Boffi A.2/titolo:The X-ray structure of ferric Escherichia coli flavohemoglobin reveals an unexpected geometry of the distal heme pocket/doi:/rivista:/anno:2002/pagina_da:23725/pagina_a:23732/intervallo_pagine:23725–23732/volume:277
The x-ray structure of ferric unliganded lipid-free Escherichia coli flavohemoglobin has been solvedto a resolution of 2.2 A and refined to an R-factor of 19%. The overall fold is similar to that of ferrous lipid-bound Alcaligenes eutrophus flavohemo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=cnr_________::aa2c8e9fe17932f221aedba9ad5664f5
https://publications.cnr.it/doc/11347
https://publications.cnr.it/doc/11347
Publikováno v:
277 (2002): 37619–37623.
info:cnr-pdr/source/autori:Ilari A. 1, Ceci P. 2, Ferrari D. 3, Rossi GL. 3, Chiancone E. 1,2/titolo:Iron incorporation into Escherichia coli Dps gives rise to a ferritin-like microcrystalline core/doi:/rivista:/anno:2002/pagina_da:37619/pagina_a:37623/intervallo_pagine:37619–37623/volume:277
info:cnr-pdr/source/autori:Ilari A. 1, Ceci P. 2, Ferrari D. 3, Rossi GL. 3, Chiancone E. 1,2/titolo:Iron incorporation into Escherichia coli Dps gives rise to a ferritin-like microcrystalline core/doi:/rivista:/anno:2002/pagina_da:37619/pagina_a:37623/intervallo_pagine:37619–37623/volume:277
Escherichia coli Dps belongs to a family of bacterial stress-induced proteins to protect DNA from oxidative damage. It shares with Listeria innocua ferritin several structural features, such as the quaternary assemblage and the presence of an unusual
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=cnr_________::57bdf70d4205b5a504ab2075fbbcde50
https://publications.cnr.it/doc/11346
https://publications.cnr.it/doc/11346