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interaction with the high-affinity uptake protein ZnuA provide insight into the management of periplasmic zinc

Autor: Ilari A, Alaleona F, Tria G, Petrarca P, Battistoni A, Zamparelli C, Verzili D

Publikováno v: Biochimica et biophysica acta
1840 (2013): 535–544.
info:cnr-pdr/source/autori:Ilari A, Alaleona F, Tria G, Petrarca P, Battistoni A, Zamparelli C, Verzili D/titolo:interaction with the high-affinity uptake protein ZnuA provide insight into the management of periplasmic zinc./doi:/rivista:Biochimica et biophysica acta (Print)/anno:2013/pagina_da:535/pagina_a:544/intervallo_pagine:535–544/volume:1840

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=cnr_________::f0d2c0073ff87098a938eb1fa432cdec
http://www.cnr.it/prodotto/i/276606

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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

Autor: Alaleona F, Franceschini S, Ceci P, Ilari A, Chiancone E.

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

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

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ZnuA, the soluble component of the bacterial Zn(II) ABC transporter, a possible target for novel antibiotics

Autor: Alaleona, F., DI SANTO, Roberto, Chiancone, Emilia, Ilari, Andrea

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3686::884403e23f9db779faf9782a11ee887b
http://hdl.handle.net/11573/684251

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The antioxidant Dps protein from the thermophilic cyanobacterium Thermosynechococcus elongatus: an intrinsically stable cage-like structure endowed with enhanced stability

Autor: Franceschini S, Ceci P, Alaleona F, Chiancone E, Ilari A

Publikováno v: The FEBS journal
273 (2006): 4913–4928.
info:cnr-pdr/source/autori:Franceschini S, Ceci P, Alaleona F, Chiancone E, Ilari A/titolo:The antioxidant Dps protein from the thermophilic cyanobacterium Thermosynechococcus elongatus: an intrinsically stable cage-like structure endowed with enhanced stability/doi:/rivista:The FEBS journal (Print)/anno:2006/pagina_da:4913/pagina_a:4928/intervallo_pagine:4913–4928/volume:273

DNA-binding proteins from starved cells (Dps proteins) protect bacteria primarily from oxidative damage. They are composed of 12 identical subunits assembled with 23-symmetry to form a compact cage-like structure known to be stable at temperatures >

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=cnr_________::960ba24755672dfff13623c91f106e0a
https://publications.cnr.it/doc/11393

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