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Bacterial superoxide dismutase and virulence.
Langford PR, Sansone A, Valenti P, Battistoni A, Kroll JS. Langford PR, et al. Among authors: battistoni a. Methods Enzymol. 2002;349:155-66. doi: 10.1016/s0076-6879(02)49331-7. Methods Enzymol. 2002. PMID: 11912905 No abstract available.
Analysis of Cu,ZnSOD conformational stability by differential scanning calorimetry.
Bonaccorsi di Patti MC, Giartosio A, Rotilio G, Battistoni A. Bonaccorsi di Patti MC, et al. Among authors: battistoni a. Methods Enzymol. 2002;349:49-61. doi: 10.1016/s0076-6879(02)49320-2. Methods Enzymol. 2002. PMID: 11912929 No abstract available.
NMR assignment of reduced form of copper, zinc superoxide dismutase from Salmonella enterica.
Jiménez B, Mori M, Battistoni A, Sette M, Piccioli M. Jiménez B, et al. Among authors: battistoni a. Biomol NMR Assign. 2007 Jul;1(1):65-7. doi: 10.1007/s12104-007-9017-0. Epub 2007 May 22. Biomol NMR Assign. 2007. PMID: 19636828
Role of prokaryotic Cu,Zn superoxide dismutase in pathogenesis.
Battistoni A. Battistoni A. Biochem Soc Trans. 2003 Dec;31(Pt 6):1326-9. doi: 10.1042/bst0311326. Biochem Soc Trans. 2003. PMID: 14641055 Review.
Finally, a striking feature of Cu,Zn superoxide dismutases from bacterial pathogens is their apparent ability to exploit the structural versatility of the enzyme to modulate its function. ...
Finally, a striking feature of Cu,Zn superoxide dismutases from bacterial pathogens is their apparent ability to exploit the structur …
Regulatory and structural differences in the Cu,Zn-superoxide dismutases of Salmonella enterica and their significance for virulence.
Ammendola S, Pasquali P, Pacello F, Rotilio G, Castor M, Libby SJ, Figueroa-Bossi N, Bossi L, Fang FC, Battistoni A. Ammendola S, et al. Among authors: battistoni a. J Biol Chem. 2008 May 16;283(20):13688-99. doi: 10.1074/jbc.M710499200. Epub 2008 Mar 24. J Biol Chem. 2008. PMID: 18362154 Free PMC article.
We have performed a detailed comparison of the functional, structural, and regulatory properties of the Salmonella SodC enzymes. ...
We have performed a detailed comparison of the functional, structural, and regulatory properties of the Salmonella SodC enzymes. ...
Unfolding and inactivation of monomeric superoxide dismutase from E. coli by SDS.
Bozzi M, Battistoni A, Sette M, Melino S, Rotilio G, Paci M. Bozzi M, et al. Among authors: battistoni a. Int J Biol Macromol. 2001 Aug 20;29(2):99-105. doi: 10.1016/s0141-8130(01)00146-5. Int J Biol Macromol. 2001. PMID: 11518581
Investigation of the active site of Escherichia coli Cu,Zn superoxide dismutase reveals the absence of the copper-coordinated water molecule. is the water molecule really necessary for the enzymatic mechanism?
Sette M, Bozzi M, Battistoni A, Fasano M, Paci M, Rotilio G. Sette M, et al. Among authors: battistoni a. FEBS Lett. 2000 Oct 13;483(1):21-6. doi: 10.1016/s0014-5793(00)02074-3. FEBS Lett. 2000. PMID: 11033349
Moreover, NMRD measurements demonstrate the lack of a copper-coordinated water molecule. In spite of these differences the enzymatic activity is still high. ...A role for the copper-coordinated water molecule is discussed in the light of recent crystallographic stud …
Moreover, NMRD measurements demonstrate the lack of a copper-coordinated water molecule. In spite of these differences the enzymatic …
The solution structure of the monomeric copper, zinc superoxide dismutase from Salmonella enterica: structural insights to understand the evolution toward the dimeric structure.
Mori M, Jiménez B, Piccioli M, Battistoni A, Sette M. Mori M, et al. Among authors: battistoni a. Biochemistry. 2008 Dec 9;47(49):12954-63. doi: 10.1021/bi801252e. Biochemistry. 2008. PMID: 19006322
This represents the first solution structure of a natural and fully active monomeric superoxide dismutase in solution, providing information useful for the interpretation of the evolutional development of these enzymes. ...SodCII presents a more rigid conformation w …
This represents the first solution structure of a natural and fully active monomeric superoxide dismutase in solution, providing info …
Purification and characterization of recombinant Caulobacter crescentus Cu,Zn superoxide dismutase.
De Domenico I, Lania A, Bonaccorsi di Patti MC, Battistoni A, Musci G, Desideri A. De Domenico I, et al. Among authors: battistoni a. Biochim Biophys Acta. 2006 Jan;1764(1):105-9. doi: 10.1016/j.bbapap.2005.08.021. Epub 2005 Sep 13. Biochim Biophys Acta. 2006. PMID: 16213200
The corresponding recombinant protein has a molecular weight typical of a homodimeric Cu,ZnSODs and an activity comparable to that of other prokaryotic enzymes. The copper active site is characterized by a peculiar axial geometry as evidenced by its electron …
The corresponding recombinant protein has a molecular weight typical of a homodimeric Cu,ZnSODs and an activity comparable to …
Functional and crystallographic characterization of Salmonella typhimurium Cu,Zn superoxide dismutase coded by the sodCI virulence gene.
Pesce A, Battistoni A, Stroppolo ME, Polizio F, Nardini M, Kroll JS, Langford PR, O'Neill P, Sette M, Desideri A, Bolognesi M. Pesce A, et al. Among authors: battistoni a. J Mol Biol. 2000 Sep 15;302(2):465-78. doi: 10.1006/jmbi.2000.4074. J Mol Biol. 2000. PMID: 10970746
The crystal structure (R-factor 22.6%, at 2.3 A resolution) indicates that the dimeric enzyme adopts the quaternary assembly typical of prokaryotic Cu,Zn superoxide dismutases. ...As a consequence, the network of structural water molecules that fill the dimer interf …
The crystal structure (R-factor 22.6%, at 2.3 A resolution) indicates that the dimeric enzyme adopts the quaternary assembly typical …
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