Desideri A - Search Results

1

Engineering a responsive DNA triple helix into an octahedral DNA nanostructure for a reversible opening/closing switching mechanism: a computational and experimental integrated study.

Ottaviani A, Iacovelli F, Idili A, Falconi M, Ricci F, Desideri A. Ottaviani A, et al. Among authors: desideri a. Nucleic Acids Res. 2018 Nov 2;46(19):9951-9959. doi: 10.1093/nar/gky857. Nucleic Acids Res. 2018. PMID: 30247614 Free PMC article.

2

Evolutionary conservativeness of electric field in the Cu,Zn superoxide dismutase active site. Evidence for co-ordinated mutation of charged amino acid residues.

Desideri A, Falconi M, Polticelli F, Bolognesi M, Djinovic K, Rotilio G. Desideri A, et al. J Mol Biol. 1992 Jan 5;223(1):337-42. doi: 10.1016/0022-2836(92)90734-2. J Mol Biol. 1992. PMID: 1731078

3

Modelling the three-dimensional structure and electrostatic potential field of the two Cu,Zn superoxide dismutase variants from Xenopus laevis.

Falconi M, Rotilio G, Desideri A. Falconi M, et al. Among authors: desideri a. Proteins. 1991;10(2):149-55. doi: 10.1002/prot.340100208. Proteins. 1991. PMID: 1896428

4

Mapping the copper ligands of Cu,Zn superoxide dismutase by nuclear Overhauser enhancement of the isotropically shifted 1H-NMR lines of the Cu,Co derivative.

Paci M, Desideri A, Sete M, Falconi M, Rotilio G. Paci M, et al. Among authors: desideri a. FEBS Lett. 1990 Feb 26;261(2):231-6. doi: 10.1016/0014-5793(90)80560-6. FEBS Lett. 1990. PMID: 2155819 Free article.

5

Conservation of local electric fields in the evolution of Cu,Zn superoxide dismutase.

Desideri A, Falconi M, Parisi V, Rotilio G. Desideri A, et al. FEBS Lett. 1989 Jun 19;250(1):45-8. doi: 10.1016/0014-5793(89)80681-7. FEBS Lett. 1989. PMID: 2737300 Free article.

6

Is the activity-linked electrostatic gradient of bovine Cu, Zn superoxide dismutases conserved in homologous enzymes irrespective of the number and distribution of charges?

Desideri A, Falconi M, Parisi V, Morante S, Rotilio G. Desideri A, et al. Free Radic Biol Med. 1988;5(5-6):313-7. doi: 10.1016/0891-5849(88)90102-5. Free Radic Biol Med. 1988. PMID: 3256530

7

Molecular modeling and electrostatic potential calculations on chemically modified Cu,Zn superoxide dismutases from Bos taurus and shark Prionace glauca: role of Lys134 in electrostatically steering the substrate to the active site.

Polticelli F, Falconi M, O'Neill P, Petruzelli R, Galtieri A, Lania A, Calabrese L, Rotilio G, Desideri A. Polticelli F, et al. Among authors: desideri a. Arch Biochem Biophys. 1994 Jul;312(1):22-30. doi: 10.1006/abbi.1994.1275. Arch Biochem Biophys. 1994. PMID: 8031131

8

Peculiar spectroscopic and kinetic properties of Cys-47 in human placental glutathione transferase. Evidence for an atypical thiolate ion pair near the active site.

Lo Bello M, Parker MW, Desideri A, Polticelli F, Falconi M, Del Boccio G, Pennelli A, Federici G, Ricci G. Lo Bello M, et al. Among authors: desideri a. J Biol Chem. 1993 Sep 5;268(25):19033-8. J Biol Chem. 1993. PMID: 8360190 Free article.

9

Electrostatic recognition in redox copper proteins: a 1H NMR study of the protonation behavior of His 19 in oxidized and reduced Cu,Zn superoxide dismutase.

Desideri A, Polticelli F, Falconi M, Sette M, Ciriolo MR, Paci M, Rotilio G. Desideri A, et al. Arch Biochem Biophys. 1993 Mar;301(2):244-50. doi: 10.1006/abbi.1993.1140. Arch Biochem Biophys. 1993. PMID: 8384828

10

Effect of Lys-->Arg mutation on the thermal stability of Cu,Zn superoxide dismutase: influence on the monomer-dimer equilibrium.

Folcarelli S, Battistoni A, Carrì MT, Polticelli F, Falconi M, Nicolini L, Stella L, Rosato N, Rotilio G, Desideri A. Folcarelli S, et al. Among authors: desideri a. Protein Eng. 1996 Apr;9(4):323-5. doi: 10.1093/protein/9.4.323. Protein Eng. 1996. PMID: 8738207

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