Capo C - Search Results

1

A histidine-rich metal binding domain at the N terminus of Cu,Zn-superoxide dismutases from pathogenic bacteria: a novel strategy for metal chaperoning.

Battistoni A, Pacello F, Mazzetti AP, Capo C, Kroll JS, Langford PR, Sansone A, Donnarumma G, Valenti P, Rotilio G. Battistoni A, et al. Among authors: capo c. J Biol Chem. 2001 Aug 10;276(32):30315-25. doi: 10.1074/jbc.M010527200. Epub 2001 May 21. J Biol Chem. 2001. PMID: 11369756 Free article.

2

The Cu,Zn superoxide dismutase from Escherichia coli retains monomeric structure at high protein concentration. Evidence for altered subunit interaction in all the bacteriocupreins.

Battistoni A, Folcarelli S, Gabbianelli R, Capo C, Rotilio G. Battistoni A, et al. Among authors: capo c. Biochem J. 1996 Dec 15;320 ( Pt 3)(Pt 3):713-6. doi: 10.1042/bj3200713. Biochem J. 1996. PMID: 9003353 Free PMC article.

3

Differential binding of anions to the active site of Cu,Zn superoxide dismutase. A study of the Co,Zn enzyme derivative.

Desideri A, Paci M, Capo C, Calabrese L, Rotilio G. Desideri A, et al. Among authors: capo c. J Inorg Biochem. 1988 Aug;33(4):277-83. doi: 10.1016/0162-0134(88)80006-0. J Inorg Biochem. 1988. PMID: 2844990

4

Effect of Val 73 --> Trp mutation on the reaction of "cambialistic" superoxide dismutase from Propionibacterium shermanii with hydrogen peroxide.

Gabbianelli R, Battistoni A, Capo C, Polticelli F, Rotilio G, Meier B, Desideri A. Gabbianelli R, et al. Among authors: capo c. Arch Biochem Biophys. 1997 Sep 1;345(1):156-9. doi: 10.1006/abbi.1997.0235. Arch Biochem Biophys. 1997. PMID: 9281323

5

The Cu,Zn superoxide dismutase isoenzymes of Xenopus laevis: purification, identification of a heterodimer and differential heat sensitivity.

Capo CR, Polticelli F, Calabrese L, Schinina ME, Carri MT, Rotilio G. Capo CR, et al. Biochem Biophys Res Commun. 1990 Dec 31;173(3):1186-93. doi: 10.1016/s0006-291x(05)80911-8. Biochem Biophys Res Commun. 1990. PMID: 2268321

6

Copper imbalance and oxidative stress in neurodegeneration.

Rossi L, Arciello M, Capo C, Rotilio G. Rossi L, et al. Among authors: capo c. Ital J Biochem. 2006 Sep-Dec;55(3-4):212-21. Ital J Biochem. 2006. PMID: 17274527 Review.

7

Primary structure of a cationic Cu,Zn superoxide dismutase. The sheep enzyme.

Schininà ME, Barra D, Gentilomo S, Bossa F, Capo C, Rotilio G, Calabrese L. Schininà ME, et al. Among authors: capo c. FEBS Lett. 1986 Oct 20;207(1):7-10. doi: 10.1016/0014-5793(86)80003-5. FEBS Lett. 1986. PMID: 3770194 Free article.

8

Benefits from dietary polyphenols for brain aging and Alzheimer's disease.

Rossi L, Mazzitelli S, Arciello M, Capo CR, Rotilio G. Rossi L, et al. Among authors: capo cr. Neurochem Res. 2008 Dec;33(12):2390-400. doi: 10.1007/s11064-008-9696-7. Epub 2008 Apr 16. Neurochem Res. 2008. PMID: 18415677 Review.

9

The effects of pH and various salts upon the activity of a series of superoxide dismutases.

O'Neill P, Davies S, Fielden EM, Calabrese L, Capo C, Marmocchi F, Natoli G, Rotilio G. O'Neill P, et al. Among authors: capo c. Biochem J. 1988 Apr 1;251(1):41-6. doi: 10.1042/bj2510041. Biochem J. 1988. PMID: 2839162 Free PMC article.

10

Characterization of Cu,Zn superoxide dismutase from the bathophile fish, Lampanyctus crocodilus.

Capo C, Stroppolo ME, Galtieri A, Lania A, Costanzo S, Petruzzelli R, Calabrese L, Polticelli F, Desideri A. Capo C, et al. Comp Biochem Physiol B Biochem Mol Biol. 1997 Jul;117(3):403-7. doi: 10.1016/s0305-0491(97)00136-3. Comp Biochem Physiol B Biochem Mol Biol. 1997. PMID: 9253177

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