Paci M - Search Results

1

Transduction of reducing power across the plasma membrane by reduced glutathione. A 1H-NMR spin-echo study of intact human erythrocytes.

Ciriolo MR, Paci M, Sette M, De Martino A, Bozzi A, Rotilio G. Ciriolo MR, et al. Among authors: paci m. Eur J Biochem. 1993 Aug 1;215(3):711-8. doi: 10.1111/j.1432-1033.1993.tb18083.x. Eur J Biochem. 1993. PMID: 8354277 Free article.

2

Formate as an NMR probe of anion binding to Cu,Zn and Cu,Co bovine erythrocyte superoxide dismutases.

Sette M, Paci M, Desideri A, Rotilio G. Sette M, et al. Among authors: paci m. Biochemistry. 1992 Dec 15;31(49):12410-5. doi: 10.1021/bi00164a016. Biochemistry. 1992. PMID: 1463727

3

A study of the intracellular effects of glutathione by 1H-spin echo NMR of intact human erythrocytes.

Ciriolo MR, Sette M, Paci M, Rotilio G. Ciriolo MR, et al. Among authors: paci m. Biochem Int. 1990;20(2):397-403. Biochem Int. 1990. PMID: 2317218

4

A two-dimensional NMR study of bovine Cu, Co superoxide dismutase. Further assignments in the region surrounding the active site.

Sette M, Paci M, Desideri A, Rotilio G. Sette M, et al. Among authors: paci m. Eur J Biochem. 1995 Jan 15;227(1-2):441-7. doi: 10.1111/j.1432-1033.1995.tb20407.x. Eur J Biochem. 1995. PMID: 7851420 Free article.

5

Two-dimensional NMR assignment of hyperfine-shifted resonances of very fast relaxing metal binding sites of proteins by NOE spectroscopy. The case of Cu, Co superoxide dismutase.

Sette M, Paci M, Desideri A, Rotilio G. Sette M, et al. Among authors: paci m. Eur J Biochem. 1993 Apr 1;213(1):391-7. doi: 10.1111/j.1432-1033.1993.tb17773.x. Eur J Biochem. 1993. PMID: 8477710 Free article.

6

Solution structure of glutathione bound to human glutathione transferase P1-1: comparison of NMR measurements with the crystal structure.

Nicotra M, Paci M, Sette M, Oakley AJ, Parker MW, Lo Bello M, Caccuri AM, Federici G, Ricci G. Nicotra M, et al. Among authors: paci m. Biochemistry. 1998 Mar 3;37(9):3020-7. doi: 10.1021/bi971902o. Biochemistry. 1998. PMID: 9485454

7

NMR evidence for perturbation of the copper coordination sphere upon chemical modification of arginine 141 in bovine Cu,Zn superoxide dismutase.

Paci M, Desideri A, Sette M, Rotilio G. Paci M, et al. Arch Biochem Biophys. 1991 Apr;286(1):222-5. doi: 10.1016/0003-9861(91)90032-e. Arch Biochem Biophys. 1991. PMID: 1654780

8

Reconstitution of Cu,Zn-superoxide dismutase by the Cu(I).glutathione complex.

Ciriolo MR, Desideri A, Paci M, Rotilio G. Ciriolo MR, et al. Among authors: paci m. J Biol Chem. 1990 Jul 5;265(19):11030-4. J Biol Chem. 1990. PMID: 2162829 Free article.

9

Assignment of imidazole resonances from two-dimensional proton NMR spectra of bovine Cu,Zn superoxide dismutase. Evidence for similar active site conformation in the oxidized and reduced enzyme.

Paci M, Desideri A, Sette M, Ciriolo MR, Rotilio G. Paci M, et al. FEBS Lett. 1990 Apr 9;263(1):127-30. doi: 10.1016/0014-5793(90)80720-4. FEBS Lett. 1990. PMID: 2332043 Free article.

10

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: paci m. J Inorg Biochem. 1988 Aug;33(4):277-83. doi: 10.1016/0162-0134(88)80006-0. J Inorg Biochem. 1988. PMID: 2844990

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