Viezzoli MS - Search Results

1

Sequence-specific assignment of the 1H and 15N nuclear magnetic resonance spectra of the reduced recombinant high-potential iron-sulfur protein I from Ectothiorhodospira halophila.

Bertini I, Felli IC, Kastrau DH, Luchinat C, Piccioli M, Viezzoli MS. Bertini I, et al. Among authors: viezzoli ms. Eur J Biochem. 1994 Oct 15;225(2):703-14. doi: 10.1111/j.1432-1033.1994.00703.x. Eur J Biochem. 1994. PMID: 7957186 Free article.

2

1H NMR investigation of reduced copper-cobalt superoxide dismutase.

Bertini I, Luchinat C, Piccioli M, Oliver MV, Viezzoli MS. Bertini I, et al. Among authors: viezzoli ms. Eur Biophys J. 1991;20(5):269-79. doi: 10.1007/BF00450562. Eur Biophys J. 1991. PMID: 1782908

3

A characterization of copper/zinc superoxide dismutase mutants at position 124. Zinc-deficient proteins.

Banci L, Bertini I, Cabelli DE, Hallewell RA, Tung JW, Viezzoli MS. Banci L, et al. Among authors: viezzoli ms. Eur J Biochem. 1991 Feb 26;196(1):123-8. doi: 10.1111/j.1432-1033.1991.tb15794.x. Eur J Biochem. 1991. PMID: 1848181 Free article.

4

Assignment of active-site protons in the 1H-NMR spectrum of reduced human Cu/Zn superoxide dismutase.

Bertini I, Capozzi F, Luchinat C, Piccioli M, Viezzoli MS. Bertini I, et al. Among authors: viezzoli ms. Eur J Biochem. 1991 May 8;197(3):691-7. doi: 10.1111/j.1432-1033.1991.tb15960.x. Eur J Biochem. 1991. PMID: 1851482 Free article.

5

Water in the active cavity of copper/zinc superoxide dismutase. A water 1H-nuclear-magnetic-relaxation-dispersion study.

Banci L, Bertini I, Hallewell RA, Luchinat C, Viezzoli MS. Banci L, et al. Among authors: viezzoli ms. Eur J Biochem. 1989 Sep 1;184(1):125-9. doi: 10.1111/j.1432-1033.1989.tb14998.x. Eur J Biochem. 1989. PMID: 2776763 Free article.

6

Active-site modification of superoxide dismutase by H2O2 studied through 1H NMR of the cobalt derivatives.

Bertini I, Luchinat C, Viezzoli MS, Wang Y. Bertini I, et al. Among authors: viezzoli ms. Arch Biochem Biophys. 1989 Mar;269(2):586-94. doi: 10.1016/0003-9861(89)90144-6. Arch Biochem Biophys. 1989. PMID: 2919884

7

Mutation of the metal-bridging proton-donor His63 residue in human Cu, Zn superoxide dismutase. Biochemical and biophysical analysis of the His63-->Cys mutant.

Banci L, Bertini I, Borsari M, Viezzoli MS, Hallewell RA. Banci L, et al. Among authors: viezzoli ms. Eur J Biochem. 1995 Aug 15;232(1):220-5. doi: 10.1111/j.1432-1033.1995.tb20802.x. Eur J Biochem. 1995. PMID: 7556154 Free article.

8

Synthesis and characterization of a monomeric mutant Cu/Zn superoxide dismutase with partially reconstituted enzymic activity.

Banci L, Bertini I, Chiu CY, Mullenbach GT, Viezzoli MS. Banci L, et al. Among authors: viezzoli ms. Eur J Biochem. 1995 Dec 15;234(3):855-60. doi: 10.1111/j.1432-1033.1995.855_a.x. Eur J Biochem. 1995. PMID: 8575445 Free article.

9

An NMR study of the 7Fe-8S ferredoxin from Rhodopseudomonas palustris and reinterpretation of data on similar systems.

Bertini I, Dikiy A, Luchinat C, Macinai R, Viezzoli MS, Vincenzini M. Bertini I, et al. Among authors: viezzoli ms. Biochemistry. 1997 Mar 25;36(12):3570-9. doi: 10.1021/bi962799q. Biochemistry. 1997. PMID: 9132008

10

Solution structure of reduced monomeric Q133M2 copper, zinc superoxide dismutase (SOD). Why is SOD a dimeric enzyme?

Banci L, Benedetto M, Bertini I, Del Conte R, Piccioli M, Viezzoli MS. Banci L, et al. Among authors: viezzoli ms. Biochemistry. 1998 Aug 25;37(34):11780-91. doi: 10.1021/bi9803473. Biochemistry. 1998. PMID: 9718300

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