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G Rotilio

Showing results (101-110 of 295) with videos related to

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Biochimica Et Biophysica Acta|August 16, 1983
Reaction of N,N-diethyldithiocarbamate and other bidentate ligands with Zn, Co and Cu bovine carbonic anhydrases. Inhibition of the enzyme activity and evidence for stable ternary enzyme-metal-ligand complexesL Morpurgo, A Desideri, A Rigo, et al.
The Journal of Biological Chemistry|September 10, 1981
Re-examination of the reaction of diethyldithiocarbamate with the copper of superoxide dismutaseD Cocco, L Calabrese, A Rigo, et al.
Cancer Biochemistry Biophysics|January 1, 1979
Differential sensitivity of tumor cells to externally generated hydrogen peroxide. Role of glutathione and related enzymesA Bozzi, I Mavelli, B Mondovì, et al.
The Journal of Biological Chemistry|March 25, 1979
Nuclear magnetic relaxation of 19F as a novel assay method of superoxide dismutaseA Rigo, P Viglino, E Argese, et al.
Free Radical Biology & Medicine|January 1, 1988
Is the activity-linked electrostatic gradient of bovine Cu, Zn superoxide dismutases conserved in homologous enzymes irrespective of the number and distribution of charges?A Desideri, M Falconi, V Parisi, et al.
Biochemical and Biophysical Research Communications|March 17, 1998
Overexpression of a hydrogen peroxide-resistant periplasmic Cu,Zn superoxide dismutase protects Escherichia coli from macrophage killingA Battistoni, G Donnarumma, R Greco, et al.
Biochemistry|February 7, 1978
On the quaternary structure of copper-zinc superoxide dismutases. Reversible dissociation into protomers of the isozyme I from wheat germA Rigo, F Marmocchi, D Cocco, et al.
FEBS Letters|February 26, 1990
Mapping the copper ligands of Cu,Zn superoxide dismutase by nuclear Overhauser enhancement of the isotropically shifted 1H-NMR lines of the Cu,Co derivativeM Paci, A Desideri, M Sete, et al.
Biochemical and Biophysical Research Communications|August 14, 1992
Temperature-dependent protein folding in vivo--lower growth temperature increases yield of two genetic variants of Xenopus laevis Cu,Zn superoxide dismutase in Escherichia coliA Battistoni, M T Carrì, A P Mazzetti, et al.
FEBS Letters|December 27, 1982
Carbamoylation of Cu,Zn-superoxide dismutase by cyanate. Role of lysines in the enzyme actionD Cocco, L Rossi, D Barra, et al.
Pageof 30

Showing results (101-110 of 295) with videos related to

Sort By:
Pageof 30
Biochimica Et Biophysica Acta|August 16, 1983
Reaction of N,N-diethyldithiocarbamate and other bidentate ligands with Zn, Co and Cu bovine carbonic anhydrases. Inhibition of the enzyme activity and evidence for stable ternary enzyme-metal-ligand complexesL Morpurgo, A Desideri, A Rigo, et al.
The Journal of Biological Chemistry|September 10, 1981
Re-examination of the reaction of diethyldithiocarbamate with the copper of superoxide dismutaseD Cocco, L Calabrese, A Rigo, et al.
Cancer Biochemistry Biophysics|January 1, 1979
Differential sensitivity of tumor cells to externally generated hydrogen peroxide. Role of glutathione and related enzymesA Bozzi, I Mavelli, B Mondovì, et al.
The Journal of Biological Chemistry|March 25, 1979
Nuclear magnetic relaxation of 19F as a novel assay method of superoxide dismutaseA Rigo, P Viglino, E Argese, et al.
Free Radical Biology & Medicine|January 1, 1988
Is the activity-linked electrostatic gradient of bovine Cu, Zn superoxide dismutases conserved in homologous enzymes irrespective of the number and distribution of charges?A Desideri, M Falconi, V Parisi, et al.
Biochemical and Biophysical Research Communications|March 17, 1998
Overexpression of a hydrogen peroxide-resistant periplasmic Cu,Zn superoxide dismutase protects Escherichia coli from macrophage killingA Battistoni, G Donnarumma, R Greco, et al.
Biochemistry|February 7, 1978
On the quaternary structure of copper-zinc superoxide dismutases. Reversible dissociation into protomers of the isozyme I from wheat germA Rigo, F Marmocchi, D Cocco, et al.
FEBS Letters|February 26, 1990
Mapping the copper ligands of Cu,Zn superoxide dismutase by nuclear Overhauser enhancement of the isotropically shifted 1H-NMR lines of the Cu,Co derivativeM Paci, A Desideri, M Sete, et al.
Biochemical and Biophysical Research Communications|August 14, 1992
Temperature-dependent protein folding in vivo--lower growth temperature increases yield of two genetic variants of Xenopus laevis Cu,Zn superoxide dismutase in Escherichia coliA Battistoni, M T Carrì, A P Mazzetti, et al.
FEBS Letters|December 27, 1982
Carbamoylation of Cu,Zn-superoxide dismutase by cyanate. Role of lysines in the enzyme actionD Cocco, L Rossi, D Barra, et al.
Pageof 30