Showing results (191-200 of 1,068) with videos related to

Sort By:
Pageof 107
Archives of Biochemistry and Biophysics|June 1, 1995
Copper, zinc superoxide dismutase in Escherichia coli: periplasmic localizationL Benov, L Y Chang, B Day, et al.
The Journal of Biological Chemistry|September 12, 1998
The ortho effect makes manganese(III) meso-tetrakis(N-methylpyridinium-2-yl)porphyrin a powerful and potentially useful superoxide dismutase mimicI Batinić-Haberle, L Benov, I Spasojević, et al.
The Journal of Biological Chemistry|August 15, 1987
Examination of the role of arginine-143 in the human copper and zinc superoxide dismutase by site-specific mutagenesisW F Beyer, I Fridovich, G T Mullenbach, et al.
Archives of Biochemistry and Biophysics|July 15, 1997
A potent superoxide dismutase mimic: manganese beta-octabromo-meso-tetrakis-(N-methylpyridinium-4-yl) porphyrinI Batinić-Haberle, S I Liochev, I Spasojević, et al.
Archives of Biochemistry and Biophysics|January 1, 1990
Superoxide dismutases enhance the rate of autoxidation of 3-hydroxyanthranilic acidT Ishii, H Iwahashi, R Sugata, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 15, 1994
NADPH: ferredoxin oxidoreductase acts as a paraquat diaphorase and is a member of the soxRS regulonS I Liochev, A Hausladen, W F Beyer, et al.
Biochemical and Biophysical Research Communications|December 15, 1986
Stabilization and partial characterization of endothelium-derived relaxing factor from cultured bovine aortic endothelial cellsJ J Murray, I Fridovich, R G Makhoul, et al.
Archives of Biochemistry and Biophysics|September 1, 1983
Positive correlation between superoxide dismutase and resistance to paraquat toxicity in the green alga Chlorella sorokinianaH D Rabinowitch, D A Clare, J D Crapo, et al.
The Biochemical Journal|September 15, 1985
Essentiality of the active-site arginine residue for the normal catalytic activity of Cu,Zn superoxide dismutaseC L Borders, J E Saunders, D M Blech, et al.
Archives of Biochemistry and Biophysics|May 20, 1998
The familial amyotrophic lateral sclerosis-associated amino acid substitutions E100G, G93A, and G93R do not influence the rate of inactivation of copper- and zinc-containing superoxide dismutase by H2O2S I Liochev, L L Chen, R A Hallewell, et al.
Pageof 107