Copper(2+) Binding to the Surface Residue Cysteine 111 of His46Arg Human Copper−Zinc Superoxide Dismutase, a Familial Amyotrophic Lateral Sclerosis Mutant
- 20 June 2000
- journal article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 39 (28) , 8125-8132
- https://doi.org/10.1021/bi000846f
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- The metal binding properties of the zinc site of yeast copper-zinc superoxide dismutase: implications for amyotrophic lateral sclerosisJBIC Journal of Biological Inorganic Chemistry, 2000
- Intracellular copper routing: the role of copper chaperonesTrends in Biochemical Sciences, 2000
- Amyotrophic lateral sclerosis associated with mutations in superoxide dismutase: a putative mechanism of degenerationPublished by Elsevier ,1998
- Impaired copper binding by the H46R mutant of human Cu,Zn superoxide dismutase, involved in amyotrophic lateral sclerosisFEBS Letters, 1994
- Familial amyotrophic lateral sclerosis (ALS) in Japan associated with H46R mutation in superoxide dismutase gene: A possible new subtype of familial ALSJournal of the Neurological Sciences, 1994
- ALS, SOD and peroxynitriteNature, 1993
- Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosisNature, 1993
- [4] Biochemical and spectroscopic probes of mercury(II) coordination environments in proteinsPublished by Elsevier ,1993
- Resonance Raman spectroscopy of blue copper proteins: ligand and coenzyme effects in copper(II)-substituted liver alcohol dehydrogenaseJournal of the American Chemical Society, 1986
- Labile Sulfur in Human Superoxide DismutaseEuropean Journal of Biochemistry, 1975