A Pivotal Role of Zn-Binding Residues in the Function of the Copper Chaperone for SOD1
- 5 October 2000
- journal article
- Published by Elsevier BV in Biochemical and Biophysical Research Communications
- Vol. 276 (3), 999-1004
- https://doi.org/10.1006/bbrc.2000.3581
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- Copper chaperone for superoxide dismutase is essential to activate mammalian Cu/Zn superoxide dismutaseProceedings of the National Academy of Sciences of the United States of America, 2000
- Gain in functions of mutant Cu,Zn-superoxide dismutases as a causative factor in familial amyotrophic lateral sclerosis: less reactive oxidant formation but high spontaneous aggregation and precipitation.Free Radical Research, 2000
- Multiple Protein Domains Contribute to the Action of the Copper Chaperone for Superoxide DismutaseJournal of Biological Chemistry, 1999
- Undetectable Intracellular Free Copper: The Requirement of a Copper Chaperone for Superoxide DismutaseScience, 1999
- Amyotrophic lateral sclerosis associated with mutations in superoxide dismutase: a putative mechanism of degenerationBrain Research Reviews, 1999
- The Copper Chaperone CCS Directly Interacts with Copper/Zinc Superoxide DismutaseJournal of Biological Chemistry, 1998
- Delivering Copper Inside Yeast and Human CellsScience, 1997
- The Copper Chaperone for Superoxide DismutasePublished by Elsevier BV ,1997
- SUPEROXIDE RADICAL AND SUPEROXIDE DISMUTASESAnnual Review of Biochemistry, 1995
- Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosisNature, 1993