The Unusually Stable Quaternary Structure of Human Cu,Zn-Superoxide Dismutase 1 Is Controlled by Both Metal Occupancy and Disulfide Status
Open Access
- 1 November 2004
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 279 (46), 47998-48003
- https://doi.org/10.1074/jbc.m406021200
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- Seeded conversion of recombinant prion protein to a disulfide-bonded oligomer by a reduction-oxidation processNature Structural & Molecular Biology, 2003
- Structure and dynamics of copper‐free SOD: The protein before binding copperProtein Science, 2002
- Mechanism of Cu,Zn-Superoxide Dismutase Activation by the Human Metallochaperone hCCSJournal of Biological Chemistry, 2001
- Heterodimer Formation between Superoxide Dismutase and Its Copper ChaperoneBiochemistry, 2000
- Undetectable Intracellular Free Copper: The Requirement of a Copper Chaperone for Superoxide DismutaseScience, 1999
- Long-Range Motional Restrictions in a Multidomain Zinc-Finger Protein from Anisotropic TumblingScience, 1995
- Conserved Patterns in the Cu,Zn Superoxide Dismutase FamilyJournal of Molecular Biology, 1994
- An interactive graphic program for calculating the secondary structure content of proteins from circular dichroism spectrumBioinformatics, 1993
- Determination of the helix and β form of proteins in aqueous solution by circular dichroismBiochemistry, 1974
- Computed circular dichroism spectra for the evaluation of protein conformationBiochemistry, 1969