Structural and Thermodynamic Effects of Post-translational Modifications in Mutant and Wild Type Cu, Zn Superoxide Dismutase
- 6 May 2011
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 408 (3), 555-567
- https://doi.org/10.1016/j.jmb.2011.03.004
Abstract
No abstract availableKeywords
This publication has 54 references indexed in Scilit:
- Peripheral hyperstimulation alters site of disease onset and course in SOD1 ratsNeurobiology of Disease, 2010
- The structural biochemistry of the superoxide dismutasesBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2009
- Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93AArchives of Biochemistry and Biophysics, 2009
- Functional features cause misfolding of the ALS-provoking enzyme SOD1Proceedings of the National Academy of Sciences, 2009
- Modifications of Superoxide Dismutase (SOD1) in Human ErythrocytesJournal of Biological Chemistry, 2009
- Dynamical roles of metal ions and the disulfide bond in Cu, Zn superoxide dismutase folding and aggregationProceedings of the National Academy of Sciences, 2008
- Initiation and elongation in fibrillation of ALS-linked superoxide dismutaseProceedings of the National Academy of Sciences of the United States of America, 2008
- Zinc Binding Modulates the Entire Folding Free Energy Surface of Human Cu,Zn Superoxide DismutaseJournal of Molecular Biology, 2008
- Ab Initio Folding of Proteins with All-Atom Discrete Molecular DynamicsStructure, 2008
- Molecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu–Zn superoxide dismutaseProceedings of the National Academy of Sciences of the United States of America, 2007