Cysteine 111 Affects Aggregation and Cytotoxicity of Mutant Cu,Zn-superoxide Dismutase Associated with Familial Amyotrophic Lateral Sclerosis*
暂无分享,去创建一个
[1] G. Sobue,et al. Disulfide Bond Mediates Aggregation, Toxicity, and Ubiquitylation of Familial Amyotrophic Lateral Sclerosis-linked Mutant SOD1* , 2007, Journal of Biological Chemistry.
[2] I. Bertini,et al. Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: A possible general mechanism for familial ALS , 2007, Proceedings of the National Academy of Sciences.
[3] J. Mieyal,et al. Glutathione Supplementation Potentiates Hypoxic Apoptosis by S-Glutathionylation of p65-NFκB* , 2007, Journal of Biological Chemistry.
[4] A. Chakrabartty,et al. An immunological epitope selective for pathological monomer-misfolded SOD1 in ALS , 2007, Nature Medicine.
[5] Robert H. Brown,et al. Increased affinity for copper mediated by cysteine 111 in forms of mutant superoxide dismutase 1 linked to amyotrophic lateral sclerosis. , 2007, Free radical biology & medicine.
[6] A. Holmgren,et al. Oxidation and S-Nitrosylation of Cysteines in Human Cytosolic and Mitochondrial Glutaredoxins , 2007, Journal of Biological Chemistry.
[7] K. Lim,et al. Relative Sensitivity of Parkin and Other Cysteine-containing Enzymes to Stress-induced Solubility Alterations* , 2007, Journal of Biological Chemistry.
[8] Bryan F. Shaw,et al. How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein? , 2007, Trends in biochemical sciences.
[9] W. Watson,et al. The Effects of Glutaredoxin and Copper Activation Pathways on the Disulfide and Stability of Cu,Zn Superoxide Dismutase* , 2006, Journal of Biological Chemistry.
[10] C. Crosio,et al. Familial ALS-superoxide dismutases associate with mitochondria and shift their redox potentials , 2006, Proceedings of the National Academy of Sciences.
[11] Barry Halliwell,et al. Oxidative stress and neurodegeneration: where are we now? , 2006, Journal of neurochemistry.
[12] E. Bigio,et al. Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria. , 2006, Proceedings of the National Academy of Sciences of the United States of America.
[13] T. Siddique,et al. Disulfide cross-linked protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregates in spinal cords of model mice. , 2006, Proceedings of the National Academy of Sciences of the United States of America.
[14] M. Carrì,et al. Targets in ALS: designing multidrug therapies. , 2006, Trends in pharmacological sciences.
[15] P. Andersen,et al. Disulphide-reduced superoxide dismutase-1 in CNS of transgenic amyotrophic lateral sclerosis models. , 2006, Brain : a journal of neurology.
[16] A. Holmgren,et al. Thiol redox control via thioredoxin and glutaredoxin systems. , 2005, Biochemical Society transactions.
[17] T. O’Halloran,et al. Amyotrophic Lateral Sclerosis Mutations Have the Greatest Destabilizing Effect on the Apo- and Reduced Form of SOD1, Leading to Unfolding and Oxidative Aggregation* , 2005, Journal of Biological Chemistry.
[18] Ole Gredal,et al. Toxicity of Familial ALS-Linked SOD1 Mutants from Selective Recruitment to Spinal Mitochondria , 2004, Neuron.
[19] D. Borchelt,et al. Copper-binding-site-null SOD1 causes ALS in transgenic mice: aggregates of non-native SOD1 delineate a common feature. , 2003, Human molecular genetics.
[20] D. Borchelt,et al. High Molecular Weight Complexes of Mutant Superoxide Dismutase 1: Age-Dependent and Tissue-Specific Accumulation , 2002, Neurobiology of Disease.
[21] A. Barzilai,et al. Glutaredoxin Protects Cerebellar Granule Neurons from Dopamine-induced Apoptosis by Dual Activation of the Ras-Phosphoinositide 3-Kinase and Jun N-terminal Kinase Pathways* , 2001, The Journal of Biological Chemistry.
[22] Freya Q. Schafer,et al. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. , 2001, Free radical biology & medicine.
[23] H. Scheraga,et al. A role for intermolecular disulfide bonds in prion diseases? , 2001, Proceedings of the National Academy of Sciences of the United States of America.
[24] A. Barzilai,et al. Glutaredoxin Protects Cerebellar Granule Neurons from Dopamine-induced Apoptosis by Activating NF-κB via Ref-1* , 2001, The Journal of Biological Chemistry.
[25] J. Holstege,et al. Human Cu/Zn Superoxide Dismutase (SOD1) Overexpression in Mice Causes Mitochondrial Vacuolization, Axonal Degeneration, and Premature Motoneuron Death and Accelerates Motoneuron Disease in Mice Expressing a Familial Amyotrophic Lateral Sclerosis Mutant SOD1 , 2000, Neurobiology of Disease.
[26] M. Gurney,et al. Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[27] L. Bruijn,et al. Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1. , 1998, Science.
[28] A. Palamara,et al. Loss of GSH, Oxidative Stress, and Decrease of Intracellular pH as Sequential Steps in Viral Infection* , 1997, The Journal of Biological Chemistry.
[29] J. Morrison,et al. Transgenic mice expressing an altered murine superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis. , 1995, Proceedings of the National Academy of Sciences of the United States of America.