Crossref journal-article
Oxford University Press (OUP)
Human Molecular Genetics (286)
Bibliography

Proescher, J. B., Son, M., Elliott, J. L., & Culotta, V. C. (2008). Biological effects of CCS in the absence of SOD1 enzyme activation: implications for disease in a mouse model for ALS. Human Molecular Genetics, 17(12), 1728–1737.

Authors 4
  1. Jody B. Proescher (first)
  2. Marjatta Son (additional)
  3. Jeffrey L. Elliott (additional)
  4. Valeria C. Culotta (additional)
References 45 Referenced 61
  1. 10.1016/S0021-9258(18)63504-5 / J. Biol. Chem. / Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein) by McCord (1969)
  2. 10.1074/jbc.272.38.23469 / J. Biol. Chem. / The copper chaperone for superoxide dismutase by Culotta (1997)
  3. 10.1038/nsb0901-751 / Nat. Struct. Biol. / Heterodimeric structure of superoxide dismutase in complex with its metallochaperone by Lamb (2001)
  4. 10.1074/jbc.M600138200 / J. Biol. Chem. / The effects of glutaredoxin and copper activation pathways on the disulfide and stability of Cu,Zn superoxide dismutase by Carroll (2006)
  5. 10.1038/sj.emboj.7600276 / Embo. J. / Oxygen-induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS by Furukawa (2004)
  6. 10.1073/pnas.0308298101 / Proc. Natl. Acad. Sci. USA / Mechanisms for activating Cu- and Zn-containing superoxide dismutase in the absence of the CCS Cu chaperone by Carroll (2004)
  7. 10.1016/S0021-9258(19)44055-6 / J. Biol. Chem. / On the stability of bovine superoxide dismutase. The effects of metals by Forman (1973)
  8. 10.1146/annurev.neuro.27.070203.144244 / Annu. Rev. Neurosci. / Unraveling the mechanisms involved in motor neuron degeneration in ALS by Bruijn (2004)
  9. 10.1073/pnas.0730423100 / Proc. Natl. Acad. Sci. USA / Misfolded CuZnSOD and amyotrophic lateral sclerosis by Valentine (2003)
  10. 10.1089/ars.2006.8.847 / Antioxid. Redox Signal. / Posttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis by Furukawa (2006)
  11. 10.1016/j.neuron.2006.09.018 / Neuron / ALS: a disease of motor neurons and their nonneuronal neighbors by Boillee (2006)
  12. 10.1006/nbdi.2001.0443 / Neurobiol. Dis. / Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues by Watanabe (2001)
  13. 10.1073/pnas.0602046103 / Proc. Natl. Acad. Sci. USA / Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria by Deng (2006)
  14. 10.1093/brain/awh005 / Brain / Minute quantities of misfolded mutant superoxide dismutase-1 cause amyotrophic lateral sclerosis by Jonsson (2004)
  15. 10.1016/j.bbrc.2006.02.170 / Biochem. Biophys. Res. Commun. / Alteration of familial ALS-linked mutant SOD1 solubility with disease progression: its modulation by the proteasome and Hsp70 by Koyama (2006)
  16. 10.1074/jbc.M604503200 / J. Biol. Chem. / Disease-associated mutations at copper ligand histidine residues of superoxide dismutase 1 diminish the binding of copper and compromise dimer stability by Wang (2007)
  17. 10.1093/hmg/ddg312 / Hum. Mol. Genet. / Copper-binding-site-null SOD1 causes ALS in transgenic mice: aggregates of non-native SOD1 delineate a common feature by Wang (2003)
  18. 10.1093/hmg/ddi236 / Hum. Mol. Genet. / Somatodendritic accumulation of misfolded SOD1-L126Z in motor neurons mediates degeneration: alphaB-crystallin modulates aggregation by Wang (2005)
  19. 10.1016/j.nbd.2005.06.005 / Neurobiol. Dis. / Coincident thresholds of mutant protein for paralytic disease and protein aggregation caused by restrictively expressed superoxide dismutase cDNA by Wang (2005)
  20. 10.1074/jbc.M010759200 / J. Biol. Chem. / Mutant Cu/Zn-superoxide dismutase proteins have altered solubility and interact with heat shock/stress proteins in models of amyotrophic lateral sclerosis by Shinder (2001)
  21. 10.1016/j.nbd.2004.12.007 / Neurobiol. Dis. / Accumulation of human SOD1 and ubiquitinated deposits in the spinal cord of SOD1G93A mice during motor neuron disease progression correlates with a decrease of proteasome by Cheroni (2005)
  22. 10.1074/jbc.M603489200 / J. Biol. Chem. / Insoluble mutant SOD1 is partly oligoubiquitinated in amyotrophic lateral sclerosis mice by Basso (2006)
  23. 10.1016/S0304-3940(03)00893-0 / Neurosci. Lett. / Neuromuscular accumulation of mutant superoxide dismutase 1 aggregates in a transgenic mouse model of familial amyotrophic lateral sclerosis by Turner (2003)
  24. 10.1074/jbc.M409744200 / J. Biol. Chem. / Dissociation of human copper-zinc superoxide dismutase dimers using chaotrope and reductant. Insights into the molecular basis for dimer stability by Doucette (2004)
  25. 10.1074/jbc.M500482200 / J. Biol. Chem. / Amyotrophic lateral sclerosis mutations have the greatest destabilizing effect on the apo- and reduced form of SOD1, leading to unfolding and oxidative aggregation by Furukawa (2005)
  26. 10.1073/pnas.0602048103 / Proc. Natl. Acad. Sci. USA / Disulfide cross-linked protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregates in spinal cords of model mice by Furukawa (2006)
  27. 10.1074/jbc.M704465200 / J. Biol. Chem. / Disulfide bond mediates aggregation, toxicity, and ubiquitylation of familial amyotrophic lateral sclerosis-linked mutant SOD1 by Niwa (2007)
  28. 10.1111/j.1471-4159.2005.03642.x / J. Neurochem. / Mapping superoxide dismutase 1 domains of non-native interaction: roles of intra- and intermolecular disulfide bonding in aggregation by Wang (2006)
  29. 10.1073/pnas.0700477104 / Proc. Natl. Acad. Sci. USA / Soluble misfolded subfractions of mutant superoxide dismutase-1s are enriched in spinal cords throughout life in murine ALS models by Zetterstrom (2007)
  30. 10.1073/pnas.0610923104 / Proc. Natl. Acad. Sci. USA / Overexpression of CCS in G93A-SOD1 mice leads to accelerated neurological deficits with severe mitochondrial pathology by Son (2007)
  31. 10.1093/brain/awh704 / Brain / Disulphide-reduced superoxide dismutase-1 in CNS of transgenic amyotrophic lateral sclerosis models by Jonsson (2006)
  32. 10.1074/jbc.M601580200 / J. Biol. Chem. / Mechanisms of the copper-dependent turnover of the copper chaperone for superoxide dismutase by Caruano-Yzermans (2006)
  33. 10.1074/jbc.274.34.23719 / J. Biol. Chem. / Multiple protein domains contribute to the action of the copper chaperone for superoxide dismutase by Schmidt (1999)
  34. 10.1021/bi700566h / Biochemistry / A multinuclear copper(I) cluster forms the dimerization interface in copper-loaded human copper chaperone for superoxide dismutase by Stasser (2007)
  35. 10.1074/jbc.M006254200 / J. Biol. Chem. / Copper activation of superoxide dismutase 1 (SOD1) in vivo. Role for protein-protein interactions with the copper chaperone for SOD1 by Schmidt (2000)
  36. 10.1002/jcb.10782 / J. Cell Biochem. / Inducible superoxide dismutase 1 aggregation in transgenic amyotrophic lateral sclerosis mouse fibroblasts by Turner (2004)
  37. 10.1038/nn823 / Nat. Neurosci. / Mutant SOD1 causes motor neuron disease independent of copper chaperone-mediated copper loading by Subramaniam (2002)
  38. 10.1074/jbc.273.37.23625 / J. Biol. Chem. / The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase by Casareno (1998)
  39. 10.1074/jbc.M210419200 / J. Biol. Chem. / Familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase are susceptible to disulfide reduction by Tiwari (2003)
  40. 10.1074/jbc.M105296200 / J. Biol. Chem. / A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage by Sturtz (2001)
  41. 10.1073/pnas.132260399 / Proc. Natl. Acad. Sci. USA / Amyotrophic lateral sclerosis: a proposed mechanism by Okado-Matsumoto (2002)
  42. 10.1038/nn1603 / Nat. Neurosci. / Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis by Urushitani (2006)
  43. 10.1073/pnas.91.17.8292 / Proc. Natl. Acad. Sci. USA / Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity by Borchelt (1994)
  44. 10.1016/S0076-6879(84)05013-8 / Methods Enzymol. / Superoxide dismutase assays by Flohe (1984)
  45. 10.1074/jbc.274.52.36952 / J. Biol. Chem. / A gain of superoxide dismutase (SOD) activity obtained with CCS, the copper metallochaperone for SOD1 by Schmidt (1999)
Dates
Type When
Created 17 years, 5 months ago (March 12, 2008, 8:35 p.m.)
Deposited 4 years ago (Sept. 5, 2021, 4:56 p.m.)
Indexed 3 hours, 31 minutes ago (Sept. 6, 2025, 3:50 p.m.)
Issued 17 years, 5 months ago (March 12, 2008)
Published 17 years, 5 months ago (March 12, 2008)
Published Online 17 years, 5 months ago (March 12, 2008)
Published Print 17 years, 2 months ago (June 15, 2008)
Funders 0

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@article{Proescher_2008, title={Biological effects of CCS in the absence of SOD1 enzyme activation: implications for disease in a mouse model for ALS}, volume={17}, ISSN={0964-6906}, url={http://dx.doi.org/10.1093/hmg/ddn063}, DOI={10.1093/hmg/ddn063}, number={12}, journal={Human Molecular Genetics}, publisher={Oxford University Press (OUP)}, author={Proescher, Jody B. and Son, Marjatta and Elliott, Jeffrey L. and Culotta, Valeria C.}, year={2008}, month=mar, pages={1728–1737} }