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Items: 1 to 20 of 212

1.

Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: a possible general mechanism for familial ALS.

Banci L, Bertini I, Durazo A, Girotto S, Gralla EB, Martinelli M, Valentine JS, Vieru M, Whitelegge JP.

Proc Natl Acad Sci U S A. 2007 Jul 3;104(27):11263-7. Epub 2007 Jun 25.

2.

The Disulfide Bond, but Not Zinc or Dimerization, Controls Initiation and Seeded Growth in Amyotrophic Lateral Sclerosis-linked Cu,Zn Superoxide Dismutase (SOD1) Fibrillation.

Chattopadhyay M, Nwadibia E, Strong CD, Gralla EB, Valentine JS, Whitelegge JP.

J Biol Chem. 2015 Dec 18;290(51):30624-36. doi: 10.1074/jbc.M115.666503. Epub 2015 Oct 28.

3.

Loss of metal ions, disulfide reduction and mutations related to familial ALS promote formation of amyloid-like aggregates from superoxide dismutase.

Oztug Durer ZA, Cohlberg JA, Dinh P, Padua S, Ehrenclou K, Downes S, Tan JK, Nakano Y, Bowman CJ, Hoskins JL, Kwon C, Mason AZ, Rodriguez JA, Doucette PA, Shaw BF, Valentine JS.

PLoS One. 2009;4(3):e5004. doi: 10.1371/journal.pone.0005004. Epub 2009 Mar 27.

4.

Disruption of mitochondrial membrane integrity induced by amyloid aggregates arising from variants of SOD1.

Oladzad Abbasabadi A, Javanian A, Nikkhah M, Meratan AA, Ghiasi P, Nemat-Gorgani M.

Int J Biol Macromol. 2013 Oct;61:212-7. doi: 10.1016/j.ijbiomac.2013.07.007. Epub 2013 Jul 17.

PMID:
23872456
6.

Aggregation of copper-zinc superoxide dismutase in familial and sporadic ALS.

Chattopadhyay M, Valentine JS.

Antioxid Redox Signal. 2009 Jul;11(7):1603-14. doi: 10.1089/ARS.2009.2536. Review.

7.

SOD1 and amyotrophic lateral sclerosis: mutations and oligomerization.

Banci L, Bertini I, Boca M, Girotto S, Martinelli M, Valentine JS, Vieru M.

PLoS One. 2008 Feb 27;3(2):e1677. doi: 10.1371/journal.pone.0001677.

8.

Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase.

Sea K, Sohn SH, Durazo A, Sheng Y, Shaw BF, Cao X, Taylor AB, Whitson LJ, Holloway SP, Hart PJ, Cabelli DE, Gralla EB, Valentine JS.

J Biol Chem. 2015 Jan 23;290(4):2405-18. doi: 10.1074/jbc.M114.588798. Epub 2014 Nov 28.

9.

SOD1 aggregation and ALS: role of metallation states and disulfide status.

Sheng Y, Chattopadhyay M, Whitelegge J, Valentine JS.

Curr Top Med Chem. 2012;12(22):2560-72. Review.

PMID:
23339308
10.

Mitochondrial membrane disruption by aggregation products of ALS-causing superoxide dismutase-1 mutants.

Salehi M, Nikkhah M, Ghasemi A, Arab SS.

Int J Biol Macromol. 2015 Apr;75:290-7. doi: 10.1016/j.ijbiomac.2015.01.022. Epub 2015 Jan 16.

PMID:
25600987
11.

Disulfide-reduced ALS variants of Cu, Zn superoxide dismutase exhibit increased populations of unfolded species.

Kayatekin C, Zitzewitz JA, Matthews CR.

J Mol Biol. 2010 Apr 30;398(2):320-31. doi: 10.1016/j.jmb.2010.02.034. Epub 2010 Feb 23.

12.
13.

Conformational Disorder of the Most Immature Cu, Zn-Superoxide Dismutase Leading to Amyotrophic Lateral Sclerosis.

Furukawa Y, Anzai I, Akiyama S, Imai M, Cruz FJ, Saio T, Nagasawa K, Nomura T, Ishimori K.

J Biol Chem. 2016 Feb 19;291(8):4144-55. doi: 10.1074/jbc.M115.683763. Epub 2015 Dec 22.

14.

Superoxide dismutase 1 mutants related to amyotrophic lateral sclerosis induce endoplasmic stress in neuro2a cells.

Oh YK, Shin KS, Yuan J, Kang SJ.

J Neurochem. 2008 Feb;104(4):993-1005. doi: 10.1111/j.1471-4159.2007.05053.x.

15.

Mutant SOD1 instability: implications for toxicity in amyotrophic lateral sclerosis.

Tiwari A, Hayward LJ.

Neurodegener Dis. 2005;2(3-4):115-27. Review.

PMID:
16909016
16.

Zinc and copper in the pathogenesis of amyotrophic lateral sclerosis.

Elliott JL.

Prog Neuropsychopharmacol Biol Psychiatry. 2001 Aug;25(6):1169-85. Review.

PMID:
11474839
17.

A role for copper in the toxicity of zinc-deficient superoxide dismutase to motor neurons in amyotrophic lateral sclerosis.

Trumbull KA, Beckman JS.

Antioxid Redox Signal. 2009 Jul;11(7):1627-39. doi: 10.1089/ARS.2009.2574. Review.

18.

Mechanism for transforming cytosolic SOD1 into integral membrane proteins of organelles by ALS-causing mutations.

Lim L, Lee X, Song J.

Biochim Biophys Acta. 2015 Jan;1848(1 Pt A):1-7. doi: 10.1016/j.bbamem.2014.10.002. Epub 2014 Oct 12.

19.

Strategies for stabilizing superoxide dismutase (SOD1), the protein destabilized in the most common form of familial amyotrophic lateral sclerosis.

Auclair JR, Boggio KJ, Petsko GA, Ringe D, Agar JN.

Proc Natl Acad Sci U S A. 2010 Dec 14;107(50):21394-9. doi: 10.1073/pnas.1015463107. Epub 2010 Nov 22.

20.

Dimerization, oligomerization, and aggregation of human amyotrophic lateral sclerosis copper/zinc superoxide dismutase 1 protein mutant forms in live cells.

Kim J, Lee H, Lee JH, Kwon DY, Genovesio A, Fenistein D, Ogier A, Brondani V, Grailhe R.

J Biol Chem. 2014 May 23;289(21):15094-103. doi: 10.1074/jbc.M113.542613. Epub 2014 Apr 1.

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