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Results: 1 to 20 of 294

Similar articles for PubMed (Select 17592131)

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.

3.

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.

4.

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.

PMID:
18233996
5.

Fully metallated S134N Cu,Zn-superoxide dismutase displays abnormal mobility and intermolecular contacts in solution.

Banci L, Bertini I, D'Amelio N, Gaggelli E, Libralesso E, Matecko I, Turano P, Valentine JS.

J Biol Chem. 2005 Oct 28;280(43):35815-21. Epub 2005 Aug 16.

6.

Initiation and elongation in fibrillation of ALS-linked superoxide dismutase.

Chattopadhyay M, Durazo A, Sohn SH, Strong CD, Gralla EB, Whitelegge JP, Valentine JS.

Proc Natl Acad Sci U S A. 2008 Dec 2;105(48):18663-8. doi: 10.1073/pnas.0807058105. Epub 2008 Nov 20.

7.

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
8.

Disulfide bond mediates aggregation, toxicity, and ubiquitylation of familial amyotrophic lateral sclerosis-linked mutant SOD1.

Niwa J, Yamada S, Ishigaki S, Sone J, Takahashi M, Katsuno M, Tanaka F, Doyu M, Sobue G.

J Biol Chem. 2007 Sep 21;282(38):28087-95. Epub 2007 Jul 31.

9.

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.

10.

Superoxide dismutase-1 mutation-related neurotoxicity in familial amyotrophic lateral sclerosis.

Shibata N, Hirano A, Yamamoto T, Kato Y, Kobayashi M.

Amyotroph Lateral Scler Other Motor Neuron Disord. 2000 Jun;1(3):143-61. Review.

PMID:
11464949
11.
13.

The ALS-associated mutation G93A in human copper-zinc superoxide dismutase selectively destabilizes the remote metal binding region.

Museth AK, Brorsson AC, Lundqvist M, Tibell LA, Jonsson BH.

Biochemistry. 2009 Sep 22;48(37):8817-29. doi: 10.1021/bi900703v.

PMID:
19655787
14.

Monomeric Cu,Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis.

Rakhit R, Crow JP, Lepock JR, Kondejewski LH, Cashman NR, Chakrabartty A.

J Biol Chem. 2004 Apr 9;279(15):15499-504. Epub 2004 Jan 20.

15.

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
16.

The metal binding properties of the zinc site of yeast copper-zinc superoxide dismutase: implications for amyotrophic lateral sclerosis.

Lyons TJ, Nersissian A, Huang H, Yeom H, Nishida CR, Graden JA, Gralla EB, Valentine JS.

J Biol Inorg Chem. 2000 Apr;5(2):189-203.

PMID:
10819464
17.
18.

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.

19.

Oxidized/misfolded superoxide dismutase-1: the cause of all amyotrophic lateral sclerosis?

Kabashi E, Valdmanis PN, Dion P, Rouleau GA.

Ann Neurol. 2007 Dec;62(6):553-9. Review.

PMID:
18074357
20.

How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein?

Shaw BF, Valentine JS.

Trends Biochem Sci. 2007 Feb;32(2):78-85. Epub 2007 Jan 5. Review.

PMID:
17208444
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