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Items: 1 to 20 of 326

1.

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.

3.

Stabilization of mutant Cu/Zn superoxide dismutase (SOD1) protein by coexpressed wild SOD1 protein accelerates the disease progression in familial amyotrophic lateral sclerosis mice.

Fukada K, Nagano S, Satoh M, Tohyama C, Nakanishi T, Shimizu A, Yanagihara T, Sakoda S.

Eur J Neurosci. 2001 Dec;14(12):2032-6.

PMID:
11860498
4.
5.

Increased affinity for copper mediated by cysteine 111 in forms of mutant superoxide dismutase 1 linked to amyotrophic lateral sclerosis.

Watanabe S, Nagano S, Duce J, Kiaei M, Li QX, Tucker SM, Tiwari A, Brown RH Jr, Beal MF, Hayward LJ, Culotta VC, Yoshihara S, Sakoda S, Bush AI.

Free Radic Biol Med. 2007 May 15;42(10):1534-42. Epub 2007 Feb 15.

PMID:
17448900
6.

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.

7.

Structural changes to monomeric CuZn superoxide dismutase caused by the familial amyotrophic lateral sclerosis-associated mutation A4V.

Schmidlin T, Kennedy BK, Daggett V.

Biophys J. 2009 Sep 16;97(6):1709-18. doi: 10.1016/j.bpj.2009.06.043.

8.

An intersubunit disulfide bond prevents in vitro aggregation of a superoxide dismutase-1 mutant linked to familial amytrophic lateral sclerosis.

Ray SS, Nowak RJ, Strokovich K, Brown RH Jr, Walz T, Lansbury PT Jr.

Biochemistry. 2004 May 4;43(17):4899-905.

PMID:
15109247
9.

Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation.

Ray SS, Nowak RJ, Brown RH Jr, Lansbury PT Jr.

Proc Natl Acad Sci U S A. 2005 Mar 8;102(10):3639-44. Epub 2005 Feb 28.

10.

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.

11.

Heterodimer formation of wild-type and amyotrophic lateral sclerosis-causing mutant Cu/Zn-superoxide dismutase induces toxicity independent of protein aggregation.

Witan H, Kern A, Koziollek-Drechsler I, Wade R, Behl C, Clement AM.

Hum Mol Genet. 2008 May 15;17(10):1373-85. doi: 10.1093/hmg/ddn025. Epub 2008 Jan 22.

PMID:
18211954
12.

Interaction between familial amyotrophic lateral sclerosis (ALS)-linked SOD1 mutants and the dynein complex.

Zhang F, Ström AL, Fukada K, Lee S, Hayward LJ, Zhu H.

J Biol Chem. 2007 Jun 1;282(22):16691-9. Epub 2007 Apr 2.

13.

Disulfide cross-linked protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregates in spinal cords of model mice.

Furukawa Y, Fu R, Deng HX, Siddique T, O'Halloran TV.

Proc Natl Acad Sci U S A. 2006 May 2;103(18):7148-53. Epub 2006 Apr 24.

14.

Palmitoylation of superoxide dismutase 1 (SOD1) is increased for familial amyotrophic lateral sclerosis-linked SOD1 mutants.

Antinone SE, Ghadge GD, Lam TT, Wang L, Roos RP, Green WN.

J Biol Chem. 2013 Jul 26;288(30):21606-17. doi: 10.1074/jbc.M113.487231. Epub 2013 Jun 12.

15.

A limited role for disulfide cross-linking in the aggregation of mutant SOD1 linked to familial amyotrophic lateral sclerosis.

Karch CM, Borchelt DR.

J Biol Chem. 2008 May 16;283(20):13528-37. doi: 10.1074/jbc.M800564200. Epub 2008 Mar 3.

16.

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.

17.

Cu/Zn superoxide dismutase (SOD1) mutations associated with familial amyotrophic lateral sclerosis (ALS) affect cellular free radical release in the presence of oxidative stress.

Cookson MR, Menzies FM, Manning P, Eggett CJ, Figlewicz DA, McNeil CJ, Shaw PJ.

Amyotroph Lateral Scler Other Motor Neuron Disord. 2002 Jun;3(2):75-85.

PMID:
12215229
18.

Heat shock factor 1 over-expression protects against exposure of hydrophobic residues on mutant SOD1 and early mortality in a mouse model of amyotrophic lateral sclerosis.

Lin PY, Simon SM, Koh WK, Folorunso O, Umbaugh CS, Pierce A.

Mol Neurodegener. 2013 Nov 21;8:43. doi: 10.1186/1750-1326-8-43.

20.

Folding of Cu, Zn superoxide dismutase and familial amyotrophic lateral sclerosis.

Khare SD, Ding F, Dokholyan NV.

J Mol Biol. 2003 Nov 28;334(3):515-25.

PMID:
14623191

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