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Items: 1 to 20 of 213

1.

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
2.
3.

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.

PMID:
26511321
4.

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.

5.

Metal deficiency increases aberrant hydrophobicity of mutant superoxide dismutases that cause amyotrophic lateral sclerosis.

Tiwari A, Liba A, Sohn SH, Seetharaman SV, Bilsel O, Matthews CR, Hart PJ, Valentine JS, Hayward LJ.

J Biol Chem. 2009 Oct 2;284(40):27746-58. doi: 10.1074/jbc.M109.043729.

7.

A common property of amyotrophic lateral sclerosis-associated variants: destabilization of the copper/zinc superoxide dismutase electrostatic loop.

Molnar KS, Karabacak NM, Johnson JL, Wang Q, Tiwari A, Hayward LJ, Coales SJ, Hamuro Y, Agar JN.

J Biol Chem. 2009 Nov 6;284(45):30965-73. doi: 10.1074/jbc.M109.023945.

8.

Structural instability and Cu-dependent pro-oxidant activity acquired by the apo form of mutant SOD1 associated with amyotrophic lateral sclerosis.

Kitamura F, Fujimaki N, Okita W, Hiramatsu H, Takeuchi H.

Biochemistry. 2011 May 24;50(20):4242-50. doi: 10.1021/bi200338h.

PMID:
21506602
9.

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.

11.

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.

12.

Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosis.

Cao X, Antonyuk SV, Seetharaman SV, Whitson LJ, Taylor AB, Holloway SP, Strange RW, Doucette PA, Valentine JS, Tiwari A, Hayward LJ, Padua S, Cohlberg JA, Hasnain SS, Hart PJ.

J Biol Chem. 2008 Jun 6;283(23):16169-77. doi: 10.1074/jbc.M801522200.

13.

Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis.

Hayward LJ, Rodriguez JA, Kim JW, Tiwari A, Goto JJ, Cabelli DE, Valentine JS, Brown RH Jr.

J Biol Chem. 2002 May 3;277(18):15923-31.

14.

An over-oxidized form of superoxide dismutase found in sporadic amyotrophic lateral sclerosis with bulbar onset shares a toxic mechanism with mutant SOD1.

Guareschi S, Cova E, Cereda C, Ceroni M, Donetti E, Bosco DA, Trotti D, Pasinelli P.

Proc Natl Acad Sci U S A. 2012 Mar 27;109(13):5074-9. doi: 10.1073/pnas.1115402109.

15.

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
16.

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.

17.

Structural consequences of the familial amyotrophic lateral sclerosis SOD1 mutant His46Arg.

Antonyuk S, Elam JS, Hough MA, Strange RW, Doucette PA, Rodriguez JA, Hayward LJ, Valentine JS, Hart PJ, Hasnain SS.

Protein Sci. 2005 May;14(5):1201-13.

18.

ALS-causing SOD1 mutations promote production of copper-deficient misfolded species.

Ip P, Mulligan VK, Chakrabartty A.

J Mol Biol. 2011 Jun 24;409(5):839-52. doi: 10.1016/j.jmb.2011.04.027.

PMID:
21549128
19.

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.

20.

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.

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