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Items: 1 to 20 of 275

1.

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.

2.

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
3.
5.

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.

6.

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.

7.

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
8.
9.

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.

10.

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. Epub 2008 Mar 31.

11.

Reduced net charge and heterogeneity of pI isoforms in familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase.

Roudeau S, Chevreux S, Carmona A, Ortega R.

Electrophoresis. 2015 Oct;36(19):2482-8. doi: 10.1002/elps.201500187. Epub 2015 Aug 18.

PMID:
26084641
12.

Inducible superoxide dismutase 1 aggregation in transgenic amyotrophic lateral sclerosis mouse fibroblasts.

Turner BJ, Lopes EC, Cheema SS.

J Cell Biochem. 2004 Apr 1;91(5):1074-84.

PMID:
15034941
13.

Unveiling the unfolding pathway of FALS associated G37R SOD1 mutant: a computational study.

Milardi D, Pappalardo M, Grasso DM, La Rosa C.

Mol Biosyst. 2010 Jun;6(6):1032-9. doi: 10.1039/b918662j. Epub 2010 Feb 23.

PMID:
20485746
15.
17.

Early steps in thermal unfolding of superoxide dismutase 1 are similar to the conformational changes associated with the ALS-associated A4V mutation.

Schmidlin T, Ploeger K, Jonsson AL, Daggett V.

Protein Eng Des Sel. 2013 Aug;26(8):503-13. doi: 10.1093/protein/gzt030. Epub 2013 Jun 19.

18.

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
19.

Structure, folding, and misfolding of Cu,Zn superoxide dismutase in amyotrophic lateral sclerosis.

Rakhit R, Chakrabartty A.

Biochim Biophys Acta. 2006 Nov-Dec;1762(11-12):1025-37. Epub 2006 May 22. Review.

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