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Items: 1 to 20 of 164

1.

Early steps in oxidation-induced SOD1 misfolding: implications for non-amyloid protein aggregation in familial ALS.

Mulligan VK, Kerman A, Laister RC, Sharda PR, Arslan PE, Chakrabartty A.

J Mol Biol. 2012 Aug 24;421(4-5):631-52. doi: 10.1016/j.jmb.2012.04.016. Epub 2012 Apr 24.

PMID:
22542526
2.

Amyotrophic lateral sclerosis is a non-amyloid disease in which extensive misfolding of SOD1 is unique to the familial form.

Kerman A, Liu HN, Croul S, Bilbao J, Rogaeva E, Zinman L, Robertson J, Chakrabartty A.

Acta Neuropathol. 2010 Mar;119(3):335-44. doi: 10.1007/s00401-010-0646-5. Epub 2010 Jan 29.

PMID:
20111867
3.

SOD1 oxidation and formation of soluble aggregates in yeast: relevance to sporadic ALS development.

Martins D, English AM.

Redox Biol. 2014 Mar 26;2:632-9. doi: 10.1016/j.redox.2014.03.005. eCollection 2014.

4.

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. Epub 2011 Apr 27.

PMID:
21549128
5.

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.

6.

Calcium ions promote superoxide dismutase 1 (SOD1) aggregation into non-fibrillar amyloid: a link to toxic effects of calcium overload in amyotrophic lateral sclerosis (ALS)?

Leal SS, Cardoso I, Valentine JS, Gomes CM.

J Biol Chem. 2013 Aug 30;288(35):25219-28. doi: 10.1074/jbc.M113.470740. Epub 2013 Jul 16.

7.

Aberrant zinc binding to immature conformers of metal-free copper-zinc superoxide dismutase triggers amorphous aggregation.

Leal SS, Cristóvão JS, Biesemeier A, Cardoso I, Gomes CM.

Metallomics. 2015 Feb;7(2):333-46. doi: 10.1039/c4mt00278d.

PMID:
25554447
8.

Identification of a misfolded region in superoxide dismutase 1 that is exposed in amyotrophic lateral sclerosis.

Rotunno MS, Auclair JR, Maniatis S, Shaffer SA, Agar J, Bosco DA.

J Biol Chem. 2014 Oct 10;289(41):28527-38. doi: 10.1074/jbc.M114.581801. Epub 2014 Aug 27.

9.

Oxidation-induced misfolding and aggregation of superoxide dismutase and its implications for amyotrophic lateral sclerosis.

Rakhit R, Cunningham P, Furtos-Matei A, Dahan S, Qi XF, Crow JP, Cashman NR, Kondejewski LH, Chakrabartty A.

J Biol Chem. 2002 Dec 6;277(49):47551-6. Epub 2002 Sep 27.

10.

Superoxide Dismutase 1 (SOD1)-Derived Peptide Inhibits Amyloid Aggregation of Familial Amyotrophic Lateral Sclerosis SOD1 Mutants.

Banerjee V, Shani T, Katzman B, Vyazmensky M, Papo N, Israelson A, Engel S.

ACS Chem Neurosci. 2016 Nov 16;7(11):1595-1606. Epub 2016 Sep 2.

PMID:
27540759
11.

Denaturational stress induces formation of zinc-deficient monomers of Cu,Zn superoxide dismutase: implications for pathogenesis in amyotrophic lateral sclerosis.

Mulligan VK, Kerman A, Ho S, Chakrabartty A.

J Mol Biol. 2008 Nov 7;383(2):424-36. doi: 10.1016/j.jmb.2008.08.024. Epub 2008 Aug 22.

PMID:
18761352
12.

Protein misfolding in the late-onset neurodegenerative diseases: common themes and the unique case of amyotrophic lateral sclerosis.

Mulligan VK, Chakrabartty A.

Proteins. 2013 Aug;81(8):1285-303. doi: 10.1002/prot.24285. Epub 2013 Jul 2. Review.

PMID:
23508986
13.

Superoxide dismutase 1 encoding mutations linked to ALS adopts a spectrum of misfolded states.

Prudencio M, Borchelt DR.

Mol Neurodegener. 2011 Nov 17;6:77. doi: 10.1186/1750-1326-6-77.

14.

Aberrant localization of FUS and TDP43 is associated with misfolding of SOD1 in amyotrophic lateral sclerosis.

Pokrishevsky E, Grad LI, Yousefi M, Wang J, Mackenzie IR, Cashman NR.

PLoS One. 2012;7(4):e35050. doi: 10.1371/journal.pone.0035050. Epub 2012 Apr 6.

15.

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
16.

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
17.

Curcumin binds to the pre-fibrillar aggregates of Cu/Zn superoxide dismutase (SOD1) and alters its amyloidogenic pathway resulting in reduced cytotoxicity.

Bhatia NK, Srivastava A, Katyal N, Jain N, Khan MA, Kundu B, Deep S.

Biochim Biophys Acta. 2015 May;1854(5):426-36. doi: 10.1016/j.bbapap.2015.01.014. Epub 2015 Feb 7.

PMID:
25666897
18.

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
19.
20.

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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