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Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis.

Furukawa Y, Kaneko K, Yamanaka K, O'Halloran TV, Nukina N.

J Biol Chem. 2008 Aug 29;283(35):24167-76. doi: 10.1074/jbc.M802083200. Epub 2008 Jun 13.


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.


Neuron-specific expression of mutant superoxide dismutase is sufficient to induce amyotrophic lateral sclerosis in transgenic mice.

Jaarsma D, Teuling E, Haasdijk ED, De Zeeuw CI, Hoogenraad CC.

J Neurosci. 2008 Feb 27;28(9):2075-88. doi: 10.1523/JNEUROSCI.5258-07.2008.


Detergent-insoluble aggregates associated with amyotrophic lateral sclerosis in transgenic mice contain primarily full-length, unmodified superoxide dismutase-1.

Shaw BF, Lelie HL, Durazo A, Nersissian AM, Xu G, Chan PK, Gralla EB, Tiwari A, Hayward LJ, Borchelt DR, Valentine JS, Whitelegge JP.

J Biol Chem. 2008 Mar 28;283(13):8340-50. doi: 10.1074/jbc.M707751200. Epub 2008 Jan 11.


Soluble misfolded subfractions of mutant superoxide dismutase-1s are enriched in spinal cords throughout life in murine ALS models.

Zetterström P, Stewart HG, Bergemalm D, Jonsson PA, Graffmo KS, Andersen PM, Brännström T, Oliveberg M, Marklund SL.

Proc Natl Acad Sci U S A. 2007 Aug 28;104(35):14157-62. Epub 2007 Aug 21.


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.


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.


An immunological epitope selective for pathological monomer-misfolded SOD1 in ALS.

Rakhit R, Robertson J, Vande Velde C, Horne P, Ruth DM, Griffin J, Cleveland DW, Cashman NR, Chakrabartty A.

Nat Med. 2007 Jun;13(6):754-9. Epub 2007 May 7.


Binding of a single zinc ion to one subunit of copper-zinc superoxide dismutase apoprotein substantially influences the structure and stability of the entire homodimeric protein.

Potter SZ, Zhu H, Shaw BF, Rodriguez JA, Doucette PA, Sohn SH, Durazo A, Faull KF, Gralla EB, Nersissian AM, Valentine JS.

J Am Chem Soc. 2007 Apr 18;129(15):4575-83. Epub 2007 Mar 24.


Kinetics and thermodynamics of amyloid fibril assembly.

Wetzel R.

Acc Chem Res. 2006 Sep;39(9):671-9. Review.


Insoluble mutant SOD1 is partly oligoubiquitinated in amyotrophic lateral sclerosis mice.

Basso M, Massignan T, Samengo G, Cheroni C, De Biasi S, Salmona M, Bendotti C, Bonetto V.

J Biol Chem. 2006 Nov 3;281(44):33325-35. Epub 2006 Aug 30.


Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria.

Deng HX, Shi Y, Furukawa Y, Zhai H, Fu R, Liu E, Gorrie GH, Khan MS, Hung WY, Bigio EH, Lukas T, Dal Canto MC, O'Halloran TV, Siddique T.

Proc Natl Acad Sci U S A. 2006 May 2;103(18):7142-7. Epub 2006 Apr 24.


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.


A native to amyloidogenic transition regulated by a backbone trigger.

Eakin CM, Berman AJ, Miranker AD.

Nat Struct Mol Biol. 2006 Mar;13(3):202-8. Epub 2006 Feb 19.


Disulphide-reduced superoxide dismutase-1 in CNS of transgenic amyotrophic lateral sclerosis models.

Jonsson PA, Graffmo KS, Andersen PM, Brännström T, Lindberg M, Oliveberg M, Marklund SL.

Brain. 2006 Feb;129(Pt 2):451-64. Epub 2005 Dec 5.


Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis.

Valentine JS, Doucette PA, Zittin Potter S.

Annu Rev Biochem. 2005;74:563-93. Review.


On the nucleation of amyloid beta-protein monomer folding.

Lazo ND, Grant MA, Condron MC, Rigby AC, Teplow DB.

Protein Sci. 2005 Jun;14(6):1581-96.


Folding of human superoxide dismutase: disulfide reduction prevents dimerization and produces marginally stable monomers.

Lindberg MJ, Normark J, Holmgren A, Oliveberg M.

Proc Natl Acad Sci U S A. 2004 Nov 9;101(45):15893-8. Epub 2004 Nov 2.


Dissociation of human copper-zinc superoxide dismutase dimers using chaotrope and reductant. Insights into the molecular basis for dimer stability.

Doucette PA, Whitson LJ, Cao X, Schirf V, Demeler B, Valentine JS, Hansen JC, Hart PJ.

J Biol Chem. 2004 Dec 24;279(52):54558-66. Epub 2004 Oct 12.


The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status.

Arnesano F, Banci L, Bertini I, Martinelli M, Furukawa Y, O'Halloran TV.

J Biol Chem. 2004 Nov 12;279(46):47998-8003. Epub 2004 Aug 23.

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