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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. Epub 2002 Feb 19.


Familial amyotrophic lateral sclerosis-associated mutations decrease the thermal stability of distinctly metallated species of human copper/zinc superoxide dismutase.

Rodriguez JA, Valentine JS, Eggers DK, Roe JA, Tiwari A, Brown RH Jr, Hayward LJ.

J Biol Chem. 2002 May 3;277(18):15932-7. Epub 2002 Feb 19.


Loss of in vitro metal ion binding specificity in mutant copper-zinc superoxide dismutases associated with familial amyotrophic lateral sclerosis.

Goto JJ, Zhu H, Sanchez RJ, Nersissian A, Gralla EB, Valentine JS, Cabelli DE.

J Biol Chem. 2000 Jan 14;275(2):1007-14.


Fibrillar inclusions and motor neuron degeneration in transgenic mice expressing superoxide dismutase 1 with a disrupted copper-binding site.

Wang J, Xu G, Gonzales V, Coonfield M, Fromholt D, Copeland NG, Jenkins NA, Borchelt DR.

Neurobiol Dis. 2002 Jul;10(2):128-38.


Normal binding and reactivity of copper in mutant superoxide dismutase isolated from amyotrophic lateral sclerosis patients.

Marklund SL, Andersen PM, Forsgren L, Nilsson P, Ohlsson PI, Wikander G, Oberg A.

J Neurochem. 1997 Aug;69(2):675-81.


Fluorescence assay for monitoring Zn-deficient superoxide dismutase in vitro.

Martyshkin DV, Mirov SB, Zhuang YX, Crow JP, Ermilov V, Beckman JS.

Spectrochim Acta A Mol Biomol Spectrosc. 2003 Nov;59(13):3165-75.


Analysis of the cytosolic proteome in a cell culture model of familial amyotrophic lateral sclerosis reveals alterations to the proteasome, antioxidant defenses, and nitric oxide synthetic pathways.

Allen S, Heath PR, Kirby J, Wharton SB, Cookson MR, Menzies FM, Banks RE, Shaw PJ.

J Biol Chem. 2003 Feb 21;278(8):6371-83. Epub 2002 Dec 9.


The metal binding properties of the zinc site of yeast copper-zinc superoxide dismutase: implications for amyotrophic lateral sclerosis.

Lyons TJ, Nersissian A, Huang H, Yeom H, Nishida CR, Graden JA, Gralla EB, Valentine JS.

J Biol Inorg Chem. 2000 Apr;5(2):189-203.


Loss of oxidation-reduction specificity in amyotrophic lateral sclerosis-associated CuZnSOD mutants.

Cafe C, Testa MP, Sheldon PJ, French WP, Ellerby LM, Bredesen DE.

J Mol Neurosci. 2000 Oct;15(2):71-83.


Fully metallated S134N Cu,Zn-superoxide dismutase displays abnormal mobility and intermolecular contacts in solution.

Banci L, Bertini I, D'Amelio N, Gaggelli E, Libralesso E, Matecko I, Turano P, Valentine JS.

J Biol Chem. 2005 Oct 28;280(43):35815-21. Epub 2005 Aug 16.


Copper and zinc metallation status of copper-zinc superoxide dismutase from amyotrophic lateral sclerosis transgenic mice.

Lelie HL, Liba A, Bourassa MW, Chattopadhyay M, Chan PK, Gralla EB, Miller LM, Borchelt DR, Valentine JS, Whitelegge JP.

J Biol Chem. 2011 Jan 28;286(4):2795-806. doi: 10.1074/jbc.M110.186999. Epub 2010 Nov 10.


The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase.

Casareno RL, Waggoner D, Gitlin JD.

J Biol Chem. 1998 Sep 11;273(37):23625-8.

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