Dissociation of human copper-zinc superoxide dismutase dimers using chaotrope and reductant. Insights into the molecular basis for dimer stability (Q45107835)

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scientific article published on 12 October 2004

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English	Dissociation of human copper-zinc superoxide dismutase dimers using chaotrope and reductant. Insights into the molecular basis for dimer stability	scientific article published on 12 October 2004

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scholarly article

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Europe PubMed Central

PubMed publication ID

9 December 2017

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

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Europe PubMed Central

PubMed publication ID

9 December 2017

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Borries Demeler

5

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Borries Demeler

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9 December 2017

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Peter A Doucette

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Lisa J Whitson

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9 December 2017

Xiaohang Cao

3

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9 December 2017

Virgil Schirf

4

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9 December 2017

Joan Selverstone Valentine

6

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9 December 2017

Jeffrey C Hansen

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P John Hart

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publication date

12 October 2004

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9 December 2017

Journal of Biological Chemistry

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9 December 2017

279

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52

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9 December 2017

54558-54566

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9 December 2017

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The copper chaperone for superoxide dismutase

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

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

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Familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase are susceptible to disulfide reduction

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21 January 2018

Dimer destabilization in superoxide dismutase may result in disease-causing properties: structures of motor neuron disease mutants.

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Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis

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Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: studies in yeast and neural cells

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The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis

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Identifiers

10.1074/JBC.M409744200

1 reference

Europe PubMed Central

PubMed publication ID

9 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

9 December 2017

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