(Q45107835)

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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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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

1

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Europe PubMed Central

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9 December 2017

Lisa J Whitson

2

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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

7

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9 December 2017

P John Hart

8

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9 December 2017

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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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9 December 2017

52

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Europe PubMed Central

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9 December 2017

54558-54566

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Europe PubMed Central

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9 December 2017

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Subunit association and side-chain reactivities of bovine erythrocyte superoxide dismutase in denaturing solvents

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

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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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