Structural Consequences of Cysteinylation of Cu/Zn-Superoxide Dismutase (Q27679379)

4

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Dagmar Ringe

5

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Heather R Brodkin

2

Heather R Brodkin

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Daniel A. Aquino

3

J Alejandro D'Aquino

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Jeffrey N Agar

6

Jeffrey N Agar

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Jared R Auclair

1

Structural switching of Cu,Zn-superoxide dismutases at loop VI: insights from the crystal structure of 2-mercaptoethanol-modified enzyme

Jared R Auclair

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language of work or name

English

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publication date

10 September 2013

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published in

Biochemistry

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volume

52

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issue

36

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page(s)

6145-50

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cites work

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A common property of amyotrophic lateral sclerosis-associated variants: destabilization of the copper/zinc superoxide dismutase electrostatic loop

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Direct probing of copper active site and free radical formed during bicarbonate-dependent peroxidase activity of bovine and human copper, zinc-superoxide dismutases. Low-temperature electron paramagnetic resonance and electron nuclear double resonan

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Monomeric Cu,Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis.

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The coupling between disulphide status, metallation and dimer interface strength in Cu/Zn superoxide dismutase

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S-cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress

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Processing of X-ray diffraction data collected in oscillation mode

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Oxygen radicals stimulate intracellular proteolysis and lipid peroxidation by independent mechanisms in erythrocytes

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Proteins damaged by oxygen radicals are rapidly degraded in extracts of red blood cells

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Cu/Zn superoxide dismutase-like immunoreactivity in Lewy body-like inclusions of sporadic amyotrophic lateral sclerosis

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