Post-translational modification by cysteine protects Cu/Zn-superoxide dismutase from oxidative damage (Q37384587)

20 August 2017

Post-translational modification by cysteine protects Cu/Zn-superoxide dismutase from oxidative damage (English)

1 reference

20 August 2017

6

Gregory A Petsko

1 reference

20 August 2017

7

Dagmar Ringe

1 reference

20 August 2017

10

Jeffrey N Agar

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20 August 2017

1

Jared R Auclair

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20 August 2017

9

Daryl A Bosco

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20 August 2017

8

Robert H Brown

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20 August 2017

Joshua L Johnson

2

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20 August 2017

Qian Liu

series ordinal

3

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20 August 2017

Joseph P Salisbury

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4

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20 August 2017

Melissa S Rotunno

series ordinal

5

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20 August 2017

language of work or name

English

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publication date

26 August 2013

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20 August 2017

8

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inferred from page(s)

published in

Biochemistry

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20 August 2017

52

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20 August 2017

36

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20 August 2017

6137-6144

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describes a project that uses

20 August 2017

ImageJ

1 reference

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC3859700/fullTextXML

inferred from PubMed Central ID database lookup

cites work

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Strategies for stabilizing superoxide dismutase (SOD1), the protein destabilized in the most common form of familial amyotrophic lateral sclerosis

6 September 2017

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Structural characterization of intact proteins is enhanced by prevalent fragmentation pathways rarely observed for peptides

6 September 2017

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6 September 2017

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Cu/Zn superoxide dismutase and age-related hearing loss

6 September 2017

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6 September 2017

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Identification and location of a cysteinyl posttranslational modification in an amyloidogenic kappa1 light chain protein by electrospray ionization and matrix-assisted laser desorption/ionization mass spectrometry.

6 September 2017

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Subunit-destabilizing mutations in Drosophila copper/zinc superoxide dismutase: neuropathology and a model of dimer dysequilibrium

6 September 2017

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Copper(2+) binding to the surface residue cysteine 111 of His46Arg human copper-zinc superoxide dismutase, a familial amyotrophic lateral sclerosis mutant

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26 June 2018

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Oxidative modification to cysteine sulfonic acid of Cys111 in human copper-zinc superoxide dismutase

26 June 2018

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Oxidative modifications and aggregation of Cu,Zn-superoxide dismutase associated with Alzheimer and Parkinson diseases

2 September 2018

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2 September 2018

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2 September 2018

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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.

2 September 2018

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2 September 2018

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Amino acid sequence of chicken Cu, Zn-containing superoxide dismutase and identification of glutathionyl adducts at exposed cysteine residues

2 September 2018

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2 September 2018

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Tryptophan 32 potentiates aggregation and cytotoxicity of a copper/zinc superoxide dismutase mutant associated with familial amyotrophic lateral sclerosis

2 September 2018

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The standard redox potential of cysteine-cystine from the thiol-disulphide exchange reaction with glutathione and lipoic acid

2 October 2018

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12 December 2020

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12 December 2020

Histochemical evaluation of glutathione in brain

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12 December 2020

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

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12 December 2020

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

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12 December 2020

Simple and defined method to detect the SOD-1 mutants from patients with familial amyotrophic lateral sclerosis by mass spectrometry

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12 December 2020

Cerebrospinal fluid S-adenosylmethionine (SAMe) and glutathione concentrations in HIV infection Effect of parenteral treatment with SAMe

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12 December 2020

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

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12 December 2020

Alteration of amino acid content of cerebrospinal fluid from patients with epilepsy

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12 December 2020

Identifiers

DOI

10.1021/BI4006122

1 reference

20 August 2017

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20 August 2017

PubMed publication ID

23927036

1 reference