Evidence map›Paper›PMID 23927036›Full record

ArticleBiochemistry2013

Post-translational modification by cysteine protects Cu/Zn-superoxide dismutase from oxidative damage.

Jared R Auclair, Joshua L Johnson, Qian Liu, Joseph P Salisbury, Melissa S Rotunno, Gregory A Petsko, Dagmar Ringe, Robert H Brown, Daryl A Bosco, Jeffrey N Agar

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.8field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
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  10. Copper ion / HRedox biology · 2019
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 1 institution in 1 country.

Jared R AuclairDepartments of Biochemistry and Chemistry and Rosenstiel Basic Medical Sciences Research Center, Brandeis University , Waltham, Massachusetts 02454, United States.
Joshua L Johnson
Qian Liu
Joseph P Salisbury
Melissa S Rotunno
Gregory A Petsko
Dagmar Ringe
Robert H Brown
Daryl A Bosco
Jeffrey N Agar
Brandeis University · US

Funding

Macromolecular Structure MechanismT32GM007596 · NIGMS · BRANDEIS UNIVERSITY · PI OPRIAN, DANIEL D · 1985 to 2019
$4.5M
Structural Consequences of ALS-related Modifications of SOD1R01NS065263 · NINDS · NORTHEASTERN UNIVERSITY · PI AGAR, JEFFREY NEIL · 2009 to 2013
$1.7M
Investigation of post-translational modifications in WT SOD1 in sporadic ALSR01NS067206 · NINDS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI BOSCO, DARYL ANGELA · 2010 to 2013
$1.4M
NIGMS NIH HHS T32 GM007596NINDS NIH HHS 1R01NS065263-01NINDS NIH HHS 1R01NS067206-02NINDS NIH HHS R01 NS065263NINDS NIH HHS R01 NS067206
6 · The paper itself

Abstract

Reactive oxygen species (ROS) are cytotoxic. To remove ROS, cells have developed ROS-specific defense mechanisms, including the enzyme Cu/Zn superoxide dismutase (SOD1), which catalyzes the disproportionation of superoxide anions into molecular oxygen and hydrogen peroxide. Although hydrogen peroxide is less reactive than superoxide, it is still capable of oxidizing, unfolding, and inactivating SOD1, at least in vitro. To explore the relevance of post-translational modification (PTM) of SOD1, including peroxide-related modifications, SOD1 was purified from postmortem human nervous tissue. As much as half of all purified SOD1 protein contained non-native post-translational modifications (PTMs), the most prevalent modifications being cysteinylation and peroxide-related oxidations. Many PTMs targeted a single reactive SOD1 cysteine, Cys111. An intriguing observation was that unlike native SOD1, cysteinylated SOD1 was not oxidized. To further characterize how cysteinylation may protect SOD1 from oxidation, cysteine-modified SOD1 was prepared in vitro and exposed to peroxide. Cysteinylation conferred nearly complete protection from peroxide-induced oxidation of SOD1. Moreover, SOD1 that has been cysteinylated and peroxide oxidized in vitro comprised a set of PTMs that bear a striking resemblance to the myriad of PTMs observed in SOD1 purified from human tissue.

Indexed as

Amino Acid SequenceAnimalsBrainCysteineHumansHydrogen PeroxideMiceOxidation-ReductionOxygenProtein Processing, Post-TranslationalSpinal CordSuperoxide DismutaseSuperoxide Dismutase-1CysteineHydrogen PeroxideOxygenSOD1 protein, humanSod1 protein, mouseSuperoxide DismutaseSuperoxide Dismutase-1

Identifiers

PMID23927036
PMCPMC3859700
OpenAlexW2037464729

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.