Evidence map›Paper›PMID 23830624›Full record

ArticleMethods in enzymology2013

Evaluating peroxiredoxin sensitivity toward inactivation by peroxide substrates.

Kimberly J Nelson, Derek Parsonage, P Andrew Karplus, Leslie B Poole

Open access · greenAbstract read
In one paragraph

Article in Methods in enzymology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
10.5field-weighted citation impact, top 2% 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

24 citing papers in PubMed, 34 citations in OpenAlex.

  1. Lipid Peroxidation-Related Redox Signaling in Osteosarcoma.International journal of molecular sciences · 2024
    Review
  2. Overoxidation and Oligomerization ofPathogens (Basel, Switzerland) · 2023
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Novel hyperoxidation resistance motifs in 2-Cys peroxiredoxins.The Journal of biological chemistry · 2018
    Article
  9. Ohr plays a central role in bacterial responses against fatty acid hydroperoxides and peroxynitrite.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  10. Peroxiredoxin Catalysis at Atomic Resolution.Structure (London, England : 1993) · 2016
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. Review
  17. A primer on peroxiredoxin biochemistry.Free radical biology & medicine · 2015
    Review
  18. Article
  19. Review
  20. Article
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

4 authors at 2 institutions in 1 country.

Kimberly J NelsonDepartment of Biochemistry, Wake Forest School of Medicine, Winston-Salem, North Carolina, USA.
Derek Parsonage
P Andrew Karplus
Leslie B Poole
Wake Forest University · USOregon State University · US

Funding

Mechanistic Studies of Alkyl Hydroperoxide Reductase and Related Redox SystemsR01GM050389 · NIGMS · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI POOLE, LESLIE B · 1994 to 2013
$4.8M
NIGMS NIH HHS GM050389NIGMS NIH HHS R01 GM050389
6 · The paper itself

Abstract

Peroxiredoxins (Prxs) not only are very effective peroxide-reducing enzymes but also are susceptible to being oxidatively inactivated by their own substrates. The level of sensitivity to such hyperoxidation varies depending on both the enzyme involved and the type of peroxide substrate. For some Prxs, the hyperoxidation has physiological relevance, so it is important to define approaches that can be used to quantify sensitivity. Here, we describe three distinct approaches that can be used to obtain quantitative or semiquantitative estimates of Prx sensitivity and define C(hyp1%) as a simple way of quantifying sensitivity so that values can easily be compared.

Indexed as

Benzene DerivativesData Interpretation, StatisticalEnzyme AssaysEscherichia coli ProteinsKineticsNADPOxidation-ReductionPeroxidesPeroxiredoxinsSubstrate SpecificityBenzene Derivativescumene hydroperoxideEscherichia coli ProteinsNADPPeroxidesPeroxiredoxinsCysteine sulfenic acidCysteine sulfinic acidHyperoxidationMass spectrometryOxidative inactivationPeroxidasePeroxide signalingRedox signaling

Identifiers

PMID23830624
PMCPMC3856590
OpenAlexW834967220

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.