Evidence map›Paper›PMID 25452140›Full record

ReviewFree radical biology & medicine2015

A primer on peroxiredoxin biochemistry.

P Andrew Karplus

Open access · greenAbstract readHistorical ArticleReview
In one paragraph

Review in Free radical biology & medicine, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
6.4field-weighted citation impact, top 3% 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

59 citing papers in PubMed, 132 citations in OpenAlex.

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  13. Review
  14. Review
  15. Article
  16. Review
  17. Article
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  19. Review
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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

1 author at 1 institution in 1 country.

P Andrew KarplusDepartment of Biochemistry and Biophysics, Oregon State University, Corvallis, OR 97331, USA. Electronic address: karplusp@science.oregonstate.edu.
Oregon 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 R01 GM050389NIGMS NIH HHS R01GM50389
6 · The paper itself

Abstract

Peroxiredoxins were not recognized as a family of enzymes until the 1990s but are now known to be the dominant peroxidases in most organisms. Here, the history and fundamental properties of peroxiredoxins are briefly reviewed, with a special focus on describing how an exquisitely tunable balance between fully folded and locally unfolded conformations plays a large role in peroxiredoxin catalytic properties.

Indexed as

AnimalsBacteriaBiocatalysisFungiHistory, 20th CenturyHistory, 21st CenturyHumansKineticsModels, MolecularMolecular ChaperonesMultigene FamilyOxidation-ReductionPeroxiredoxinsProtein ConformationProtein FoldingProtein MultimerizationMolecular ChaperonesPeroxiredoxinsSulfhydryl CompoundsChaperoneFloodgate hypothesisHydrogen peroxideOxidative stressRedox signaling

Identifiers

PMID25452140
PMCPMC4355262
OpenAlexW2013421642

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.