Evidence map›Paper›PMID 31201851›Full record

ReviewFree radical biology & medicine2019

The role of thiols in antioxidant systems.

Kathrin Ulrich, Ursula Jakob

Open access · greenAbstract readReview
In one paragraph

Review in Free radical biology & medicine, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 234 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
234citing papers in PubMed, 3 pooled it
15.4field-weighted citation impact, top 1% 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

234 citing papers in PubMed, 3 syntheses or guidelines pooled it, 525 citations in OpenAlex.

  1. Pooled it
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  8. Disulphide maintenance systems and proteostasis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
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  16. Potential Antidote Against Lead Toxicity-A Review.International journal of molecular sciences · 2026
    Review
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174 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Kathrin UlrichDepartment of Molecular, Cellular, and Developmental Biology, University of Michgan, Ann Arbor, MI, 48109, USA.
Ursula JakobDepartment of Molecular, Cellular, and Developmental Biology, University of Michgan, Ann Arbor, MI, 48109, USA; Department of Biological Chemistry, University of Michigan, Ann Arbor, MI, 48109, USA. Electronic address: ujakob@umich.edu.
University of Michigan–Ann Arbor · US

Funding

Role of Molecular Chaperones in Stress Response and DiseaseR35GM122506 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Ursula H. Jakob · 2017 to 2026
$6.8M
NIGMS NIH HHS R35 GM122506
6 · The paper itself

Abstract

The sulfur biochemistry of the thiol group endows cysteines with a number of highly specialized and unique features that enable them to serve a variety of different functions in the cell. Typically highly conserved in proteins, cysteines are predominantly found in functionally or structurally crucial regions, where they act as stabilizing, catalytic, metal-binding and/or redox-regulatory entities. As highly abundant low molecular weight thiols, cysteine thiols and their oxidized disulfide counterparts are carefully balanced to maintain redox homeostasis in various cellular compartments, protect organisms from oxidative and xenobiotic stressors and partake actively in redox-regulatory and signaling processes. In this review, we will discuss the role of protein thiols as scavengers of hydrogen peroxide in antioxidant enzymes, use thiol peroxidases to exemplify how protein thiols contribute to redox signaling, provide an overview over the diverse set of low molecular weight thiol-based redox systems found in biology, and illustrate how thiol-based redox systems have evolved not only to protect against but to take full advantage of a world full of molecular oxygen.

Indexed as

AntioxidantsCatalysisCysteineFree Radical ScavengersGlutathioneHumansHydrogen PeroxideOxygenPeroxidasesProteinsSulfhydryl CompoundsAntioxidantsCysteineFree Radical ScavengersGlutathioneHydrogen PeroxideOxygenPeroxidasesProteinsSulfhydryl Compounds

Identifiers

PMID31201851
PMCPMC7041647
OpenAlexW2951027422

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.