Evidence map›Paper›PMID 35691509›Full record

ReviewFree radical biology & medicine2022

The role of glutathione peroxidase-1 in health and disease.

Diane E Handy, Joseph Loscalzo

Open access · greenAbstract readReview
In one paragraph

Review in Free radical biology & medicine, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 177 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
177citing papers in PubMed, 3 pooled it
24.4field-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

177 citing papers in PubMed, 3 syntheses or guidelines pooled it, 240 citations in OpenAlex.

  1. Pooled it
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  3. Pooled it
  4. Trial
  5. Review
  6. Review
  7. Article
  8. Wound Healing Potential of Selenium and Nanoselenium.Biological trace element research · 2026
    Review
  9. Review
  10. Article
  11. On the Edge of Benefit and Harm: Reactive Oxygen Species in Cancer.International journal of molecular sciences · 2026
    Review
  12. Article
  13. Article
  14. Review
  15. Review
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  17. Review
  18. Article
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  20. Exercise Training Stimulates the Release of Glutathione Peroxidase 1 (GPX1)-Enriched Extracellular Vesicles That Promote Angiogenesis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article

117 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.

Diane E HandyDivision of Cardiovascular Medicine, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, MA, 02115, USA. Electronic address: dhandy@rics.bwh.harvard.edu.
Joseph LoscalzoDivision of Cardiovascular Medicine, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, MA, 02115, USA. Electronic address: jloscalzo@rics.bwh.harvard.edu.
Brigham and Women's Hospital · US

Funding

TRANSLATIONAL PHARMACOLOGY COREP50GM107618 · NIGMS · HARVARD MEDICAL SCHOOL · PI GOLAN, DAVID E. · 2014 to 2018
$10.8M
Center for Integrated Approaches to Undiagnosed DiseasesU01HG007690 · NHGRI · BRIGHAM AND WOMEN'S HOSPITAL · PI LOSCALZO, JOSEPH · 2014 to 2022
$10.4M
GPx-3 and Peroxide Flux in the Endothelial CellR37HL061795 · NHLBI · BRIGHAM AND WOMEN'S HOSPITAL · PI LOSCALZO, JOSEPH · 2007 to 2016
$4.3M
L-2-Hydroxyglutarate and Metabolic Remodeling in HypoxiaR01HL155107 · NHLBI · BRIGHAM AND WOMEN'S HOSPITAL · PI Joseph Loscalzo · 2021 to 2026
$4.1M
PLATELET DERIVED REACTIVE OXYGEN SPECIES AND PLAQUER01HL061795 · NHLBI · BRIGHAM AND WOMEN'S HOSPITAL · PI LOSCALZO, JOSEPH · 1998 to 2006
$1.6M
NHGRI NIH HHS U01 HG007690NHLBI NIH HHS R01 HL061795NHLBI NIH HHS R01 HL155107NHLBI NIH HHS R37 HL061795NIGMS NIH HHS P50 GM107618
6 · The paper itself

Abstract

Glutathione peroxidase 1 (GPx1) is an important cellular antioxidant enzyme that is found in the cytoplasm and mitochondria of mammalian cells. Like most selenoenzymes, it has a single redox-sensitive selenocysteine amino acid that is important for the enzymatic reduction of hydrogen peroxide and soluble lipid hydroperoxides. Glutathione provides the source of reducing equivalents for its function. As an antioxidant enzyme, GPx1 modulates the balance between necessary and harmful levels of reactive oxygen species. In this review, we discuss how selenium availability and modifiers of selenocysteine incorporation alter GPx1 expression to promote disease states. We review the role of GPx1 in cardiovascular and metabolic health, provide examples of how GPx1 modulates stroke and provides neuroprotection, and consider how GPx1 may contribute to cancer risk. Overall, GPx1 is protective against the development and progression of many chronic diseases; however, there are some situations in which increased expression of GPx1 may promote cellular dysfunction and disease owing to its removal of essential reactive oxygen species.

Indexed as

SeleniumSelenocysteineAnimalsAntioxidantsGlutathione PeroxidaseGlutathione Peroxidase GPX1MammalsOxidative StressReactive Oxygen SpeciesAntioxidantsGlutathione PeroxidaseGlutathione Peroxidase GPX1Reactive Oxygen SpeciesSeleniumSelenocysteineAngiogenesisAtherosclerosisCancerCardiac protectionEndothelial dysfunctionGlutathione peroxidase 1InflammationNeurodegenerationOxidative stressSeleniumSelenocysteineStroke

Identifiers

PMID35691509
PMCPMC9586416
OpenAlexW4281748239

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.