Evidence map›Paper›PMID 38150990›Full record

ArticleRedox biology2024

The architecture of redox microdomains: Cascading gradients and peroxiredoxins' redox-oligomeric coupling integrate redox signaling and antioxidant protection.

Matthew Griffith, Adérito Araújo, Rui Travasso, Armindo Salvador

Open access · goldAbstract read
In one paragraph

Article in Redox biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.7field-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

4 citing papers in PubMed, 11 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. 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 2 countries.

Matthew GriffithCNC - Centre for Neuroscience Cell Biology, University of Coimbra, UC-Biotech, Parque Tecnológico de Cantanhede, Núcleo 4, Lote 8, 3060-197, Cantanhede, Portugal; Department of Mathematical Sciences, University of Bath, Claverton Down, Bath, BA2 7AY, UK.
Adérito AraújoCMUC, Department of Mathematics, University of Coimbra, Largo D. Dinis, 3004-143, Coimbra, Portugal. Electronic address: alma@mat.uc.pt.
Rui TravassoCFisUC, Department of Physics, University of Coimbra, Coimbra, Rua Larga, 3004-516, Coimbra, Portugal. Electronic address: ruit@fis.uc.pt.
Armindo SalvadorCNC - Centre for Neuroscience Cell Biology, University of Coimbra, UC-Biotech, Parque Tecnológico de Cantanhede, Núcleo 4, Lote 8, 3060-197, Cantanhede, Portugal; Coimbra Chemistry Center - Institute of Molecular Sciences (CQC-IMS), University of Coimbra, Rua Larga, 3004-535, Coimbra, Portugal; Institute for Interdisciplinary Research, University of Coimbra, Casa Costa Alemão, Rua Dom Francisco de Lemos, 3030-789, Coimbra, Portugal. Electronic address: salvador@cnc.uc.pt.
University of Coimbra · PTUniversity of Bath · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the cytosol of human cells under low oxidative loads, hydrogen peroxide is confined to microdomains around its supply sites, due to its fast consumption by peroxiredoxins. So are the sulfenic and disulfide forms of the 2-Cys peroxiredoxins, according to a previous theoretical analysis [Travasso et al., Redox Biology 15 (2017) 297]. Here, an extended reaction-diffusion model that for the first time considers the differential properties of human peroxiredoxins 1 and 2 and the thioredoxin redox cycle predicts important new aspects of the dynamics of redox microdomains. The peroxiredoxin 1 sulfenates and disulfides are more localized than the corresponding peroxiredoxin 2 forms, due to the former peroxiredoxin's faster resolution step. The thioredoxin disulfides are also localized. As the H

Indexed as

AntioxidantsPeroxiredoxinsDisulfidesHumansHydrogen PeroxideOxidation-ReductionThioredoxin-Disulfide ReductaseThioredoxinsAntioxidantsDisulfidesHydrogen PeroxidePeroxiredoxinsThioredoxin-Disulfide ReductaseThioredoxinsHydrogen peroxidePeroxiredoxinsReaction-diffusion modelRedox microdomainsRedox signalingTotal protein concentration gradients

Identifiers

PMID38150990
PMCPMC10829873
OpenAlexW4390024084

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.