Evidence map›Paper›PMID 30576927›Full record

ArticleRedox biology2019

Red fluorescent redox-sensitive biosensor Grx1-roCherry.

Arina G Shokhina, Alexander I Kostyuk, Yulia G Ermakova, Anastasiya S Panova, Dmitry B Staroverov, Evgeny S Egorov, Mikhail S Baranov, Gijsbert J van Belle, Dörthe M Katschinski, Vsevolod V Belousov and 1 more

Abstract read
In one paragraph

Article in Redox biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
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

13 citing papers in PubMed.

  1. Review
  2. Article
  3. Dynamic redox monitoring in differentiated human neuroblastoma models of Parkinson's disease.Redox report : communications in free radical research · 2025
    Article
  4. Review
  5. Review
  6. Review
  7. Review
  8. Review
  9. Article
  10. In Vivo Imaging with Genetically Encoded Redox Biosensors.International journal of molecular sciences · 2020
    Review
  11. Article
  12. Review
  13. 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

11 authors.

Arina G ShokhinaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow 117997, Russia.
Alexander I KostyukShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow 117997, Russia.
Yulia G ErmakovaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow 117997, Russia; European Molecular Biology Laboratory, Heidelberg 69117, Germany.
Anastasiya S PanovaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow 117997, Russia.
Dmitry B StaroverovShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow 117997, Russia.
Evgeny S EgorovShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow 117997, Russia.
Mikhail S BaranovShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow 117997, Russia.
Gijsbert J van BelleInstitute for Cardiovascular Physiology, Georg August University Göttingen, Göttingen 37073, Germany.
Dörthe M KatschinskiInstitute for Cardiovascular Physiology, Georg August University Göttingen, Göttingen 37073, Germany.
Vsevolod V BelousovShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow 117997, Russia; Institute for Cardiovascular Physiology, Georg August University Göttingen, Göttingen 37073, Germany; Pirogov Russian National Research Medical University, Moscow 117997, Russia. Electronic address: belousov@ibch.ru.
Dmitry S BilanShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow 117997, Russia; Pirogov Russian National Research Medical University, Moscow 117997, Russia. Electronic address: d.s.bilan@gmail.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Redox-sensitive fluorescent proteins (roFPs) are a powerful tool for imaging intracellular redox changes. The structure of these proteins contains a pair of cysteines capable of forming a disulfide upon oxidation that affects the protein conformation and spectral characteristics. To date, a palette of such biosensors covers the spectral range from blue to red. However, most of the roFPs suffer from either poor brightness or high pH-dependency, or both. Moreover, there is no roRFP with the redox potential close to that of 2GSH/GSSG redox pair. In the present work, we describe Grx1-roCherry, the first red roFP with canonical FP topology and fluorescent excitation/emission spectra of typical RFP. Grx1-roCherry, with a midpoint redox potential of - 311 mV, is characterized by high brightness and increased pH stability (pKa 6.7). We successfully used Grx1-roCherry in combination with other biosensors in a multiparameter imaging mode to demonstrate redox changes in cells under various metabolic perturbations, including hypoxia/reoxygenation. In particular, using simultaneous expression of Grx1-roCherry and its green analog in various compartments of living cells, we demonstrated that local H

Indexed as

Biosensing TechniquesOxidation-ReductionRecombinant Fusion ProteinsAnimalsGene ExpressionGenes, ReporterGlutaredoxinsGlutathioneGlutathione DisulfideGlycolysisHEK293 CellsHeLa CellsHumansHypoxiaLuminescent ProteinsMiceGLRX protein, humanGlutaredoxinsGlutathioneGlutathione DisulfideLuminescent ProteinsRecombinant Fusion Proteins2GSH/GSSGBiosensorGrx1-roCherryMultiparameter imagingRedox-sensitive fluorescent protein

Identifiers

PMID30576927
PMCPMC6302151

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Registered trials

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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.