Evidence map›Paper›PMID 27391469›Full record

ArticlePloS one2016

Oxidation of Са2+-Binding Domain of NADPH Oxidase 5 (NOX5): Toward Understanding the Mechanism of Inactivation of NOX5 by ROS.

Irina Yu Petrushanko, Vladimir M Lobachev, Alexey S Kononikhin, Alexander A Makarov, Francois Devred, Hervé Kovacic, Aslan A Kubatiev, Philipp O Tsvetkov

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

18 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Mechanism of ZnBiomolecules · 2021
    Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. NOX5: Molecular biology and pathophysiology.Experimental physiology · 2019
    Review
  13. Article
  14. Reactive oxygen species and male reproductive hormones.Reproductive biology and endocrinology : RB&E · 2018
    Review
  15. Article
  16. Article
  17. Article
  18. 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

8 authors at 5 institutions in 2 countries.

Irina Yu PetrushankoEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov Street 32, 119991 Moscow, Russia.
Vladimir M LobachevEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov Street 32, 119991 Moscow, Russia.
Alexey S KononikhinMoscow Institute of Physics and Technology, 141700 Dolgoprudnyi, Moscow Region, Russia.
Alexander A MakarovEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov Street 32, 119991 Moscow, Russia.
Francois DevredAix-Marseille University, Inserm, CRO2 UMR_S 911, Faculté de Pharmacie, 13385 Marseille, France.
Hervé KovacicAix-Marseille University, Inserm, CRO2 UMR_S 911, Faculté de Pharmacie, 13385 Marseille, France.
Aslan A KubatievInstitute of General Pathology and Pathophysiology, RAMS, 125315, Moscow, Russian Federation.
Philipp O TsvetkovAix-Marseille University, Inserm, CRO2 UMR_S 911, Faculté de Pharmacie, 13385 Marseille, France.
Engelhardt Institute of Molecular Biology · RUResearch Institute of General Pathology and Pathophysiology, the Russian Academy of Medical Sciences · RUAix-Marseille Université · FRInserm · FRMoscow Institute of Physics and Technology · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NOX5 protein, one of the most active generators of reactive oxygen species (ROS), plays an important role in many processes, including regulation of cell growth, death and differentiation. Because of its central role in ROS generation, it needs to be tightly regulated to guarantee cellular homeostasis. Contrary to other members of NADPH-oxidases family, NOX5 has its own regulatory calcium-binding domain and thus could be activated directly by calcium ions. While several mechanisms of activation have been described, very little is known about the mechanisms that could prevent the overproduction of ROS by NOX5. In the present study using calorimetric methods and circular dichroism we found that oxidation of cysteine and methionine residues of NOX5 decreases binding of Ca2+ ions and perturbs both secondary and tertiary structure of protein. Our data strongly suggest that oxidation of calcium-binding domain of NOX5 could be implicated in its inactivation, serving as a possible defense mechanism against oxidative stress.

Indexed as

Amino Acid SequenceCalorimetryCalorimetry, Differential ScanningChromatography, LiquidCircular DichroismCysteineHomeostasisHumansMembrane ProteinsMethionineMolecular Sequence DataNADPH Oxidase 5NADPH OxidasesOxidation-ReductionProtein DomainsReactive Oxygen SpeciesCysteineMembrane ProteinsMethionineNADPH Oxidase 5NADPH OxidasesNOX5 protein, humanReactive Oxygen Species

Identifiers

PMID27391469
PMCPMC4938588
OpenAlexW2462445719

What OpenQuestion holds

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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.