Evidence map›Paper›PMID 30584462›Full record

ArticleOxidative medicine and cellular longevity2018

Nucleoredoxin-Dependent Targets and Processes in Neuronal Cells.

Claudia Urbainsky, Rolf Nölker, Marcel Imber, Adrian Lübken, Jörg Mostertz, Falko Hochgräfe, José R Godoy, Eva-Maria Hanschmann, Christopher Horst Lillig

Open access · hybridAbstract read
In one paragraph

Article in Oxidative medicine and cellular longevity, 2018. 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
1.0field-weighted citation impact, top 23% 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

13 citing papers in PubMed, 24 citations in OpenAlex.

  1. Lipid Peroxidation-Related Redox Signaling in Osteosarcoma.International journal of molecular sciences · 2024
    Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Nucleoredoxin GeneFrontiers in plant science · 2021
    Article
  10. Observational
  11. Article
  12. Article
  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

9 authors at 4 institutions in 2 countries.

Claudia UrbainskyThe Institute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald, Germany.ORCID 0000-0002-3509-433X
Rolf NölkerCompetence Center Functional Genomics, Junior Research Group Pathoproteomics, University of Greifswald, Germany.
Marcel ImberInstitute for Biology-Microbiology, Freie Universität Berlin, Germany.
Adrian LübkenThe Institute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald, Germany.
Jörg MostertzCompetence Center Functional Genomics, Junior Research Group Pathoproteomics, University of Greifswald, Germany.
Falko HochgräfeCompetence Center Functional Genomics, Junior Research Group Pathoproteomics, University of Greifswald, Germany.
José R GodoyFaculty of Biomedical Sciences, Ross University School of Veterinary Medicine, Basseterre, Saint Kitts and Nevis.
Eva-Maria HanschmannThe Institute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald, Germany.ORCID 0000-0003-1114-7262
Christopher Horst LilligThe Institute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald, Germany.ORCID 0000-0003-2509-5117
Universitätsmedizin Greifswald · DEUniversität Greifswald · DEFreie Universität Berlin · DERoss University School of Veterinary Medicine · KN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nucleoredoxin (Nrx) is an oxidoreductase of the thioredoxin family of proteins. It was shown to act as a signal transducer in some pathways; however, so far, no comprehensive analysis of its regulated substrates and functions was available. Here, we used a combination of two different strategies to fill this gap. First, we analyzed the thiol-redox state of the proteome of SH-SY5Y neuroblastoma cells depleted of Nrx compared to control cells using a differential thiol-labeling technique and quantitative mass spectrometry. 171 proteins were identified with an altered redox state; 161 of these were more reduced in the absence of Nrx. This suggests functions of Nrx in the oxidation of protein thiols. Second, we utilized the active site mutant Cys208Ser of Nrx, which stabilizes a mixed disulfide intermediate with its substrates and therefore trapped interacting proteins from the mouse brain (identifying 1710 proteins) and neuronal cell culture extracts (identifying 609 proteins). Profiling of the affected biological processes and molecular functions in cells of neuronal origin suggests numerous functions of Nrx in the redox regulation of metabolic pathways, cellular morphology, and signal transduction. These results characterize Nrx as a cellular oxidase that itself may be oxidized by the formation of disulfide relays with peroxiredoxins.

Indexed as

AnimalsBlotting, WesternBrainCell Line, TumorElectrophoresis, Polyacrylamide GelHumansMiceNeuronsNuclear ProteinsOxidation-ReductionOxidoreductasesNuclear ProteinsnucleoredoxinOxidoreductases

Identifiers

PMID30584462
PMCPMC6280245
OpenAlexW2901809253

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.