Evidence map›Paper›PMID 30531830›Full record

ArticleScientific reports2018

The reduced activity of PP-1α under redox stress condition is a consequence of GSH-mediated transient disulfide formation.

Simranjit Singh, Simon Lämmle, Heiko Giese, Susanne Kämmerer, Stefanie Meyer-Roxlau, Ezzaldin Ahmed Alfar, Hassan Dihazi, Kaomei Guan, Ali El-Armouche, Florian Richter

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

7 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. A druggable redox switch on SHP1 controls macrophage inflammation.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Regulation of Cardiac PKA Signaling by cAMP and Oxidants.Antioxidants (Basel, Switzerland) · 2021
    Review
  6. Mass Spectrometry-Based Redox and Protein Profiling of Failing Human Hearts.International journal of molecular sciences · 2021
    Article
  7. 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

10 authors at 3 institutions in 1 country.

Simranjit SinghInstitute of Pharmacology and Toxicology, Technische Universität Dresden, Dresden, Germany.
Simon LämmleInstitute of Pharmacology and Toxicology, Technische Universität Dresden, Dresden, Germany.
Heiko GieseMolecular Bioinformatics, Goethe-Universität Frankfurt am Main, Frankfurt, Germany.
Susanne KämmererInstitute of Pharmacology and Toxicology, Technische Universität Dresden, Dresden, Germany.
Stefanie Meyer-RoxlauInstitute of Pharmacology and Toxicology, Technische Universität Dresden, Dresden, Germany.
Ezzaldin Ahmed AlfarInstitute of Pharmacology and Toxicology, Technische Universität Dresden, Dresden, Germany.
Hassan DihaziClinic for Nephrology and Rheumatology, UMG, Göttingen, Germany.
Kaomei GuanInstitute of Pharmacology and Toxicology, Technische Universität Dresden, Dresden, Germany.
Ali El-ArmoucheInstitute of Pharmacology and Toxicology, Technische Universität Dresden, Dresden, Germany. ali.el-armouche@tu-dresden.de.
Florian RichterFunctional Proteomics at the Faculty of Medicine, Goethe-Universität Frankfurt am Main, Frankfurt, Germany. f.richter@med.uni-frankfurt.de.
TU Dresden · DEGoethe University Frankfurt · DEUniversitätsmedizin Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heart failure is the most common cause of morbidity and hospitalization in the western civilization. Protein phosphatases play a key role in the basal cardiac contractility and in the responses to β-adrenergic stimulation with type-1 phosphatase (PP-1) being major contributor. We propose here that formation of transient disulfide bridges in PP-1α might play a leading role in oxidative stress response. First, we established an optimized workflow, the so-called "cross-over-read" search method, for the identification of disulfide-linked species using permutated databases. By applying this method, we demonstrate the formation of unexpected transient disulfides in PP-1α to shelter against over-oxidation. This protection mechanism strongly depends on the fast response in the presence of reduced glutathione. Our work points out that the dimerization of PP-1α involving Cys

Indexed as

AnimalsCatalytic DomainCysteineDimerizationDisulfidesElectron TransportGlutathioneMyocytes, CardiacOxidation-ReductionOxidative StressPhosphoric Monoester HydrolasesRatsCysteineDisulfidesGlutathionePhosphoric Monoester Hydrolases

Identifiers

PMID30531830
PMCPMC6286341
OpenAlexW2902052573

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.