Evidence map›Paper›PMID 25893721›Full record

ArticleBiomolecules2015

PTPIP51—A New RelA-tionship with the NFκB Signaling Pathway.

Alexander Brobeil, Fabian Kämmerer, Claudia Tag, Klaus Steger, Stefan Gattenlöhner, Monika Wimmer

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

9 citing papers in PubMed, 10 citations in OpenAlex.

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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

6 authors at 1 institution in 1 country.

Alexander BrobeilInstitute of Anatomy and Cell Biology, Justus-Liebig-University, Gießen 35392, Germany. alexander.brobeil@patho.med.uni-giessen.de.
Fabian KämmererInstitute of Anatomy and Cell Biology, Justus-Liebig-University, Gießen 35392, Germany. fabian.kaemmerer@med.uni-giessen.de.
Claudia TagInstitute of Anatomy and Cell Biology, Justus-Liebig-University, Gießen 35392, Germany. claudia.tag@anatomie.med.uni-giessen.de.
Klaus StegerDepartment of Urology and Pediatric Urology, Justus-Liebig-University, Gießen 35392, Germany. klaus.steger@chiru.med.uni-giessen.de.
Stefan GattenlöhnerInstitute of Pathology, Justus-Liebig-University, Gießen 35392, Germany. stefan.gattenloehner@patho.med.uni-giessen.de.
Monika WimmerInstitute of Anatomy and Cell Biology, Justus-Liebig-University, Gießen 35392, Germany. monika.wimmer@anatomie.med.uni-giessen.de.
University of Giessen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The present study shows a new connection of protein tyrosine phosphatase interacting protein 51 (PTPIP51) to the nuclear factor κB (NFκB) signalling pathway. PTPIP51 mRNA and protein expression is regulated by RelA. If bound to the PTPIP51 promoter, RelA repress the mRNA and protein expression of PTPIP51. The parallel treatment with pyrrolidine dithiocarbamate (PDTC) reversed the suppression of PTPIP51 protein expression induced by TNFα. Using the intensity correlation analysis PTPIP51 verified a co-localization with RelA, which is also regulated by TNFα administration. Moreover, the direct interaction of PTPIP51 and RelA was established using the DuoLink proximity ligation assay. IκBα, the known inhibitor of RelA, also interacted with PTPIP51. This hints to the fact that in un-stimulated conditions PTPIP51 forms a complex with RelA and IκBα. The PTPIP51/RelA/IκBα complex is modulated by TNFα. Interestingly, the impact on the mitogen activated protein kinase pathway was negligible except in highest TNFα concentration. Here, PTPIP51 and Raf-1 interactions were slightly repressed. The newly established relationship of PTPIP51 and the NFκB signaling pathway provides the basis for a possible therapeutic impact.

Indexed as

MAP Kinase Signaling SystemCell LineHumansKeratinocytesMitochondrial ProteinsProtein BindingProtein Tyrosine PhosphatasesPyrrolidinesThiocarbamatesTranscription Factor RelATumor Necrosis Factor-alphaMitochondrial ProteinsProtein Tyrosine Phosphatasespyrrolidine dithiocarbamic acidPyrrolidinesRMDN3 protein, humanThiocarbamatesTranscription Factor RelATumor Necrosis Factor-alpha

Identifiers

PMID25893721
PMCPMC4496682
OpenAlexW1981799337

What OpenQuestion holds

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LicenceCC BY
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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.