Evidence map›Paper›PMID 31035605›Full record

ArticleInternational journal of molecular sciences2019

Dynamics of Dual Specificity Phosphatases and Their Interplay with Protein Kinases in Immune Signaling.

Yashwanth Subbannayya, Sneha M Pinto, Korbinian Bösl, T S Keshava Prasad, Richard K Kandasamy

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

27 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. LRRK2NPJ Parkinson's disease · 2026
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  3. Resident CD49aScience advances · 2026
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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

5 authors at 3 institutions in 2 countries.

Yashwanth SubbannayyaCentre of Molecular Inflammation Research (CEMIR), Department of Clinical and Molecular Medicine (IKOM), Norwegian University of Science and Technology, N-7491 Trondheim, Norway. yashwanth.subbannayya@ntnu.no.ORCID 0000-0002-3885-3514
Sneha M PintoCentre of Molecular Inflammation Research (CEMIR), Department of Clinical and Molecular Medicine (IKOM), Norwegian University of Science and Technology, N-7491 Trondheim, Norway. sneha.pinto@ntnu.no.
Korbinian BöslCentre of Molecular Inflammation Research (CEMIR), Department of Clinical and Molecular Medicine (IKOM), Norwegian University of Science and Technology, N-7491 Trondheim, Norway. korbinian.bosl@ntnu.no.ORCID 0000-0003-0498-4273
T S Keshava PrasadCenter for Systems Biology and Molecular Medicine, Yenepoya (Deemed to be University), Mangalore 575018, India. keshav@yenepoya.edu.in.ORCID 0000-0002-6206-2384
Richard K KandasamyCentre of Molecular Inflammation Research (CEMIR), Department of Clinical and Molecular Medicine (IKOM), Norwegian University of Science and Technology, N-7491 Trondheim, Norway. richard.k.kandasamy@ntnu.no.ORCID 0000-0002-0894-1222
Yenepoya University · INNorwegian University of Science and Technology · NOOslo University Hospital · NO

Funding

Research Council of Norway 223255/F50Research Council of Norway 263168
6 · The paper itself

Abstract

Dual specificity phosphatases (DUSPs) have a well-known role as regulators of the immune response through the modulation of mitogen-activated protein kinases (MAPKs). Yet the precise interplay between the various members of the DUSP family with protein kinases is not well understood. Recent multi-omics studies characterizing the transcriptomes and proteomes of immune cells have provided snapshots of molecular mechanisms underlying innate immune response in unprecedented detail. In this study, we focus on deciphering the interplay between members of the DUSP family with protein kinases in immune cells using publicly available omics datasets. Our analysis resulted in the identification of potential DUSP-mediated hub proteins including MAPK7, MAPK8, AURKA, and IGF1R. Furthermore, we analyzed the association of DUSP expression with TLR4 signaling and identified VEGF, FGFR, and SCF-KIT pathway modules to be regulated by the activation of TLR4 signaling. Finally, we identified several important kinases including LRRK2, MAPK8, and cyclin-dependent kinases as potential DUSP-mediated hubs in TLR4 signaling. The findings from this study have the potential to aid in the understanding of DUSP signaling in the context of innate immunity. Further, this will promote the development of therapeutic modalities for disorders with aberrant DUSP signaling.

Indexed as

ImmunomodulationSignal TransductionAnimalsBiological EvolutionBlood CellsDual-Specificity PhosphatasesHumansImmune SystemLymphoid TissueMiceProtein Interaction MappingProtein Interaction MapsProtein KinasesProteomeProteomicsDual-Specificity PhosphatasesProtein KinasesProteomehematopoietic cellsintegrated omics analysisTLR signaling

Identifiers

PMID31035605
PMCPMC6539644
OpenAlexW2951592889

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.