Evidence map›Paper›PMID 31753918›Full record

ArticleThe Journal of biological chemistry2019

Protein phosphatase 2A-mediated flotillin-1 dephosphorylation up-regulates endothelial cell migration and angiogenesis regulation.

Zsófia Thalwieser, Nikolett Király, Márton Fonódi, Csilla Csortos, Anita Boratkó

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. 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 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

13 citing papers in PubMed, 17 citations in OpenAlex.

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  12. Review
  13. Flotillins: At the Intersection of ProteinInternational journal of molecular sciences · 2020
    Review
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 1 institution in 1 country.

Zsófia ThalwieserDepartment of Medical Chemistry, Faculty of Medicine, University of Debrecen, Egyetem tér 1, 4032 Debrecen, Hungary.
Nikolett KirályDepartment of Medical Chemistry, Faculty of Medicine, University of Debrecen, Egyetem tér 1, 4032 Debrecen, Hungary.
Márton FonódiDepartment of Medical Chemistry, Faculty of Medicine, University of Debrecen, Egyetem tér 1, 4032 Debrecen, Hungary.
Csilla CsortosDepartment of Medical Chemistry, Faculty of Medicine, University of Debrecen, Egyetem tér 1, 4032 Debrecen, Hungary.
Anita BoratkóDepartment of Medical Chemistry, Faculty of Medicine, University of Debrecen, Egyetem tér 1, 4032 Debrecen, Hungary boratko@med.unideb.hu.
University of Debrecen · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Endothelial cells have key functions in endothelial barrier integrity and in responses to angiogenic signals that promote cell proliferation, cell migration, cytoskeletal reorganization, and formation of new blood vessels. These functions highly depend on protein-protein interactions in cell-cell junction and cell attachment complexes and on interactions with cytoskeletal proteins. Protein phosphatase 2A (PP2A) dephosphorylates several target proteins involved in cytoskeletal dynamics and cell adhesion. Our goal was to find new interacting and substrate proteins of the PP2A-B55α holoenzyme in bovine pulmonary endothelial cells. Using LC-MS/MS analysis, we identified flotillin-1 as a protein that binds recombinant GSH

Indexed as

Neovascularization, PhysiologicAnimalsCarbazolesCattleCell MovementCells, CulturedEndothelial CellsHoloenzymesMembrane ProteinsMutagenesis, Site-DirectedPhosphorylationProtein Interaction Domains and MotifsProtein Kinase CProtein Phosphatase 2Protein SubunitsRNA InterferenceCarbazolesflotillinsGo 6976HoloenzymesMembrane ProteinsProtein Kinase CProtein Phosphatase 2Protein SubunitsRNA, Small Interferingangiogenesiscell migrationendothelial cellphosphorylationprotein phosphatase 2 (PP2A)

Identifiers

PMID31753918
PMCPMC6937586
OpenAlexW2990584396

What OpenQuestion holds

Textmetadata
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.