Evidence map›Paper›PMID 28536193›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

The FERM protein EPB41L5 regulates actomyosin contractility and focal adhesion formation to maintain the kidney filtration barrier.

Christoph Schell, Manuel Rogg, Martina Suhm, Martin Helmstädter, Dominik Sellung, Mako Yasuda-Yamahara, Oliver Kretz, Victoria Küttner, Hani Suleiman, Laxmikanth Kollipara and 12 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

38 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. WNK1 Kinase Activity Is Required for the Functional Maintenance of Podocyte Structure.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  3. Article
  4. The Life of a Kidney Podocyte.Acta physiologica (Oxford, England) · 2025
    Review
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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

22 authors at 7 institutions in 5 countries.

Christoph SchellInstitute of Surgical Pathology, Medical Center - University of Freiburg, Faculty of Medicine, University of Freiburg, 79106 Freiburg, Germany; t.huber@uke.de christoph.schell@uniklinik-freiburg.de.
Manuel RoggDepartment of Medicine IV, Medical Center - University of Freiburg, Faculty of Medicine, University of Freiburg, 79106 Freiburg, Germany.
Martina SuhmDepartment of Medicine IV, Medical Center - University of Freiburg, Faculty of Medicine, University of Freiburg, 79106 Freiburg, Germany.
Martin HelmstädterDepartment of Medicine IV, Medical Center - University of Freiburg, Faculty of Medicine, University of Freiburg, 79106 Freiburg, Germany.
Dominik SellungDepartment of Medicine IV, Medical Center - University of Freiburg, Faculty of Medicine, University of Freiburg, 79106 Freiburg, Germany.
Mako Yasuda-YamaharaDepartment of Medicine IV, Medical Center - University of Freiburg, Faculty of Medicine, University of Freiburg, 79106 Freiburg, Germany.
Oliver KretzDepartment of Medicine IV, Medical Center - University of Freiburg, Faculty of Medicine, University of Freiburg, 79106 Freiburg, Germany.
Victoria KüttnerDepartment of Dermatology, Faculty of Medicine, Medical Center, University of Freiburg, 79106 Freiburg, Germany.
Hani SuleimanDepartment of Pathology, Washington University in St. Louis, MO 63130.
Laxmikanth KolliparaLeibniz-Institut für Analytische Wissenschaften - ISAS - e.V., 44139 Dortmund, Germany.
René P ZahediLeibniz-Institut für Analytische Wissenschaften - ISAS - e.V., 44139 Dortmund, Germany.
Albert SickmannLeibniz-Institut für Analytische Wissenschaften - ISAS - e.V., 44139 Dortmund, Germany.
Stefan EimerBIOSS Centre for Biological Signalling Studies, Albert-Ludwigs-University Freiburg, 79106 Freiburg, Germany.
Andrey S ShawDepartment of Pathology, Washington University in St. Louis, MO 63130.
Albrecht Kramer-ZuckerDepartment of Medicine IV, Medical Center - University of Freiburg, Faculty of Medicine, University of Freiburg, 79106 Freiburg, Germany.
Mariko Hirano-KobayashiLaboratory for Vertebrate Body Plan, Center for Developmental Biology, RIKEN Kobe, Kobe 650-0047, Japan.
Takaya AbeGenetic Engineering Team, RIKEN Center for Life Science Technologies, Kobe 650-0047, Japan.
Shinichi AizawaGenetic Engineering Team, RIKEN Center for Life Science Technologies, Kobe 650-0047, Japan.
Florian GrahammerDepartment of Medicine IV, Medical Center - University of Freiburg, Faculty of Medicine, University of Freiburg, 79106 Freiburg, Germany.
Björn HartlebenDepartment of Medicine IV, Medical Center - University of Freiburg, Faculty of Medicine, University of Freiburg, 79106 Freiburg, Germany.
Jörn DengjelBIOSS Centre for Biological Signalling Studies, Albert-Ludwigs-University Freiburg, 79106 Freiburg, Germany.
Tobias B HuberDepartment of Medicine IV, Medical Center - University of Freiburg, Faculty of Medicine, University of Freiburg, 79106 Freiburg, Germany; t.huber@uke.de christoph.schell@uniklinik-freiburg.de.
University of Freiburg · DELeibniz Institute for Analytical Sciences - ISAS · DEWashington University in St. Louis · USShiga University of Medical Science · JPUniversität Hamburg · DEUniversity Medical Center Freiburg · DEUniversity of Aberdeen · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Podocytes form the outer part of the glomerular filter, where they have to withstand enormous transcapillary filtration forces driving glomerular filtration. Detachment of podocytes from the glomerular basement membrane precedes most glomerular diseases. However, little is known about the regulation of podocyte adhesion in vivo. Thus, we systematically screened for podocyte-specific focal adhesome (FA) components, using genetic reporter models in combination with iTRAQ-based mass spectrometry. This approach led to the identification of FERM domain protein EPB41L5 as a highly enriched podocyte-specific FA component in vivo. Genetic deletion of

Indexed as

ActomyosinAnimalsCytoskeletal ProteinsFemaleFocal AdhesionsGene Knockout TechniquesGlomerulosclerosis, Focal SegmentalHumansMembrane ProteinsMiceMice, KnockoutNephrotic SyndromePodocytesPregnancyProteomicsRho Guanine Nucleotide Exchange FactorsActomyosinARHGEF18 protein, humanCytoskeletal ProteinsEPB41L5 protein, humanEPB41L5 protein, mouseMembrane ProteinsRho Guanine Nucleotide Exchange Factorsactomyosinfocal adhesionFSGSpodocyte

Identifiers

PMID28536193
PMCPMC5468651
OpenAlexW2618780560

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.