Evidence map›Paper›PMID 22792268›Full record

ArticlePloS one2012

Functional study of mammalian Neph proteins in Drosophila melanogaster.

Martin Helmstädter, Kevin Lüthy, Markus Gödel, Matias Simons, Ashish, Deepak Nihalani, Stefan A Rensing, Karl-Friedrich Fischbach, Tobias B Huber

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

16 citing papers in PubMed, 33 citations in OpenAlex.

  1. The Life of a Kidney Podocyte.Acta physiologica (Oxford, England) · 2025
    Review
  2. Review
  3. Insights into human kidney function from the study of Drosophila.Pediatric nephrology (Berlin, Germany) · 2023
    Review
  4. Article
  5. Article
  6. Review
  7. MOLECULAR DESIGN OF THE KIDNEY FILTRATION BARRIER.Transactions of the American Clinical and Climatological Association · 2020
    Article
  8. Article
  9. Article
  10. Review
  11. Modeling Monogenic Human Nephrotic Syndrome in theJournal of the American Society of Nephrology : JASN · 2017
    Article
  12. Using theFrontiers in pediatrics · 2017
    Review
  13. Podocyte-actin dynamics in health and disease.Nature reviews. Nephrology · 2016
    Review
  14. Article
  15. Molecular understanding of the slit diaphragm.Pediatric nephrology (Berlin, Germany) · 2013
    Review
  16. 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

9 authors at 4 institutions in 3 countries.

Martin HelmstädterRenal Division, University Hospital Freiburg, Freiburg, Germany.
Kevin Lüthy
Markus Gödel
Matias Simons
Ashish
Deepak Nihalani
Stefan A Rensing
Karl-Friedrich Fischbach
Tobias B Huber
University of Freiburg · DEInstitute of Microbial Technology · INUniversity Medical Center Freiburg · DEUniversity of Pennsylvania · US

Funding

Myo1c Participates in Podocyte Junction Formation Through Interaction with Neph1R01DK087956 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI NIHALANI, DEEPAK · 2010 to 2018
$3.5M
NIDDK NIH HHS R01 DK087956
6 · The paper itself

Abstract

Neph molecules are highly conserved immunoglobulin superfamily proteins (IgSF) which are essential for multiple morphogenetic processes, including glomerular development in mammals and neuronal as well as nephrocyte development in D. melanogaster. While D. melanogaster expresses two Neph-like proteins (Kirre and IrreC/Rst), three Neph proteins (Neph1-3) are expressed in the mammalian system. However, although these molecules are highly abundant, their molecular functions are still poorly understood. Here we report on a fly system in which we overexpress and replace endogenous Neph homologs with mammalian Neph1-3 proteins to identify functional Neph protein networks required for neuronal and nephrocyte development. Misexpression of Neph1, but neither Neph2 nor Neph3, phenocopies the overexpression of endogenous Neph molecules suggesting a functional diversity of mammalian Neph family proteins. Moreover, structure-function analysis identified a conserved and specific Neph1 protein motif that appears to be required for the functional replacement of Kirre. Hereby, we establish D. melanogaster as a genetic system to specifically model molecular Neph1 functions in vivo and identify a conserved amino acid motif linking Neph1 to Drosophila Kirre function.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsCell Adhesion Molecules, NeuronalCell FusionConsensus SequenceDrosophila melanogasterDrosophila ProteinsEvolution, MolecularEye ProteinsGene ExpressionImmunoglobulinsLarvaMembrane ProteinsMiceMuscle ProteinsCell Adhesion Molecules, NeuronalDrosophila ProteinsEye ProteinsImmunoglobulinsKirrel1 protein, mouseKirrel3 protein, mousekirre protein, DrosophilaMembrane ProteinsMuscle ProteinsNeph3 protein, mouserst protein, Drosophila

Identifiers

PMID22792268
PMCPMC3391254
OpenAlexW2083746704

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.