Evidence map›Paper›PMID 12221118›Full record

ArticleMolecular biology of the cell2002

Inversin forms a complex with catenins and N-cadherin in polarized epithelial cells.

Jens Nürnberger, Robert L Bacallao, Carrie L Phillips

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

34 citing papers in PubMed, 107 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Nephronophthisis: a pathological and genetic perspective.Pediatric nephrology (Berlin, Germany) · 2024
    Review
  5. Review
  6. Inactivation ofeLife · 2023
    Article
  7. Review
  8. Article
  9. Renal Ciliopathies: Sorting Out Therapeutic Approaches for Nephronophthisis.Frontiers in cell and developmental biology · 2021
    Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Inversin modulates the cortical actin network during mitosis.American journal of physiology. Cell physiology · 2013
    Article
  15. Current insights into renal ciliopathies: what can genetics teach us?Pediatric nephrology (Berlin, Germany) · 2013
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

3 authors at 1 institution in 1 country.

Jens NürnbergerIndiana University School of Medicine Department of Medicine, Division of Nephrology, Indianapolis 46202-5116, USA.
Robert L Bacallao
Carrie L Phillips
Indiana University School of Medicine

Funding

Pathologic Mechanisms of Polycystic Kidney DiseaseR01DK050141 · NIDDK · UNIVERSITY OF NEW MEXICO · PI WANDINGER-NESS, ANGELA · 1995 to 2010
$2.7M
CYSTIC DILATATION OF NEPHRONS IN TRANSGENIC INV MICEK08DK002785 · NIDDK · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI PHILLIPS, CARRIE L · 2001 to 2005
$634k
NIDDK NIH HHS K08 DK002785NIDDK NIH HHS R01 DK050141NIDDK NIH HHS R01 DK50141
6 · The paper itself

Abstract

Nephrogenesis starts with the reciprocal induction of two embryonically distinct analages, metanephric mesenchyme and ureteric bud. This complex process requires the refined and coordinated expression of numerous developmental genes, such as inv. Mice that are homozygous for a mutation in the inv gene (inv/inv) develop renal cysts resembling autosomal-recessive polycystic kidney disease. The gene locus containing inv has been proposed to serve as a common modifier for some human and rodent polycystic kidney disease phenotypes. We generated polyclonal antibodies to inversin to study its subcellular distribution, potential binding partners, and functional aspects in cultured murine proximal tubule cells. A 125-kDa inversin protein isoform was found at cell-cell junctions. Two inversin isoforms, 140- and 90-kDa, were identified in the nuclear and perinuclear compartments. Plasma membrane allocation of inversin is dependent upon cell-cell contacts and was redistributed when cell adhesion was disrupted after incubation of the cell monolayer with low-calcium/EGTA medium. We further show that the membrane-associated 125-kDa inversin forms a complex with N-cadherin and the catenins. The 90-kDa nuclear inversin complexes with beta-catenin. These findings indicate that the inv gene product functions in several cellular compartments, including the nucleus and cell-cell adhesion sites.

Indexed as

Transcription FactorsAnimalsbeta CateninBody PatterningCadherinsCalciumCell AdhesionCell MembraneCell NucleusCells, CulturedCytoskeletal ProteinsElectrophoresis, Polyacrylamide GelEpithelial CellsHomozygoteImmunoblottingImmunohistochemistrybeta CateninCadherinsCalciumCTNNB1 protein, mouseCytoskeletal ProteinsINVS protein, humanInvs protein, mouseiodixanolProtein IsoformsProteinsTrans-ActivatorsTranscription FactorsTriiodobenzoic Acids

Identifiers

PMID12221118
PMCPMC124145
OpenAlexW2165273480

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.