Evidence map›Paper›PMID 21327781›Full record

ReviewPflugers Archiv : European journal of physiology2011

Mechanisms of cell polarity and aquaporin sorting in the nephron.

Bayram Edemir, Hermann Pavenstädt, Eberhard Schlatter, Thomas Weide

Abstract readReview
PubMed Publisher
In one paragraph

Review in Pflugers Archiv : European journal of physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

  1. Unveiling the Potential of Three EndemicAntioxidants (Basel, Switzerland) · 2025
    Article
  2. Article
  3. Expression Regulation and Trafficking of Aquaporins.Advances in experimental medicine and biology · 2023
    Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. 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

4 authors at 2 institutions in 1 country.

Bayram EdemirMedizinische Klinik und Poliklinik D, Experimentelle und Molekulare Nephrologie, Universität Münster, Germany. edemir@uni-muenster.de
Hermann Pavenstädt
Eberhard Schlatter
Thomas Weide
University of Münster · DEKlinik und Poliklinik für Psychosomatik und Psychotherapie · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The kidneys participate in whole-body homeostasis, regulating acid-base balance, electrolyte concentrations, extracellular fluid volume, and regulation of blood pressure. Many of the kidney's functions are accomplished by relatively simple mechanisms of filtration, reabsorption, and secretion, which take place in the nephron. The kidneys generate 140-180 l of primary urine per day, while reabsorbing a large percentage, allowing for only the excretion of approximately 2 l of urine. Within the nephron, the majority of the filtered water and solutes are reabsorbed. This is mainly facilitated by specialized transporters and channels which are localized at different segments of the nephron and asymmetrically localized within the polarized epithelial cells. The asymmetric localization of these transporters and channels is essential for the physiological tasks of the renal tissues. One family of these proteins are the water-permeable aquaporins which are selectively expressed in cells along the nephron and localized at different compartments. Here, we discuss potential molecular links between mechanisms involved in the establishment of cell polarity and the members of the aquaporin family. In the first part of this review, we will focus on aspects of apical cell polarity. In the second part, we will review the motifs identified so far that are involved in aquaporin sorting and point out potential molecular links.

Indexed as

AnimalsAquaporinsCell PolarityEpithelial CellsEye ProteinsHumansMembrane ProteinsNephronsNerve Tissue ProteinsNucleoside-Phosphate KinaseTight Junction ProteinsAquaporinsCRB1 protein, humanEye ProteinsMembrane ProteinsMPP5 protein, humanNerve Tissue ProteinsNucleoside-Phosphate KinasePATJ protein, humanTight Junction Proteins

Identifiers

PMID21327781
OpenAlexW2042124408

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.