Evidence map›Paper›PMID 18957374›Full record

ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2009

Review. Leaky Cl--HCO3- exchangers: cation fluxes via modified AE1.

J C Ellory, H Guizouarn, F Borgese, L J Bruce, R J Wilkins, G W Stewart

Open access · greenAbstract readReview
In one paragraph

Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2009. 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
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

11 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Observational
  3. Ion Transport in Eryptosis, the Suicidal Death of Erythrocytes.Frontiers in cell and developmental biology · 2020
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Introduction. The blurred boundary between channels and transporters.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2009
    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

6 authors at 4 institutions in 2 countries.

J C ElloryDepartment of Physiology, Anatomy and Genetics, University of Oxford, Oxford, UK. clive.ellory@dpag.ox.ac.uk
H Guizouarn
F Borgese
L J Bruce
R J Wilkins
G W Stewart
Centre National de la Recherche Scientifique · FRUniversity of Oxford · GBBristol Institute for Transfusion Sciences · GBUniversity College London · GB

Funding

Medical Research Council G0700759
6 · The paper itself

Abstract

The abundant membrane protein AE1 normally functions as an obligate anion exchanger, with classical carrier properties, in human red blood cells. Recently, four single point mutations of hAE1 have been identified that have lost the anion exchange function, and act as non-selective monovalent cation channels, as shown in both red cell flux and oocyte expression studies. The red cell transport function shows a paradoxical temperature dependence, and is associated with spherocytic and stomatocytic red cell defects, and haemolytic anaemias. Other forms of AE1, including the native AE1 in trout red cells, and the human mutation R760Q show both channel-like and anion exchange properties. The present results point to membrane domains 9 and 10 being important in the functional modification of AE1 activity.

Indexed as

Anion Exchange Protein 1, ErythrocyteCationsMutationProtein ConformationAnion Exchange Protein 1, ErythrocyteCations

Identifiers

PMID18957374
PMCPMC2674097
OpenAlexW2143778937

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.