Evidence map›Paper›PMID 24515290›Full record

ReviewPflugers Archiv : European journal of physiology2014

NBCe1 as a model carrier for understanding the structure-function properties of Na⁺ -coupled SLC4 transporters in health and disease.

Ira Kurtz

Open access · greenAbstract readReview
In one paragraph

Review in Pflugers Archiv : European journal of physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

23 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Potential Theranostic Roles of SLC4 Molecules in Human Diseases.International journal of molecular sciences · 2023
    Review
  7. Article
  8. Understanding the Physiological Role of Electroneutral NaPharmaceuticals (Basel, Switzerland) · 2022
    Review
  9. Article
  10. Article
  11. Review
  12. Bicarbonate ion transport by the electrogenic NaNeurogastroenterology and motility · 2021
    Article
  13. Article
  14. Review
  15. Article
  16. Expression of the B splice variant of NBCe1 (SLC4A4) in the mouse kidney.American journal of physiology. Renal physiology · 2018
    Article
  17. Renal Tubular Acidosis: HAdvances in chronic kidney disease · 2018
    Review
  18. Article
  19. NaWorld journal of gastroenterology · 2016
    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

1 author at 1 institution in 1 country.

Ira KurtzDivision of Nephrology, David Geffen School of Medicine, and Brain Research Institute, UCLA, Los Angeles, CA, USA, ikurtz@mednet.ucla.edu.
UCLA Health · US

Funding

The Biology of NBCe1 in Health and DiseaseR01DK077162 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI IRA KURTZ · 2007 to 2026
$6.7M
BIOLOGY OF SODIUM BICARBONATE TRANSPORTR01DK058563 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KURTZ, IRA · 2001 to 2011
$3.1M
NIDDK NIH HHS DK058563NIDDK NIH HHS DK077162NIDDK NIH HHS R01 DK058563NIDDK NIH HHS R01 DK077162
6 · The paper itself

Abstract

SLC4 transporters are membrane proteins that in general mediate the coupled transport of bicarbonate (carbonate) and share amino acid sequence homology. These proteins differ as to whether they also transport Na(+) and/or Cl(-), in addition to their charge transport stoichiometry, membrane targeting, substrate affinities, developmental expression, regulatory motifs, and protein-protein interactions. These differences account in part for the fact that functionally, SLC4 transporters have various physiological roles in mammals including transepithelial bicarbonate transport, intracellular pH regulation, transport of Na(+) and/or Cl(-), and possibly water. Bicarbonate transport is not unique to the SLC4 family since the structurally unrelated SLC26 family has at least three proteins that mediate anion exchange. The present review focuses on the first of the sodium-dependent SLC4 transporters that was identified whose structure has been most extensively studied: the electrogenic Na(+)-base cotransporter NBCe1. Mutations in NBCe1 cause proximal renal tubular acidosis (pRTA) with neurologic and ophthalmologic extrarenal manifestations. Recent studies have characterized the important structure-function properties of the transporter and how they are perturbed as a result of mutations that cause pRTA. It has become increasingly apparent that the structure of NBCe1 differs in several key features from the SLC4 Cl(-)-HCO3 (-) exchanger AE1 whose structural properties have been well-studied. In this review, the structure-function properties and regulation of NBCe1 will be highlighted, and its role in health and disease will be reviewed in detail.

Indexed as

Acidosis, Renal TubularAnimalsBiological TransportChloride-Bicarbonate AntiportersHumansMembrane Transport ProteinsSLC4A ProteinsSodium-Bicarbonate SymportersStructure-Activity RelationshipChloride-Bicarbonate AntiportersMembrane Transport ProteinsSLC4A ProteinsSodium-Bicarbonate Symporters

Identifiers

PMID24515290
PMCPMC4096079
OpenAlexW2031187658

What OpenQuestion holds

Textmetadata
LicenceTDM
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.