Evidence map›Paper›PMID 25680790›Full record

ReviewCellular and molecular life sciences : CMLS2015

Na+-H+ exchanger-1 (NHE1) regulation in kidney proximal tubule.

Mark D Parker, Evan J Myers, Jeffrey R Schelling

Abstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2015. 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
1.5field-weighted citation impact, top 18% 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, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. NaPharmaceuticals (Basel, Switzerland) · 2022
    Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Contribution of NHE3 and dietary phosphate to lithium pharmacokinetics.European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences · 2019
    Article
  13. Review
  14. AMP-Activated Protein Kinase (AMPK)-Dependent Regulation of Renal Transport.International journal of molecular sciences · 2018
    Review
  15. Article
  16. 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 2 institutions in 1 country.

Mark D ParkerDepartment of Physiology and Biophysics, University at Buffalo: The State University of New York, Buffalo, NY, 14214, USA.
Evan J Myers
Jeffrey R Schelling
University at Buffalo, State University of New York · USMetroHealth · US

Funding

Mechanisms of tubular atrophy in renal diseaseR01DK067528 · NIDDK · CASE WESTERN RESERVE UNIVERSITY · PI SCHELLING, JEFFREY R · 2005 to 2025
$7.1M
NIDDK NIH HHS R01 DK067528
6 · The paper itself

Abstract

The ubiquitously expressed plasma membrane Na(+)-H(+) exchanger NHE1 is a 12 transmembrane-spanning protein that directs important cell functions such as homeostatic intracellular volume and pH control. The 315 amino acid cytosolic tail of NHE1 binds plasma membrane phospholipids and multiple proteins that regulate additional, ion-translocation independent functions. This review focuses on NHE1 structure/function relationships, as well as the role of NHE1 in kidney proximal tubule functions, including pH regulation, vectorial Na(+) transport, cell volume control and cell survival. The implications of these functions are particularly critical in the setting of progressive, albuminuric kidney diseases, where the accumulation of reabsorbed fatty acids leads to disruption of NHE1-membrane phospholipid interactions and tubular atrophy, which is a poor prognostic factor for progression to end stage renal disease. This review amplifies the vital role of the proximal tubule NHE1 Na(+)-H(+) exchanger as a kidney cell survival factor.

Indexed as

Acute Kidney InjuryAmino Acid SequenceAnimalsCation Transport ProteinsCell MembraneCell SurvivalHumansIon TransportKidney Failure, ChronicKidney Tubules, ProximalMembrane ProteinsMiceModels, AnimalProtein BindingProtein Structure, TertiarySodium-Hydrogen Exchanger 1Cation Transport ProteinsMembrane ProteinsSLC9A1 protein, humanSodium-Hydrogen Exchanger 1Sodium-Hydrogen Exchangers

Identifiers

PMID25680790
PMCPMC4993044
OpenAlexW2078098315

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.