Evidence map›Paper›PMID 25631710›Full record

ReviewMolecular neurobiology2016

P2C-Type ATPases and Their Regulation.

Rocío Retamales-Ortega, Carlos P Vio, Nibaldo C Inestrosa

Open access · greenAbstract readReview
PubMed Publisher
In one paragraph

Review in Molecular neurobiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.5field-weighted citation impact, top 34% 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

7 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
  2. Influence of Anticholinesterase Drugs on Activity and Properties of NaBulletin of experimental biology and medicine · 2024
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
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.

Rocío Retamales-OrtegaCentro de Envejecimiento y Regeneración (CARE), Departamento de Biología Celular y Molecular, Santiago, Chile.
Carlos P VioCentro de Envejecimiento y Regeneración (CARE), Departamento de Biología Celular y Molecular, Santiago, Chile.
Nibaldo C InestrosaCentro de Envejecimiento y Regeneración (CARE), Departamento de Biología Celular y Molecular, Santiago, Chile. ninestrosa@bio.puc.cl.
Universidad de Magallanes · CL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

P2C-type ATPases are a subfamily of P-type ATPases comprising Na(+)/K(+)-ATPase and H(+)/K(+)-ATPase. Na(+)/K(+)-ATPase is ubiquitously expressed and has been implicated in several neurological diseases, whereas H(+)/K(+)-ATPase is found principally in the colon, stomach, and kidney. Both ATPases have two subunits, α and β, but Na(+)/K(+)-ATPase also has a regulatory subunit called FXYD, which has an important role in cancer. The most important functions of these ATPases are homeostasis, potassium regulation, and maintaining a gradient in different cell types, like epithelial cells. Na(+)/K(+)-ATPase has become a center of attention ever since it was proposed that it might play a crucial role in neurological disorders such as bipolar disorder, mania, depression, familial hemiplegic migraine, rapid-onset dystonia parkinsonism, chronic stress, epileptogenesis, and Alzheimer's disease. On the other hand, it has been reported that lithium could have a neuroprotective effect against ouabain, which is the best known Na(+)/K(+)-ATPase inhibitor, but and high concentrations of lithium could affect negatively H(+)/K(+)-ATPase activity, that has a key role in regulating acidosis and potassium deficiencies. Finally, potassium homeostasis regulation is composed of two main mechanisms, extrarenal and renal. Extrarenal mechanism controls plasma levels, shifting potassium from the extracellular to the intracellular, whereas renal mechanism concerns with body balance and is influenced by potassium intake and its urinary excretion. In this article, we discuss the functions, isoforms, and localization of P2C-type ATPases, describe some of their modulators, and discuss their implications in some diseases.

Indexed as

Adenosine TriphosphatasesAnimalsDiseaseHealthHumansIsoenzymesModels, BiologicalPotassium, DietaryAdenosine TriphosphatasesIsoenzymesPotassium, DietaryAlzheimer’s diseaseH+/K+-ATPaseHypertensionNa+/K+-ATPasePotassium

Identifiers

PMID25631710
OpenAlexW1992095164

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.