Evidence map›Paper›PMID 23958189›Full record

ReviewJournal of pharmacy & pharmaceutical sciences : a publication of the Canadian Society for Pharmaceutical Sciences, Societe canadienne des sciences pharmaceutiques2013

Plasma membrane calcium ATPases as novel candidates for therapeutic agent development.

Emanuel E Strehler

Open access · diamondAbstract readReview
In one paragraph

Review in Journal of pharmacy & pharmaceutical sciences : a publication of the Canadian Society for Pharmaceutical Sciences, Societe canadienne des sciences pharmaceutiques, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

26 citing papers in PubMed, 48 citations in OpenAlex.

  1. Review
  2. Review
  3. Analysis of cholesterol-recognition motifs of the plasma membrane CaJournal of bioenergetics and biomembranes · 2024
    Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Crosstalk among Calcium ATPases: PMCA, SERCA and SPCA in Mental Diseases.International journal of molecular sciences · 2021
    Review
  9. Article
  10. Calcium Metabolism and Breast Cancer: Echoes of Lactation?Current opinion in endocrine and metabolic research · 2020
    Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Resveratrol inhibits plasma membrane CaBiochemistry and biophysics reports · 2016
    Article
  20. PMCA2 regulates HER2 protein kinase localization and signaling and promotes HER2-mediated breast cancer.Proceedings of the National Academy of Sciences of the United States of America · 2016
    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.

Emanuel E StrehlerDepartment of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, Rochester, MN, USA. strehler.emanuel@mayo.edu
Mayo Clinic in Arizona · US

Funding

PURIFICATION AND PROPERTIES OF CA2+ PUMPING ATPASER01GM028835 · NIGMS · MAYO CLINIC ROCHESTER · PI STREHLER, EMANUEL ERNST · 1986 to 2006
$1.8M
Membrane Targeting of Calcium-Pumping ATPaseR01NS051769 · NINDS · MAYO CLINIC ROCHESTER · PI STREHLER, EMANUEL ERNST · 2007 to 2010
$1.4M
NIGMS NIH HHS R01 GM028835NIGMS NIH HHS R01 GM28835NINDS NIH HHS R01 NS051769NINDS NIH HHS R01 NS51769
6 · The paper itself

Abstract

Plasma membrane Ca2+ ATPases (PMCAs) are highly regulated transporters responsible for Ca2+ extrusion from all eukaryotic cells. Different PMCA isoforms are implicated in various tasks of Ca2+ regulation including bulk Ca2+ transport and localized Ca2+ signaling in specific membrane microdomains. Accumulating evidence shows that loss, mutation or inappropriate expression of different PMCAs is associated with pathologies ranging from hypertension, low bone density and male infertility to hearing loss and cerebellar ataxia. Compared to Ca2+ influx channels, PMCAs have lagged far behind as targets for drug development, mainly due to the lack of detailed understanding of their structure and specific function. This is rapidly changing thanks to integrated efforts combining biochemical, structural, cellular and physiological studies suggesting that selective modulation of PMCA isoforms may be of therapeutic value in the management of different and complex diseases. Both structurally informed rational design and high-throughput small molecule library screenings are promising strategies that are expected to lead to specific and isoform-selective modulators of PMCA function. This short review will provide an overview of the diverse roles played by PMCA isoforms in different cells and tissues and their emerging involvement in pathophysiological processes, summarize recent progress in obtaining structural information on the PMCAs, and discuss current and future strategies to develop specific PMCA inhibitors and activators for potential therapeutic applications.

Indexed as

AnimalsDiseaseDrug DesignEnzyme InhibitorsHumansIsoenzymesPlasma Membrane Calcium-Transporting ATPasesEnzyme InhibitorsIsoenzymesPlasma Membrane Calcium-Transporting ATPases

Identifiers

PMID23958189
PMCPMC3869240
OpenAlexW1606206403

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.