Evidence map›Paper›PMID 17979874›Full record

ReviewJournal of cellular and molecular medicine

The calcium-sensing receptor and its interacting proteins.

Chunfa Huang, R Tyler Miller

Open access · bronzeAbstract readReview
In one paragraph

Review in Journal of cellular and molecular medicine. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

27 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Molecular regulation of calcium-sensing receptor (CaSR)-mediated signaling.Chronic diseases and translational medicine · 2024
    Review
  3. Review
  4. High Salt Upregulates CaThe Journal of pharmacology and experimental therapeutics · 2022
    Article
  5. Review
  6. Article
  7. Review
  8. Pathogenic role of calcium-sensing receptors in the development and progression of pulmonary hypertension.American journal of physiology. Lung cellular and molecular physiology · 2016
    Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Sleeping parathyroid tumor: rapid hyperfunction after removal of the dominant tumor.The Journal of clinical endocrinology and metabolism · 2012
    Article
  19. 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

2 authors at 2 institutions in 1 country.

Chunfa HuangDepartment of Medicine and Physiology, Case-Western Reserve University, Louis Stokes VAMC Rammelkamp Center for Research, Metro Health Medical Center, Cleveland, Ohio, USA.
R Tyler Miller
Louis Stokes Cleveland VA Medical Center · USMetroHealth Medical Center · US

Funding

Signaling Complexes in Renal Epithelial CellsR01DK059985 · NIDDK · CASE WESTERN RESERVE UNIVERSITY · PI MILLER, RICHARD TYLER · 2002 to 2005
$908k
NIDDK NIH HHS DK-59985NIDDK NIH HHS R01 DK059985
6 · The paper itself

Abstract

Seven membrane-spanning, or G protein-coupled receptors were originally thought to act through het-erotrimeric G proteins that in turn activate intracellular enzymes or ion channels, creating relatively simple, linear signalling pathways. Although this basic model remains true in that this family does act via a relatively small number of G proteins, these signalling systems are considerably more complex because the receptors interact with or are located near additional proteins that are often unique to a receptor or subset of receptors. These additional proteins give receptors their unique signalling personalities. The extracellular Ca-sensing receptor (CaR) signals via Galpha(i), Galpha(q) and Galpha(12/13), but its effects in vivo demonstrate that the signalling pathways controlled by these subunits are not sufficient to explain all its biologic effects. Additional structural or signalling proteins that interact with the CaR may explain its behaviour more fully. Although the CaR is less well studied in this respect than other receptors, several CaR-interacting proteins such as filamin, a potential scaffolding protein, receptor activity modifying proteins (RAMPs) and potassium channels may contribute to the unique characteristics of the CaR. The CaR also appears to interact with additional proteins common to other G protein-coupled receptors such as arrestins, G protein receptor kinases, protein kinase C, caveolin and proteins in the ubiquitination pathway. These proteins probably represent a few initial members of CaR-based signalling complex. These and other proteins may not all be associated with the CaR in all tissues, but they form the basis for understanding the complete nature of CaR signalling.

Indexed as

AnimalsContractile ProteinsFilaminsHumansIntracellular Signaling Peptides and ProteinsMembrane ProteinsMicrofilament ProteinsPotassium ChannelsProtein BindingReceptor Activity-Modifying ProteinsReceptors, Calcium-SensingSignal TransductionContractile ProteinsFilaminsIntracellular Signaling Peptides and ProteinsMembrane ProteinsMicrofilament ProteinsPotassium ChannelsReceptor Activity-Modifying ProteinsReceptors, Calcium-Sensing

Identifiers

PMID17979874
PMCPMC4401264
OpenAlexW2023517521

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.