Evidence map›Paper›PMID 21470201›Full record

ReviewBritish journal of pharmacology2012

Behind the curtain: cellular mechanisms for allosteric modulation of calcium-sensing receptors.

Alice Cavanaugh, Ying Huang, Gerda E Breitwieser

Open access · bronzeAbstract readReview
In one paragraph

Review in British journal of pharmacology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

13 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Pharmacology of the calcium sensing receptor.Clinical cases in mineral and bone metabolism : the official journal of the Italian Society of Osteoporosis, Mineral Metabolism, and Skeletal Diseases · 2013
    Review
  10. Article
  11. Review
  12. Themed section: molecular pharmacology of GPCRs.British journal of pharmacology · 2012
    Article
  13. The role of allostery in the ubiquitin-proteasome system.Critical reviews in biochemistry and molecular biology
    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 2 institutions in 2 countries.

Alice CavanaughWeis Center for Research, Geisinger Clinic, Danville, PA, USACancer Drug Research Laboratory, McGill University/Royal Victoria Hospital, Montreal, QC, Canada.
Ying HuangWeis Center for Research, Geisinger Clinic, Danville, PA, USACancer Drug Research Laboratory, McGill University/Royal Victoria Hospital, Montreal, QC, Canada.
Gerda E BreitwieserWeis Center for Research, Geisinger Clinic, Danville, PA, USACancer Drug Research Laboratory, McGill University/Royal Victoria Hospital, Montreal, QC, Canada.
Geisinger Medical Center · USRoyal Victoria Hospital · CA

Funding

Calcium sensing receptor and scaffoldsR01GM077563 · NIGMS · GEISINGER CLINIC · PI BREITWIESER, GERDA E · 2006 to 2009
$1.2M
MOLECULAR DETERMINANTS OF CALCIUM RECEPTOR FUNCTIONR01GM058578 · NIGMS · SYRACUSE UNIVERSITY · PI BREITWIESER, GERDA E · 1999 to 2002
$951k
NIGMS NIH HHS GM77563NIGMS NIH HHS R01 GM058578NIGMS NIH HHS R01 GM077563NIGMS NIH HHS R01 GM58578
6 · The paper itself

Abstract

Calcium-sensing receptors (CaSR) are integral to regulation of systemic Ca(2+) homeostasis. Altered expression levels or mutations in CaSR cause Ca(2+) handling diseases. CaSR is regulated by both endogenous allosteric modulators and allosteric drugs, including the first Food and Drug Administration-approved allosteric agonist, Cinacalcet HCl (Sensipar®). Recent studies suggest that allosteric modulators not only alter function of plasma membrane-localized CaSR, but regulate CaSR stability at the endoplasmic reticulum. This brief review summarizes our current understanding of the role of membrane-permeant allosteric agonists in cotranslational stabilization of CaSR, and highlights additional, indirect, signalling-dependent role(s) for membrane-impermeant allosteric drugs. Overall, these studies suggest that allosteric drugs act at multiple cellular organelles to control receptor abundance and hence function, and that drug hydrophobicity can bias the relative contributions of plasma membrane and intracellular organelles to CaSR abundance and signalling.

Indexed as

AnimalsBinding SitesCell MembraneDrug DesignHumansReceptors, Calcium-SensingSignal TransductionReceptors, Calcium-Sensing

Identifiers

PMID21470201
PMCPMC3372821
OpenAlexW1581940992

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.