Evidence map›Paper›PMID 24661201›Full record

ReviewEndocrine reviews2014

Chaperoning G protein-coupled receptors: from cell biology to therapeutics.

Ya-Xiong Tao, P Michael Conn

Open access · bronzeAbstract readReview
In one paragraph

Review in Endocrine reviews, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

67 citing papers in PubMed, 143 citations in OpenAlex.

  1. Glycemic and bodyweight effects ofScience advances · 2026
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  7. Atropine Eye Drops in Childhood Myopia Control: A Review.International journal of medical sciences · 2026
    Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Molecular Determinants of TMC Protein Biogenesis and Trafficking.International journal of molecular sciences · 2025
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Article

7 more citing papers are in PubMed but not listed here.

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.

Ya-Xiong TaoDepartment of Anatomy, Physiology, and Pharmacology (Y.-X.T.), College of Veterinary Medicine, Auburn University, Auburn, Alabama 36849-5519; and Departments of Internal Medicine and Cell Biology (P.M.C.), Texas Tech University Health Science Center, Lubbock, Texas 79430-6252.
P Michael Conn
Auburn University · USTexas Tech University Health Sciences Center · US

Funding

High Throughput Screening for Pharmacoperones of the V2 ReceptorR01DK099090 · NIDDK · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI JANOVICK, JO ANN, SCAMPAVIA, LOUIS DANIEL · 2013 to 2015
$1.7M
High Throughput Screening Assay Development for PharmacoperonesR01DK085040 · NIDDK · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI CONN, P. MICHAEL · 2010 to 2012
$1.1M
Molecular mechanism of G protein coupling to the melanocortin-3 receptorR15DK077213 · NIDDK · AUBURN UNIVERSITY AT AUBURN · PI TAO, YA-XIONG · 2008 to 2008
$219k
Mouse Model for Diseases of Protein MisfoldingR21OD012220 · OD · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI CONN, P. MICHAEL · 2012 to 2012
$213k
NIDDK NIH HHS DK077213NIDDK NIH HHS DK085040NIDDK NIH HHS DK099090NIDDK NIH HHS R01 DK085040NIDDK NIH HHS R01 DK099090NIDDK NIH HHS R15 DK077213NIH HHS OD012220NIH HHS R21 OD012220
6 · The paper itself

Abstract

G protein-coupled receptors (GPCRs) are membrane proteins that traverse the plasma membrane seven times (hence, are also called 7TM receptors). The polytopic structure of GPCRs makes the folding of GPCRs difficult and complex. Indeed, many wild-type GPCRs are not folded optimally, and defects in folding are the most common cause of genetic diseases due to GPCR mutations. Both general and receptor-specific molecular chaperones aid the folding of GPCRs. Chemical chaperones have been shown to be able to correct the misfolding in mutant GPCRs, proving to be important tools for studying the structure-function relationship of GPCRs. However, their potential therapeutic value is very limited. Pharmacological chaperones (pharmacoperones) are potentially important novel therapeutics for treating genetic diseases caused by mutations in GPCR genes that resulted in misfolded mutant proteins. Pharmacoperones also increase cell surface expression of wild-type GPCRs; therefore, they could be used to treat diseases that do not harbor mutations in GPCRs. Recent studies have shown that indeed pharmacoperones work in both experimental animals and patients. High-throughput assays have been developed to identify new pharmacoperones that could be used as therapeutics for a number of endocrine and other genetic diseases.

Indexed as

Amino Acid SequenceAnimalsDisease Models, AnimalDrug TherapyGenetic Diseases, InbornHumansMolecular ChaperonesMolecular Sequence DataMutationProtein FoldingReceptors, G-Protein-CoupledMolecular ChaperonesReceptors, G-Protein-Coupled

Identifiers

PMID24661201
PMCPMC4105357
OpenAlexW2028547572

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.