Evidence map›Paper›PMID 32389798›Full record

ReviewMolecular and cellular endocrinology2020

Molecular chaperones and G protein-coupled receptor maturation and pharmacology.

Ya-Xiong Tao

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular and cellular endocrinology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed, 1 pooled it
1.8field-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

20 citing papers in PubMed, 1 synthesis or guideline pooled it, 28 citations in OpenAlex.

  1. Association of Mutations in theInternational journal of molecular sciences · 2026
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

Ya-Xiong TaoDepartment of Anatomy, Physiology and Pharmacology, College of Veterinary Medicine, Auburn University, Auburn, AL, 36849-5519, USA. Electronic address: taoyaxi@auburn.edu.
Auburn University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

G protein-coupled receptors (GPCRs) are highly conserved versatile signaling molecules located at the plasma membrane that respond to diverse extracellular signals. They regulate almost all physiological processes in the vertebrates. About 35% of current drugs target these receptors. Mutations in these genes have been identified as causes of numerous diseases. The seven transmembrane domain structure of GPCRs implies that the folding of these transmembrane proteins is extremely complicated and difficult. Indeed, many wild type GPCRs are not folded optimally. The most common defect in genetic diseases caused by GPCR mutations is misfolding and failure to reach the plasma membrane where it functions. General molecular chaperones aid the folding of all proteins, including GPCRs, by preventing aggregation, promoting folding and disaggregating small aggregates. Some GPCRs need additional receptor-specific chaperones to assist their folding. Many of these receptor-specific chaperones interact with additional receptors and alter receptor pharmacology, expanding the understanding of these chaperone proteins.

Indexed as

AnimalsCell MembraneGenetic Diseases, InbornHumansMolecular ChaperonesMutant ProteinsProtein FoldingReceptors, G-Protein-CoupledMolecular ChaperonesMutant ProteinsReceptors, G-Protein-CoupledCalnexinG protein-coupled receptorHeat shock proteinMelanocortin-2 receptor accessory proteinMolecular chaperoneReceptor activity modifying protein

Identifiers

PMID32389798
OpenAlexW3022710891

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.