Evidence map›Paper›PMID 27871057›Full record

ReviewCurrent opinion in structural biology2016

Mechanistic insights into GPCR-G protein interactions.

Jacob P Mahoney, Roger K Sunahara

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
6.4field-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

77 citing papers in PubMed, 132 citations in OpenAlex.

  1. Article
  2. The role of the tryptophan-rich allosteric network and sodium egress in GPCR activation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
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  6. Article
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  8. GPCRVS - AI-driven Decision Support System for GPCR Virtual Screening.International journal of molecular sciences · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. A molten globule ensemble primes Arf1-GDP for the nucleotide switch.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Stabilization of interdomain closure by a G protein inhibitor.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

17 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.

Jacob P MahoneyDepartment of Pharmacology, University of Michigan Medical School, Ann Arbor, MI 48109, United States.
Roger K SunaharaDepartment of Pharmacology, University of California at San Diego, La Jolla, CA 92093, United States. Electronic address: rsunahara@ucsd.edu.
University of California San Diego · USUniversity of Michigan · US

Funding

PUBLIC HEALTH DEMONSTRATIONP60DK020572 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MYERS, MARTIN G · 1985 to 2012
$26.5M
INTERDEPARTMENTAL TRAINING IN PHARMACOLOGICAL SCIENCEST32GM007767 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ISOM, LORI L. · 1985 to 2019
$10.2M
Structure and dynamics of G protein coupled receptor-G protein complexesR01GM083118 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KOBILKA, BRIAN K, SKINIOTIS, GEORGIOS · 2008 to 2023
$8.3M
Structure-based discovery of allosteric ligands for G Protein Coupled ReceptorsU19GM106990 · NIGMS · STANFORD UNIVERSITY · PI KOBILKA, BRIAN K · 2013 to 2017
$6.3M
Structure and mechanism of beta2-adrenergic receptorR01GM068603 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SUNAHARA, ROGER K · 2003 to 2008
$1.6M
NIDDK NIH HHS P60 DK020572NIGMS NIH HHS R01 GM068603NIGMS NIH HHS R01 GM083118NIGMS NIH HHS T32 GM007767NIGMS NIH HHS U19 GM106990
6 · The paper itself

Abstract

G protein-coupled receptors (GPCRs) respond to extracellular stimuli and interact with several intracellular binding partners to elicit cellular responses, including heterotrimeric G proteins. Recent structural and biophysical studies have highlighted the dynamic nature of GPCRs and G proteins and have identified specific conformational changes important for receptor-mediated nucleotide exchange on Gα. While domain separation within Gα is necessary for GDP release, opening the inter-domain interface is insufficient to stimulate nucleotide exchange. Rather, an activated receptor promotes GDP release by allosterically disrupting the nucleotide-binding site via interactions with the Gα N-termini and C-termini. Highlighting the allosteric nature of GPCRs, recent studies suggest that agonist binding alone poorly stabilizes an active conformation of several receptors. Rather, full stabilization of the receptor in an active state requires formation of the agonist-receptor-G protein ternary complex. In turn, nucleotide-free Gα is able to stabilize conformational changes around the receptor's agonist-binding site to enhance agonist affinity.

Indexed as

Binding SitesGTP-Binding ProteinsHumansNucleotidesProtein BindingProtein DomainsReceptors, G-Protein-CoupledGTP-Binding ProteinsNucleotidesReceptors, G-Protein-Coupled

Identifiers

PMID27871057
PMCPMC5363957
OpenAlexW2552525175

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.