Evidence map›Paper›PMID 23602809›Full record

ReviewJournal of molecular biology2013

Conformational flexibility and structural dynamics in GPCR-mediated G protein activation: a perspective.

Anita M Preininger, Jens Meiler, Heidi E Hamm

Abstract readReview
In one paragraph

Review in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing 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

59 citing papers in PubMed, 101 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The Role and Mechanisms of G protein-coupled receptors in Parkinson's disease.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2025
    Review
  6. Article
  7. Article
  8. Review
  9. Exploring G Protein-Coupled Receptors in Hematological Cancers.ACS pharmacology & translational science · 2024
    Article
  10. Molecular basis for chemokine recognition and activation of XCR1.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Review
  12. Alchemical Free Energy Calculations on Membrane-Associated Proteins.Journal of chemical theory and computation · 2023
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  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

3 authors at 1 institution in 1 country.

Anita M PreiningerDepartment of Pharmacology, Vanderbilt University Medical Center, Nashville, TN 37232-6600, USA. Anita.Preininger@vanderbilt.edu
Jens Meiler
Heidi E Hamm
Vanderbilt University Medical Center · US

Funding

IMMUNOLOGICAL STUDIES OF VISUAL TRANSDUCTION PATHWAYSR01EY006062 · NEI · VANDERBILT UNIVERSITY · PI HAMM, HEIDI E · 1985 to 2017
$5.6M
Membrane Protein Structure Elucidation from sparse NMR data (KAMP)R01GM080403 · NIGMS · VANDERBILT UNIVERSITY · PI MEILER, JENS · 2007 to 2019
$3.0M
Cheminformatics of Allosteric mGluR Modulation promotes Therapeutic DevelopmentR01MH090192 · NIMH · VANDERBILT UNIVERSITY · PI MEILER, JENS · 2010 to 2013
$1.5M
Computational Design of Protein-Ligand Interfaces - a Therapeutic StrategyR01GM099842 · NIGMS · VANDERBILT UNIVERSITY · PI MEILER, JENS · 2012 to 2015
$1.3M
Stabilization of Membrane Protein Signaling ComplexesR01GM095633 · NIGMS · VANDERBILT UNIVERSITY · PI IVERSON, T M · 2010 to 2013
$1.2M
Small Molecule Probes to Investigate Structure and Function of Y ReceptorsR01DK097376 · NIDDK · VANDERBILT UNIVERSITY · PI MEILER, JENS, WEAVER, C DAVID · 2013 to 2015
$1.0M
NEI NIH HHS EY006062NEI NIH HHS R01 EY006062NIDDK NIH HHS R01 DK097376NIGMS NIH HHS GM080403NIGMS NIH HHS GM095633NIGMS NIH HHS GM099842NIGMS NIH HHS R01 GM080403NIGMS NIH HHS R01 GM095633NIGMS NIH HHS R01 GM099842NIMH NIH HHS MH090192NIMH NIH HHS R01 MH090192
6 · The paper itself

Abstract

Structure and dynamics of G proteins and their cognate receptors, both alone and in complex, are becoming increasingly accessible to experimental techniques. Understanding the conformational changes and timelines that govern these changes can lead to new insights into the processes of ligand binding and associated G protein activation. Experimental systems may involve the use of, or otherwise stabilize, non-native environments. This can complicate our understanding of structural and dynamic features of processes such as the ionic lock, tryptophan toggle, and G protein flexibility. While elements in the receptor's transmembrane helices and the C-terminal α5 helix of Gα undergo well-defined structural changes, regions subject to conformational flexibility may be important in fine-tuning the interactions between activated receptors and G proteins. The pairing of computational and experimental approaches will continue to provide powerful tools to probe the conformation and dynamics of receptor-mediated G protein activation.

Indexed as

Allosteric RegulationSignal TransductionCrystallography, X-RayGTP-Binding ProteinsModels, MolecularMolecular Dynamics SimulationProtein ConformationReceptors, G-Protein-CoupledGTP-Binding ProteinsReceptors, G-Protein-Coupled

Identifiers

PMID23602809
PMCPMC3686903
OpenAlexW2064856742

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.