Evidence map›Paper›PMID 29401433›Full record

ArticleBiophysical journal2018

Lipids Alter Rhodopsin Function via Ligand-like and Solvent-like Interactions.

Leslie A Salas-Estrada, Nicholas Leioatts, Tod D Romo, Alan Grossfield

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

29 citing papers in PubMed, 52 citations in OpenAlex.

  1. Hydrophobic mismatch induces lipid sorting based on tail unsaturation.bioRxiv : the preprint server for biology · 2026
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  4. Impact of aging on the GABAbioRxiv : the preprint server for biology · 2024
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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

4 authors at 3 institutions in 2 countries.

Leslie A Salas-EstradaDepartment of Biochemistry and Biophysics, University of Rochester Medical Center, Rochester, New York.
Nicholas LeioattsDepartment of Theoretical and Computational Biophysics, Max Plank Institute for Biophysical Chemistry, Göttingen, Germany.
Tod D RomoCenter for Integrated Research Computing, University of Rochester, Rochester, New York.
Alan GrossfieldDepartment of Biochemistry and Biophysics, University of Rochester Medical Center, Rochester, New York. Electronic address: alan_grossfield@urmc.rochester.edu.
University of Rochester Medical Center · USMax Planck Institute for Biophysical Chemistry · DEUniversity of Rochester · US

Funding

Multiscale modeling of G protein-coupled receptorsR01GM095496 · NIGMS · UNIVERSITY OF ROCHESTER · PI GROSSFIELD, ALAN · 2011 to 2015
$1.3M
NIGMS NIH HHS R01 GM095496
6 · The paper itself

Abstract

Rhodopsin, a prototypical G protein-coupled receptor, is a membrane protein that can sense dim light. This highly effective photoreceptor is known to be sensitive to the composition of its lipidic environment, but the molecular mechanisms underlying this fine-tuned modulation of the receptor's function and structural stability are not fully understood. There are two competing hypotheses to explain how this occurs: 1) lipid modulation occurs via solvent-like interactions, where lipid composition controls membrane properties like hydrophobic thickness, which in turn modulate the protein's conformational equilibrium; or 2) protein-lipid interactions are ligand-like, with specific hot spots and long-lived binding events. By analyzing an ensemble of all-atom molecular dynamics simulations of five different states of rhodopsin, we show that a local ordering effect takes place in the membrane upon receptor activation. Likewise, docosahexaenoic acid acyl tails and phosphatidylethanolamine headgroups behave like weak ligands, preferentially binding to the receptor in inactive-like conformations and inducing subtle but significant structural changes.

Indexed as

AnimalsCattleIntracellular SpaceLigandsMolecular Dynamics SimulationPhosphatidylethanolaminesProtein ConformationRhodopsinSolvents1-stearoyl-2-docosahexaenoyl--sn-glycerophosphoethanolamineLigandsPhosphatidylethanolaminesRhodopsinSolvents

Identifiers

PMID29401433
PMCPMC5984976
OpenAlexW2784805083

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.