Evidence map›Paper›PMID 40945563›Full record

ReviewBiochimica et biophysica acta. Biomembranes2025

Small angle neutron scattering study of rhodopsin oligomerization and G-protein coupling in a physiologically relevant lipid membrane.

Olivier Soubias, Jonathan D Nickels, Kirk G Hines, Walter E Teague, John K Northup, John Katsaras, Klaus Gawrisch

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Biomembranes, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

7 authors.

Olivier SoubiasLaboratory of Membrane Biochemistry and Biophysics, NIAAA, NIH, Bethesda, MD, 20892, United States. Electronic address: soubiaso@mail.nih.gov.
Jonathan D NickelsDepartment of Chemical and Environmental Engineering, University of Cincinnati, OH, 45221, United States.
Kirk G HinesLaboratory of Membrane Biochemistry and Biophysics, NIAAA, NIH, Bethesda, MD, 20892, United States.
Walter E TeagueLaboratory of Membrane Biochemistry and Biophysics, NIAAA, NIH, Bethesda, MD, 20892, United States.
John K NorthupLaboratory of Membrane Biochemistry and Biophysics, NIAAA, NIH, Bethesda, MD, 20892, United States; Laboratory of Sensory Signaling, NIDCD, NIH, Bethesda, MD, 20892, United States.
John KatsarasLabs and Soft Matter Group, Oak Ridge National Laboratory, Oak Ridge, TN, 37831, United States; Shull Wollan Center, Oak Ridge National Laboratory, Oak Ridge, TN, 37831, United States.
Klaus GawrischLaboratory of Membrane Biochemistry and Biophysics, NIAAA, NIH, Bethesda, MD, 20892, United States.

Funding

NMR Investigations Of Cell Membrane StructureZIAAA000003 · NIAAA · NATIONAL INSTITUTE ON ALCOHOL ABUSE AND ALCOHOLISM · PI GAWRISCH, KLAUS · 2009 to 2020
$23.2M
REGULATION OF ADP-RIBOSYLATION FACTORZ01BC007365 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI RANDAZZO, PAUL A · 1996 to 2008
$3.3M
Intramural NIH HHS Z01 BC007365Intramural NIH HHS Z99 CA999999Intramural NIH HHS ZIA AA000003
6 · The paper itself

Abstract

Although the oligomeric states of G-protein-coupled receptors (GPCRs) and interactions with cognate G proteins are central to their signal transduction capabilities, they remain poorly defined. In this study, we used small-angle neutron scattering (SANS) and a neutron contrast matching approach to elucidate the oligomeric states of the archetypal GPCR, rhodopsin, and its interaction with the G protein transducin (G

Indexed as

GTP-Binding ProteinsMembrane LipidsRhodopsinTransducinAnimalsCattleLipid BilayersNeutron DiffractionProtein MultimerizationScattering, Small AngleGTP-Binding ProteinsLipid BilayersMembrane LipidsRhodopsinTransducinG proteinG protein-coupled membrane receptorLipid bilayersRhodopsinSmall angle neutron scatteringTransducin

Identifiers

PMID40945563
PMCPMC12709549

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.