Evidence map›Paper›PMID 26633591›Full record

ArticleAngewandte Chemie (International ed. in English)2016

A Usual G-Protein-Coupled Receptor in Unusual Membranes.

Udeep Chawla, Yunjiang Jiang, Wan Zheng, Liangju Kuang, Suchithranga M D C Perera, Michael C Pitman, Michael F Brown, Hongjun Liang

Open access · greenAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

8 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Hydration-mediated G-protein-coupled receptor activation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Powdered G-Protein-Coupled Receptors.The journal of physical chemistry letters · 2016
    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

8 authors at 3 institutions in 1 country.

Udeep ChawlaDepartment of Chemistry & Biochemistry, Department of Physics University of Arizona, Tucson, AZ 85721 (USA).
Yunjiang JiangDepartment of Metallurgical & Materials Engineering, Colorado School of Mines, Golden, CO 80401 (USA).
Wan ZhengDepartment of Metallurgical & Materials Engineering, Colorado School of Mines, Golden, CO 80401 (USA).
Liangju KuangDepartment of Metallurgical & Materials Engineering, Colorado School of Mines, Golden, CO 80401 (USA).
Suchithranga M D C PereraDepartment of Chemistry & Biochemistry, Department of Physics University of Arizona, Tucson, AZ 85721 (USA).
Michael C PitmanDepartment of Chemistry & Biochemistry, Department of Physics University of Arizona, Tucson, AZ 85721 (USA).
Michael F BrownDepartment of Chemistry & Biochemistry, Department of Physics University of Arizona, Tucson, AZ 85721 (USA). mfbrown@u.arizona.edu.
Hongjun LiangDepartment of Metallurgical & Materials Engineering, Colorado School of Mines, Golden, CO 80401 (USA). H.liang@ttuhsc.edu.
Colorado School of Mines · USUniversity of Arizona · USTexas Tech University Health Sciences Center · US

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
MEMBRANE BASIS OF VISUAL EXCITATIONR01EY012049 · NEI · UNIVERSITY OF ARIZONA · PI BROWN, MICHAEL F · 1998 to 2012
$3.3M
LIPID MODULATION OF RHODOPSIN SIGNALING IN MEMBRANESR01EY018891 · NEI · UNIVERSITY OF ARIZONA · PI BROWN, MICHAEL F · 2008 to 2010
$1.1M
MEMBRANE BASIS OF VISUAL EXCITATIONR01EY026041 · NEI · UNIVERSITY OF ARIZONA · PI BROWN, MICHAEL F · 2016 to 2018
$1.1M
NEI NIH HHS R01 EY012049NEI NIH HHS R01 EY018891NEI NIH HHS R01 EY026041NIGMS NIH HHS P41GM103393
6 · The paper itself

Abstract

G-protein-coupled receptors (GPCRs) are the largest family of membrane-bound receptors and constitute about 50% of all known drug targets. They offer great potential for membrane protein nanotechnologies. We report here a charge-interaction-directed reconstitution mechanism that induces spontaneous insertion of bovine rhodopsin, the eukaryotic GPCR, into both lipid- and polymer-based artificial membranes. We reveal a new allosteric mode of rhodopsin activation incurred by the non-biological membranes: the cationic membrane drives a transition from the inactive MI to the activated MII state in the absence of high [H(+)] or negative spontaneous curvature. We attribute this activation to the attractive charge interaction between the membrane surface and the deprotonated Glu134 residue of the rhodopsin-conserved ERY sequence motif that helps break the cytoplasmic "ionic lock". This study unveils a novel design concept of non-biological membranes to reconstitute and harness GPCR functions in synthetic systems.

Indexed as

AnimalsCattleCell MembraneFatty Acids, MonounsaturatedQuaternary Ammonium CompoundsReceptors, G-Protein-CoupledScattering, Small AngleSpectrophotometry, UltravioletSpectroscopy, Fourier Transform InfraredX-Ray Diffraction1,2-dioleoyloxy-3-(trimethylammonium)propaneFatty Acids, MonounsaturatedQuaternary Ammonium CompoundsReceptors, G-Protein-Coupledbiophysicsflexible surface modelG-protein-coupled receptorphotoactivationrhodopsin

Identifiers

PMID26633591
PMCPMC5233722
OpenAlexW2183023998

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.