Evidence map›Paper›PMID 21375271›Full record

ArticleBiochemistry2011

Coupling efficiency of rhodopsin and transducin in bicelles.

Ali I Kaya, Tarjani M Thaker, Anita M Preininger, T M Iverson, Heidi E Hamm

Abstract read
In one paragraph

Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

15 citing papers in PubMed, 28 citations in OpenAlex.

  1. Local membrane charge regulates βNature communications · 2019
    Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. When detergent meets bilayer: birth and coming of age of lipid bicelles.Progress in nuclear magnetic resonance spectroscopy · 2013
    Review
  8. Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. 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

5 authors at 1 institution in 1 country.

Ali I KayaDepartment of Pharmacology, Vanderbilt University Medical Center, Nashville, Tennessee 37232-6600, United States.
Tarjani M Thaker
Anita M Preininger
T M Iverson
Heidi E Hamm
Vanderbilt University Medical Center · US

Funding

Shop Module CoreP30EY008126 · NEI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI Kevin L Schey · 1989 to 2026
$19.6M
IMMUNOLOGICAL STUDIES OF VISUAL TRANSDUCTION PATHWAYSR01EY006062 · NEI · VANDERBILT UNIVERSITY · PI HAMM, HEIDI E · 1985 to 2017
$5.6M
Stabilization of Membrane Protein Signaling ComplexesR01GM095633 · NIGMS · VANDERBILT UNIVERSITY · PI IVERSON, T M · 2010 to 2013
$1.2M
Overcoming the Barriers to Structural Analysis of GPCRsR01GM081816 · NIGMS · VANDERBILT UNIVERSITY · PI SANDERS, CHARLES R · 2007 to 2009
$966k
Transition states in G-protein coupled receptor signalingR21EY018435 · NEI · VANDERBILT UNIVERSITY · PI IVERSON, T M · 2009 to 2010
$415k
NEI NIH HHS EY006062NEI NIH HHS EY018435NEI NIH HHS P30 EY008126NEI NIH HHS P30EY008126NEI NIH HHS R01 EY006062NEI NIH HHS R21 EY018435NIGMS NIH HHS GM081816NIGMS NIH HHS GM0956633NIGMS NIH HHS R01 GM081816NIGMS NIH HHS R01 GM095633
6 · The paper itself

Abstract

G protein coupled receptors (GPCRs) can be activated by various extracellular stimuli, including hormones, peptides, odorants, neurotransmitters, nucleotides, or light. After activation, receptors interact with heterotrimeric G proteins and catalyze GDP release from the Gα subunit, the rate limiting step in G protein activation, to form a high affinity nucleotide-free GPCR-G protein complex. In vivo, subsequent GTP binding reduces affinity of the Gα protein for the activated receptor. In this study, we investigated the biochemical and structural characteristics of the prototypical GPCR, rhodopsin, and its signaling partner, transducin (G(t)), in bicelles to better understand the effects of membrane composition on high affinity complex formation, stability, and receptor mediated nucleotide release. Our results demonstrate that the high-affinity complex (rhodopsin-G(t)(empty)) forms more readily and has dramatically increased stability when rhodopsin is integrated into bicelles of a defined composition. We increased the half-life of functional complex to 1 week in the presence of negatively charged phospholipids. These data suggest that a membrane-like structure is an important contributor to the formation and stability of functional receptor-G protein complexes and can extend the range of studies that investigate properties of these complexes.

Indexed as

MicellesBiocatalysisCell MembraneDetergentsHalf-LifeHydrogen-Ion ConcentrationLightNucleotidesProtein BindingRhodopsinScattering, RadiationTemperatureTransducinDetergentsMicellesNucleotidesRhodopsinTransducin

Identifiers

PMID21375271
PMCPMC3119548
OpenAlexW2085563968

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.