Evidence map›Paper›PMID 23434406›Full record

ArticleStructure (London, England : 1993)2013

Kinetic, energetic, and mechanical differences between dark-state rhodopsin and opsin.

Shiho Kawamura, Moritz Gerstung, Alejandro T Colozo, Jonne Helenius, Akiko Maeda, Niko Beerenwinkel, Paul S-H Park, Daniel J Müller

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.1field-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

37 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
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  13. Review
  14. Apo-Opsin Exists in Equilibrium Between a Predominant Inactive and a Rare Highly Active State.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2019
    Article
  15. Article
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  20. Effect of material flexibility on the thermodynamics and kinetics of hydrophobically induced evaporation of water.Proceedings of the National Academy of Sciences of the United States of America · 2017
    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 3 countries.

Shiho KawamuraDepartment of Biosystems Science and Engineering, ETH Zürich, Basel, Switzerland.
Moritz Gerstung
Alejandro T Colozo
Jonne Helenius
Akiko Maeda
Niko Beerenwinkel
Paul S-H Park
Daniel J Müller
Case Western Reserve University · USETH Zurich · CHSIB Swiss Institute of Bioinformatics · CH

Funding

TISSUE CULTURE AND HYBRIDOMA MODULEP30EY011373 · NEI · CASE WESTERN RESERVE UNIVERSITY · PI Irina A Pikuleva · 1997 to 2026
$17.7M
PHOTOTRANSDUCTION IN HEALTH AND DISEASE - Administrative SupplementR01EY021731 · NEI · CASE WESTERN RESERVE UNIVERSITY · PI Paul S Park · 2011 to 2026
$6.5M
Towards a structural and temporal understanding of phototransductionR00EY018085 · NEI · CASE WESTERN RESERVE UNIVERSITY · PI PARK, PAUL S · 2008 to 2010
$825k
Retinal degeneration diseases and the visual retinoid cycleK08EY019031 · NEI · CASE WESTERN RESERVE UNIVERSITY · PI MAEDA, AKIKO · 2008 to 2012
$430k
NEI NIH HHS K08 EY019031NEI NIH HHS K08EY019031NEI NIH HHS P30 EY011373NEI NIH HHS P30EY011373NEI NIH HHS R00 EY018085NEI NIH HHS R00EY018085NEI NIH HHS R01 EY021731NEI NIH HHS R01EY021731
6 · The paper itself

Abstract

Rhodopsin, the photoreceptor pigment of the retina, initiates vision upon photon capture by its covalently linked chromophore 11-cis-retinal. In the absence of light, the chromophore serves as an inverse agonist locking the receptor in the inactive dark state. In the absence of chromophore, the apoprotein opsin shows low-level constitutive activity. Toward revealing insight into receptor properties controlled by the chromophore, we applied dynamic single-molecule force spectroscopy to quantify the kinetic, energetic, and mechanical differences between dark-state rhodopsin and opsin in native membranes from the retina of mice. Both rhodopsin and opsin are stabilized by ten structural segments. Compared to dark-state rhodopsin, the structural segments stabilizing opsin showed higher interaction strengths and mechanical rigidities and lower conformational variabilities, lifetimes, and free energies. These changes outline a common mechanism toward activating G-protein-coupled receptors. Additionally, we detected that opsin was more pliable and frequently stabilized alternate structural intermediates.

Indexed as

Amino Acid SequenceAnimalsCell Membranecis-trans-IsomerasesDarknessKineticsMiceMice, KnockoutMolecular Dynamics SimulationMolecular Sequence DataOpsinsProtein FoldingProtein Structure, SecondaryProtein Structure, TertiaryRetinaldehydeRetinoid Isomerohydrolasecis-trans-IsomerasesOpsinsRetinaldehydeRetinoid IsomerohydrolaseRhodopsin

Identifiers

PMID23434406
PMCPMC3806332
OpenAlexW2163132804

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.