Evidence map›Paper›PMID 29454859›Full record

ArticleExperimental eye research2018

Tauroursodeoxycholic acid binds to the G-protein site on light activated rhodopsin.

E Lobysheva, C M Taylor, G R Marshall, O G Kisselev

Open access · hybridAbstract read
In one paragraph

Article in Experimental eye research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

11 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
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  3. Article
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  6. Article
  7. Review
  8. Bile Acid Signaling in Neurodegenerative and Neurological Disorders.International journal of molecular sciences · 2020
    Review
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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 2 institutions in 1 country.

E LobyshevaDepartment of Ophthalmology, Saint Louis University School of Medicine, Saint Louis, MO 63104, USA.
C M TaylorDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110, USA.
G R MarshallDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110, USA.
O G KisselevDepartment of Ophthalmology, Saint Louis University School of Medicine, Saint Louis, MO 63104, USA. Electronic address: kisselev@slu.edu.
Saint Louis University · USWashington University in St. Louis · US

Funding

BIOPHYSICS OF RECEPTOR/G-PROTEIN INTERACTIONSR01GM063203 · NIGMS · SAINT LOUIS UNIVERSITY · PI KISSELEV, OLEG G · 2002 to 2011
$2.0M
DISCOVERY OF NEW THERAPEUTICS FOR DRUG-FREE REMISSION OF HIVR01GM106974 · NIGMS · WASHINGTON UNIVERSITY · PI MARSHALL, GARLAND ROSS · 2013 to 2016
$1.5M
Regulation of retinal rod transducinR01EY028914 · NEI · SAINT LOUIS UNIVERSITY · PI KISSELEV, OLEG G · 2018 to 2020
$1.1M
G-proteins and mechanisms of signal transduction in visionR21EY018107 · NEI · SAINT LOUIS UNIVERSITY · PI KISSELEV, OLEG G · 2009 to 2010
$387k
Biophsyics of Receptor/G-protein InteractionsR56GM063203 · NIGMS · SAINT LOUIS UNIVERSITY · PI KISSELEV, OLEG G · 2007 to 2007
$294k
NEI NIH HHS R01 EY028914NEI NIH HHS R21 EY018107NIGMS NIH HHS R01 GM063203NIGMS NIH HHS R01 GM106974NIGMS NIH HHS R56 GM063203
6 · The paper itself

Abstract

The heterotrimeric G-protein binding site on G-protein coupled receptors remains relatively unexplored regarding its potential as a new target of therapeutic intervention or as a secondary site of action by the existing drugs. Tauroursodeoxycholic acid bears structural resemblance to several compounds that were previously identified to specifically bind to the light-activated form of the visual receptor rhodopsin and to inhibit its activation of transducin. We show that TUDCA stabilizes the active form of rhodopsin, metarhodopsin II, and does not display the detergent-like effects of common amphiphilic compounds that share the cholesterol scaffold structure, such as deoxycholic acid. Computer docking of TUDCA to the model of light-activated rhodopsin revealed that it interacts using similar mode of binding to the C-terminal domain of transducin alpha subunit. The ring regions of TUDCA made hydrophobic contacts with loop 3 region of rhodopsin, while the tail of TUDCA is exposed to solvent. The results show that TUDCA interacts specifically with rhodopsin, which may contribute to its wide-ranging effects on retina physiology and as a potential therapeutic compound for retina degenerative diseases.

Indexed as

LightAnimalsCattleCholagogues and CholereticsGTP-Binding ProteinsOpsinsProtein BindingProtein Structure, SecondaryReceptors, G-Protein-CoupledRhodopsinSignal TransductionTaurochenodeoxycholic AcidCholagogues and CholereticsGTP-Binding ProteinsmetarhodopsinsOpsinsReceptors, G-Protein-CoupledRhodopsinTaurochenodeoxycholic AcidursodoxicoltaurineBile acidChemical biologyG proteinG protein‐coupled receptor (GPCR)Molecular dockingPhotoreceptorPhototransductionRetinaRhodopsinSignal transduction

Identifiers

PMID29454859
PMCPMC5983371
OpenAlexW2794426711

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.