Evidence map›Paper›PMID 20923672›Full record

ArticleBiophysical journal2010

Binding of more than one retinoid to visual opsins.

Clint L Makino, Charles K Riley, James Looney, Rosalie K Crouch, Tetsuji Okada

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2010. 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
1.6field-weighted citation impact, top 18% 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, 32 citations in OpenAlex.

  1. Article
  2. Structural aspects of rod opsin and their implication in genetic diseases.Pflugers Archiv : European journal of physiology · 2021
    Review
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  11. Experimental phasing using zinc anomalous scattering.Acta crystallographica. Section D, Biological crystallography · 2012
    Article
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  13. Article
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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

5 authors at 4 institutions in 2 countries.

Clint L MakinoDepartment of Ophthalmology, Massachusetts Eye and Ear Infirmary, Boston, MA, USA. cmakino@meei.harvard.edu
Charles K Riley
James Looney
Rosalie K Crouch
Tetsuji Okada
Gakushuin University · JPHarvard University · USMassachusetts Eye and Ear Infirmary · USMedical University of South Carolina · US

Funding

P30 Core Grant for Vision ResearchP30EY014104 · NEI · MASSACHUSETTS EYE AND EAR INFIRMARY · PI Eric A Pierce · 2002 to 2026
$15.1M
SYNTHETIC RETINAL PIGMENTS AND BINDING PROTEINSR01EY004939 · NEI · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI CROUCH, ROSALIE K · 1985 to 2011
$4.2M
Multiple Ligand Binding Sites of Rod and Cone OpsinsR01EY011358 · NEI · MASSACHUSETTS EYE AND EAR INFIRMARY · PI MAKINO, CLINT L · 2002 to 2011
$2.9M
Cone Opsin-Ligand Interactions and Photoreceptor HealthR01EY019515 · NEI · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI KONO, MASAHIRO · 2009 to 2014
$1.8M
PROPERTIES OF LIGHT-MODULATED ION CHANNELS IN THE RETINAR01EY007774 · NEI · BROWN UNIVERSITY · PI ZIMMERMAN, ANITA L · 1988 to 2005
$1.8M
REGULATION OF PHOTORECEPTORS SPECTRAL SENSITIVITYR29EY011358 · NEI · MASSACHUSETTS EYE AND EAR INFIRMARY · PI MAKINO, CLINT L · 1997 to 2001
$227k
NEI NIH HHS EY011358NEI NIH HHS EY014104NEI NIH HHS EY019515NEI NIH HHS EY04939NEI NIH HHS P30 EY014104NEI NIH HHS R01 EY004939NEI NIH HHS R01 EY011358NEI NIH HHS R01 EY019515NEI NIH HHS R29 EY011358
6 · The paper itself

Abstract

Visual opsins bind 11-cis retinal at an orthosteric site to form rhodopsins but increasing evidence suggests that at least some are capable of binding an additional retinoid(s) at a separate, allosteric site(s). Microspectrophotometric measurements on isolated, dark-adapted, salamander photoreceptors indicated that the truncated retinal analog, β-ionone, partitioned into the membranes of green-sensitive rods; however, in blue-sensitive rod outer segments, there was an enhanced uptake of four or more β-ionones per rhodopsin. X-ray crystallography revealed binding of one β-ionone to bovine green-sensitive rod rhodopsin. Cocrystallization only succeeded with extremely high concentrations of β-ionone and binding did not alter the structure of rhodopsin from the inactive state. Salamander green-sensitive rod rhodopsin is also expected to bind β-ionone at sufficiently high concentrations because the binding site is present on its surface. Therefore, both blue- and green-sensitive rod rhodopsins have at least one allosteric binding site for retinoid, but β-ionone binds to the latter type of rhodopsin with low affinity and low efficacy.

Indexed as

AnimalsCattleCaudataCrystallography, X-RayMicrospectrophotometryNorisoprenoidsProtein BindingRetinal Rod Photoreceptor CellsRetinoidsRhodopsinRod Cell Outer Segmentbeta-iononeNorisoprenoidsRetinoidsRhodopsin

Identifiers

PMID20923672
PMCPMC3042582
OpenAlexW2007484534

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.