Evidence map›Paper›PMID 21039965›Full record

ArticleThe European journal of neuroscience2010

Lack of protein-tyrosine sulfation disrupts photoreceptor outer segment morphogenesis, retinal function and retinal anatomy.

David M Sherry, Anne R Murray, Yogita Kanan, Kelsey L Arbogast, Robert A Hamilton, Steven J Fliesler, Marie E Burns, Kevin L Moore, Muayyad R Al-Ubaidi

Open access · greenAbstract read
In one paragraph

Article in The European journal of neuroscience, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed, 29 citations in OpenAlex.

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  16. Focus on molecules: sulfotyrosine.Experimental eye research · 2012
    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

9 authors at 3 institutions in 1 country.

David M SherryDepartment of Cell Biology, University of Oklahoma Health Sciences Center, BMSB 781, 940 Stanton L. Young Blvd., Oklahoma City, OK 73104, USA.
Anne R Murray
Yogita Kanan
Kelsey L Arbogast
Robert A Hamilton
Steven J Fliesler
Marie E Burns
Kevin L Moore
Muayyad R Al-Ubaidi
University of Oklahoma Health Sciences Center · USUniversity of California, Davis · USVA Western New York Healthcare System · US

Funding

UNDERSTANDING THE ROLE OF RETINOL DEHYDROGENASES RDH11 AND RDH12 IN VISIONP20RR017703 · NCRR · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI MANDAL, NAWAJES · 2002 to 2011
$23.6M
ZEBRAFISH INTERNATIONAL RESOURCE CENTERP40RR012546 · NCRR · UNIVERSITY OF OREGON · PI WESTERFIELD, MONTE · 1998 to 2011
$21.9M
Translational Core for Therapeutic and Diagnostic DevelopmentP30EY001792 · NEI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI MCANANY, JAMES JASON · 1985 to 2025
$14.8M
Deactivation Mechanisms of Rod PhototransductionR01EY014047 · NEI · UNIVERSITY OF CALIFORNIA DAVIS · PI BURNS, MARIE E · 2002 to 2020
$8.5M
CORE--MOLECULAR BIOLOGYP30EY012190 · NEI · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI ANDERSON, ROBERT E · 1999 to 2009
$5.2M
ISOPRENOID METABOLISM IN THE RETINAR01EY007361 · NEI · UNIVERSITY OF SOUTH FLORIDA · PI FLIESLER, STEVEN J. · 1988 to 2015
$4.4M
RETINAL DEGENERATION: MOLECULAR AND BIOCHEMICAL ASPECTSR01EY014052 · NEI · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI AL-UBAIDI, MUAYYAD R · 2003 to 2006
$1.6M
Identification of Tyrosine-Sulfated Proteins in the Male Genital TractR01HD056022 · NICHD · OKLAHOMA MEDICAL RESEARCH FOUNDATION · PI MOORE, KEVIN L · 2008 to 2012
$1.6M
Retinal degeneration caused by alterations in protein tyrosine O-sulfationR01EY018137 · NEI · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI AL-UBAIDI, MUAYYAD R · 2009 to 2013
$1.1M
NCRR NIH HHS P20 RR017703NCRR NIH HHS P40 RR012546NEI NIH HHS P30 EY001792NEI NIH HHS P30 EY012190NEI NIH HHS R01 EY007361NEI NIH HHS R01 EY014047NEI NIH HHS R01 EY014052NEI NIH HHS R01 EY018137NICHD NIH HHS R01 HD056022
6 · The paper itself

Abstract

To investigate the role(s) of protein-tyrosine sulfation in the retina, we examined retinal function and structure in mice lacking tyrosylprotein sulfotransferases (TPST) 1 and 2. Tpst double knockout (DKO; Tpst1(-/-) /Tpst2 (-/-) ) retinas had drastically reduced electroretinographic responses, although their photoreceptors exhibited normal responses in single cell recordings. These retinas appeared normal histologically; however, the rod photoreceptors had ultrastructurally abnormal outer segments, with membrane evulsions into the extracellular space, irregular disc membrane spacing and expanded intradiscal space. Photoreceptor synaptic terminals were disorganized in Tpst DKO retinas, but established ultrastructurally normal synapses, as did bipolar and amacrine cells; however, the morphology and organization of neuronal processes in the inner retina were abnormal. These results indicate that protein-tyrosine sulfation is essential for proper outer segment morphogenesis and synaptic function, but is not critical for overall retinal structure or synapse formation, and may serve broader functions in neuronal development and maintenance.

Indexed as

RetinaSulfotransferasesAnimalsElectroretinographyFemaleMaleMiceMice, KnockoutMorphogenesisRetinal Cone Photoreceptor CellsRod Cell Outer SegmentSynapsesTyrosineprotein-tyrosine sulfotransferaseSulfotransferasesTPST2 protein, mouseTyrosine

Identifiers

PMID21039965
PMCPMC3058723
OpenAlexW1908750190

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.