Evidence map›Paper›PMID 29410696›Full record

ArticleNutrition & metabolism2018

The interaction of selenoprotein F (SELENOF) with retinol dehydrogenase 11 (RDH11) implied a role of SELENOF in vitamin A metabolism.

Jing Tian, Jiapan Liu, Jieqiong Li, Jingxin Zheng, Lifang Chen, Yujuan Wang, Qiong Liu, Jiazuan Ni

Open access · goldAbstract read
In one paragraph

Article in Nutrition & metabolism, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

7 citing papers in PubMed, 16 citations in OpenAlex.

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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

8 authors at 2 institutions in 1 country.

Jing Tian1College of Life Sciences and Oceanography, Shenzhen Key Laboratory of Marine Bioresources and Eco-environmental Science, Shenzhen University, Shenzhen, 518060 China.ORCID 0000-0003-2969-0781
Jiapan Liu1College of Life Sciences and Oceanography, Shenzhen Key Laboratory of Marine Bioresources and Eco-environmental Science, Shenzhen University, Shenzhen, 518060 China.
Jieqiong Li2College of Life Sciences and Oceanography, Shenzhen Key Laboratory of Microbial Genetic Engineering, Shenzhen University, Shenzhen, 518060 China.
Jingxin Zheng3College of Life Sciences and Oceanography, Shenzhen Engineering Laboratory for Marine Algal Biotechnology, Shenzhen University, Shenzhen, 518060 China.
Lifang Chen4Department of Neurology, Shenzhen University 1st Affiliated Hospital, Shenzhen Second People's Hospital, Sungang West Road, Shenzhen, China.
Yujuan Wang1College of Life Sciences and Oceanography, Shenzhen Key Laboratory of Marine Bioresources and Eco-environmental Science, Shenzhen University, Shenzhen, 518060 China.
Qiong Liu1College of Life Sciences and Oceanography, Shenzhen Key Laboratory of Marine Bioresources and Eco-environmental Science, Shenzhen University, Shenzhen, 518060 China.
Jiazuan Ni1College of Life Sciences and Oceanography, Shenzhen Key Laboratory of Marine Bioresources and Eco-environmental Science, Shenzhen University, Shenzhen, 518060 China.
Shenzhen University · CNShenzhen Second People's Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundSelenoprotein F (SELENOF, was named as 15-kDa selenoprotein) has been reported to play important roles in oxidative stress, endoplasmic reticulum (ER) stress and carcinogenesis. However, the biological function of SELENOF is still unclear.

methodsA yeast two-hybrid system was used to screen the interactive protein of SELENOF in a human fetal brain cDNA library. The interaction between SELENOF and interactive protein was validated by fluorescence resonance energy transfer (FRET), co-immunoprecipitation (co-IP) and pull-down assays. The production of retinol was detected by high performance liquid chromatograph (HPLC).

resultsRetinol dehydrogenase 11 (RDH11) was found to interact with SELENOF. RDH11 is an enzyme for the reduction of all-trans-retinaldehyde to all-trans-retinol (vitamin A). The production of retinol was decreased by SELENOF overexpression, resulting in more retinaldehyde.

conclusionsSELENOF interacts with RDH11 and blocks its enzyme activity to reduce all-trans-retinaldehyde.

Indexed as

Co-immunoprecipitation (co-IP)Fluorescence resonance energy transfer (FRET)Protein-protein interactionPull-downRetinaldehydeRetinol dehydrogenase 11 (RDH11)Retinol (vitamin a)SELENOF (Seleonoprotein F)Yeast two hybrid system

Identifiers

PMID29410696
PMCPMC5778809
OpenAlexW2794508976

What OpenQuestion holds

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LicenceCC BY
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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.