Evidence map›Paper›PMID 29157307›Full record

ArticleParasites & vectors2017

Multidrug resistance-associated protein 4 is a bile transporter of Clonorchis sinensis simulated by in silico docking.

Fuhong Dai, Won Gi Yoo, Ji-Yun Lee, Yanyan Lu, Jhang Ho Pak, Woon-Mok Sohn, Sung-Jong Hong

Open access · goldAbstract read
In one paragraph

Article in Parasites & vectors, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.7field-weighted citation impact, top 27% 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

6 citing papers in PubMed, 10 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

7 authors at 3 institutions in 1 country.

Fuhong DaiDepartment of Medical Environmental Biology, Chung-Ang University College of Medicine, Seoul, 06974, South Korea.
Won Gi YooDepartment of Medical Environmental Biology, Chung-Ang University College of Medicine, Seoul, 06974, South Korea.
Ji-Yun LeeDepartment of Medical Environmental Biology, Chung-Ang University College of Medicine, Seoul, 06974, South Korea.
Yanyan LuDepartment of Medical Environmental Biology, Chung-Ang University College of Medicine, Seoul, 06974, South Korea.
Jhang Ho PakDepartment of Convergence Medicine, University of Ulsan College of Medicine and Asan Institute for Life Sciences, Asan Medical Center, Seoul, 05505, South Korea.
Woon-Mok SohnDepartment of Parasitology and Institute of Health Sciences, Gyeongsang National University School of Medicine, Jinju, 52828, South Korea.
Sung-Jong HongDepartment of Medical Environmental Biology, Chung-Ang University College of Medicine, Seoul, 06974, South Korea. hongsj@cau.ac.kr.
Chung-Ang University · KRGyeongsang National University · KRUniversity of Ulsan · KR

Funding

National Research Foundation of Korea (KR) 2014R1A2A1A11051870
6 · The paper itself

Abstract

backgroundMultidrug resistance-associated protein 4 (MRP4) is a member of the C subfamily of the ABC family of ATP-binding cassette (ABC) transporters. MRP4 regulates ATP-dependent efflux of various organic anionic substrates and bile acids out of cells. Since Clonorchis sinensis lives in host's bile duct, accumulation of bile juice can be toxic to the worm's tissues and cells. Therefore, C. sinensis needs bile transporters to reduce accumulation of bile acids within its body.

resultsWe cloned MRP4 (CsMRP4) from C. sinensis and obtained a cDNA encoding an open reading frame of 1469 amino acids. Phylogenetic analysis revealed that CsMRP4 belonged to the MRP/SUR/CFTR subfamily. A tertiary structure of CsMRP4 was generated by homology modeling based on multiple structures of MRP1 and P-glycoprotein. CsMRP4 had two membrane-spanning domains (MSD1 & 2) and two nucleotide-binding domains (NBD1 & 2) as common structural folds. Docking simulation with nine bile acids showed that CsMRP4 transports bile acids through the inner cavity. Moreover, it was found that CsMRP4 mRNA was more abundant in the metacercariae than in the adults. Mouse immune serum, generated against the CsMRP4-NBD1 (24.9 kDa) fragment, localized CsMRP4 mainly in mesenchymal tissues and oral and ventral suckers of the metacercariae and the adults.

conclusionsOur findings shed new light on MRPs and their homologs and provide a platform for further structural and functional investigations on the bile transporters and parasites' survival.

Indexed as

Molecular Dynamics SimulationAnimalsATP-Binding Cassette, Sub-Family C ProteinsBile Acids and SaltsBile DuctsBiological TransportCloning, MolecularClonorchis sinensisHelminth ProteinsPhylogenyProtein DomainsATP-Binding Cassette, Sub-Family C ProteinsBile Acids and SaltsHelminth ProteinsABCC4Bile transporterClonorchis sinensisLocalizationMRP4Structure

Identifiers

PMID29157307
PMCPMC5697364
OpenAlexW2770866775

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.