Evidence map›Paper›PMID 25050817›Full record

ArticlePloS one2014

An approach to identify SNPs in the gene encoding acetyl-CoA acetyltransferase-2 (ACAT-2) and their proposed role in metabolic processes in pig.

Simrinder Singh Sodhi, Mrinmoy Ghosh, Ki Duk Song, Neelesh Sharma, Jeong Hyun Kim, Nam Eun Kim, Sung Jin Lee, Chul Woong Kang, Sung Jong Oh, Dong Kee Jeong

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

8 citing papers in PubMed, 31 citations in OpenAlex.

  1. The Protective Effects of Astaxanthin (AST) in the Liver of Weaned Piglets.Animals : an open access journal from MDPI · 2023
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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

10 authors at 3 institutions in 1 country.

Simrinder Singh SodhiDepartment of Animal Biotechnology, Faculty of Biotechnology, Jeju National University, Jeju-si, Jeju-do, South Korea.
Mrinmoy GhoshDepartment of Animal Biotechnology, Faculty of Biotechnology, Jeju National University, Jeju-si, Jeju-do, South Korea.
Ki Duk SongThe Animal Genomics and Breeding Center, Hankyong National University, Anseong-si, Gyeonggi-do, South Korea.
Neelesh SharmaDepartment of Animal Biotechnology, Faculty of Biotechnology, Jeju National University, Jeju-si, Jeju-do, South Korea.
Jeong Hyun KimDepartment of Animal Biotechnology, Faculty of Biotechnology, Jeju National University, Jeju-si, Jeju-do, South Korea.
Nam Eun KimDepartment of Animal Biotechnology, Faculty of Biotechnology, Jeju National University, Jeju-si, Jeju-do, South Korea.
Sung Jin LeeDepartment of Animal Biotechnology, College of Animal Bioscience and Technology, Kangwon National University, Chuncheon, South Korea.
Chul Woong KangDepartment of Mechanical and System Engineering, College of Engineering, Jeju National University, Jeju-si, Jeju-do, South Korea.
Sung Jong OhDepartment of Animal Biotechnology, Faculty of Biotechnology, Jeju National University, Jeju-si, Jeju-do, South Korea.
Dong Kee JeongDepartment of Animal Biotechnology, Faculty of Biotechnology, Jeju National University, Jeju-si, Jeju-do, South Korea; Sustainable Agriculture Research Institute (SARI), Jeju National University, Jeju-si, Jeju-do, South Korea.
Jeju National University · KRHankyong National University · KRKangwon National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The novel liver protein acetyl-CoA acetyltransferase-2 (ACAT2) is involved in the beta-oxidation and lipid metabolism. Its comprehensive relative expression, in silico non-synonymous single nucleotide polymorphism (nsSNP) analysis, as well as its annotation in terms of metabolic process with another protein from the same family, namely, acetyl-CoA acyltransferase-2 (ACAA2) was performed in Sus scrofa. This investigation was conducted to understand the most important nsSNPs of ACAT2 in terms of their effects on metabolic activities and protein conformation. The two most deleterious mutations at residues 122 (I to V) and 281 (R to H) were found in ACAT2. Validation of expression of genes in the laboratory also supported the idea of differential expression of ACAT2 and ACAA2 conceived through the in silico analysis. Analysis of the relative expression of ACAT2 and ACAA2 in the liver tissue of Jeju native pig showed that the former expressed significantly higher (P<0.05). Overall, the computational prediction supported by wet laboratory analysis suggests that ACAT2 might contribute more to metabolic processes than ACAA2 in swine. Further associations of SNPs in ACAT2 with production traits might guide efforts to improve growth performance in Jeju native pigs.

Indexed as

Polymorphism, Single NucleotideAcetyl-CoA C-AcyltransferaseAnimalsBreedingCattleEnzyme StabilityGene ExpressionGene OntologyGenetic Association StudiesGenotyping TechniquesLiverMolecular Sequence AnnotationSterol O-AcyltransferaseSterol O-Acyltransferase 2Sus scrofaAcetyl-CoA C-AcyltransferaseSterol O-AcyltransferaseSterol O-Acyltransferase 2

Identifiers

PMID25050817
PMCPMC4106792
OpenAlexW1969453866

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.