Evidence map›Paper›PMID 24792929›Full record

ArticleJournal of lipid research2014

Diversification of substrate specificities in teleostei Fads2: characterization of Δ4 and Δ6Δ5 desaturases of Chirostoma estor.

Jorge Fonseca-Madrigal, Juan C Navarro, Francisco Hontoria, Douglas R Tocher, Carlos A Martínez-Palacios, Óscar Monroig

Open access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
23.8field-weighted citation impact, top 1% 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

28 citing papers in PubMed, 114 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

6 authors at 3 institutions in 3 countries.

Jorge Fonseca-MadrigalLaboratorio de Acuicultura, Instituto de Investigaciones Agropecuarias y Forestales, Universidad Michoacana de San Nicolás de Hidalgo (UMSNH), Morelia 58330, Michoacán, Mexico.
Juan C NavarroInstituto de Acuicultura Torre de la Sal-Consejo Superior de Investigaciones Científicas (IATS-CSIC), Ribera de Cabanes 12595, Castellón, Spain.
Francisco HontoriaInstituto de Acuicultura Torre de la Sal-Consejo Superior de Investigaciones Científicas (IATS-CSIC), Ribera de Cabanes 12595, Castellón, Spain.
Douglas R TocherInstitute of Aquaculture, School of Natural Sciences, University of Stirling, Stirling FK9 4LA, Scotland, UK.
Carlos A Martínez-PalaciosLaboratorio de Acuicultura, Instituto de Investigaciones Agropecuarias y Forestales, Universidad Michoacana de San Nicolás de Hidalgo (UMSNH), Morelia 58330, Michoacán, Mexico.
Óscar MonroigInstituto de Acuicultura Torre de la Sal-Consejo Superior de Investigaciones Científicas (IATS-CSIC), Ribera de Cabanes 12595, Castellón, Spain Laboratorio de Acuicultura, Instituto de Investigaciones Agropecuarias y Forestales, Universidad Michoacana de San Nicolás de Hidalgo (UMSNH), Morelia 58330, Michoacán, Mexico.
Consejo Superior de Investigaciones Científicas · ESUniversidad Michoacana de San Nicolás de Hidalgo · MXUniversity of Stirling · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Currently existing data show that the capability for long-chain PUFA (LC-PUFA) biosynthesis in teleost fish is more diverse than in other vertebrates. Such diversity has been primarily linked to the subfunctionalization that teleostei fatty acyl desaturase (Fads)2 desaturases have undergone during evolution. We previously showed that Chirostoma estor, one of the few representatives of freshwater atherinopsids, had the ability for LC-PUFA biosynthesis from C18 PUFA precursors, in agreement with this species having unusually high contents of DHA. The particular ancestry and pattern of LC-PUFA biosynthesis activity of C. estor make this species an excellent model for study to gain further insight into LC-PUFA biosynthetic abilities among teleosts. The present study aimed to characterize cDNA sequences encoding fatty acyl elongases and desaturases, key genes involved in the LC-PUFA biosynthesis. Results show that C. estor expresses an elongase of very long-chain FA (Elovl)5 elongase and two Fads2 desaturases displaying Δ4 and Δ6/Δ5 specificities, thus allowing us to conclude that these three genes cover all the enzymatic abilities required for LC-PUFA biosynthesis from C18 PUFA. In addition, the specificities of the C. estor Fads2 enabled us to propose potential evolutionary patterns and mechanisms for subfunctionalization of Fads2 among fish lineages.

Indexed as

Fatty Acid DesaturasesFatty Acids, UnsaturatedFishesFish ProteinsAnimalsSubstrate SpecificityFatty Acid DesaturasesFatty Acids, UnsaturatedFish Proteinsbiosynthesiselongase of very long-chain fatty acidsevolutionfatty acyl desaturase 2long-chain polyunsaturated fatty acidsteleosts

Identifiers

PMID24792929
PMCPMC4076095
OpenAlexW1970891161

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.