Evidence map›Paper›PMID 11785933›Full record

ArticlePlant molecular biology2001

Characterization of a novel plant acyl-coA synthetase that is expressed in lipogenic tissues of Brassica napus L.

P Pongdontri, M Hills

Abstract read
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In one paragraph

Article in Plant molecular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.3field-weighted citation impact, top 15% 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

12 citing papers in PubMed, 47 citations in OpenAlex.

  1. Functional Analysis of Rice Long-Chain Acyl-CoA Synthetase 9 (International journal of molecular sciences · 2020
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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

2 authors at 2 institutions in 1 country.

P PongdontriJohn Innes Centre, Norwich Research Park, UK.
M Hills
John Innes Centre · GBNorwich Research Park · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A cDNA encoding a novel isoform of acyl-CoA synthetase (ACS6) was isolated from embryos of oilseed rape. Homology searches show it is most closely related to ACS4 from rat and human brain rather than the other oilseed rape ACSs. The ACS6 is strongly expressed in embryos and flowers, tissues of Brassica napus that synthesize lipids at high rates. The activity of recombinantly expressed ACS6 was recovered in the insoluble fraction (214,000 x g, 1 h pellet). CHAPS-solubilized recombinant ACS6 protein preferred utilising long-chain fatty acids that contained a cis-9 double bond, i.e. palmitoleic, oleic, linoleic and linolenic acids. Western blot analysis showed that the ACS6 protein is membrane-bound.

Indexed as

Plant ProteinsAmino Acid SequenceBrassica napusCoenzyme A LigasesDNA, ComplementaryEscherichia coliGene Expression Regulation, EnzymologicGene Expression Regulation, PlantLipidsMolecular Sequence DataPhylogenyRecombinant ProteinsSeedsSequence AlignmentSequence Analysis, DNASequence Homology, Amino AcidACS6 protein, Brassica napusCoenzyme A LigasesDNA, ComplementaryLipidsPlant ProteinsRecombinant Proteins

Identifiers

PMID11785933
OpenAlexW265020886

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.