Evidence map›Paper›PMID 11368765›Full record

ArticleThe Biochemical journal2001

A surface-associated retinol- and fatty acid-binding protein (Gp-FAR-1) from the potato cyst nematode Globodera pallida: lipid binding activities, structural analysis and expression pattern.

A Prior, J T Jones, V C Blok, J Beauchamp, L McDermott, A Cooper, M W Kennedy

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
6.2field-weighted citation impact, top 4% 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

62 citing papers in PubMed, 125 citations in OpenAlex.

  1. Article
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  4. A secreted fatty acid- and retinol- binding protein frombioRxiv : the preprint server for biology · 2025
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  6. Exploring the mechanisms of host-specificity of a hyperparasitic bacterium (Frontiers in cellular and infection microbiology · 2023
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  7. International journal of molecular sciences · 2022
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  11. Transcriptomic Analysis ofFrontiers in physiology · 2022
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  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Article

2 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

A PriorMycology, Bacteriology and Nematology Unit, Scottish Crop Research Institute, Invergowrie, Dundee DD2 5DA, UK. aprior@scri.sari.ac.uk
J T Jones
V C Blok
J Beauchamp
L McDermott
A Cooper
M W Kennedy
University of Glasgow · GBJames Hutton Institute · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Parasitic nematodes produce at least two structurally novel classes of small helix-rich retinol- and fatty-acid-binding proteins that have no counterparts in their plant or animal hosts and thus represent potential targets for new nematicides. Here we describe a protein (Gp-FAR-1) from the plant-parasitic nematode Globodera pallida, which is a member of the nematode-specific fatty-acid- and retinol-binding (FAR) family of proteins but localizes to the surface of this species, placing it in a strategic position for interaction with the host. Recombinant Gp-FAR-1 was found to bind retinol, cis-parinaric acid and the fluorophore-tagged lipids 11-(dansylamino)undecanoic acid and dansyl-D,L-alpha-amino-octanoic acid. The fluorescence emission characteristics of the dansylated analogues indicated that the entire ligand enters the binding cavity. Fluorescence competition experiments showed that Gp-FAR-1 binds fatty acids in the range C(11) to C(24), with optimal binding at C(15). Intrinsic fluorescence analysis of a mutant protein into which a tryptophan residue had been inserted supported computer-based predictions of the position of this residue at the protein's interior and possibly also at the binding site. Of direct relevance to plant defence systems was the observation that Gp-FAR-1 binds two lipids (linolenic and linoleic acids) that are precursors of plant defence compounds and the jasmonic acid signalling pathway. Moreover, Gp-FAR-1 was found to inhibit the lipoxygenase-mediated modification of these substrates in vitro. Thus not only does Gp-FAR-1 function as a broad-spectrum retinol- and fatty-acid-binding protein, the results are consistent with the idea that Gp-FAR-1 is involved in the evasion of primary host plant defence systems.

Indexed as

Amino Acid SequenceAnimalsBase SequenceCarrier ProteinsCloning, MolecularDNA, ComplementaryDNA PrimersFatty Acid-Binding ProteinsFatty AcidsGene ExpressionHelminth ProteinsLigandsMolecular Sequence DataMutagenesis, Site-DirectedRecombinant ProteinsSequence Homology, Amino AcidCarrier ProteinsDNA, ComplementaryDNA PrimersFAR-1 protein, Globodera pallidaFatty Acid-Binding ProteinsFatty AcidsHelminth ProteinsLigandsRecombinant ProteinsVitamin A

Identifiers

PMID11368765
PMCPMC1221849
OpenAlexW2073012949

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.