Evidence map›Paper›PMID 31273060›Full record

ArticleBioscience reports2019

Structure and ligand binding of As-p18, an extracellular fatty acid binding protein from the eggs of a parasitic nematode.

Marina Ibáñez-Shimabukuro, M Florencia Rey-Burusco, Mads Gabrielsen, Gisela R Franchini, Alan Riboldi-Tunnicliffe, Andrew J Roe, Kate Griffiths, Alan Cooper, Betina Córsico, Malcolm W Kennedy and 1 more

Open access · goldAbstract read
In one paragraph

Article in Bioscience reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

5 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Lipid and fatty acid metabolism in trypanosomatids.Microbial cell (Graz, Austria) · 2021
    Review
  5. Article
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

11 authors at 3 institutions in 3 countries.

Marina Ibáñez-ShimabukuroInstituto de Investigaciones Bioquímicas de La Plata, CONICET-UNLP, Facultad de Ciencias Médicas, calles 60 y 120, 1900-La Plata, Argentina.ORCID 0000-0002-8612-3057
M Florencia Rey-BuruscoInstituto de Investigaciones Bioquímicas de La Plata, CONICET-UNLP, Facultad de Ciencias Médicas, calles 60 y 120, 1900-La Plata, Argentina.ORCID 0000-0002-1373-0622
Mads GabrielsenInstitute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow G12 8QQ, UK.ORCID 0000-0002-9848-2276
Gisela R FranchiniInstituto de Investigaciones Bioquímicas de La Plata, CONICET-UNLP, Facultad de Ciencias Médicas, calles 60 y 120, 1900-La Plata, Argentina.ORCID 0000-0002-8355-357X
Alan Riboldi-TunnicliffeAustralian Synchrotron, Clayton, Victoria, Australia.
Andrew J RoeInstitute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow G12 8QQ, UK.ORCID 0000-0003-3698-6134
Kate GriffithsInstitute of Biodiversity, Animal Health and Comparative Medicine, University of Glasgow, G12 8QQ, UK.
Alan CooperSchool of Chemistry, University of Glasgow, Glasgow G12 8QQ, UK.
Betina CórsicoInstituto de Investigaciones Bioquímicas de La Plata, CONICET-UNLP, Facultad de Ciencias Médicas, calles 60 y 120, 1900-La Plata, Argentina.ORCID 0000-0003-2606-5606
Malcolm W KennedyInstitute of Biodiversity, Animal Health and Comparative Medicine, University of Glasgow, G12 8QQ, UK Brian.Smith@glasgow.ac.uk Malcolm.Kennedy@glasgow.ac.uk.ORCID 0000-0002-0970-5264
Brian O SmithInstitute of Molecular, Cell and Systems Biology, University of Glasgow, Glasgow G12 8QQ, UK Brian.Smith@glasgow.ac.uk Malcolm.Kennedy@glasgow.ac.uk.ORCID 0000-0003-3363-4168
University of Glasgow · GBConsejo Nacional de Investigaciones Científicas y Técnicas · ARAustralian Synchrotron · AU

Funding

Biotechnology and Biological Sciences Research Council BB/G011389/1Wellcome Trust 083625
6 · The paper itself

Abstract

Intracellular lipid-binding proteins (iLBPs) of the fatty acid-binding protein (FABP) family of animals transport, mainly fatty acids or retinoids, are confined to the cytosol and have highly similar 3D structures. In contrast, nematodes possess fatty acid-binding proteins (nemFABPs) that are secreted into the perivitelline fluid surrounding their developing embryos. We report structures of As-p18, a nemFABP of the large intestinal roundworm

Indexed as

AnimalsAscaris suumFatty Acid-Binding ProteinsHelminth ProteinsLigandsOvumProtein BindingProtein DomainsProtein Structure, SecondaryAs-p18 protein, Ascaris suumFatty Acid-Binding ProteinsHelminth ProteinsLigandsAscaris suumAs-p18fatty acid binding proteinnematodenemFABPparasite

Identifiers

PMID31273060
PMCPMC6646235
OpenAlexW2963177741

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.