Evidence map›Paper›PMID 25110551›Full record

ReviewDairy science & technology2014

Bovine β-lactoglobulin/fatty acid complexes: binding, structural, and biological properties.

Solène Le Maux, Saïd Bouhallab, Linda Giblin, André Brodkorb, Thomas Croguennec

Open access · hybridAbstract readReview
In one paragraph

Review in Dairy science & technology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
11.0field-weighted citation impact, top 2% 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

33 citing papers in PubMed, 154 citations in OpenAlex.

  1. Review
  2. Review
  3. Advanced Oral Delivery Systems for Nutraceuticals.Advanced healthcare materials · 2025
    Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Asthma-protective agents in dust from traditional farm environments.The Journal of allergy and clinical immunology · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. A Double Payload Complex between Hypericin and All-Antibiotics (Basel, Switzerland) · 2022
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. 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

5 authors at 2 institutions in 3 countries.

Solène Le MauxINRA, UMR1253 STLO, 65 rue de Saint Brieuc, 35042 Rennes, France ; AGROCAMPUS OUEST, UMR1253 STLO, 65 rue de Saint Brieuc, 35042 Rennes, France ; Teagasc Food Research Centre, Moorepark, Fermoy, Co. Cork Ireland.
Saïd BouhallabINRA, UMR1253 STLO, 65 rue de Saint Brieuc, 35042 Rennes, France ; AGROCAMPUS OUEST, UMR1253 STLO, 65 rue de Saint Brieuc, 35042 Rennes, France.
Linda GiblinTeagasc Food Research Centre, Moorepark, Fermoy, Co. Cork Ireland.
André BrodkorbTeagasc Food Research Centre, Moorepark, Fermoy, Co. Cork Ireland.
Thomas CroguennecINRA, UMR1253 STLO, 65 rue de Saint Brieuc, 35042 Rennes, France ; AGROCAMPUS OUEST, UMR1253 STLO, 65 rue de Saint Brieuc, 35042 Rennes, France.
Institut National de la Recherche Agronomique · MATeagasc - The Irish Agriculture and Food Development Authority · IE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ligand-binding properties of β-lactoglobulin (β-lg) are well documented, but the subsequent biological functions are still unclear. Focusing on fatty acids/β-lg complexes, the structure-function relationships are reviewed in the light of the structural state of the protein (native versus non-native aggregated proteins). After a brief description of β-lg native structure, the review takes an interest in the binding properties of native β-lg (localization of binding sites, stoichiometry, and affinity) and the way the interaction affects the biological properties of the protein and the ligand. The binding properties of non-native aggregated forms of β-lg that are classically generated during industrial processing are also related. Structural changes modify the stoichiometry and the affinity of β-lg for fatty acids and consequently the biological functions of the complex. Finally, the fatty acid-binding properties of other whey proteins (α-lactalbumin, bovine serum albumin) and some biological properties of the complexes are also addressed. These proteins affect β-lg/fatty acids complex in whey given their competition with β-lg for fatty acids.

Indexed as

Binding propertiesBiological propertiesBovine β-lactoglobulinFatty acidProtein structure

Identifiers

PMID25110551
PMCPMC4121524
OpenAlexW2021022993

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.