Evidence map›Paper›PMID 12479567›Full record

ReviewMolecular and cellular biochemistry2002

Insights into binding of fatty acids by fatty acid binding proteins.

Thorsten Hanhoff, Christian Lücke, Friedrich Spener

Abstract readReview
PubMed
In one paragraph

Review in Molecular and cellular biochemistry, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

76 citing papers in PubMed, 204 citations in OpenAlex.

  1. Trial
  2. Review
  3. Functional thermodynamics govern the ligand binding to human cytosolic transport proteins.Protein science : a publication of the Protein Society · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Fatty Acid-Binding Protein 4 is Essential for the Inflammatory and Metabolic Response of Microglia to Lipopolysaccharide.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2023
    Article
  12. Review
  13. Article
  14. Article
  15. Structural Insights into Mouse H-FABP.Life (Basel, Switzerland) · 2022
    Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

16 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

3 authors at 2 institutions in 1 country.

Thorsten HanhoffDepartment of Biochemistry, University of Münster, Münster, Germany.
Christian Lücke
Friedrich Spener
University of Münster · DEGoethe University Frankfurt · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Members of the phylogenetically related intracellular lipid binding protein (iLBP) are characterized by a highly conserved tertiary structure, but reveal distinct binding preferences with regard to ligand structure and conformation, when binding is assessed by the Lipidex method (removal of unbound ligand by hydrophobic polymer) or by isothermal titration calorimetry, a true equilibrium method. Subfamily proteins bind retinoids, subfamily II proteins bind bulky ligands, examples are intestinal bile acid binding protein (I-BABP) and liver fatty acid binding protein (L-FABP) which binds 2 ligand molecules, preferably monounsaturated and n-3 fatty acids. Subfamily III intestinal fatty acid binding protein (I-FABP) binds fatty acid in a bent conformation. The fatty acid bound by subfamily IV FABPs has a U-shaped conformation; here heart (H-) FABP preferably binds n-6, brain (B-) FABP n-3 fatty acids. The ADIFAB-method is a fluorescent test for fatty acid in equilibrium with iLBP and reveals some correlation of binding affinity to fatty acid solubility in the aqueous phase; these data are often at variance with those obtained by the other methods. Thus, in this review published binding data are critically discussed, taking into account on the one hand binding increments calculated for fatty acid double bonds on the basis of the 'solubility' hypothesis, on the other hand the interpretation of calorimetric data on the basis of crystallographic and solution structures of iLBPs.

Indexed as

Neoplasm ProteinsTumor Suppressor ProteinsAnimalsCarrier ProteinsFatty Acid Binding Protein 3Fatty Acid-Binding Protein 7Fatty Acid-Binding ProteinsFatty AcidsHumansLigandsModels, MolecularProtein BindingProtein Structure, TertiaryThermodynamicsCarrier ProteinsFABP1 protein, humanFabp1 protein, mouseFABP3 protein, humanFABP7 protein, humanFatty Acid Binding Protein 3Fatty Acid-Binding Protein 7Fatty Acid-Binding ProteinsFatty AcidsLigandsNeoplasm ProteinsTumor Suppressor Proteins

Identifiers

PMID12479567
OpenAlexW1604376892

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.