Evidence map›Paper›PMID 24299557›Full record

ArticleBiochemistry2013

The human liver fatty acid binding protein T94A variant alters the structure, stability, and interaction with fibrates.

Gregory G Martin, Avery L McIntosh, Huan Huang, Shipra Gupta, Barbara P Atshaves, Kerstin K Landrock, Danilo Landrock, Ann B Kier, Friedhelm Schroeder

Open access · greenAbstract readComparative Study
In one paragraph

Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

30 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. ΔJournal of lipid research · 2018
    Article
  14. Article
  15. Journal of Cancer · 2018
    Article
  16. Impact ofJournal of lipid research · 2017
    Article
  17. Article
  18. Impact of dietary phytol on lipid metabolism in SCP2/SCPX/L-FABP null mice.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017
    Article
  19. Article
  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

9 authors at 2 institutions in 1 country.

Gregory G MartinDepartment of Physiology and Pharmacology, Texas A&M University , TVMC, College Station, Texas 77843-4466, United States.
Avery L McIntosh
Huan Huang
Shipra Gupta
Barbara P Atshaves
Kerstin K Landrock
Danilo Landrock
Ann B Kier
Friedhelm Schroeder
Texas A&M University · USMichigan State University · US

Funding

Regional Pilot And Feasibility Study Grants ProgramP30DK020572 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Mehboob A Hussain · 2013 to 2026
$24.3M
FATTY ACID BINDING PROTEINS-LIGAND SPECIFICITYR01DK041402 · NIDDK · UNIVERSITY OF CINCINNATI · PI SCHROEDER, FRIEDHELM · 1989 to 2010
$4.4M
Lipid droplet domains foster lipid storageR01DK070965 · NIDDK · TEXAS A&M AGRILIFE RESEARCH · PI ATSHAVES, BARBARA P · 2007 to 2011
$1.4M
Lipid droplet domains foster lipid storageR56DK070965 · NIDDK · TEXAS A&M UNIVERSITY SYSTEM · PI ATSHAVES, BARBARA P · 2005 to 2005
$73k
NIDDK NIH HHS DK41402NIDDK NIH HHS DK70965NIDDK NIH HHS P30 DK020572NIDDK NIH HHS R01 DK041402NIDDK NIH HHS R01 DK070965NIDDK NIH HHS R56 DK070965
6 · The paper itself

Abstract

Although the human liver fatty acid binding protein (L-FABP) T94A variant arises from the most commonly occurring single-nucleotide polymorphism in the entire FABP family, there is a complete lack of understanding regarding the role of this polymorphism in human disease. It has been hypothesized that the T94A substitution results in the complete loss of ligand binding ability and function analogous to that seen with L-FABP gene ablation. This possibility was addressed using the recombinant human wild-type (WT) T94T and T94A variant L-FABP and cultured primary human hepatocytes. Nonconservative replacement of the medium-sized, polar, uncharged T residue with a smaller, nonpolar, aliphatic A residue at position 94 of the human L-FABP significantly increased the L-FABP α-helical structure content at the expense of β-sheet content and concomitantly decreased the thermal stability. T94A did not alter the binding affinities for peroxisome proliferator-activated receptor α (PPARα) agonist ligands (phytanic acid, fenofibrate, and fenofibric acid). While T94A did not alter the impact of phytanic acid and only slightly altered that of fenofibrate on the human L-FABP secondary structure, the active metabolite fenofibric acid altered the T94A secondary structure much more than that of the WT T94T L-FABP. Finally, in cultured primary human hepatocytes, the T94A variant exhibited a significantly reduced extent of fibrate-mediated induction of PPARα-regulated proteins such as L-FABP, FATP5, and PPARα itself. Thus, while the T94A substitution did not alter the affinity of the human L-FABP for PPARα agonist ligands, it significantly altered the human L-FABP structure, stability, and conformational and functional response to fibrate.

Indexed as

Polymorphism, Single NucleotideAmino Acid SubstitutionAnimalsBinding SitesCells, CulturedFatty Acid-Binding ProteinsFatty Acid Transport ProteinsFenofibrateFibric AcidsGene Expression RegulationHot TemperatureHumansHypolipidemic AgentsLigandsLiverMiceFABP1 protein, humanFatty Acid-Binding ProteinsFatty Acid Transport ProteinsFenofibratefenofibric acidFibric AcidsHypolipidemic AgentsLigandsPhytanic AcidPPAR alphaRecombinant ProteinsSLC27A5 protein, human

Identifiers

PMID24299557
PMCPMC3930105
OpenAlexW2326457293

What OpenQuestion holds

Textmetadata
LicenceTDM
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.