Evidence map›Paper›PMID 21504868›Full record

ReviewHuman genomics2011

The human fatty acid-binding protein family: evolutionary divergences and functions.

Rebecca L Smathers, Dennis R Petersen

Open access · goldAbstract readReview
In one paragraph

Review in Human genomics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 232 papers.

0numbers the graph read from it
0cells of the map it votes in
232citing papers in PubMed
8.3field-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

232 citing papers in PubMed, 487 citations in OpenAlex.

  1. Trial
  2. Review
  3. Review
  4. Article
  5. Article
  6. Functional thermodynamics govern the ligand binding to human cytosolic transport proteins.Protein science : a publication of the Protein Society · 2026
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Evaluating FABP5 as a Therapeutic Target for Pain Management.European journal of pain (London, England) · 2026
    Review
  13. Insulin Resistance and Inflammation.International journal of molecular sciences · 2026
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Chemical Probes for Investigating the Endocannabinoid System.Current topics in behavioral neurosciences · 2026
    Review
  20. Review

172 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

2 authors at 1 institution in 1 country.

Rebecca L SmathersMolecular Toxicology and Environmental Health Sciences Program, Department of Pharmaceutical Sciences, University of Colorado Denver, Aurora, CO 80045, USA.
Dennis R Petersen
University of Colorado Denver · US

Funding

Lipid Aldehyde and Ethanol Induced Liver DamageR37AA009300 · NIAAA · UNIVERSITY OF COLORADO DENVER · PI PETERSEN, DENNIS · 2008 to 2017
$4.4M
Proteomic profiling of NASH: disease mechanisms and novel treatmentR01DK074487 · NIDDK · UNIVERSITY OF COLORADO DENVER · PI PETERSEN, DENNIS · 2007 to 2011
$1.5M
Modifications of L-FABP by Reactive Aldehydes in a Model of Chronic ALDF31AA018898 · NIAAA · UNIVERSITY OF COLORADO DENVER · PI SMATHERS MCCULLOUGH, REBECCA LEANNE · 2009 to 2011
$96k
NIAAA NIH HHS 5 F31 AA018898-02NIAAA NIH HHS F31 AA018898NIAAA NIH HHS R37AA09300NIDDK NIH HHS R01 DK074487-01
6 · The paper itself

Abstract

Fatty acid-binding proteins (FABPs) are members of the intracellular lipid-binding protein (iLBP) family and are involved in reversibly binding intracellular hydrophobic ligands and trafficking them throughout cellular compartments, including the peroxisomes, mitochondria, endoplasmic reticulum and nucleus. FABPs are small, structurally conserved cytosolic proteins consisting of a water-filled, interior-binding pocket surrounded by ten anti-parallel beta sheets, forming a beta barrel. At the superior surface, two alpha-helices cap the pocket and are thought to regulate binding. FABPs have broad specificity, including the ability to bind long-chain (C16-C20) fatty acids, eicosanoids, bile salts and peroxisome proliferators. FABPs demonstrate strong evolutionary conservation and are present in a spectrum of species including Drosophila melanogaster, Caenorhabditis elegans, mouse and human. The human genome consists of nine putatively functional protein-coding FABP genes. The most recently identified family member, FABP12, has been less studied.

Indexed as

Evolution, MolecularMultigene FamilyAmino Acid SequenceAnimalsCaenorhabditis elegansDrosophila melanogasterFatty Acid-Binding ProteinsGenome, HumanHumansMiceMolecular Sequence DataProtein Structure, TertiarySpecies SpecificityFatty Acid-Binding Proteins

Identifiers

PMID21504868
PMCPMC3500171
OpenAlexW1972168184

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.