Evidence map›Paper›PMID 24692551›Full record

ArticleThe Journal of biological chemistry2014

Structural basis for ligand regulation of the fatty acid-binding protein 5, peroxisome proliferator-activated receptor β/δ (FABP5-PPARβ/δ) signaling pathway.

Eric H Armstrong, Devrishi Goswami, Patrick R Griffin, Noa Noy, Eric A Ortlund

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

71 citing papers in PubMed, 125 citations in OpenAlex.

  1. Trial
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  4. Functional thermodynamics govern the ligand binding to human cytosolic transport proteins.Protein science : a publication of the Protein Society · 2026
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11 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

5 authors at 3 institutions in 1 country.

Eric H ArmstrongFrom the Department of Biochemistry, Discovery and Developmental Therapeutics, Winship Cancer Institute, Emory University School of Medicine, Atlanta, Georgia 30322.
Devrishi Goswamithe Department of Molecular Therapeutics, The Scripps Research Institute, Jupiter, Florida 33458, and.
Patrick R Griffinthe Department of Molecular Therapeutics, The Scripps Research Institute, Jupiter, Florida 33458, and.
Noa Noythe Departments of Pharmacology and Nutrition, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106.
Eric A OrtlundFrom the Department of Biochemistry, Discovery and Developmental Therapeutics, Winship Cancer Institute, Emory University School of Medicine, Atlanta, Georgia 30322, eortlun@emory.edu.
Emory University · USScripps Research Institute · USUniversity School · US

Funding

Winship Cancer Institute Cancer Center Support GrantP30CA138292 · NCI · EMORY UNIVERSITY · PI Suresh S Ramalingam · 2009 to 2026
$47.5M
Graduate Training in the Pharmacological StudiesT32GM008602 · NIGMS · EMORY UNIVERSITY · PI HALL, RANDY A. · 1996 to 2021
$5.1M
FUNCTIONS OF INTRACELLULAR LIPID-BINDING PROTEINSR01DK060684 · NIDDK · CORNELL UNIVERSITY ITHACA · PI BROWN, JONATHAN MARK · 2002 to 2015
$4.3M
Acquisition of a LTQ/Orbitrap MS to advance the study of protein dynamicsS10RR027270 · NCRR · SCRIPPS RESEARCH INSTITUTE, THE · PI GRIFFIN, PATRICK ROBERT · 2010 to 2010
$500k
NCI NIH HHS P30 CA138292NCI NIH HHS P30CA138292NCRR NIH HHS S10 RR027270NIDDK NIH HHS R01 DK060684NIGMS NIH HHS 5T32GM008602NIGMS NIH HHS T32 GM008602
6 · The paper itself

Abstract

Fatty acid-binding proteins (FABPs) are a widely expressed group of calycins that play a well established role in solubilizing cellular fatty acids. Recent studies, however, have recast FABPs as active participants in vital lipid-signaling pathways. FABP5, like its family members, displays a promiscuous ligand binding profile, capable of interacting with numerous long chain fatty acids of varying degrees of saturation. Certain "activating" fatty acids induce the protein's cytoplasmic to nuclear translocation, stimulating PPARβ/δ transactivation; however, the rules that govern this process remain unknown. Using a range of structural and biochemical techniques, we show that both linoleic and arachidonic acid elicit FABP5's translocation by permitting allosteric communication between the ligand-sensing β2 loop and a tertiary nuclear localization signal within the α-helical cap of the protein. Furthermore, we show that more saturated, nonactivating fatty acids inhibit nuclear localization signal formation by destabilizing this activation loop, thus implicating FABP5 specifically in cis-bonded, polyunsaturated fatty acid signaling.

Indexed as

AnimalsArachidonic AcidBinding SitesCell NucleusChlorocebus aethiopsCOS CellsCytoplasmFatty Acid-Binding ProteinsFatty AcidsHumansLigandsLinoleic AcidMCF-7 CellsModels, MolecularMolecular StructureMutationArachidonic AcidFABP5 protein, humanFatty Acid-Binding ProteinsFatty AcidsLigandsLinoleic AcidNuclear Localization SignalsPPAR-betaPPAR gammaFatty AcidFatty Acid-binding ProteinLipidsNuclear ReceptorsPolyunsaturated Fatty AcidsStructural Biology

Identifiers

PMID24692551
PMCPMC4031543
OpenAlexW2800440062

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.