Evidence map›Paper›PMID 24628888›Full record

ArticleThe FEBS journal2014

Structural and functional interaction of fatty acids with human liver fatty acid-binding protein (L-FABP) T94A variant.

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

Open access · greenAbstract read
In one paragraph

Article in The FEBS journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

27 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
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  8. ΔJournal of lipid research · 2018
    Article
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  10. Impact ofJournal of lipid research · 2017
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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.

Huan HuangDepartment of Physiology and Pharmacology, Texas A&M University, TVMC, College Station, TX, USA.
Avery L McIntosh
Gregory G Martin
Kerstin K Landrock
Danilo Landrock
Shipra Gupta
Barbara P Atshaves
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

The human liver fatty acid-binding protein (L-FABP) T94A variant, the most common in the FABP family, has been associated with elevated liver triglyceride levels. How this amino acid substitution elicits these effects is not known. This issue was addressed using human recombinant wild-type (WT) and T94A variant L-FABP proteins as well as cultured primary human hepatocytes expressing the respective proteins (genotyped as TT, TC and CC). The T94A substitution did not alter or only slightly altered L-FABP binding affinities for saturated, monounsaturated or polyunsaturated long chain fatty acids, nor did it change the affinity for intermediates of triglyceride synthesis. Nevertheless, the T94A substitution markedly altered the secondary structural response of L-FABP induced by binding long chain fatty acids or intermediates of triglyceride synthesis. Finally, the T94A substitution markedly decreased the levels of induction of peroxisome proliferator-activated receptor α-regulated proteins such as L-FABP, fatty acid transport protein 5 and peroxisome proliferator-activated receptor α itself meditated by the polyunsaturated fatty acids eicosapentaenoic acid and docosahexaenoic acid in cultured primary human hepatocytes. Thus, although the T94A substitution did not alter the affinity of human L-FABP for long chain fatty acids, it significantly altered human L-FABP structure and stability, as well as the conformational and functional response to these ligands.

Indexed as

Anilino NaphthalenesulfonatesAnimalsBlotting, WesternCircular DichroismElectrophoresis, Polyacrylamide GelFatty Acid-Binding ProteinsFatty AcidsHumansModels, MolecularProtein Structure, SecondaryRatsRecombinant ProteinsSpectrometry, FluorescenceTriglycerides1-anilino-8-naphthalenesulfonateAnilino NaphthalenesulfonatesFatty Acid-Binding ProteinsFatty AcidsRecombinant ProteinsTriglyceridesfatty acidsL-FABPliverPUFATG

Identifiers

PMID24628888
PMCPMC4014002
OpenAlexW2000409509

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.