Evidence map›Paper›PMID 26443794›Full record

ReviewJournal of lipid research2015

Recent insights into the biological functions of liver fatty acid binding protein 1.

GuQi Wang, Herbert L Bonkovsky, Andrew de Lemos, Frank J Burczynski

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of lipid research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 150 papers.

0numbers the graph read from it
0cells of the map it votes in
150citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

150 citing papers in PubMed, 257 citations in OpenAlex.

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  19. Physiological and Metabolic Effects ofAnimals : an open access journal from MDPI · 2026
    Article
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90 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

4 authors at 2 institutions in 3 countries.

GuQi WangJiangxi Normal University, Nanchang, Jiangxi, People's Republic of China Department of Biology, University of North Carolina at Charlotte, Charlotte, NC Carolinas HealthCare System, Charlotte, NC burczyn@cc.umanitoba.ca guqiwang@yahoo.com.
Herbert L BonkovskyDepartment of Biology, University of North Carolina at Charlotte, Charlotte, NC Carolinas HealthCare System, Charlotte, NC Wake Forest Baptist Medical Center, Winston-Salem, NC.
Andrew de LemosCarolinas HealthCare System, Charlotte, NC Wake Forest Baptist Medical Center, Winston-Salem, NC.
Frank J BurczynskiFaculty of Pharmacy, University of Manitoba, Winnipeg, Manitoba, Canada burczyn@cc.umanitoba.ca guqiwang@yahoo.com.
Carolinas Healthcare System · USUniversity of Manitoba · CA

Funding

Porphyrias Consortium: SupplementU54DK083909 · NIDDK · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI BALWANI, MANISHA, DESNICK, ROBERT J · 2009 to 2023
$18.5M
University of North Carolina Clinical Center for DILINU01DK065201 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI PAUL B WATKINS · 2003 to 2026
$7.3M
Effect of Heme on mRNA and miRNA ProfilesR15HL117199 · NHLBI · WINSTON-SALEM STATE UNIVERSITY · PI BONKOVSKY, HERBERT L · 2013 to 2013
$432k
NHLBI NIH HHS HL117199NHLBI NIH HHS R15 HL117199NIDDK NIH HHS DK065201NIDDK NIH HHS DK083909NIDDK NIH HHS U01 DK065201NIDDK NIH HHS U54 DK083909
6 · The paper itself

Abstract

Over four decades have passed since liver fatty acid binding protein (FABP)1 was first isolated. There are few protein families for which most of the complete tertiary structures, binding properties, and tissue occurrences are described in such detail and yet new functions are being uncovered for this protein. FABP1 is known to be critical for fatty acid uptake and intracellular transport and also has an important role in regulating lipid metabolism and cellular signaling pathways. FABP1 is an important endogenous cytoprotectant, minimizing hepatocyte oxidative damage and interfering with ischemia-reperfusion and other hepatic injuries. The protein may be targeted for metabolic activation through the cross-talk among many transcriptional factors and their activating ligands. Deficiency or malfunction of FABP1 has been reported in several diseases. FABP1 also influences cell proliferation during liver regeneration and may be considered as a prognostic factor for hepatic surgery. FABP1 binds and modulates the action of many molecules such as fatty acids, heme, and other metalloporphyrins. The ability to bind heme is another cytoprotective property and one that deserves closer investigation. The role of FABP1 in substrate availability and in protection from oxidative stress suggests that FABP1 plays a pivotal role during intracellular bacterial/viral infections by reducing inflammation and the adverse effects of starvation (energy deficiency).

Indexed as

AnimalsFatty Acid-Binding ProteinsHumansLipid MetabolismLiverOxidative StressFatty Acid-Binding Proteinsfatty liverhemeinfectioninflammationliver regenerationmetalloporphyrinsnonalcoholic fatty liver diseaseoxidative stresssteatosis

Identifiers

PMID26443794
PMCPMC4655993
OpenAlexW2179972854

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.