Evidence map›Paper›PMID 28011707›Full record

ArticleJournal of lipid research2017

Fatty acid binding profile of the liver X receptor α.

Shimpi Bedi, Genesis Victoria Hines, Valery V Lozada-Fernandez, Camila de Jesus Piva, Alagammai Kaliappan, S Dean Rider, Heather A Hostetler

Open access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed, 21 citations in OpenAlex.

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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

7 authors at 1 institution in 1 country.

Shimpi BediDepartment of Biochemistry and Molecular Biology, Boonshoft School of Medicine, Wright State University, Dayton, OH 45435.
Genesis Victoria HinesDepartment of Biochemistry and Molecular Biology, Boonshoft School of Medicine, Wright State University, Dayton, OH 45435.
Valery V Lozada-FernandezDepartment of Biochemistry and Molecular Biology, Boonshoft School of Medicine, Wright State University, Dayton, OH 45435.
Camila de Jesus PivaDepartment of Biochemistry and Molecular Biology, Boonshoft School of Medicine, Wright State University, Dayton, OH 45435.
Alagammai KaliappanDepartment of Biochemistry and Molecular Biology, Boonshoft School of Medicine, Wright State University, Dayton, OH 45435.
S Dean RiderDepartment of Biochemistry and Molecular Biology, Boonshoft School of Medicine, Wright State University, Dayton, OH 45435 s.dean.rider@wright.edu.
Heather A HostetlerDepartment of Biochemistry and Molecular Biology, Boonshoft School of Medicine, Wright State University, Dayton, OH 45435.
Wright State University · US

Funding

PREP ScholarsR25GM086257 · NIGMS · WRIGHT STATE UNIVERSITY · PI CZERWINSKI, STEFAN A. · 2010 to 2013
$1.2M
The role of long chain acyl-CoAs in nuclear receptor regulationR00DK077573 · NIDDK · WRIGHT STATE UNIVERSITY · PI HOSTETLER, HEATHER A · 2009 to 2011
$747k
The role of long chain acyl-CoAs in nuclear receptor regulationK99DK077573 · NIDDK · TEXAS A&M AGRILIFE RESEARCH · PI HOSTETLER, HEATHER A · 2007 to 2008
$179k
NIDDK NIH HHS K99 DK077573NIDDK NIH HHS R00 DK077573NIGMS NIH HHS R25 GM086257
6 · The paper itself

Abstract

Liver X receptor (LXR)α is a nuclear receptor that responds to oxysterols and cholesterol overload by stimulating cholesterol efflux, transport, conversion to bile acids, and excretion. LXRα binds to and is regulated by synthetic (T-0901317, GW3695) and endogenous (oxysterols) ligands. LXRα activity is also modulated by FAs, but the ligand binding specificity of FA and acyl-CoA derivatives for LXRα remains unknown. We investigated whether LXRα binds FA or FA acyl-CoA with affinities that mimic in vivo concentrations, examined the effect of FA chain length and the degree of unsaturation on binding, and investigated whether FAs regulate LXRα activation. Saturated medium-chain FA (MCFA) displayed binding affinities in the low nanomolar concentration range, while long-chain fatty acyl-CoA did not bind or bound weakly to LXRα. Circular dichroic spectra and computational docking experiments confirmed that MCFA bound to the LXRα ligand binding pocket similar to the known synthetic agonist of LXRα (T0901317), but with limited change to the conformation of the receptor. Transactivation assays showed that MCFA activated LXRα, whereas long-chain FA caused no effect. Our results suggest that LXRα functions as a receptor for saturated FA or acyl-CoA of C

Indexed as

Acyl Coenzyme AAnimalsBenzenesulfonamidesChlorocebus aethiopsCholesterolCOS CellsFatty AcidsFluorocarbonsHumansHydrocarbons, FluorinatedLigandsLiver X ReceptorsOxysterolsProtein BindingSulfonamidesAcyl Coenzyme ABenzenesulfonamidesCholesterolFatty AcidsFluorocarbonsHydrocarbons, FluorinatedLigandsLiver X ReceptorsOxysterolsSulfonamidesT0901317endogenous ligandhuman liver X receptor αlong-chain fatty acidlong-chain fatty acyl-coenzyme Amedium-chain fatty acidperoxisome proliferator-activated receptortranscription factor

Identifiers

PMID28011707
PMCPMC5282955
OpenAlexW2567363250

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.