Evidence map›Paper›PMID 18757836›Full record

ReviewJournal of lipid research2008

Thematic review series: glycerolipids. DGAT enzymes and triacylglycerol biosynthesis.

Chi-Liang Eric Yen, Scot J Stone, Suneil Koliwad, Charles Harris, Robert V Farese

Registry-linked trialOpen access · hybridAbstract readReview
In one paragraph

Review in Journal of lipid research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT02366156 (A Randomized, Double-Blind, 3-Period Crossover Study to Evaluate the Effects of a Dietary Supplement Containing Botanical Extracts on Fasting and Postprandial Lipid Metabolism in Apparently Healthy, Overweight and Obese Individuals), which is not on this map. Cited by 530 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
530citing papers in PubMed, 2 pooled it
27.0field-weighted citation impact, top 1% 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.

NCT02366156 nacompletednot on this mapstarted 2014, after this paper: background citation

A Randomized, Double-Blind, 3-Period Crossover Study to Evaluate the Effects of a Dietary Supplement Containing Botanical Extracts on Fasting and Postprandial Lipid Metabolism in Apparently Healthy, Overweight and Obese Individuals

TypeinterventionalSponsorAccess Business GroupRan2014 to 2015Enrolled93ConditionsHyperlipidemiaArmsPlacebo, Low Dose Grape Blend, High Dose Grape Blend
3 · Its place in the literature

Who cites it

530 citing papers in PubMed, 2 syntheses or guidelines pooled it, 1,067 citations in OpenAlex.

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470 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 4 institutions in 2 countries.

Chi-Liang Eric YenDepartment of Nutritional Sciences, University of Wisconsin, Madison, WI 53706, USA.
Scot J Stone
Suneil Koliwad
Charles Harris
Robert V Farese
Gladstone Institutes · USUniversity of California, San Francisco · USUniversity of Saskatchewan · CAUniversity of Wisconsin–Madison · US

Funding

ROLE OF DGAT IN TRIACYLGLYCEROL METABOLISMR01DK056084 · NIDDK · J. DAVID GLADSTONE INSTITUTES · PI FARESE, ROBERT V · 2000 to 2014
$6.4M
Role of DGAT in Triacyglycerol MetabolismR56DK056084 · NIDDK · J. DAVID GLADSTONE INSTITUTES · PI FARESE, ROBERT V · 2010 to 2010
$290k
NIDDK NIH HHS DK-56084NIDDK NIH HHS R01 DK056084NIDDK NIH HHS R56 DK056084
6 · The paper itself

Abstract

Triacylglycerols (triglycerides) (TGs) are the major storage molecules of metabolic energy and FAs in most living organisms. Excessive accumulation of TGs, however, is associated with human diseases, such as obesity, diabetes mellitus, and steatohepatitis. The final and the only committed step in the biosynthesis of TGs is catalyzed by acyl-CoA:diacylglycerol acyltransferase (DGAT) enzymes. The genes encoding two DGAT enzymes, DGAT1 and DGAT2, were identified in the past decade, and the use of molecular tools, including mice deficient in either enzyme, has shed light on their functions. Although DGAT enzymes are involved in TG synthesis, they have distinct protein sequences and differ in their biochemical, cellular, and physiological functions. Both enzymes may be useful as therapeutic targets for diseases. Here we review the current knowledge of DGAT enzymes, focusing on new advances since the cloning of their genes, including possible roles in human health and diseases.

Indexed as

AnimalsDiacylglycerol O-AcyltransferaseGlycerolHumansIsoenzymesLipogenesisTriglyceridesDGAT1 protein, humanDGAT2 protein, humanDiacylglycerol O-AcyltransferaseGlycerolIsoenzymesTriglycerides

Identifiers

PMID18757836
PMCPMC3837458
OpenAlexW2011185005

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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.