Evidence map›Paper›PMID 20846931›Full record

ArticleHuman genomics2010

Evolutionary divergence and functions of the human acyl-CoA thioesterase gene ( ACOT ) family.

Chad Brocker, Christopher Carpenter, Daniel W Nebert, Vasilis Vasiliou

Open access · goldAbstract read
In one paragraph

Article in Human genomics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

56 citing papers in PubMed, 89 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

4 authors at 2 institutions in 1 country.

Chad BrockerMolecular Toxicology and Environmental Health Sciences Program, Department of Pharmaceutical Sciences, University of Colorado Denver, Aurora, CO 80045, USA.
Christopher Carpenter
Daniel W Nebert
Vasilis Vasiliou
University of Colorado Denver · USUniversity of Cincinnati · US

Funding

REPRODUCTIVE AND DEVELOPMENTAL TOXICOLOGY RESEARCHP30ES006096 · NIEHS · UNIVERSITY OF CINCINNATI · PI YADAV, JAGJIT S · 1992 to 2022
$35.4M
Novel Role of Corneal Crystallins as Modulators of Cell Growth and TransparencyR01EY017963 · NEI · YALE UNIVERSITY · PI VASILIOU, VASILIS · 2007 to 2019
$3.7M
Role of Mitochondrial Aldehyde Dehydrogenases in Ethanol Metabolism and ToxicityR21AA017754 · NIAAA · UNIVERSITY OF COLORADO DENVER · PI VASILIOU, VASILIS · 2009 to 2010
$411k
NEI NIH HHS R01EY17963NIAAA NIH HHS R21AA017754NIEHS NIH HHS P30ES06096
6 · The paper itself

Abstract

The acyl-CoA thioesterase gene (ACOT ) family encodes enzymes that catalyse the hydrolysis of acyl-CoA thioester compounds, also known as activated fatty acids, to their corresponding non-esterified (free) fatty acid and coenzyme A (CoASH). These enzymes play a very important role in lipid metabolism by maintaining cellular levels and proper ratios of free and activated fatty acids, as well as CoASH. Within the acyl-CoA family there are two distinct subgroups, type I and type II. Despite catalysing the same reaction, the two groups are not structurally similar and do not share sequence homology, strongly suggesting convergent evolution. This suggestion is further supported if one compares the human with the mouse and rat ACOT gene families. To date, four human type I ACOTs have been identified which belong to the α/β-hydrolase fold enzyme superfamily. Type II ACOTs fall into the 'hot dog' fold superfamily. There are currently six human type II genes; however, two homologous proteins, thioesterase superfamily members 4 (THEM4) and 5 (THEM5) share common type II structural features and, in the case of THEM4, acyl-CoA thioesterase activity--suggesting that the family may be larger than previously realised. Although recent studies have greatly expanded the current understanding of these proteins and their physiological importance, there are a number of members whose functions are relatively unexplored and which warrant further investigation.

Indexed as

Evolution, MolecularGenetic VariationAnimalsHumansMiceMultigene FamilyPhylogenyProtein Structure, TertiaryRatsSequence Homology, Amino AcidThiolester HydrolasesThiolester Hydrolases

Identifiers

PMID20846931
PMCPMC3525216
OpenAlexW2111993410

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.