Evidence map›Paper›PMID 19141679›Full record

ReviewAmerican journal of physiology. Endocrinology and metabolism2009

Acyl-coenzyme A:cholesterol acyltransferases.

Ta-Yuan Chang, Bo-Liang Li, Catherine C Y Chang, Yasuomi Urano

Open access · greenAbstract readReview
In one paragraph

Review in American journal of physiology. Endocrinology and metabolism, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 244 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
244citing papers in PubMed, 1 pooled it
21.8field-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.

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

244 citing papers in PubMed, 1 synthesis or guideline pooled it, 503 citations in OpenAlex.

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184 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 1 institution in 1 country.

Ta-Yuan ChangDepartment of Biochemistry, Dartmouth Medical School, 1 Rope Ferry Rd., Hanover, NH 03755-1404, USA. Ta.Yuan.Chang@Dartmouth.edu
Bo-Liang Li
Catherine C Y Chang
Yasuomi Urano
Dartmouth College · US

Funding

STRUCTURE/FUNCTION ANALYSIS OF ACATR01HL060306 · NHLBI · DARTMOUTH COLLEGE · PI CHANG, TA YUAN · 1998 to 2015
$5.5M
NHLBI NIH HHS HL-36705NHLBI NIH HHS HL-60306
6 · The paper itself

Abstract

The enzymes acyl-coenzyme A (CoA):cholesterol acyltransferases (ACATs) are membrane-bound proteins that utilize long-chain fatty acyl-CoA and cholesterol as substrates to form cholesteryl esters. In mammals, two isoenzymes, ACAT1 and ACAT2, encoded by two different genes, exist. ACATs play important roles in cellular cholesterol homeostasis in various tissues. This chapter summarizes the current knowledge on ACAT-related research in two areas: 1) ACAT genes and proteins and 2) ACAT enzymes as drug targets for atherosclerosis and for Alzheimer's disease.

Indexed as

Amino Acid SequenceAnimalsHumansLipid MetabolismModels, BiologicalMolecular Sequence DataProtein ConformationSterol O-AcyltransferaseSterol O-Acyltransferase

Identifiers

PMID19141679
PMCPMC2711667
OpenAlexW3185413432

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.