Evidence map›Paper›PMID 21399642›Full record

ArticleNature structural & molecular biology2011

Apolipoprotein A-I structural organization in high-density lipoproteins isolated from human plasma.

Rong Huang, R A Gangani D Silva, W Gray Jerome, Anatol Kontush, M John Chapman, Linda K Curtiss, Timothy J Hodges, W Sean Davidson

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 113 papers.

0numbers the graph read from it
0cells of the map it votes in
113citing papers in PubMed
17.4field-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

113 citing papers in PubMed, 241 citations in OpenAlex.

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53 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

8 authors at 4 institutions in 2 countries.

Rong HuangDepartment of Pathology and Laboratory Medicine, University of Cincinnati, Cincinnati, Ohio, USA.
R A Gangani D Silva
W Gray Jerome
Anatol Kontush
M John Chapman
Linda K Curtiss
Timothy J Hodges
W Sean Davidson
University of Cincinnati · USSorbonne Université · FRScripps Research Institute · USVanderbilt University Medical Center · US

Funding

Tumor Immunology and Microenvironment Research ProgramP30CA068485 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI MATTHEW J TYSKA · 1995 to 2026
$172.8M
Translational Analysis CoreP30DK058404 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI RICHARD M. PEEK · 2002 to 2026
$29.9M
Vanderbilt Diabetes Research CenterP30DK020593 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI OWEN P MCGUINNESS · 2012 to 2026
$29.3M
TRANSGENIC MOUSE/ ES CELL SHARES RESOURCESP60DK020593 · NIDDK · VANDERBILT UNIVERSITY · PI MCGUINNESS, OWEN P · 1986 to 2011
$28.1M
Apolipoprotein A-I structure in high density lipoproteinsR01HL067093 · NHLBI · UNIVERSITY OF CINCINNATI · PI DAVIDSON, W SEAN · 2002 to 2016
$4.3M
The role of apolipoprotein A-II in the modulation of HDL functionR00HL087561 · NHLBI · UNIVERSITY OF CINCINNATI · PI SILVA, RANASINGHE · 2009 to 2011
$742k
The Role of Apolipoprotein A-II in the Modulation of HDL FunctionK99HL087561 · NHLBI · UNIVERSITY OF CINCINNATI · PI SILVA, RANASINGHE · 2007 to 2008
$174k
GENDER DIFFERENCES IN FAMILIAL RISKR01HL048148 · NHLBI · VIRGINIA COMMONWEALTH UNIVERSITY · PI EAVES, LINDON J · 1993 to 1995
–
NCI NIH HHS CA68485NCI NIH HHS P30 CA068485NHLBI NIH HHS HL087561NHLBI NIH HHS HL48148NHLBI NIH HHS HL67093NHLBI NIH HHS K99 HL087561NHLBI NIH HHS R00 HL087561NHLBI NIH HHS R01 HL067093NIDDK NIH HHS DK20593NIDDK NIH HHS DK58404NIDDK NIH HHS P30 DK020593NIDDK NIH HHS P30 DK058404NIDDK NIH HHS P60 DK020593
6 · The paper itself

Abstract

High-density lipoproteins (HDLs) mediate cholesterol transport and protection from cardiovascular disease. Although synthetic HDLs have been studied for 30 years, the structures of human plasma-derived HDL and its major protein apolipoprotein apoA-I are unknown. We separated normal human HDL into five density subfractions and then further isolated those containing predominantly apoA-I (LpA-I). Using cross-linking chemistry and mass spectrometry, we found that apoA-I adopts a structural framework in these particles that closely mirrors that in synthetic HDL. We adapted established structures for synthetic HDL to generate the first detailed models of authentic human plasma HDL in which apoA-I adopts a symmetrical cage-like structure. The models suggest that HDL particle size is modulated by means of a twisting motion of the resident apoA-I molecules. This understanding offers insights into how apoA-I structure modulates HDL function and its interactions with other apolipoproteins.

Indexed as

Apolipoprotein A-IElectrophoresis, Polyacrylamide GelHumansLipoproteins, HDLProtein ConformationSpectrometry, Mass, Electrospray IonizationTandem Mass SpectrometryApolipoprotein A-ILipoproteins, HDL

Identifiers

PMID21399642
PMCPMC3079355
OpenAlexW1964556269

What OpenQuestion holds

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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.