Evidence map›Paper›PMID 25737239›Full record

ArticleScientific reports2015

HDL surface lipids mediate CETP binding as revealed by electron microscopy and molecular dynamics simulation.

Meng Zhang, River Charles, Huimin Tong, Lei Zhang, Mili Patel, Francis Wang, Matthew J Rames, Amy Ren, Kerry-Anne Rye, Xiayang Qiu and 3 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
8.3field-weighted citation impact, top 2% 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

36 citing papers in PubMed, 59 citations in OpenAlex.

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  8. Clot or Not? Reviewing the Reciprocal Regulation Between Lipids and Blood Clotting.Arteriosclerosis, thrombosis, and vascular biology · 2024
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    Article
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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

13 authors at 3 institutions in 1 country.

Meng ZhangThe Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720.
River CharlesThe Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720.
Huimin TongThe Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720.
Lei ZhangThe Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720.
Mili PatelCentre for Vascular Research, University of New South Wales, Kensington, Sydney, NSW 2052, Australia.
Francis WangThe Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720.
Matthew J RamesThe Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720.
Amy RenThe Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720.
Kerry-Anne RyeCentre for Vascular Research, University of New South Wales, Kensington, Sydney, NSW 2052, Australia.
Xiayang QiuPfizer Inc., Groton, Connecticut 06340, USA.
Douglas G JohnsMerck Research Laboratories, Rahway, New Jersey 07065, USA.
M Arthur CharlesSchool of Medicine, University of California, San Francisco, California 94115, USA.
Gang RenThe Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720.
Lawrence Berkeley National Laboratory · USMerck & Co., Inc., Rahway, NJ, USA (United States) · USPfizer (United States) · US

Funding

Structure-Function Relationship Studies of the Plasma Lipid Transfer Proteins CETP and PLTPR01HL115153 · NHLBI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI REN, GANG · 2012 to 2021
$3.9M
Lipoprotein Structure and Function by Individual Particle Electron TomographyR01GM104427 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI REN, GANG · 2013 to 2016
$1.3M
NHLBI NIH HHS R01 HL115153NHLBI NIH HHS R01HL115153NIGMS NIH HHS R01 GM104427
6 · The paper itself

Abstract

Cholesteryl ester transfer protein (CETP) mediates the transfer of cholesterol esters (CE) from atheroprotective high-density lipoproteins (HDL) to atherogenic low-density lipoproteins (LDL). CETP inhibition has been regarded as a promising strategy for increasing HDL levels and subsequently reducing the risk of cardiovascular diseases (CVD). Although the crystal structure of CETP is known, little is known regarding how CETP binds to HDL. Here, we investigated how various HDL-like particles interact with CETP by electron microscopy and molecular dynamics simulations. Results showed that CETP binds to HDL via hydrophobic interactions rather than protein-protein interactions. The HDL surface lipid curvature generates a hydrophobic environment, leading to CETP hydrophobic distal end interaction. This interaction is independent of other HDL components, such as apolipoproteins, cholesteryl esters and triglycerides. Thus, disrupting these hydrophobic interactions could be a new therapeutic strategy for attenuating the interaction of CETP with HDL.

Indexed as

Molecular Dynamics SimulationCholesterol Ester Transfer ProteinsCryoelectron MicroscopyElectron Microscope TomographyHumansHydrophobic and Hydrophilic InteractionsImaging, Three-DimensionalLipoproteins, HDLLiposomesMembrane LipidsMicroscopy, Electron, TransmissionProtein BindingRecombinant ProteinsCETP protein, humanCholesterol Ester Transfer ProteinsLipoproteins, HDLLiposomesMembrane LipidsRecombinant Proteins

Identifiers

PMID25737239
PMCPMC4348656
OpenAlexW1981899962

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.