Evidence map›Paper›PMID 25211142›Full record

ArticleBiochemistry2014

SR-BI/CD36 chimeric receptors define extracellular subdomains of SR-BI critical for cholesterol transport.

Gabriella A Kartz, Rebecca L Holme, Kay Nicholson, Daisy Sahoo

Abstract read
In one paragraph

Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

17 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
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  9. High-density lipoprotein receptor SCARB1 is required for carotenoid coloration in birds.Proceedings of the National Academy of Sciences of the United States of America · 2017
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  14. Scavenger receptor class B, type I-mediated uptake of A1AT by pulmonary endothelial cells.American journal of physiology. Lung cellular and molecular physiology · 2015
    Article
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  17. Review
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.

Gabriella A KartzDepartments of Pharmacology & Toxicology, ‡Biochemistry, and §Medicine, Medical College of Wisconsin , Milwaukee, Wisconsin 53226, United States.
Rebecca L Holme
Kay Nicholson
Daisy Sahoo
Medical College of Wisconsin · US

Funding

Selective Uptake and Hydrolysis of Cholesteryl Ester by SR-BIR01HL058012 · NHLBI · STATE UNIVERSITY NEW YORK STONY BROOK · PI SAHOO, DAISY · 1997 to 2023
$8.6M
NHLBI NIH HHS R01 HL058012NHLBI NIH HHS R01HL058012
6 · The paper itself

Abstract

High-density lipoproteins (HDLs) are athero-protective, primarily because of their ability to promote cholesterol flux from peripheral tissues to the liver by reverse cholesterol transport (RCT). The delivery of HDL-cholesteryl esters (CE) into cells is mediated by the HDL receptor, scavenger receptor class B type I (SR-BI), a promising target for enhancing whole body cholesterol disposal and preventing cardiovascular disease. A detailed understanding of the structural determinants underlying proper SR-BI/HDL alignment that supports the selective uptake of HDL-CE into cells remains lacking. To this end, we exploited CD36, a class B scavenger receptor with a predicted topology similar to that of SR-BI that binds HDL but is unable to mediate efficient selective uptake of HDL-CE. We generated a series of SR-BI/CD36 chimeric receptors that span the extracellular (EC) domain of SR-BI to delineate regions that are essential for SR-BI's cholesterol transport functions. All 16 SR-BI/CD36 chimeras were transiently expressed in COS-7 cells, and their plasma membrane localization was confirmed. The majority of SR-BI/CD36 chimeric receptors displayed significant reductions in their ability to (i) bind HDL, (ii) deliver HDL-CE to cells, (iii) mediate efflux of free cholesterol (FC) to HDL, and (iv) redistribute plasma membrane domains of FC. We also demonstrated that changes in SR-BI function were independent of receptor oligomerization. Altogether, we have identified discrete subdomains, particularly in the N-terminal and C-terminal regions of the EC domain of SR-BI, that are critical for productive receptor-ligand interactions and the various cholesterol transport functions of SR-BI.

Indexed as

Amino Acid SequenceAnimalsBinding SitesBiological TransportCD36 AntigensChlorocebus aethiopsCholesterolCOS CellsElectrophoresis, Polyacrylamide GelLipoproteins, HDLMiceMolecular Sequence DataProtein MultimerizationProtein Structure, TertiaryRatsRecombinant Fusion ProteinsCD36 AntigensCholesterolLipoproteins, HDLRecombinant Fusion Proteins

Identifiers

PMID25211142
PMCPMC4188264
OpenAlexW2317344102

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.