ArticleArchives of biochemistry and biophysics2010
Extracellular hydrophobic regions in scavenger receptor BI play a key role in mediating HDL-cholesterol transport.
Article in Archives of biochemistry and biophysics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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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.
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Who cites it
22 citing papers in PubMed, 35 citations in OpenAlex.
- HDLR-SR-BI Expression and Cholesterol Uptake are Regulated via Indoleamine-2,3-dioxygenase 1 in Macrophages under Inflammation.Langmuir : the ACS journal of surfaces and colloids · 2025Article
- SR-B1's Next Top Model: Structural Perspectives on the Functions of the HDL Receptor.Current atherosclerosis reports · 2022Review
- Expression of SR-BI and LXRContrast media & molecular imaging · 2022Article
- Good Cholesterol Gone Bad? HDL and COVID-19.International journal of molecular sciences · 2021Review
- Human variant of scavenger receptor BI (R174C) exhibits impaired cholesterol transport functions.Journal of lipid research · 2021Article
- Proline residues in scavenger receptor-BI's C-terminal region support efficient cholesterol transport.The Biochemical journal · 2019Article
- Scavenger receptor B type 1: expression, molecular regulation, and cholesterol transport function.Journal of lipid research · 2018Review
- Single amino acid mutation of SR-BI decreases infectivity of hepatitis C virus derived from cell culture in a cell culture model.World journal of gastroenterology · 2017Article
- NMR Structure of the C-Terminal Transmembrane Domain of the HDL Receptor, SR-BI, and a Functionally Relevant Leucine Zipper Motif.Structure (London, England : 1993) · 2017Article
- Tryptophan 415 Is Critical for the Cholesterol Transport Functions of Scavenger Receptor BI.Biochemistry · 2016Article
- Oxidized LDL-bound CD36 recruits an Na⁺/K⁺-ATPase-Lyn complex in macrophages that promotes atherosclerosis.Science signaling · 2015Article
- Expression, purification and reconstitution of the C-terminal transmembrane domain of scavenger receptor BI into detergent micelles for NMR analysis.Protein expression and purification · 2015Article
- Article
- SR-BI/CD36 chimeric receptors define extracellular subdomains of SR-BI critical for cholesterol transport.Biochemistry · 2014Article
- New developments in selective cholesteryl ester uptake.Current opinion in lipidology · 2013Review
- Functional genomics of the human high-density lipoprotein receptor scavenger receptor BI: an old dog with new tricks.Current opinion in endocrinology, diabetes, and obesity · 2013Review
- CD36 homolog divergence is responsible for the selectivity of carotenoid species migration to the silk gland of the silkworm Bombyx mori.Journal of lipid research · 2013Article
- Article
- C323 of SR-BI is required for SR-BI-mediated HDL binding and cholesteryl ester uptake.Journal of lipid research · 2011Article
- Extracellular disulfide bonds support scavenger receptor class B type I-mediated cholesterol transport.Biochemistry · 2011Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The binding of high density lipoprotein (HDL) to scavenger receptor BI (SR-BI) is responsible for whole-body cholesterol disposal via reverse cholesterol transport. The extracellular domain of SR-BI is required for HDL binding and selective uptake of HDL-cholesterol. We identified six highly hydrophobic regions in this domain that may be important for receptor activity and performed site-directed mutagenesis to investigate the importance of these regions in SR-BI-mediated cholesterol transport. Non-conservative mutation of the regions encompassing V67, L140/L142, V164 or V221 reduced hydrophobicity and impaired the ability of SR-BI to bind HDL, mediate selective uptake of HDL-cholesterol, promote cholesterol efflux, and enlarge the cholesterol oxidase-sensitive pool of membrane free cholesterol. In contrast, conservative mutations at V67, V164 or V221 did not affect the hydrophobicity or these cholesterol transport activities. We conclude that the hydrophobicity of N-terminal extracellular regions of SR-BI is critical for cholesterol transport, possibly by mediating receptor-ligand and/or receptor-membrane interactions.
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Registered trials
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.