ArticleBiochimica et biophysica acta2007
Scavenger receptor class B, type I (SR-BI) homo-dimerizes via its C-terminal region: fluorescence resonance energy transfer analysis.
Article in Biochimica et biophysica acta, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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The trial behind it
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Who cites it
25 citing papers in PubMed, 36 citations in OpenAlex.
- High-density lipoprotein cholesterol: how studying the 'good cholesterol' could improve cardiovascular health.Open biology · 2025Review
- SR-B1's Next Top Model: Structural Perspectives on the Functions of the HDL Receptor.Current atherosclerosis reports · 2022Review
- Pathways and Mechanisms of Cellular Cholesterol Efflux-Insight From Imaging.Frontiers in cell and developmental biology · 2022Review
- Inherited Variants inCirculation research · 2021Article
- Endothelial Cell Receptors in Tissue Lipid Uptake and Metabolism.Circulation research · 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
- SR-BI: A Multifunctional Receptor in Cholesterol Homeostasis and Atherosclerosis.Trends in endocrinology and metabolism: TEM · 2017Review
- Critical residues and motifs for homodimerization of the first transmembrane domain of the plasma membrane glycoprotein CD36.The Journal of biological chemistry · 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
- What does procollagen C-endopeptidase enhancer protein 2 have to do with HDL-cholesteryl ester uptake? Or how I learned to stop worrying and love reverse cholesterol transport?Current opinion in lipidology · 2015Review
- Procollagen C-endopeptidase Enhancer Protein 2 (PCPE2) Reduces Atherosclerosis in Mice by Enhancing Scavenger Receptor Class B1 (SR-BI)-mediated High-density Lipoprotein (HDL)-Cholesteryl Ester Uptake.The Journal of biological chemistry · 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
- 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
- Extracellular disulfide bonds support scavenger receptor class B type I-mediated cholesterol transport.Biochemistry · 2011Article
- Glycine dimerization motif in the N-terminal transmembrane domain of the high density lipoprotein receptor SR-BI required for normal receptor oligomerization and lipid transport.The Journal of biological chemistry · 2011Article
- Scavenger receptor class B member 1 protein: hepatic regulation and its effects on lipids, reverse cholesterol transport, and atherosclerosis.Hepatic medicine : evidence and research · 2011Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Expression of the scavenger receptor class B, type I (SR-BI) receptor facilitates high density lipoprotein cholesterol transport and correlates with protection against atherosclerosis. Studies have shown that SR-BI self-associates, but many of the techniques used to characterize SR-BI homo-oligomerization were wrought with the prospect of producing artifacts. Therefore, we employed fluorescence resonance energy transfer (FRET) to visualize SR-BI homo-oligomerization with the benefit of gaining information about its quaternary structure in the absence of typical membrane receptor artifacts. To this end, SR-BI was tagged at the N- or C-termini with either cyan (CFP) or yellow (YFP) fluorescent protein. To test whether SR-BI subunits oligomerize through N-N, N-C or C-C terminal interactions, we co-expressed the appropriate SR-BI fusion protein combinations in COS-7 cells and measured live-cell FRET following acceptor photobleaching. We did not observe FRET with co-transfection of SR-BI with CFP and YFP at the N-termini nor at the N- and C-termini, suggesting that the N-termini are not proximal to each other or to the C-termini. However, FRET was observed with co-transfection of SR-BI with CFP and YFP at the C-termini, suggesting that the C-terminal ends are within 10 nm of each other, consistent with SR-BI dimerization via its C-terminal region.
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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.