ArticleBiophysical journal2018
Sphingomyelin Stereoisomers Reveal That Homophilic Interactions Cause Nanodomain Formation.
Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 9 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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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.
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Who cites it
9 citing papers in PubMed, 26 citations in OpenAlex.
- Sphingomyelin slows interfacial hydrogen-bonding dynamics in lipid membranes.Biophysical journal · 2025Article
- Polar Glycerolipids and Membrane Lipid Rafts.International journal of molecular sciences · 2024Review
- Molecular substructure of the liquid-ordered phase formed by sphingomyelin and cholesterol: sphingomyelin clusters forming nano-subdomains are a characteristic feature.Biophysical reviews · 2022Article
- Effect of cholesterol on the lactosylceramide domains in phospholipid bilayers.Biophysical journal · 2022Article
- Using cyclodextrin-induced lipid substitution to study membrane lipid and ordered membrane domain (raft) function in cells.Biochimica et biophysica acta. Biomembranes · 2022Review
- Dynamic "Molecular Portraits" of Biomembranes Drawn by Their Lateral Nanoscale Inhomogeneities.International journal of molecular sciences · 2021Review
- Lateral heterogeneity and domain formation in cellular membranes.Chemistry and physics of lipids · 2020Article
- Sphingomyelins and ent-Sphingomyelins Form Homophilic Nano-Subdomains within Liquid Ordered Domains.Biophysical journal · 2020Article
- Cholesterol-Induced Conformational Change in the Sphingomyelin Headgroup.Biophysical journal · 2019Article
Corrections and comments
- Erratum issued
Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sphingomyelin is an abundant lipid in some cellular membrane domains, such as lipid rafts. Hydrogen bonding and hydrophobic interactions of the lipid with surrounding components such as neighboring sphingomyelin and cholesterol (Cho) are widely considered to stabilize the raft-like liquid-ordered (Lo) domains in membrane bilayers. However, details of their interactions responsible for the formation of Lo domains remain largely unknown. In this study, the enantiomer of stearoyl sphingomyelin (ent-SSM) was prepared, and its physicochemical properties were compared with the natural SSM and the diastereomer of SSM to examine possible stereoselective lipid-lipid interactions. Interestingly, differential scanning calorimetry experiments demonstrated that palmitoyl sphingomyelin, with natural stereochemistry, exhibited higher miscibility with SSM bilayers than with ent-SSM bilayers, indicating that the homophilic sphingomyelin interactions occurred in a stereoselective manner. Solid-state
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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.