ArticleJournal of the American Chemical Society2026
Distinct, Phase-Dependent Orientations of GPI and GPI-Anchored Proteins in Lipid Bilayers Revealed Using Spin Labeling and Power Saturation Electron Paramagnetic Resonance Depth Profiling.
Article in Journal of the American Chemical Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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.
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.
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Who cites it
1 citing paper in PubMed.
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Authors and funding
6 authors.
Funding
Abstract
Glycosylphosphatidylinositols (GPIs) help anchor and organize surface proteins, while the interfacial conformations of GPIs and GPI-anchored proteins (GPI-APs) on cells, which determine their functions, remain unclear. In this work, a bifunctional GPI anchor bearing clickable azide and biotin─an affinity tag─was used to access labeled GPI anchors and GPI-AP analogs. Employing spin-labeled GPI and GPI-streptavidin conjugate as probes, together with spin-labeled "ruler" lipids and power saturation electron paramagnetic resonance (EPR) profiling, we quantified their accessibilities to membrane-tethered and soluble spin relaxants, with the probes and rulers incorporated in 1-palmitoyl-2-oleoyl-
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Registered trials
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