ArticleRSC advances2025
Non-erythrocyte spectrin network preferentially stabilizes flat membrane and enhances cell stiffness.
Article in RSC advances, 2025. 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
1 citing paper in PubMed.
- An Unbiased Geometry-Resolved Membrane Platform for Proteome-Scale Discovery of Membrane Curvature Sensors.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Spectrin αII and βII, the predominant non-erythroid isoforms, assemble into cytoskeletal networks that shape the plasma membrane. However, how these networks interact with membranes of different curvatures remains unclear. Using microfluidic deformation cytometry, we show that spectrin βII overexpression increases the apparent stiffness of MDA-MB-231 breast cancer cells. Fluorescence microscopy further demonstrates that spectrin is excluded from highly curved regions and enriched on flatter membranes
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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.