ArticleeLife2021
Cryo-EM structures of the caspase-activated protein XKR9 involved in apoptotic lipid scrambling.
Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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.
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
27 citing papers in PubMed, 40 citations in OpenAlex.
- The SLC-ome of membrane transport: from molecular discovery to physiology and clinical applications.Physiological reviews · 2026Review
- Article
- The Xkr protein family-From apoptosis executors to diverse physiological functions regulators.FEBS letters · 2026Review
- Strategic advances for cryo-EM structural studies of small (<100 kDa) GPCRs.Communications biology · 2026Review
- Structure and function of the human apoptotic scramblase Xkr4.Nature communications · 2025Article
- Validation of Polymorphisms Associated with the Immune Response After Vaccination Against Porcine Reproductive and Respiratory Syndrome Virus in Yorkshire Gilts.Veterinary sciences · 2025Article
- Rigid enlargement of sybodies with antibody fragments for cryo-EM analyses of small membrane proteins.Scientific reports · 2025Article
- Dys-regulated phosphatidylserine externalization as a cell intrinsic immune escape mechanism in cancer.Cell communication and signaling : CCS · 2025Review
- TMEM16 and OSCA/TMEM63 proteins share a conserved potential to permeate ions and phospholipids.eLife · 2024Article
- Structural basis of closed groove scrambling by a TMEM16 protein.Nature structural & molecular biology · 2024Article
- TMEM16 and OSCA/TMEM63 proteins share a conserved potential to permeate ions and phospholipids.bioRxiv : the preprint server for biology · 2024Article
- In or out of the groove? Mechanisms of lipid scrambling by TMEM16 proteins.Cell calcium · 2024Review
- Extracellular calcium functions as a molecular glue for transmembrane helices to activate the scramblase Xkr4.Nature communications · 2023Article
- Lipid scrambling is a general feature of protein insertases.bioRxiv : the preprint server for biology · 2023Article
- Structural basis of closed groove scrambling by a TMEM16 protein.Research square · 2023Article
- Regulation of phospholipid distribution in the lipid bilayer by flippases and scramblases.Nature reviews. Molecular cell biology · 2023Review
- Article
- Activation of TMEM16F by inner gate charged mutations and possible lipid/ion permeation mechanisms.Biophysical journal · 2022Article
- Article
- A partnership between the lipid scramblase XK and the lipid transfer protein VPS13A at the plasma membrane.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
Abstract
The exposure of the negatively charged lipid phosphatidylserine on the cell surface, catalyzed by lipid scramblases, is an important signal for the clearance of apoptotic cells by macrophages. The protein XKR9 is a member of a conserved family that has been associated with apoptotic lipid scrambling. Here, we describe structures of full-length and caspase-treated XKR9 from
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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.