ArticleNature communications2024
The structure and function of P5A-ATPases.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
3 citing papers in PubMed.
- Tail-anchored protein C-terminal domains stimulate ATP hydrolysis by the P5A-ATPase Spf1p.The Journal of biological chemistry · 2026Article
- ATP13A1 engages SEC61 to facilitate substrate-specific translocation.Science advances · 2025Article
- A novel YGGT family protein is localized in the apicoplast and is essential for the organelle inheritance.Frontiers in cellular and infection microbiology · 2025Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Endoplasmic reticulum (ER) membrane resident P5A-ATPases broadly affect protein biogenesis and quality control, and yet their molecular function remains debated. Here, we report cryo-EM structures of a P5A-ATPase, CtSpf1, covering multiple transport intermediates of the E1 → E1-ATP → E1P-ADP → E1P → E2P → E2.P
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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.