ArticleeLife2018
The CryoEM structure of the
Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 30 citations in OpenAlex.
- NorQD AAA+ complex drives metal insertion by a twisting mechanism.Nature communications · 2026Article
- PELP1 coordinates the modular assembly and enzymatic activity of the rixosome complex.Science advances · 2025Article
- Highly conserved ribosome biogenesis pathways between human and yeast revealed by the MDN1-NLE1 interaction and NLE1 containing pre-60S subunits.Nucleic acids research · 2025Article
- Remodelling of Rea1 linker domain drives the removal of assembly factors from pre-ribosomal particles.Nature communications · 2024Article
- Arabidopsis NOTCHLESS plays an important role in root and embryo development.Plant signaling & behavior · 2023Article
- Multi-Omics Profiling ofMicroorganisms · 2023Article
- Concurrent remodelling of nucleolar 60S subunit precursors by the Rea1 ATPase and Spb4 RNA helicase.eLife · 2023Article
- Identification of novel interferon responsive protein partners of human leukocyte antigen A (HLA-A) using cross-linking mass spectrometry (CLMS) approach.Scientific reports · 2022Article
- The AAA+ ATPase RavA and its binding partner ViaA modulate E. coli aminoglycoside sensitivity through interaction with the inner membrane.Nature communications · 2022Article
- The MIDAS domain of AAA mechanoenzyme Mdn1 forms catch bonds with two different substrates.eLife · 2022Article
- Structural overview of macromolecular machines involved in ribosome biogenesis.Current opinion in structural biology · 2021Review
- AAA+ ATPases: structural insertions under the magnifying glass.Current opinion in structural biology · 2021Review
- Long-range intramolecular allostery and regulation in the dynein-like AAA protein Mdn1.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Insights into the mechanism and regulation of the CbbQO-type Rubisco activase, a MoxR AAA+ ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Shaping the Nascent Ribosome: AAA-ATPases in Eukaryotic Ribosome Biogenesis.Biomolecules · 2019Review
- Crystal structures of Rea1-MIDAS bound to its ribosome assembly factor ligands resembling integrin-ligand-type complexes.Nature communications · 2019Article
- The AAA-ATPase MIDASIN 1 Functions in Ribosome Biogenesis and Is Essential for Embryo and Root Development.Plant physiology · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The biogenesis of 60S ribosomal subunits is initiated in the nucleus where rRNAs and proteins form pre-60S particles. These pre-60S particles mature by transiently interacting with various assembly factors. The ~5000 amino-acid AAA+ ATPase Rea1 (or Midasin) generates force to mechanically remove assembly factors from pre-60S particles, which promotes their export to the cytosol. Here we present three Rea1 cryoEM structures. We visualise the Rea1 engine, a hexameric ring of AAA+ domains, and identify an α-helical bundle of AAA2 as a major ATPase activity regulator. The α-helical bundle interferes with nucleotide-induced conformational changes that create a docking site for the substrate binding MIDAS domain on the AAA +ring. Furthermore, we reveal the architecture of the Rea1 linker, which is involved in force generation and extends from the AAA+ ring. The data presented here provide insights into the mechanism of one of the most complex ribosome maturation factors.
Indexed as
Identifiers
What OpenQuestion holds
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.