ReviewRNA (New York, N.Y.)2009
Powering through ribosome assembly.
Review in RNA (New York, N.Y.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 133 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
133 citing papers in PubMed, 198 citations in OpenAlex.
- Key Points to Consider When Studying RNA Remodeling by Proteins.Methods in molecular biology (Clifton, N.J.) · 2027Review
- Celery root-plant derived vesicles: comprehensive isolation, characterization and proteomic analysis.Molecular biology reports · 2025Article
- DNA aptamer AptScientific reports · 2025Article
- ZNF574 is a quality control factor for defective ribosome biogenesis intermediates.Molecular cell · 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
- Reducing the metabolic burden of rRNA synthesis promotes healthy longevity in Caenorhabditis elegans.Nature communications · 2024Article
- Loss of N-terminal acetyltransferase A activity induces thermally unstable ribosomal proteins and increases their turnover in Saccharomyces cerevisiae.Nature communications · 2023Article
- mRNA Turnover Protein 4 Is Vital for Fungal Pathogenicity and Response to Oxidative Stress inPathogens (Basel, Switzerland) · 2023Article
- Simulation toolkits at the molecular scale for trans-scale thermal signaling.Computational and structural biotechnology journal · 2023Review
- Archaea/eukaryote-specific ribosomal proteins - guardians of a complex structure.Computational and structural biotechnology journal · 2023Review
- Evolutionary scaling of maximum growth rate with organism size.Scientific reports · 2022Article
- Moderate activity of RNA chaperone maximizes the yield of self-spliced pre-RNA in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structural dynamics of AAA + ATPase Drg1 and mechanism of benzo-diazaborine inhibition.Nature communications · 2022Article
- Exploring protein symmetry at the RCSB Protein Data Bank.Emerging topics in life sciences · 2022Article
- Article
- Using DMS-MaPseq to uncover the roles of DEAD-box proteins in ribosome assembly.Methods (San Diego, Calif.) · 2022Article
- Ribosome assembly factor PNO1 is associated with progression and promotes tumorigenesis in triple‑negative breast cancer.Oncology reports · 2022Article
- Chemical Modifications of Ribosomal RNA.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Attacking a DEAD problem: The role of DEAD-box ATPases in ribosome assembly and beyond.Methods in enzymology · 2022Article
- Article
73 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribosome assembly is required for cell growth in all organisms. Classic in vitro work in bacteria has led to a detailed understanding of the biophysical, thermodynamic, and structural basis for the ordered and correct assembly of ribosomal proteins on ribosomal RNA. Furthermore, it has enabled reconstitution of active subunits from ribosomal RNA and proteins in vitro. Nevertheless, recent work has shown that eukaryotic ribosome assembly requires a large macromolecular machinery in vivo. Many of these assembly factors such as ATPases, GTPases, and kinases hydrolyze nucleotide triphosphates. Because these enzymes are likely regulatory proteins, much work to date has focused on understanding their role in the assembly process. Here, we review these factors, as well as other sources of energy, and their roles in the ribosome assembly process. In addition, we propose roles of energy-releasing enzymes in the assembly process, to explain why energy is used for a process that occurs largely spontaneously in bacteria. Finally, we use literature data to suggest testable models for how these enzymes could be used as targets for regulation of ribosome assembly.
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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.