ArticleJournal of bacteriology2008
Protein folding by domain V of Escherichia coli 23S rRNA: specificity of RNA-protein interactions.
Article in Journal of bacteriology, 2008. 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
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
27 citing papers in PubMed, 45 citations in OpenAlex.
- Roles of Nucleic Acids in Protein Folding, Aggregation, and Disease.ACS chemical biology · 2024Review
- Computationally-guided design and selection of high performing ribosomal active site mutants.Nucleic acids research · 2022Article
- Modulating co-translational protein folding by rational design and ribosome engineering.Nature communications · 2022Article
- Chaperna: linking the ancient RNA and protein worlds.RNA biology · 2021Review
- Ribosomal RNA Modulates Aggregation of theInternational journal of molecular sciences · 2020Article
- RNA modulates aggregation of the recombinant mammalian prion protein by direct interaction.Scientific reports · 2019Article
- Distinct modulatory role of RNA in the aggregation of the tumor suppressor protein p53 core domain.The Journal of biological chemistry · 2017Article
- The double life of the ribosome: When its protein folding activity supports prion propagation.Prion · 2017Review
- Sequestration of Ribosome during Protein Aggregate Formation: Contribution of ribosomal RNA.Scientific reports · 2017Article
- A Possible Role of the Full-Length Nascent Protein in Post-Translational Ribosome Recycling.PloS one · 2017Article
- Protein Folding Activity of the Ribosome is involved in Yeast Prion Propagation.Scientific reports · 2016Article
- Do nucleic acids moonlight as molecular chaperones?Nucleic acids research · 2016Article
- Article
- M1 RNA is important for the in-cell solubility of its cognate C5 protein: Implications for RNA-mediated protein folding.RNA biology · 2015Article
- Review
- Impact of P-Site tRNA and antibiotics on ribosome mediated protein folding: studies using the Escherichia coli ribosome.PloS one · 2014Article
- The ribosome can prevent aggregation of partially folded protein intermediates: studies using the Escherichia coli ribosome.PloS one · 2014Article
- The antiprion compound 6-aminophenanthridine inhibits the protein folding activity of the ribosome by direct competition.The Journal of biological chemistry · 2013Article
- Identical RNA-protein interactions in vivo and in vitro and a scheme of folding the newly synthesized proteins by ribosomes.The Journal of biological chemistry · 2012Article
- Macromolecule-assisted de novo protein folding.International journal of molecular sciences · 2012Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The peptidyl transferase center, present in domain V of 23S rRNA of eubacteria and large rRNA of plants and animals, can act as a general protein folding modulator. Here we show that a few specific nucleotides in Escherichia coli domain V RNA bind to unfolded proteins and, as shown previously, bring the trapped proteins to a folding-competent state before releasing them. These nucleotides are the same for the proteins studied so far: bovine carbonic anhydrase, lactate dehydrogenase, malate dehydrogenase, and chicken egg white lysozyme. The amino acids that interact with these nucleotides are also found to be specific in the two cases tested: bovine carbonic anhydrase and lysozyme. They are either neutral or positively charged and are present in random coils on the surface of the crystal structure of both the proteins. In fact, two of these amino acid-nucleotide pairs are identical in the two cases. How these features might help the process of protein folding is discussed.
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.