ArticleACS chemical biology2012
Role of pseudouridine in structural rearrangements of helix 69 during bacterial ribosome assembly.
Article in ACS chemical biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
13 citing papers in PubMed, 25 citations in OpenAlex.
- Nanopore Dwell Time Analysis Permits Sequencing and Conformational Assignment of Pseudouridine in SARS-CoV-2.ACS central science · 2021Article
- Pseudouridine modifications influence binding of aminoglycosides to helix 69 of bacterial ribosomes.Organic & biomolecular chemistry · 2017Article
- Small methyltransferase RlmH assembles a composite active site to methylate a ribosomal pseudouridine.Scientific reports · 2017Article
- The development of peptide ligands that target helix 69 rRNA of bacterial ribosomes.Bioorganic & medicinal chemistry · 2016Article
- Cisplatin Targeting of Bacterial Ribosomal RNA Hairpins.International journal of molecular sciences · 2015Article
- Major centers of motion in the large ribosomal RNAs.Nucleic acids research · 2015Article
- Dye label interference with RNA modification reveals 5-fluorouridine as non-covalent inhibitor.Nucleic acids research · 2014Article
- Structure modulation of helix 69 from Escherichia coli 23S ribosomal RNA by pseudouridylations.Nucleic acids research · 2014Article
- Pseudouridine: still mysterious, but never a fake (uridine)!RNA biology · 2014Review
- Interplay of the bacterial ribosomal A-site, S12 protein mutations and paromomycin binding: a molecular dynamics study.PloS one · 2014Article
- Ligand- and pH-induced conformational changes of RNA domain helix 69 revealed by 2-aminopurine fluorescence.Angewandte Chemie (International ed. in English) · 2012Article
- Impact of base pair identity 5' to the spliceosomal branch site adenosine on branch site conformation.RNA (New York, N.Y.) · 2012Article
- Modulation of conformational changes in helix 69 mutants by pseudouridine modifications.Biophysical chemistryArticle
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
Abstract
As part of the central core domain of the ribosome, helix 69 of 23S rRNA participates in an important intersubunit bridge and contacts several protein translation factors. Helix 69 is believed to play key roles in protein synthesis. Even though high-resolution crystal structures of the ribosome exist, the solution dynamics and roles of individual nucleotides in H69 are still not well-defined. To better understand the influence of modified nucleotides, specifically pseudouridine, on the multiple conformational states of helix 69 in the context of 50S subunits and 70S ribosomes, chemical probing analyses were performed on wild-type and pseudouridine-deficient bacterial ribosomes. Local structural rearrangements of helix 69 upon ribosomal subunit association and interactions with its partner, helix 44 of 16S rRNA, are observed. The helix 69 conformational states are also magnesium-dependent. The probing data presented in this study provide insight into the functional role of helix 69 dynamics and regulation of these conformational states by post-transcriptional pseudouridine modification.
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.