ArticleNucleic acids research2004
Conserved tertiary base pairing ensures proper RNA folding and efficient assembly of the signal recognition particle Alu domain.
Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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
20 citing papers in PubMed, 30 citations in OpenAlex.
- Reading the SINEs - functionality in noncoding RNA 'cheap genes'.RNA biology · 2026Review
- Lysosomal RNA profiling reveals targeting of specific types of RNAs for degradation.bioRxiv : the preprint server for biology · 2025Article
- Alu RNA pseudoknot alterations influence SRP9/SRP14 association.RNA (New York, N.Y.) · 2025Article
- Massively parallel jumping assay decodes Alu retrotransposition activity.Nature communications · 2025Article
- PERFUMES: pipeline to extract RNA functional motifs and exposed structures.Bioinformatics (Oxford, England) · 2024Article
- The role of SRP9/SRP14 in regulating Alu RNA.RNA biology · 2024Review
- Alu RNA fold links splicing with signal recognition particle proteins.Nucleic acids research · 2023Article
- Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation.Communications biology · 2021Article
- Sequential activation of human signal recognition particle by the ribosome and signal sequence drives efficient protein targeting.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- A Role for the Mutagenic DNA Self-Catalyzed Depurination Mechanism in the Evolution of 7SL-Derived RNAs.Journal of molecular evolution · 2017Article
- Inverted repeat Alu elements in the human lincRNA-p21 adopt a conserved secondary structure that regulates RNA function.Nucleic acids research · 2016Article
- Crystal structure of a signal recognition particle Alu domain in the elongation arrest conformation.RNA (New York, N.Y.) · 2014Article
- cis-Acting determinants of 7SL RNA packaging by HIV-1.Journal of virology · 2012Article
- Efficient secretion of small proteins in mammalian cells relies on Sec62-dependent posttranslational translocation.Molecular biology of the cell · 2012Article
- Residues in SRP9/14 essential for elongation arrest activity of the signal recognition particle define a positively charged functional domain on one side of the protein.RNA (New York, N.Y.) · 2010Article
- Compositional properties and thermal adaptation of SRP-RNA in bacteria and archaea.Journal of molecular evolution · 2010Article
- Three-way RNA junctions with remote tertiary contacts: a recurrent and highly versatile fold.RNA (New York, N.Y.) · 2009Review
- Anti-cooperative assembly of the SRP19 and SRP68/72 components of the signal recognition particle.The Biochemical journal · 2008Article
- Article
- Alu RNP and Alu RNA regulate translation initiation in vitro.Nucleic acids research · 2006Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Proper folding of the RNA is an essential step in the assembly of functional ribonucleoprotein complexes. We examined the role of conserved base pairs formed between two distant loops in the Alu portion of the mammalian signal recognition particle RNA (SRP RNA) in SRP assembly and functions. Mutations disrupting base pairing interfere with folding of the Alu portion of the SRP RNA as monitored by probing the RNA structure and the binding of the protein SRP9/14. Complementary mutations rescue the defect establishing a role of the tertiary loop-loop interaction in RNA folding. The same mutations in the Alu domain have no major effect on binding of proteins to the S domain suggesting that the S domain can fold independently. Once assembled into a complete SRP, even particles that contain mutant RNA are active in arresting nascent chain elongation and translocation into microsomes, and, therefore, tertiary base pairing does not appear to be essential for these activities. Our results suggest a model in which the loop-loop interaction and binding of the protein SRP9/14 play an important role in the early steps of SRP RNA folding and assembly.
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.