Evidence map›Paper›PMID 15659579›Full record

ArticleNucleic acids research2005

Ribosomal protein L1 recognizes the same specific structural motif in its target sites on the autoregulatory mRNA and 23S rRNA.

Natalia Nevskaya, Svetlana Tishchenko, Azat Gabdoulkhakov, Ekaterina Nikonova, Oleg Nikonov, Alexei Nikulin, Olga Platonova, Maria Garber, Stanislav Nikonov, Wolfgang Piendl

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.6field-weighted citation impact, top 18% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

26 citing papers in PubMed, 62 citations in OpenAlex.

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  9. Rerouting of ribosomal proteins into splicing in plant organelles.Proceedings of the National Academy of Sciences of the United States of America · 2020
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  15. Article
  16. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 1 institution in 1 country.

Natalia NevskayaInstitute of Protein Research, Russian Academy of Sciences 142290 Pushchino, Moscow region, Russia.
Svetlana Tishchenko
Azat Gabdoulkhakov
Ekaterina Nikonova
Oleg Nikonov
Alexei Nikulin
Olga Platonova
Maria Garber
Stanislav Nikonov
Wolfgang Piendl
Institute of Protein Research · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The RNA-binding ability of ribosomal protein L1 is of profound interest since the protein has a dual function as a ribosomal protein binding rRNA and as a translational repressor binding its mRNA. Here, we report the crystal structure of ribosomal protein L1 in complex with a specific fragment of its mRNA and compare it with the structure of L1 in complex with a specific fragment of 23S rRNA determined earlier. In both complexes, a strongly conserved RNA structural motif is involved in L1 binding through a conserved network of RNA-protein H-bonds inaccessible to the solvent. These interactions should be responsible for specific recognition between the protein and RNA. A large number of additional non-conserved RNA-protein H-bonds stabilizes both complexes. The added contribution of these non-conserved H-bonds makes the ribosomal complex much more stable than the regulatory one.

Indexed as

Binding SitesHomeostasisModels, MolecularNucleic Acid ConformationRibosomal ProteinsRNA, ArchaealRNA-Binding ProteinsRNA, MessengerRNA, Ribosomal, 23Sribosomal protein L1Ribosomal ProteinsRNA, ArchaealRNA-Binding ProteinsRNA, MessengerRNA, Ribosomal, 23S

Identifiers

PMID15659579
PMCPMC548342
OpenAlexW1992791303

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.