Evidence map›Paper›PMID 40553498›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2025

The RRM domain-containing protein Rbp3 interacts with ribosomes and the 3' ends of mRNAs encoding photosynthesis proteins.

Luisa Hemm, Elisabeth Lichtenberg, Stefan Tholen, Viktoria Reimann, Kenta Kakazu, Sotaro Machida, Moontaha Mahbub, Oliver Schilling, Annegret Wilde, Satoru Watanabe and 2 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

5 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. The RRM domain-containing protein Rbp3 interacts with ribosomes and the 3' ends of mRNAs encoding photosynthesis proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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

12 authors.

Luisa HemmDivision of Genetics and Experimental Bioinformatics, Faculty of Biology, Institute of Biology III, University of Freiburg, Freiburg 79104, Germany.
Elisabeth LichtenbergDivision of Molecular Genetics of Prokaryotes, Faculty of Biology, Institute of Biology III, University of Freiburg, Freiburg 79104, Germany.ORCID 0009-0004-5114-9160
Stefan TholenInstitute for Surgical Pathology, Medical Center-University of Freiburg, Faculty of Medicine, Freiburg 79106, Germany.ORCID 0009-0008-4746-2356
Viktoria ReimannDivision of Genetics and Experimental Bioinformatics, Faculty of Biology, Institute of Biology III, University of Freiburg, Freiburg 79104, Germany.ORCID 0000-0002-9643-4553
Kenta KakazuDepartment of Bioscience, Tokyo University of Agriculture, Setagaya-ku, Tokyo 156-8502, Japan.
Sotaro MachidaDepartment of Bioscience, Tokyo University of Agriculture, Setagaya-ku, Tokyo 156-8502, Japan.
Moontaha MahbubSchool of Biological and Behavioural Sciences, Queen Mary University of London, London E1 4NS, United Kingdom.
Oliver SchillingInstitute for Surgical Pathology, Medical Center-University of Freiburg, Faculty of Medicine, Freiburg 79106, Germany.
Annegret WildeDivision of Molecular Genetics of Prokaryotes, Faculty of Biology, Institute of Biology III, University of Freiburg, Freiburg 79104, Germany.ORCID 0000-0003-0935-8415
Satoru WatanabeDepartment of Bioscience, Tokyo University of Agriculture, Setagaya-ku, Tokyo 156-8502, Japan.ORCID 0000-0001-7456-5053
Conrad W MullineauxSchool of Biological and Behavioural Sciences, Queen Mary University of London, London E1 4NS, United Kingdom.ORCID 0000-0001-7194-9916
Wolfgang R HessDivision of Genetics and Experimental Bioinformatics, Faculty of Biology, Institute of Biology III, University of Freiburg, Freiburg 79104, Germany.ORCID 0000-0002-5340-3423

Funding

Deutsche Forschungsgemeinschaft (DFG) 322977937/GRK2344Deutsche Forschungsgemeinschaft (DFG) HE 2544/22-1Deutsche Forschungsgemeinschaft (DFG) SCHI 871/11-1Medical Faculty of the University of Freiburg 2021/A3-SchUKRI | Biotechnology and Biological Sciences Research Council (BBSRC) BB/W001012/1
6 · The paper itself

Abstract

RNA recognition motif (RRM) domain proteins are crucial RNA-binding proteins across all domains of life. In cyanobacteria, single RRM domain proteins are involved in mRNA targeting to the thylakoid membrane and acclimation to certain stress conditions, but many details of their physiological functions and molecular targets have remained unknown. The model cyanobacterium

Indexed as

Bacterial ProteinsPhotosynthesisRibosomesRNA-Binding ProteinsRNA, MessengerSynechocystisProtein BindingRNA Recognition MotifBacterial ProteinsRNA-Binding ProteinsRNA, Messengercyanobacteriagene expressionmRNA transportphotosynthesisRNA binding proteins

Identifiers

PMID40553498
PMCPMC12232666

What OpenQuestion holds

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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.