Evidence map›Paper›PMID 24643059›Full record

ReviewRNA biology2014

Novel regulatory principles of the spliceosomal Brr2 RNA helicase and links to retinal disease in humans.

Sina Mozaffari-Jovin, Traudy Wandersleben, Karine F Santos, Cindy L Will, Reinhard Lührmann, Markus C Wahl

Open access · bronzeAbstract readReview
In one paragraph

Review in RNA biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

35 citing papers in PubMed, 49 citations in OpenAlex.

  1. Neurodegenerative spliceosomopathies.Frontiers in cell and developmental biology · 2026
    Review
  2. Review
  3. Article
  4. Structural Chemistry of Helicase Inhibition.Journal of medicinal chemistry · 2025
    Review
  5. Research Progress on the Relationship Between PRPF8 and Cancer.Current issues in molecular biology · 2025
    Review
  6. Addressing the tissue specificity of U5 snRNP spliceosomopathies.Frontiers in cell and developmental biology · 2025
    Article
  7. A de novoHormone research in paediatrics · 2025
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. The determinants of alternative RNA splicing in human cells.Molecular genetics and genomics : MGG · 2017
    Review
  19. Article
  20. 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

6 authors at 2 institutions in 1 country.

Sina Mozaffari-JovinDept. of Cellular Biochemistry; Max Planck Institute for Biophysical Chemistry; Am Fassberg 11; Göttingen, Germany.
Traudy WanderslebenLaboratory of Structural Biochemistry; Freie Universität Berlin; Takustr. 6; Berlin, Germany.
Karine F SantosLaboratory of Structural Biochemistry; Freie Universität Berlin; Takustr. 6; Berlin, Germany.
Cindy L WillDept. of Cellular Biochemistry; Max Planck Institute for Biophysical Chemistry; Am Fassberg 11; Göttingen, Germany.
Reinhard LührmannDept. of Cellular Biochemistry; Max Planck Institute for Biophysical Chemistry; Am Fassberg 11; Göttingen, Germany.
Markus C WahlLaboratory of Structural Biochemistry; Freie Universität Berlin; Takustr. 6; Berlin, Germany.
Freie Universität Berlin · DEMax Planck Institute for Biophysical Chemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

For each round of pre-mRNA splicing, a spliceosome is assembled anew on its substrate. RNA-protein remodeling events required for spliceosome assembly, splicing catalysis, and spliceosome disassembly are driven and controlled by a conserved group of ATPases/RNA helicases. The activities of most of these enzymes are timed by their recruitment to the spliceosome. The Brr2 enzyme, however, which mediates spliceosome catalytic activation, is a stable subunit of the spliceosome, and thus, requires special regulation. Recent structural and functional studies have revealed diverse mechanisms whereby an RNaseH-like and a Jab1/MPN-like domain of the Prp8 protein regulate Brr2 activity during splicing both positively and negatively. Reversible Brr2 inhibition might in part be achieved via an intrinsically unstructured element of the Prp8 Jab1/MPN domain, a concept widespread in biological systems. Mutations leading to changes in the Prp8 Jab1/MPN domain, which are linked to a severe form of retinitis pigmentosa, disrupt Jab1/MPN-mediated regulation of Brr2.

Indexed as

Gene Expression RegulationCOP9 Signalosome ComplexHumansIntracellular Signaling Peptides and ProteinsPeptide HydrolasesProtein BindingProtein ConformationProtein Interaction Domains and MotifsRetinal DiseasesRibonucleoproteins, Small NuclearRNA-Binding ProteinsRNA PrecursorsRNA SplicingSpliceosomesSubstrate SpecificityCOP9 Signalosome ComplexCOPS5 protein, humanIntracellular Signaling Peptides and ProteinsPeptide HydrolasesPRPF8 protein, humanRibonucleoproteins, Small NuclearRNA-Binding ProteinsRNA PrecursorsSNRNP200 protein, humanPre-mRNA splicingretinitis pigmentosaRNA helicaseRNA-protein complexspliceosome catalytic activation

Identifiers

PMID24643059
PMCPMC4075514
OpenAlexW1985905136

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.