Evidence map›Paper›PMID 19282290›Full record

ArticleThe Journal of biological chemistry2009

Heterogeneous nuclear ribonucleoprotein G regulates splice site selection by binding to CC(A/C)-rich regions in pre-mRNA.

Bettina Heinrich, Zhaiyi Zhang, Oleg Raitskin, Michael Hiller, Natalya Benderska, Annette M Hartmann, Laurent Bracco, David Elliott, Shani Ben-Ari, Hermona Soreq and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
3.5field-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

70 citing papers in PubMed, 111 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Nuclear Roles of Spliceosome-Associated microRNAs in Neuronal Cancer Cells.International journal of molecular sciences · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Deciphering 3'UTR Mediated Gene Regulation Using Interpretable Deep Representation Learning.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Interconnections between mLife science alliance · 2024
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

10 more citing papers are in PubMed but not listed here.

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

13 authors at 7 institutions in 5 countries.

Bettina HeinrichInstitute for Biochemistry, University of Erlangen, Fahrstrasse 17, 91054 Erlangen, Germany.
Zhaiyi Zhang
Oleg Raitskin
Michael Hiller
Natalya Benderska
Annette M Hartmann
Laurent Bracco
David Elliott
Shani Ben-Ari
Hermona Soreq
Joseph Sperling
Ruth Sperling
Stefan Stamm
Friedrich-Alexander-Universität Erlangen-Nürnberg · DEHebrew University of Jerusalem · ILHiFiBiO Therapeutics (France) · FRNewcastle University · GBUniversity of Freiburg · DEUniversity of Kentucky · USWeizmann Institute of Science · IL

Funding

UNDERSTANDING THE MOLECULAR BASIS OF EPIGENETIC TRANSCRIPTIONAL SILENCINGP20RR020171 · NCRR · UNIVERSITY OF KENTUCKY · PI LOUIS HERSH, LOUIS HERSH LOUIS HERSH · 2004 to 2011
$16.5M
The Mammalian Cellular Splicing Machine - Structure and FunctionR01GM079549 · NIGMS · HEBREW UNIVERSITY OF JERUSALEM · PI SPERLING, RUTH · 2008 to 2011
$836k
Tau missplicing caused by RNA processing proteins located on chromosome 21R21HD056195 · NICHD · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI ANDREADIS, ATHENA · 2007 to 2008
$379k
NCRR NIH HHS P20 RR020171NICHD NIH HHS R21HD056195-01NIGMS NIH HHS GM079549NIGMS NIH HHS R01 GM079549
6 · The paper itself

Abstract

Almost every protein-coding gene undergoes pre-mRNA splicing, and the majority of these pre-mRNAs are alternatively spliced. Alternative exon usage is regulated by the transient formation of protein complexes on the pre-mRNA that typically contain heterogeneous nuclear ribonucleoproteins (hnRNPs). Here we characterize hnRNP G, a member of the hnRNP class of proteins. We show that hnRNP G is a nuclear protein that is expressed in different concentrations in various tissues and that interacts with other splicing regulatory proteins. hnRNP G is part of the supraspliceosome, where it regulates alternative splice site selection in a concentration-dependent manner. Its action on alternative exons can occur without a functional RNA-recognition motif by binding to other splicing regulatory proteins. The RNA-recognition motif of hnRNP G binds to a loose consensus sequence containing a CC(A/C) motif, and hnRNP G preferentially regulates alternative exons where this motif is clustered in close proximity. The X-chromosomally encoded hnRNP G regulates different RNAs than its Y-chromosomal paralogue RNA-binding motif protein, Y-linked (RBMY), suggesting that differences in alternative splicing, evoked by the sex-specific expression of hnRNP G and RBMY, could contribute to molecular sex differences in mammals.

Indexed as

AnimalsBase SequenceCell LineCell NucleusExonsGenes, ReporterHeterogeneous-Nuclear RibonucleoproteinsHumansMolecular Sequence DataNuclear ProteinsProtein BindingProtein Structure, TertiaryProtein TransportRatsRNA PrecursorsRNA Splice SitesHeterogeneous-Nuclear RibonucleoproteinsNuclear ProteinsRBMX protein, ratRNA PrecursorsRNA Splice Sites

Identifiers

PMID19282290
PMCPMC2682879
OpenAlexW1970302143

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.