Evidence map›Paper›PMID 9858532›Full record

ArticleMolecular and cellular biology1999

hnRNP H is a component of a splicing enhancer complex that activates a c-src alternative exon in neuronal cells.

M Y Chou, N Rooke, C W Turck, D L Black

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 129 papers.

0numbers the graph read from it
0cells of the map it votes in
129citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

129 citing papers in PubMed, 253 citations in OpenAlex.

  1. Article
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  3. CAR-SPLASH identifies nascent pre-mRNA structures implicated in kinetic coupling and alternative splicing.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  9. The RNA-binding proteins hnRNP H and F regulate splicing of a MYC-dependent HRAS exon in prostate cancer cells.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Article
  11. Article
  12. Review
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  14. A Mutation inThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2020
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  15. Article
  16. Article
  17. Review
  18. The Hairpin Form of r(GCell chemical biology · 2019
    Article
  19. Article
  20. Article

69 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

4 authors at 2 institutions in 1 country.

M Y ChouHoward Hughes Medical Institute, University of California, Los Angeles, Los Angeles, California 90095, USA.
N Rooke
C W Turck
D L Black
Howard Hughes Medical Institute · USUniversity of California, Los Angeles · US

Funding

The Regulation of Neuronal Exon SplicingR01GM049662 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI BLACK, DOUGLAS L · 1998 to 2019
$6.5M
NEURON-SPECIFIC REGULATION OF C-SRC ALTERNATIVE SPLICINGR29GM049662 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI BLACK, DOUGLAS L. · 1993 to 1997
–
NIGMS NIH HHS R01 GM049662NIGMS NIH HHS R29 GM49662
6 · The paper itself

Abstract

The regulation of the c-src N1 exon is mediated by an intronic splicing enhancer downstream of the N1 5' splice site. Previous experiments showed that a set of proteins assembles onto the most conserved core of this enhancer sequence specifically in neuronal WERI-1 cell extracts. The most prominent components of this enhancer complex are the proteins hnRNP F, KSRP, and an unidentified protein of 58 kDa (p58). This p58 protein was purified from the WERI-1 cell nuclear extract by ammonium sulfate precipitation, Mono Q chromatography, and immunoprecipitation with anti-Sm antibody Y12. Peptide sequence analysis of purified p58 protein identified it as hnRNP H. Immunoprecipitation of hnRNP H cross-linked to the N1 enhancer RNA, as well as gel mobility shift analysis of the enhancer complex in the presence of hnRNP H-specific antibodies, confirmed that hnRNP H is a protein component of the splicing enhancer complex. Immunoprecipitation of splicing intermediates from in vitro splicing reactions with anti-hnRNP H antibody indicated that hnRNP H remains bound to the src pre-mRNA after the assembly of spliceosome. Partial immunodepletion of hnRNP H from the nuclear extract partially inactivated the splicing of the N1 exon in vitro. This inhibition of splicing can be restored by the addition of recombinant hnRNP H, indicating that hnRNP H is an important factor for N1 splicing. Finally, in vitro binding assays demonstrate that hnRNP H can interact with the related protein hnRNP F, suggesting that hnRNPs H and F may exist as a heterodimer in a single enhancer complex. These two proteins presumably cooperate with each other and with other enhancer complex proteins to direct splicing to the N1 exon upstream.

Indexed as

Alternative SplicingEnhancer Elements, GeneticExonsDimerizationGene Expression RegulationHeLa CellsHeterogeneous-Nuclear Ribonucleoprotein Group F-HHeterogeneous-Nuclear RibonucleoproteinsHumansNeuronsProto-Oncogene Proteins pp60(c-src)RibonucleoproteinsRNA PrecursorsSpliceosomesHeterogeneous-Nuclear Ribonucleoprotein Group F-HHeterogeneous-Nuclear RibonucleoproteinsProto-Oncogene Proteins pp60(c-src)RibonucleoproteinsRNA Precursors

Identifiers

PMID9858532
PMCPMC83866
OpenAlexW2100998712

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.