Evidence map›Paper›PMID 9630249›Full record

ArticleRNA (New York, N.Y.)1998

Regulated tissue-specific expression of antagonistic pre-mRNA splicing factors.

A Hanamura, J F Cáceres, A Mayeda, B R Franza, A R Krainer

Open access · greenAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 160 papers.

0numbers the graph read from it
0cells of the map it votes in
160citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

160 citing papers in PubMed, 331 citations in OpenAlex.

  1. Trial
  2. Article
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  4. SRSF1 interactome determined by proximity labeling reveals direct interaction with spliceosomal RNA helicase DDX23.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  9. Review
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  11. hnRNP A1B, a Splice Variant ofFrontiers in neuroscience · 2021
    Article
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  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

100 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

5 authors at 1 institution in 1 country.

A HanamuraCold Spring Harbor Laboratory, New York 11724-2208, USA.
J F Cáceres
A Mayeda
B R Franza
A R Krainer
Cold Spring Harbor Laboratory · US

Funding

VIRAL TRANSACTIVATIONP01CA013106 · NCI · COLD SPRING HARBOR LABORATORY · PI William Richard McCombie · 1985 to 2026
$116.8M
BIOCHEMISTRY OF PREMRNA SPLICINGR01GM042699 · NIGMS · COLD SPRING HARBOR LABORATORY · PI Adrian R Krainer · 1989 to 2026
$8.8M
Biochemistry of Pre-mRNA SplicingR37GM042699 · NIGMS · COLD SPRING HARBOR LABORATORY · PI KRAINER, ADRIAN R · 2012 to 2021
$7.7M
NCI NIH HHS CA13106NIGMS NIH HHS GM42699
6 · The paper itself

Abstract

The SR proteins are essential metazoan pre-mRNA splicing factors that can also influence the selection of alternative 5' splice sites in a concentration-dependent manner. Their activity in alternative splicing in vitro is antagonized by members of the hnRNP A/B family of proteins. The opposite effects of members of these two families of antagonistic splicing factors in vitro and upon overexpression in vivo suggest that changes in their relative levels may be a natural mechanism for the regulation of alternative splicing in vivo. One prediction of this model is that the ratios of these antagonists should vary in different cell types and in other situations in which cellular or viral transcripts are differentially spliced. We raised monoclonal antibodies specific for SF2/ASF and used them to measure the abundance of SF2/ASF protein and its isoforms, its phosphorylation state in vivo and during splicing in vitro, and its association with the spliceosome. SF2/ASF exists predominantly or exclusively in a highly phosphorylated state in vivo in all cell types examined, and unphosphorylated protein was not detectable. Unphosphorylated recombinant SF2/ASF becomes rapidly phosphorylated under splicing conditions in HeLa cell extracts and associates stably with one or more exons of beta-globin pre-mRNA. This interaction appears to persist through the splicing reaction and SF2/ASF remains bound to spliced mRNA. We compared the distribution of SF2/ASF to that of its antagonist, hnRNP A1, in different rat tissues and in immortal and transformed cell lines. We found that the protein levels of these antagonistic splicing factors vary naturally over a very wide range, supporting the notion that changes in the ratio of these proteins can affect alternative splicing of a variety of pre-mRNAs in vivo.

Indexed as

Alternative SplicingGene Expression RegulationHeterogeneous-Nuclear Ribonucleoprotein Group A-BAdenoviridaeAnimalsAntibodies, MonoclonalCell Line, TransformedEpitope MappingGlobinsHeLa CellsHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear RibonucleoproteinsHumansNuclear ProteinsPhosphoproteinsPhosphorylationAntibodies, MonoclonalGlobinsHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsNuclear ProteinsPhosphoproteinsRibonucleoproteinsRNA-Binding ProteinsRNA PrecursorsSerine-Arginine Splicing Factors

Identifiers

PMID9630249
PMCPMC1369629
OpenAlexW2116178342

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.