Evidence map›Paper›PMID 10668804›Full record

ArticleRNA (New York, N.Y.)2000

The SRm160/300 splicing coactivator subunits.

B J Blencowe, G Baurén, A G Eldridge, R Issner, J A Nickerson, E Rosonina, P A Sharp

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

66 citing papers in PubMed, 124 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. A Prion-Like Domain in EBV EBNA1 Promotes Phase Separation and Enables SRRM1 Splicing.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  6. Article
  7. RareFrontiers in medicine · 2025
    Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

6 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

7 authors at 4 institutions in 3 countries.

B J BlencoweCenter for Cancer Research and Department of Biology, Massachusetts Institute of Technology, Cambridge 02139, USA.
G Baurén
A G Eldridge
R Issner
J A Nickerson
E Rosonina
P A Sharp
Center for Cancer Research · USUniversity of Toronto · CAIdera Pharmaceuticals (United States) · USUniversity of Massachusetts Chan Medical School · US

Funding

VIRUS PRODUCTION COREP30CA014051 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI MATTHEW G. VANDER HEIDEN · 1985 to 2026
$93.9M
REGULATION OF MRNA PROCESSINGR37GM034277 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SHARP, PHILLIP A · 1995 to 2004
$2.1M
MECHANISM OF ACTIVITIES OF TAT AND REV OF HIV1R01AI032486 · NIAID · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SHARP, PHILLIP A · 1992 to 2001
$679k
NCI NIH HHS P30-CA14051NIAID NIH HHS R01-AI32486NIGMS NIH HHS R37-GM34277
6 · The paper itself

Abstract

The SRm160/300 splicing coactivator, which consists of the serine/arginine (SR)-related nuclear matrix protein of 160 kDa and a 300-kDa nuclear matrix antigen, functions in splicing by promoting critical interactions between splicing factors bound to pre-mRNA, including snRNPs and SR family proteins. In this article we report the isolation of a cDNA encoding the 300-kDa antigen and investigate the activity of it and SRm160 in splicing. Like SRm160, the 300-kDa antigen contains domains rich in alternating S and R residues but lacks an RNA recognition motif; the protein is accordingly named "SRm300." SRm300 also contains a novel and highly conserved N-terminal domain, several unique repeated motifs rich in S, R, and proline residues, and two very long polyserine tracts. Surprisingly, specific depletion of SRm300 does not prevent the splicing of pre-mRNAs shown previously to require SRm160/300. Addition of recombinant SRm160 alone to SRm160/300-depleted reactions specifically activates splicing. The results indicate that SRm160 may be the more critical component of the SRm160/300 coactivator in the splicing of SRm160/300-dependent pre-mRNAs.

Indexed as

Antigens, NuclearNuclear Matrix-Associated ProteinsAmino Acid SequenceAntibodies, MonoclonalCell NucleusCells, CulturedCloning, MolecularDNA, ComplementaryHumansMolecular Sequence DataNuclear ProteinsPrecipitin TestsRNA-Binding ProteinsRNA, MessengerRNA SplicingSpliceosomesAntibodies, MonoclonalAntigens, NuclearDNA, ComplementaryNuclear Matrix-Associated ProteinsNuclear ProteinsRNA-Binding ProteinsRNA, MessengerSRRM1 protein, humanSRRM2 protein, human

Identifiers

PMID10668804
PMCPMC1369899
OpenAlexW2124646855

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.