Evidence map›Paper›PMID 20502437›Full record

ArticleThe EMBO journal2010

Stoichiometry of a regulatory splicing complex revealed by single-molecule analyses.

Dmitry Cherny, Clare Gooding, Giles E Eperon, Miguel B Coelho, Clive R Bagshaw, Christopher W J Smith, Ian C Eperon

Abstract read
In one paragraph

Article in The EMBO journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
–field-weighted citation impact
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

34 citing papers in PubMed.

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  13. JIP3 Activates Kinesin-1 Motility to Promote Axon Elongation.The Journal of biological chemistry · 2015
    Article
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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.

Dmitry ChernyDepartment of Biochemistry, University of Leicester, Leicester, UK.
Clare Gooding
Giles E Eperon
Miguel B Coelho
Clive R Bagshaw
Christopher W J Smith
Ian C Eperon

Funding

Biotechnology and Biological Sciences Research Council BBS/B/0367XWellcome TrustWellcome Trust 077877
6 · The paper itself

Abstract

Splicing is regulated by complex interactions of numerous RNA-binding proteins. The molecular mechanisms involved remain elusive, in large part because of ignorance regarding the numbers of proteins in regulatory complexes. Polypyrimidine tract-binding protein (PTB), which regulates tissue-specific splicing, represses exon 3 of alpha-tropomyosin through distant pyrimidine-rich tracts in the flanking introns. Current models for repression involve either PTB-mediated looping or the propagation of complexes between tracts. To test these models, we used single-molecule approaches to count the number of bound PTB molecules both by counting the number of bleaching steps of GFP molecules linked to PTB within complexes and by analysing their total emissions. Both approaches showed that five or six PTB molecules assemble. Given the domain structures, this suggests that the molecules occupy primarily multiple overlapping potential sites in the polypyrimidine tracts, excluding propagation models. As an alternative to direct looping, we propose that repression involves a multistep process in which PTB binding forms small local loops, creating a platform for recruitment of other proteins that bring these loops into close proximity.

Indexed as

Alternative SplicingAnimalsBase SequenceCell NucleolusExonsModels, GeneticMolecular Sequence DataPhotobleachingPolypyrimidine Tract-Binding ProteinProtein BindingRatsRNA, MessengerTropomyosinPolypyrimidine Tract-Binding ProteinRNA, MessengerTpm1 protein, ratTropomyosin

Identifiers

PMID20502437
PMCPMC2905242

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.