Evidence map›Paper›PMID 11003644›Full record

ArticleMolecular and cellular biology2000

Cooperative assembly of an hnRNP complex induced by a tissue-specific homolog of polypyrimidine tract binding protein.

V Markovtsov, J M Nikolic, J A Goldman, C W Turck, M Y Chou, D L Black

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. 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
8.3field-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, 316 citations in OpenAlex.

  1. Article
  2. Article
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  4. Expanding the Functions of KHSRP Protein: Insights into DNA G-Quadruplex Binding.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
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  7. Review
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  11. Article
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  14. Article
  15. Alternative splicing programming of axon formation.Wiley interdisciplinary reviews. RNA · 2020
    Review
  16. Targeting mRNA processing as an anticancer strategy.Nature reviews. Drug discovery · 2020
    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

6 authors at 1 institution in 1 country.

V MarkovtsovDepartment of Microbiology and Molecular Genetics, University of California, Los Angeles, California 90095, USA.
J M Nikolic
J A Goldman
C W Turck
M Y Chou
D L Black
Howard Hughes Medical Institute · US

Funding

The Regulation of Neuronal Exon SplicingR01GM049662 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI BLACK, DOUGLAS L · 1998 to 2019
$6.5M
NIGMS NIH HHS R01 GM049662NIGMS NIH HHS R01 GM49662
6 · The paper itself

Abstract

Splicing of the c-src N1 exon in neuronal cells depends in part on an intronic cluster of RNA regulatory elements called the downstream control sequence (DCS). Using site-specific cross-linking, RNA gel shift, and DCS RNA affinity chromatography assays, we characterized the binding of several proteins to specific sites along the DCS RNA. Heterogeneous nuclear ribonucleoprotein (hnRNP) H, polypyrimidine tract binding protein (PTB), and KH-type splicing-regulatory protein (KSRP) each bind to distinct elements within this sequence. We also identified a new 60-kDa tissue-specific protein that binds to the CUCUCU splicing repressor element of the DCS RNA. This protein was purified, partially sequenced, and cloned. The new protein (neurally enriched homolog of PTB [nPTB]) is highly homologous to PTB. Unlike PTB, nPTB is enriched in the brain and in some neural cell lines. Although similar in sequence, nPTB and PTB show significant differences in their properties. nPTB binds more stably to the DCS RNA than PTB does but is a weaker repressor of splicing in vitro. nPTB also greatly enhances the binding of two other proteins, hnRNP H and KSRP, to the DCS RNA. These experiments identify specific cooperative interactions between the proteins that assemble onto an intricate splicing-regulatory sequence and show how this hnRNP assembly is altered in different cell types by incorporating different but highly related proteins.

Indexed as

Trans-ActivatorsAmino Acid SequenceBase SequenceCell LineChromatography, AffinityCloning, MolecularHeterogeneous-Nuclear Ribonucleoprotein Group F-HHeterogeneous-Nuclear RibonucleoproteinsHumansModels, GeneticMolecular Sequence DataNerve Tissue ProteinsNuclear ProteinsOrgan SpecificityPhylogenyPolypyrimidine Tract-Binding ProteinHeterogeneous-Nuclear Ribonucleoprotein Group F-HHeterogeneous-Nuclear RibonucleoproteinsKHSRP protein, humanNerve Tissue ProteinsNuclear ProteinsPolypyrimidine Tract-Binding ProteinRibonucleoproteinsRNA-Binding ProteinsRNA, Heterogeneous NuclearRNA, MessengerTrans-Activators

Identifiers

PMID11003644
PMCPMC86300
OpenAlexW2004509913

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.