Evidence map›Paper›PMID 26381213›Full record

ArticleScientific reports2015

Small angle X-ray scattering studies of CTNNBL1 dimerization and CTNNBL1/CDC5L complex.

Jae-Woo Ahn, Kyeong Sik Jin, Hyeoncheol Francis Son, Jeong Ho Chang, Kyung-Jin Kim

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 86% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. Article
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 2 institutions in 1 country.

Jae-Woo AhnSchool of Life Sciences, KNU Creative BioResearch Group, Kyungpook National University, Daehak-ro 80, Buk-ku, Daegu 702-701, Korea.
Kyeong Sik JinPohang Accelerator Laboratory, Pohang University of Science and Technology, Jigok-ro 80, Pohang, Kyungbuk 790-784, Korea.
Hyeoncheol Francis SonSchool of Life Sciences, KNU Creative BioResearch Group, Kyungpook National University, Daehak-ro 80, Buk-ku, Daegu 702-701, Korea.
Jeong Ho ChangDepartment of Biology, Teachers College, Kyungpook National University, Daehak-ro 80, Buk-ku, Daegu 702-701, Korea.
Kyung-Jin KimSchool of Life Sciences, KNU Creative BioResearch Group, Kyungpook National University, Daehak-ro 80, Buk-ku, Daegu 702-701, Korea.
Kyungpook National University · KRPohang University of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The hPrp19/CDC5L complex is a non-snRNP spliceosome complex that plays a key role in the spliceosome activation during pre-mRNA splicing, and CTNNBL1 and CDC5L are essential components of the complex. In this study, to investigate the oligomeric state of CTNNBL1 in solution, we performed small angle X-ray scattering experiments in various concentrations of NaCl. We observed that CTNNBL1 existed as a dimer in physiological NaCl concentrations. Site-directed mutagenesis experiment of CTNNBL1 confirmed that N-terminal capping region and the first four ARM repeats are important for dimerization of the protein. We also found that the positively-charged NLS3-containing region (residues 197-235) of CDC5L bound to the negatively-charged patch of CTNNBL1 and that the CTNNBL1/CDC5L complex formed a heterotetramer consisting of one CTNNBL1 dimer and one CDC5L dimer. Moreover, reconstruction of 3D models of CTNNBL1/CDC5L complexes containing CTNNBL1 and three different truncated forms of CDC5L showed that the CDC5L(141-196) region and the CDC5L(236-377) region were positioned at the top of the N-terminal capping region and at the bottom of ARM VII of CTNNBL1, respectively.

Indexed as

Protein MultimerizationApoptosis Regulatory ProteinsCell Cycle ProteinsHumansModels, MolecularNuclear ProteinsProtein BindingProtein ConformationProtein Interaction Domains and MotifsRNA-Binding ProteinsScattering, Small AngleSolutionsX-Ray DiffractionApoptosis Regulatory ProteinsCDC5L protein, humanCell Cycle ProteinsCTNNBL1 protein, humanNuclear ProteinsRNA-Binding ProteinsSolutions

Identifiers

PMID26381213
PMCPMC4585563
OpenAlexW2396387988

What OpenQuestion holds

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LicenceCC BY
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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.