Evidence map›Paper›PMID 25671812›Full record

ArticleInternational journal of molecular sciences2015

Identification of the specific interactors of the human lariat RNA debranching enzyme 1 protein.

So Masaki, Rei Yoshimoto, Daisuke Kaida, Asuka Hata, Takayuki Satoh, Mutsuhito Ohno, Naoyuki Kataoka

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.3field-weighted citation impact, top 38% 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

9 citing papers in PubMed, 16 citations in OpenAlex.

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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 at 3 institutions in 1 country.

So MasakiMedical Innovation Center, Laboratory for Malignancy Control Research, Kyoto University Graduate School of Medicine, Sakyo-ku, Kyoto 606-8507, Japan. masaki@dsk.med.kyoto-u.ac.jp.
Rei YoshimotoChemical Genetics Laboratory, RIKEN Advanced Science Institute, Wako, Saitama 351-0198, Japan. hitoohno@virus.kyoto-u.ac.jp.
Daisuke KaidaFrontier Research Core for Life Sciences, University of Toyama, 2630 Sugitani, Toyama-shi, Toyama 930-0194, Japan. kaida@med.u-toyama.ac.jp.
Asuka HataMedical Innovation Center, Laboratory for Malignancy Control Research, Kyoto University Graduate School of Medicine, Sakyo-ku, Kyoto 606-8507, Japan. akusa.atah@gmail.com.
Takayuki SatohFrontier Research Core for Life Sciences, University of Toyama, 2630 Sugitani, Toyama-shi, Toyama 930-0194, Japan. tsatoh@med.u-toyama.ac.jp.
Mutsuhito OhnoInstitute for Virus Research, Kyoto University, Sakyo-ku, Kyoto 606-8507, Japan. hitoohno@virus.kyoto-u.ac.jp.
Naoyuki KataokaMedical Innovation Center, Laboratory for Malignancy Control Research, Kyoto University Graduate School of Medicine, Sakyo-ku, Kyoto 606-8507, Japan. kataoka.naoyuki.6m@kyoto-u.ac.jp.
Kyoto University · JPUniversity of Toyama · JPRIKEN Advanced Science Institute · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In eukaryotes, pre-mRNA splicing is an essential step for gene expression. We have been analyzing post-splicing intron turnover steps in higher eukaryotes. Here, we report protein interaction between human Debranching enzyme 1 (hDbr1) and several factors found in the Intron Large (IL) complex, which is an intermediate complex of the intron degradation pathway. The hDbr1 protein specifically interacts with xeroderma pigmentosum, complementeation group A (XPA)-binding protein 2 (Xab2). We also attempted to identify specific interactors of hDbr1. Co-immunoprecipitation experiments followed by mass spectrometry analysis identified a novel protein as one of the specific interactors of hDbr1. This protein is well conserved among many species and shows the highest similarity to yeast Drn1, so it is designated as human Dbr1 associated ribonuclease 1 (hDrn1). hDrn1 directly interacts with hDbr1 through protein-protein interaction. Furthermore, hDrn1 shuttles between the nucleus and the cytoplasm, as hDbr1 protein does. These findings suggest that hDrn1 has roles in both the nucleus and the cytoplasm, which are highly likely to involve hDbr1.

Indexed as

AnimalsCell Cycle ProteinsCell NucleusCoculture TechniquesCytoplasmHEK293 CellsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHumansImmunoprecipitationMass SpectrometryMiceNIH 3T3 CellsProtein Interaction MapsRNA NucleotidyltransferasesRNA Splicing FactorsCell Cycle ProteinsCWF19L1 protein, humanDbr1 protein, humanHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsRNA NucleotidyltransferasesRNA Splicing FactorsTranscription FactorsXAB2 protein, human

Identifiers

PMID25671812
PMCPMC4346921
OpenAlexW2020987336

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.