Evidence map›Paper›PMID 29082557›Full record

ArticleProteins2018

The nuclear DEK interactome supports multi-functionality.

Eric A Smith, Eric F Krumpelbeck, Anil G Jegga, Malte Prell, Marie M Matrka, Ferdinand Kappes, Kenneth D Greis, Abdullah M Ali, Amom R Meetei, Susanne I Wells

Open access · greenAbstract read
In one paragraph

Article in Proteins, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

13 citing papers in PubMed, 27 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

10 authors at 4 institutions in 3 countries.

Eric A SmithDepartment of Oncology, Cincinnati Children's Hospital Medical Center, Cincinnati, Ohio, 45219.
Eric F KrumpelbeckDepartment of Oncology, Cincinnati Children's Hospital Medical Center, Cincinnati, Ohio, 45219.
Anil G JeggaDivision of Biomedical Informatics, Cincinnati Children's Hospital Medical Center, Cincinnati, Ohio, 45219.
Malte PrellInstitute of Biochemistry and Molecular Biology, Medical School, RWTH Aachen University, Aachen, 52074, Germany.
Marie M MatrkaDepartment of Oncology, Cincinnati Children's Hospital Medical Center, Cincinnati, Ohio, 45219.
Ferdinand KappesInstitute of Biochemistry and Molecular Biology, Medical School, RWTH Aachen University, Aachen, 52074, Germany.
Kenneth D GreisDepartment of Cancer Biology, University of Cincinnati College of Medicine, Cincinnati, Ohio, 45219.
Abdullah M AliDepartment of Oncology, Cincinnati Children's Hospital Medical Center, Cincinnati, Ohio, 45219.
Amom R MeeteiDepartment of Oncology, Cincinnati Children's Hospital Medical Center, Cincinnati, Ohio, 45219.
Susanne I WellsDepartment of Oncology, Cincinnati Children's Hospital Medical Center, Cincinnati, Ohio, 45219.ORCID http://orcid.org/0000-0002-7234-676X
Cincinnati Children's Hospital Medical Center · USRWTH Aachen University · DEUniversity of Cincinnati Medical Center · USXi’an Jiaotong-Liverpool University · CN

Funding

Role and Regulaton of the Human DEK Proto-OncogeneR01CA116316 · NCI · CINCINNATI CHILDRENS HOSP MED CTR · PI WELLS, SUSANNE I · 2006 to 2016
$2.9M
Papillomavirus Proteins Mediating Cancer and SenescenceR01CA102357 · NCI · CINCINNATI CHILDRENS HOSP MED CTR · PI WELLS, SUSANNE I · 2004 to 2013
$2.6M
NCI NIH HHS R01 CA102357NCI NIH HHS R01 CA116316
6 · The paper itself

Abstract

DEK is an oncoprotein that is overexpressed in many forms of cancer and participates in numerous cellular pathways. Of these different pathways, relevant interacting partners and functions of DEK are well described in regard to the regulation of chromatin structure, epigenetic marks, and transcription. Most of this understanding was derived by investigating DNA-binding and chromatin processing capabilities of the oncoprotein. To facilitate the generation of mechanism-driven hypotheses regarding DEK activities in underexplored areas, we have developed the first DEK interactome model using tandem-affinity purification and mass spectrometry. With this approach, we identify IMPDH2, DDX21, and RPL7a as novel DEK binding partners, hinting at new roles for the oncogene in de novo nucleotide biosynthesis and ribosome formation. Additionally, a hydroxyurea-specific interaction with replication protein A (RPA) was observed, suggesting that a DEK-RPA complex may form in response to DNA replication fork stalling. Taken together, these findings highlight diverse activities for DEK across cellular pathways and support a model wherein this molecule performs a plethora of functions.

Indexed as

Binding SitesChromatinChromatography, High Pressure LiquidChromosomal Proteins, Non-HistoneDNADNA-Binding ProteinsHEK293 CellsHeLa CellsHumansMolecular StructureOncogene ProteinsPoly-ADP-Ribose Binding ProteinsProtein BindingProtein ConformationStructure-Activity RelationshipTandem Mass SpectrometryChromatinChromosomal Proteins, Non-HistoneDEK protein, humanDNADNA-Binding ProteinsOncogene ProteinsPoly-ADP-Ribose Binding ProteinsDDX21DEKIMPDH2interactomemass spectrometryribosomeRPA

Identifiers

PMID29082557
PMCPMC5730476
OpenAlexW2767093360

What OpenQuestion holds

Textmetadata
LicenceTDM
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.