Evidence map›Paper›PMID 15199153›Full record

ArticleMolecular and cellular biology2004

Functional domains of the ubiquitous chromatin protein DEK.

Ferdinand Kappes, Ingo Scholten, Nicole Richter, Claudia Gruss, Tanja Waldmann

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

53 citing papers in PubMed, 98 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

5 authors at 1 institution in 1 country.

Ferdinand KappesDepartment of Biology, University of Konstanz, Germany.
Ingo Scholten
Nicole Richter
Claudia Gruss
Tanja Waldmann
University of Konstanz · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DEK was originally described as a proto-oncogene protein and is now known to be a major component of metazoan chromatin. DEK is able to modify the structure of DNA by introducing supercoils. In order to find interaction partners and functional domains of DEK, we performed yeast two-hybrid screens and mutational analyses. Two-hybrid screening yielded C-terminal fragments of DEK, suggesting that DEK is able to multimerize. We could localize the domain to amino acids 270 to 350 and show that multimerization is dependent on phosphorylation by CK2 kinase in vitro. We also found two DNA binding domains of DEK, one on a fragment including amino acids 87 to 187 and containing the SAF-box DNA binding motif, which is located between amino acids 149 and 187. This region is sufficient to introduce supercoils into DNA. The second DNA binding domain is located between amino acids 270 and 350 and thus overlaps the multimerization domain. We show that the two DNA-interacting domains differ in their binding properties and in their abilities to respond to CK2 phosphorylation.

Indexed as

Amino Acid SequenceBinding SitesCasein Kinase IIChromosomal Proteins, Non-HistoneDimerizationDNA, SuperhelicalHeLa CellsHumansOncogene ProteinsPhosphorylationPoly-ADP-Ribose Binding ProteinsProtein Serine-Threonine KinasesProtein Structure, TertiaryProto-Oncogene MasTwo-Hybrid System TechniquesCasein Kinase IIChromosomal Proteins, Non-HistoneDEK protein, humanDNA, SuperhelicalMAS1 protein, humanOncogene ProteinsPoly-ADP-Ribose Binding ProteinsProtein Serine-Threonine KinasesProto-Oncogene Mas

Identifiers

PMID15199153
PMCPMC480879
OpenAlexW2166130130

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.