Evidence map›Paper›PMID 25484205›Full record

ArticleActa crystallographica. Section F, Structural biology communications2014

Structures of heterodimeric POZ domains of Miz1/BCL6 and Miz1/NAC1.

Mark Alexander Stead, Stephanie Claire Wright

Open access · bronzeAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

15 citing papers in PubMed, 31 citations in OpenAlex.

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  10. Structural analysis of the PATZ1 BTB domain homodimer.Acta crystallographica. Section D, Structural biology · 2020
    Article
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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

2 authors at 1 institution in 1 country.

Mark Alexander SteadSchool of Biology, University of Leeds, Leeds LS2 9JT, England.
Stephanie Claire WrightSchool of Biology, University of Leeds, Leeds LS2 9JT, England.
University of Leeds · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The POZ domain is an evolutionarily conserved protein-protein interaction domain that is found in approximately 40 mammalian transcription factors. POZ domains mediate both homodimerization and the heteromeric interactions of different POZ-domain transcription factors with each other. Miz1 is a POZ-domain transcription factor that regulates cell-cycle arrest and DNA-damage responses. The activities of Miz1 are altered by its interaction with the POZ-domain transcriptional repressors BCL6 and NAC1, and these interactions have been implicated in tumourigenesis in B-cell lymphomas and in ovarian serous carcinomas that overexpress BCL6 and NAC1, respectively. A strategy for the purification of tethered POZ domains that form forced heterodimers is described, and crystal structures of the heterodimeric POZ domains of Miz1/BCL6 and of Miz1/NAC1 are reported. These structures will be relevant for the design of therapeutics that target POZ-domain interaction interfaces.

Indexed as

Crystallography, X-RayDimerizationDNA-Binding ProteinsHumansKruppel-Like Transcription FactorsNeoplasm ProteinsProtein ConformationProto-Oncogene Proteins c-bcl-6Repressor ProteinsBCL6 protein, humanDNA-Binding ProteinsKruppel-Like Transcription FactorsNACC1 protein, humanNeoplasm ProteinsProto-Oncogene Proteins c-bcl-6Repressor ProteinsZBTB17 protein, humanBTB domainforced heterodimerMiz1/BCL6Miz1/NAC1tethered heterodimertranscriptional repressor

Identifiers

PMID25484205
PMCPMC4259219
OpenAlexW2038169075

What OpenQuestion holds

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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.