Evidence map›Paper›PMID 19407373›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2009

Structure of the human Nac1 POZ domain.

Mark A Stead, Stephen B Carr, Stephanie C Wright

Abstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
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

12 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Structures of heterodimeric POZ domains of Miz1/BCL6 and Miz1/NAC1.Acta crystallographica. Section F, Structural biology communications · 2014
    Article
  7. Article
  8. Identification of the NAC1-regulated genes in ovarian cancer.The American journal of pathology · 2014
    Article
  9. Article
  10. Article
  11. Article
  12. 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

3 authors.

Mark A SteadInstitute of Molecular and Cellular Biology, University of Leeds, England, UK.
Stephen B Carr
Stephanie C Wright

Funding

Biotechnology and Biological Sciences Research Council
6 · The paper itself

Abstract

Nac1 is a POZ-domain transcription factor that is involved in the self-renewal of embryonic stem cells. It is overexpressed in ovarian serous carcinoma and targeting the interactions of its POZ domain is a potential therapeutic strategy. Nac1 lacks a zinc-finger DNA-binding domain and thereby differs from most other POZ-domain transcription factors. Here, the crystal structure of the Nac1 POZ domain at 2.1 A resolution is reported. The Nac1 POZ domain crystallized as a dimer in which the interaction interfaces between subunits resemble those found in the POZ-zinc finger transcription factors. The organization of the Nac1 POZ-domain core resembles reported POZ-domain structures, whereas the C-terminus differs markedly. The C-terminal alpha-helix of the Nac1 POZ domain is shorter than that observed in most other POZ-domain transcription factors; variation in the organization of this region may be a general feature of POZ-domain structures.

Indexed as

Amino Acid SequenceConserved SequenceCrystallography, X-RayHumansModels, MolecularMolecular Sequence DataNeoplasm ProteinsProtein Structure, TertiaryRepressor ProteinsSequence AlignmentNACC1 protein, humanNeoplasm ProteinsRepressor Proteins

Identifiers

PMID19407373
PMCPMC2675581

What OpenQuestion holds

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Registered trials

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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.