Evidence map›Paper›PMID 9858592›Full record

ArticleMolecular and cellular biology1999

Characterization of the DNA-binding and dimerization properties of the nuclear orphan receptor germ cell nuclear factor.

H Greschik, J M Wurtz, P Hublitz, F Köhler, D Moras, R Schüle

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1999. 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
2.0field-weighted citation impact, top 13% 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, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Multi-faceted regulation of CREB family transcription factors.Frontiers in molecular neuroscience · 2024
    Review
  4. The expanding roles of Nr6a1 in development and evolution.Frontiers in cell and developmental biology · 2024
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. 0610009K11Rik, a testis-specific and germ cell nuclear receptor-interacting protein.Biochemical and biophysical research communications · 2008
    Article
  13. Article
  14. Article
  15. 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

6 authors at 1 institution in 1 country.

H GreschikInstitut für Experimentelle Krebsforschung, Klinik für Tumorbiologie an der Universität Freiburg, D-79106 Freiburg, Germany.
J M Wurtz
P Hublitz
F Köhler
D Moras
R Schüle
Institut de génétique et de biologie moléculaire et cellulaire · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The orphan receptor germ cell nuclear factor (GCNF) is a member of the superfamily of nuclear receptors. During development, GCNF exhibits a restricted brain-specific expression pattern, whereas GCNF expression in the adult is germ cell specific. Therefore, the receptor may participate in the regulation of neurogenesis and reproductive functions. No natural GCNF target gene has yet been identified, but recent data demonstrate specific and high-affinity binding of GCNF either to the direct repeat DNA element AGGTCAAGGTCA (DR0) or to extended half-sites, such as TCAAGGTCA. In this study, we show that murine GCNF (mGCNF) can bind as a homodimer to extended half-sites, thus describing a novel property within the nuclear receptor superfamily. Homodimeric binding to extended half-sites requires the presence of a dimerization function within the mGCNF DNA-binding domain (DBD) and a novel dimerization surface encompassing the putative helix 3 and the helix 12 region of the mGCNF ligand-binding domain (LBD). In addition, the mGCNF LBD has the potential to adopt different conformations with distinct dimerization properties. The helix 12 region of the mGCNF LBD not only regulates the switch between these dimerization conformations but also dictates the DNA-binding behavior and transcriptional properties of the different dimerization conformations. In summary, our findings describe unique DNA-binding and dimerization properties of a nuclear receptor and suggest a novel mechanism that allows mGCNF to modulate target gene activity.

Indexed as

Amino Acid SequenceAnimalsBinding, CompetitiveBinding SitesCell LineCell Line, TransformedCOUP Transcription Factor ICricetinaeDimerizationDNADNA-Binding ProteinsHumansLigandsMiceMolecular Sequence DataMutagenesisCOUP Transcription Factor IDNADNA-Binding ProteinsLigandsNR2F1 protein, humanNr2f1 protein, mouseNR6A1 protein, humanNr6a1 protein, mouseNuclear Receptor Subfamily 6, Group A, Member 1Receptors, Cytoplasmic and NuclearReceptors, Retinoic AcidRetinoid X ReceptorsTranscription Factors

Identifiers

PMID9858592
PMCPMC83926
OpenAlexW2099000680

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.