Evidence map›Paper›PMID 22833610›Full record

ArticleNucleic acids research2012

NF45 dimerizes with NF90, Zfr and SPNR via a conserved domain that has a nucleotidyltransferase fold.

Urszula M Wolkowicz, Atlanta G Cook

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

40 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. The Ubiquitination ofBiology · 2025
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  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. The Polyvalent Role of NF90 in RNA Biology.International journal of molecular sciences · 2022
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. The World of Cyclic Dinucleotides in Bacterial Behavior.Molecules (Basel, Switzerland) · 2020
    Review
  18. Article
  19. Article
  20. 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

2 authors at 2 institutions in 1 country.

Urszula M WolkowiczWellcome Trust Centre for Cell Biology, University of Edinburgh, Michael Swann Building, Edinburgh, Midlothian EH9 3JR, UK.
Atlanta G Cook
University of Edinburgh · GBWellcome Centre for Cell Biology · GB

Funding

Medical Research Council G1000520Wellcome Trust 077707Wellcome Trust 092076
6 · The paper itself

Abstract

Nuclear factors NF90 and NF45 form a complex involved in a variety of cellular processes and are thought to affect gene expression both at the transcriptional and translational level. In addition, this complex affects the replication of several viruses through direct interactions with viral RNA. NF90 and NF45 dimerize through their common 'DZF' domain (domain associated with zinc fingers). NF90 has additional double-stranded RNA-binding domains that likely mediate its association with target RNAs. We present the crystal structure of the NF90/NF45 dimerization complex at 1.9-Å resolution. The DZF domain shows structural similarity to the template-free nucleotidyltransferase family of RNA modifying enzymes. However, both NF90 and NF45 have lost critical catalytic residues during evolution and are therefore not functional enzymes. Residues on NF90 that make up its interface with NF45 are conserved in two related proteins, spermatid perinuclear RNA-binding protein (SPNR) and zinc-finger RNA-binding protein (Zfr). Using a co-immunoprecipitation assay and site-specific mutants, we demonstrate that NF45 is also able to recognize SPNR and Zfr through the same binding interface, revealing that NF45 is able to form a variety of cellular complexes with other DZF-domain proteins.

Indexed as

Amino Acid SequenceAnimalsConserved SequenceDimerizationHumansMiceMicrotubule-Associated ProteinsModels, MolecularMolecular Sequence DataNuclear Factor 45 ProteinNuclear Factor 90 ProteinsNucleotidesNucleotidyltransferasesPolynucleotide AdenylyltransferaseProtein FoldingProtein Structure, TertiaryIlf2 protein, mouseMicrotubule-Associated ProteinsNuclear Factor 45 ProteinNuclear Factor 90 ProteinsNucleotidesNucleotidyltransferasesPolynucleotide AdenylyltransferaseRNA-Binding ProteinsSTRBP protein, humanZFR protein, human

Identifiers

PMID22833610
PMCPMC3467086
OpenAlexW1971773731

What OpenQuestion holds

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LicenceCC BY-NC
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.