Evidence map›Paper›PMID 18458058›Full record

ArticleMolecular and cellular biology2008

Nuclear factor 45 (NF45) is a regulatory subunit of complexes with NF90/110 involved in mitotic control.

Deyu Guan, Nihal Altan-Bonnet, Andrew M Parrott, Cindy J Arrigo, Quan Li, Mohammed Khaleduzzaman, Hong Li, Chee-Gun Lee, Tsafi Pe'ery, Michael B Mathews

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

83 citing papers in PubMed, 128 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Negative regulation ofTranslational pediatrics · 2023
    Article
  11. Article
  12. Article
  13. The Polyvalent Role of NF90 in RNA Biology.International journal of molecular sciences · 2022
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

23 more citing papers are in PubMed but not listed here.

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

10 authors at 2 institutions in 1 country.

Deyu GuanDepartments of Biochemistry and Molecular Biology, New Jersey Medical School, University of Medicine and Dentistry of New Jersey, Newark, New Jersey 07103-1709, USA.
Nihal Altan-Bonnet
Andrew M Parrott
Cindy J Arrigo
Quan Li
Mohammed Khaleduzzaman
Hong Li
Chee-Gun Lee
Tsafi Pe'ery
Michael B Mathews
Rutgers New Jersey Medical SchoolRutgers, The State University of New Jersey · US

Funding

Functions of Double-stranded RNA Binding ProteinsR01AI034552 · NIAID · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI MATHEWS, MICHAEL B · 1993 to 2008
$4.4M
Proteomic Analysis of NF90 (Family) ComplexesF32GM069139 · NIGMS · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI ARRIGO, CINDY J · 2003 to 2004
$70k
NIAID NIH HHS AI34552NIAID NIH HHS R01 AI034552NIGMS NIH HHS F32 GM069139NIGMS NIH HHS GM069139
6 · The paper itself

Abstract

Nuclear factor 90 (NF90) and its C-terminally extended isoform, NF110, have been isolated as DNA- and RNA-binding proteins together with the less-studied protein NF45. These complexes have been implicated in gene regulation, but little is known about their cellular roles and whether they are redundant or functionally distinct. We show that heterodimeric core complexes, NF90-NF45 and NF110-NF45, exist within larger complexes that are more labile and contain multiple NF90/110 isoforms and additional proteins. Depletion of the NF45 subunit by RNA interference is accompanied by a dramatic decrease in the levels of NF90 and NF110. Reciprocally, depletion of NF90 but not of NF110 greatly reduces the level of NF45. Coregulation of NF90 and NF45 is a posttranscriptional phenomenon, resulting from protein destabilization in the absence of partners. Depletion of NF90-NF45 complexes retards cell growth by inhibition of DNA synthesis. Giant multinucleated cells containing nuclei attached by constrictions accumulate when either NF45 or NF90, but not NF110, is depleted. This study identified NF45 as an unstable regulatory subunit of NF90-NF45 complexes and uncovered their critical role in normal cell division. Furthermore, the study revealed that NF90 is functionally distinct from NF110 and is more important for cell growth.

Indexed as

MitosisCell LineCell NucleusGiant CellsHeLa CellsHumansNuclear Factor 45 ProteinNuclear Factor 90 ProteinsProtein Processing, Post-TranslationalRNA InterferenceILF2 protein, humanILF3 protein, humanNuclear Factor 45 ProteinNuclear Factor 90 Proteins

Identifiers

PMID18458058
PMCPMC2447130
OpenAlexW2114262960

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.