Evidence map›Paper›PMID 12058066›Full record

ArticleMolecular biology of the cell2002

The RNA binding activity of a ribosome biogenesis factor, nucleophosmin/B23, is modulated by phosphorylation with a cell cycle-dependent kinase and by association with its subtype.

Mitsuru Okuwaki, Masafumi Tsujimoto, Kyosuke Nagata

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

79 citing papers in PubMed, 177 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. Multiscale biophysical analysis of nucleolus disassembly during mitosis.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Article
  9. The Role of Nucleophosmin 1 (Life (Basel, Switzerland) · 2022
    Review
  10. Dephosphorylation in nuclear reassembly after mitosis.Frontiers in cell and developmental biology · 2022
    Review
  11. Article
  12. Nucleophosmin in Its Interaction with Ligands.International journal of molecular sciences · 2020
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Glycogen synthase kinase-3 and alternative splicing.Wiley interdisciplinary reviews. RNA · 2018
    Review
  19. Article
  20. Nucleolar Division in the Promastigote Stage ofBioMed research international · 2018
    Article

19 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

3 authors at 2 institutions in 1 country.

Mitsuru OkuwakiDepartment of Infection Biology, Institute of Basic Medical Sciences, University of Tsukuba, 1-1-1 Tennohdai, Tsukuba 305-8575, Japan.
Masafumi Tsujimoto
Kyosuke Nagata
University of Tsukuba · JPRIKEN · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nucleophosmin/B23 is a nucleolar phosphoprotein. It has been shown that B23 binds to nucleic acids, digests RNA, and is localized in nucleolar granular components from which preribosomal particles are transported to cytoplasm. The intracellular localization of B23 is significantly changed during the cell cycle. Here, we have examined the cellular localization of B23 proteins and the effect of mitotic phosphorylation of B23.1 on its RNA binding activity. Two splicing variants of B23 proteins, termed B23.1 and B23.2, were complexed both in vivo and in vitro. The RNA binding activity of B23.1 was impaired by hetero-oligomer formation with B23.2. Both subtypes of B23 proteins were phosphorylated during mitosis by cyclin B/cdc2. The RNA binding activity of B23.1 was repressed through cyclin B/cdc2-mediated phosphorylation at specific sites in B23. Thus, the RNA binding activity of B23.1 is stringently modulated by its phosphorylation and subtype association. Interphase B23.1 was mainly localized in nucleoli, whereas B23.2 and mitotic B23.1, those of which were incapable of binding to RNA, were dispersed throughout the nucleoplasm and cytoplasm, respectively. These results suggest that nucleolar localization of B23.1 is mediated by its ability to associate with RNA.

Indexed as

ActinsAlternative SplicingAmino Acid SubstitutionAnimalsBase SequenceCell NucleolusChickensCyclin-Dependent KinasesDeoxyribonuclease IDNA PrimersEnhancer Elements, GeneticGenes, Immediate-EarlyGenetic VariationHeLa CellsHumansIsoenzymesActinsCyclin-Dependent KinasesDeoxyribonuclease IDNA PrimersIsoenzymesNPM1 protein, humanNuclear ProteinsNucleophosminProtein IsoformsRecombinant ProteinsRibonuclease, PancreaticRNA-Binding Proteins

Identifiers

PMID12058066
PMCPMC117621
OpenAlexW2113433319

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.