Evidence map›Paper›PMID 9190204›Full record

ArticleMolecular biology of the cell1997

Topogenesis of a nucleolar protein: determination of molecular segments directing nucleolar association.

R F Zirwes, A P Kouzmenko, J M Peters, W W Franke, M S Schmidt-Zachmann

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

18 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Nucleophosmin and human cancer.Cancer detection and prevention · 2006
    Review
  9. Article
  10. Article
  11. Conventional and nonconventional roles of the nucleolus.International review of cytology · 2002
    Review
  12. Identification of a sequence element directing a protein to nuclear speckles.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Identification of a small, very acidic constitutive nucleolar protein (NO29) as a member of the nucleoplasmin family.Proceedings of the National Academy of Sciences of the United States of America · 1997
    Article
  18. Review
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

5 authors at 1 institution in 1 country.

R F ZirwesDivision of Cell Biology, German Cancer Research Center, Heidelberg, Federal Republic of Germany.
A P Kouzmenko
J M Peters
W W Franke
M S Schmidt-Zachmann
German Cancer Research Center · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To identify the element(s) in nucleolar proteins which determine nucleolus-specific topogenesis, we have used different kinds of cDNA constructs encoding various chimeric combinations of mutants of the constitutive nucleolar protein NO38 (B23): 1) with an amino terminally placed short "myc tag"; 2) with two different carboxyl terminally attached large alpha-helical coiled coil structures, the lamin A rod domain or the rod domain of vimentin; 3) with the sequence-related nucleoplasmic histone-binding protein nucleo-plasmin; and 4) with the soluble cytoplasmic protein pyruvate kinase. To avoid the problem of formation of complexes with endogenous wild-type (wt) molecules and "piggyback" localization, special care was taken to secure that the mutants and chimeras used did not oligomerize as is typical of protein NO38 (B23). Using microinjection and transfection of cultured cells, we found that the segment comprising the amino-terminal 123 amino acids (aa) alone was sufficient to effect nucleolar accumulation of the construct molecules, including the chimeras with the entire rod domains of lamin A and vimentin. However, when the amino-terminal 109 aa were deleted, the molecules still associated with the nucleolus. The results of further deletion experiments and of domain swaps with nucleoplasmin all point to the topogenic importance of two independent molecular regions located at both the amino- and carboxyl-terminal end. Our definition of dominant elements determining the nucleolar localization of protein NO38 (B23) as well as of diverse nonnucleolar proteins will help to identify its local binding partner(s) and functions, the construction of probes examining other proteins or sequence elements within the nucleolar microenvironment, and the generation of cells with an altered nuclear architecture.

Indexed as

AnimalsBinding SitesCell NucleolusDNA Mutational AnalysisEpitopesHumansLaminsLamin Type AMicroinjectionsMutationNuclear ProteinsNucleophosminRecombinant Fusion ProteinsRNA, MessengerXenopus laevisEpitopesLaminsLamin Type ANuclear ProteinsNucleophosminRecombinant Fusion ProteinsRNA, Messenger

Identifiers

PMID9190204
PMCPMC276076
OpenAlexW1979572236

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.