Evidence map›Paper›PMID 3119324›Full record

ArticleThe EMBO journal1987

The nuclear migration signal of Xenopus laevis nucleoplasmin.

T R Bürglin, E M De Robertis

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
14.3field-weighted citation impact, top 1% 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

65 citing papers in PubMed, 177 citations in OpenAlex.

  1. Review
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  12. Nucleocytoplasmic transport.The Biochemical journal · 1994
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. The T-DNA-linked VirD2 protein contains two distinct functional nuclear localization signals.Proceedings of the National Academy of Sciences of the United States of America · 1992
    Article
  19. Article
  20. Article

5 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

2 authors at 1 institution in 1 country.

T R BürglinBiocenter of the University of Basel, Switzerland.
E M De Robertis
University of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nucleoplasmin is the most abundant protein in the nucleus of Xenopus laevis oocytes. Its ability to target to the nucleus when microinjected into the cytoplasm has been the subject of many studies central to our understanding of how proteins segregate into nuclei. Using a cDNA clone we constructed beta-galactosidase-nucleoplasmin hybrids in modified bacterial expression vectors. The fusion proteins were expressed in Escherichia coli, purified and injected into the cytoplasm of X. laevis oocytes. The distribution of the fusion proteins between the cytoplasmic and nuclear compartments were analysed after incubation of various lengths of time. The results show that the signal sequence for nuclear transport is located close to the carboxy terminus of the protein. The signal sequence has been mapped to a small stretch of amino acids, containing a stretch of four lysines analogous to the SV40 large-T antigen signal.

Indexed as

Cloning, MolecularGenesPhosphoproteinsAmino Acid SequenceAnimalsBase Sequencebeta-GalactosidaseChromosome DeletionEscherichia coliFemaleGenetic VectorsMolecular Sequence DataNuclear ProteinsNucleoplasminsOocytesProtein Biosynthesisbeta-GalactosidaseNuclear ProteinsNucleoplasminsPhosphoproteins

Identifiers

PMID3119324
PMCPMC553682
OpenAlexW1549525782

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.