Evidence map›Paper›PMID 1824847›Full record

ArticleThe Journal of cell biology1991

Multiple pathways in nuclear transport: the import of U2 snRNP occurs by a novel kinetic pathway.

N Michaud, D S Goldfarb

Abstract read
In one paragraph

Article in The Journal of cell biology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
–field-weighted citation impact
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

35 citing papers in PubMed.

  1. Review
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  6. Inhibition of mRNA export in vertebrate cells by nuclear export signal conjugates.Proceedings of the National Academy of Sciences of the United States of America · 1997
    Article
  7. Article
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  9. A novel class of RanGTP binding proteins.The Journal of cell biology · 1997
    Article
  10. Article
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  12. Article
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  15. Article
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  17. Article
  18. Nucleocytoplasmic transport.The Biochemical journal · 1994
    Review
  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.

N MichaudDepartment of Biology, University of Rochester, New York 14627.
D S Goldfarb

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein import to the nucleus is a signal-mediated process that exhibits saturation kinetics. We investigated whether signal bearing proteins compete with U2 and U6 snRNPs during import. When injected into Xenopus oocytes, saturating concentrations of P(Lys)-BSA, a protein bearing multiple nuclear localization signals from SV40 large T-antigen, reduce the rate of [125I]P(Lys)-BSA and of [125I]nucleoplasmin import, consistent with their competing for and sharing the same limiting component of the import apparatus. In contrast, saturating concentrations of P(Lys)-BSA do not reduce the rate of HeLa [32P]U2 snRNP assembly or import. The import of U6 snRNP is also competed by P(Lys)-BSA. We conclude that U2 snRNP is imported into oocyte nuclei by a kinetic pathway that is distinct from the one followed by P(Lys)-BSA, nucleoplasmin, and U6 snRNP.

Indexed as

AnimalsBiological TransportCell NucleusFemaleHeLa CellsHumansKineticsOocytesPrecipitin TestsRibonucleoproteinsRibonucleoproteins, Small NuclearSerum Albumin, BovineSignal TransductionXenopus laevisRibonucleoproteinsRibonucleoproteins, Small NuclearSerum Albumin, Bovine

Identifiers

PMID1824847
PMCPMC2288826

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LicenceCC BY-NC-SA
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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.