Evidence map›Paper›PMID 3097026›Full record

ArticleThe Journal of cell biology1986

In vitro transport of a fluorescent nuclear protein and exclusion of non-nuclear proteins.

D D Newmeyer, D R Finlay, D J Forbes

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1986. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

81 citing papers in PubMed, 211 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Small-molecule high-throughput screening utilizing Xenopus egg extract.Methods in molecular biology (Clifton, N.J.) · 2015
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  12. Cell-cycle-dependent phosphorylation of the nuclear pore Nup107-160 subcomplex.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
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  16. Kinetics and mechanism of DNA uptake into the cell nucleus.Proceedings of the National Academy of Sciences of the United States of America · 2001
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  17. Article
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21 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.

D D Newmeyer
D R Finlay
D J Forbes

Funding

FUNCTIONAL STUDY OF NATIVE AND SYNTHETIC NUCLEIR01GM033279 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI FORBES, DOUGLASS JANE · 1985 to 2015
$7.0M
NIGMS NIH HHS GM-33279NIGMS NIH HHS R01 GM033279
6 · The paper itself

Abstract

An in vitro system was developed that provides a quick microscopic assay for nuclear transport. The assay uses an extract of Xenopus eggs, normal or synthetic nuclei, and a fluorescently labeled nuclear protein, nucleoplasmin. This in vitro system accurately mimics in vivo nuclear transport, both in exclusivity and in the amount of accumulation observed (up to 17-fold). Selective accumulation of fluorescent nucleoplasmin is observed microscopically within 30 min with rat liver nuclei, Xenopus embryonic nuclei, regrown Xenopus sperm nuclei, or nuclei reconstituted in vitro from bacteriophage lambda DNA. This transport requires the signal domain of nucleoplasmin. Furthermore, the ability of nuclei to accumulate nucleoplasmin directly correlates with their ability to exclude the fluorescent non-nuclear proteins, FITC-immunoglobulin and phycoerythrin. An active transport model would predict that nuclear transport be temperature- and energy-dependent and that inhibition of transport by either low temperature or energy depletion would be reversible. Both predictions were confirmed in our system. Nucleoplasmin accumulation increases with temperature, while the protein is completely excluded at 0 degrees C. The effects of low temperature are reversible. As found for 125I-labeled nucleoplasmin (Newmeyer, D. D., J. M. Lucocq, T. R. Bürglin, and E. M. De Robertis, 1986, EMBO (Eur. Mol. Biol. Organ.) J., 5:501-510), transport of fluorescent nucleoplasmin is inhibited by ATP depletion. This effect is reversed by later ATP addition. Under ATP-depleted conditions non-nuclear proteins continue to be excluded. These results argue for a direct role of ATP in transport rather than for a simple role in preserving envelope integrity. In a first step towards defining the minimum requirements for a transport medium, egg extracts were depleted of membrane vesicles. Membrane-depleted extracts neither support transport nor maintain the integrity of the nuclear envelope.

Indexed as

Nuclear ProteinsPhosphoproteinsAnimalsCell NucleusFemaleFluorescein-5-isothiocyanateFluoresceinsLiverMicroscopy, FluorescenceNucleoplasminsNucleoproteinsOocytesProteinsRatsThiocyanatesXenopusFluorescein-5-isothiocyanateFluoresceinsNuclear ProteinsNucleoplasminsNucleoproteinsPhosphoproteinsProteinsThiocyanates

Identifiers

PMID3097026
PMCPMC2114618
OpenAlexW2112284540

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.