Evidence map›Paper›PMID 7876300›Full record

ArticleThe Journal of cell biology1995

Reconstituted nuclei depleted of a vertebrate GLFG nuclear pore protein, p97, import but are defective in nuclear growth and replication.

M A Powers, C Macaulay, F R Masiarz, D J Forbes

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

69 citing papers in PubMed, 126 citations in OpenAlex.

  1. Article
  2. NovelCancers · 2023
    Article
  3. Article
  4. Article
  5. O-GlcNAc-ylation in the Nuclear Pore Complex.Cellular and molecular bioengineering · 2016
    Article
  6. Intranuclear dynamics of the Nup107-160 complex.Molecular biology of the cell · 2015
    Article
  7. Article
  8. Article
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  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
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  20. Article

9 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

4 authors at 1 institution in 1 country.

M A PowersDepartment of Biology 0347, University of California at San Diego, La Jolla 92093-0347.
C Macaulay
F R Masiarz
D J Forbes
University of California San Diego · US

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 R01 GM033279NIGMS NIH HHS R01 GM33279
6 · The paper itself

Abstract

Xenopus egg extracts provide a powerful system for in vitro reconstitution of nuclei and analysis of nuclear transport. Such cell-free extracts contain three major N-acetylglucosaminylated proteins: p200, p97, and p60. Both p200 and p60 have been found to be components of the nuclear pore. Here, the role of p97 has been investigated. Xenopus p97 was isolated and antisera were raised and affinity purified. Immunolocalization experiments indicate that p97 is present in a punctate pattern on the nuclear envelope and also in the nuclear interior. Peptide sequence analysis reveals that p97 contains a GLFG motif which defines a family of yeast nuclear pore proteins, as well as a peptide that is identical at 11/15 amino acids to a specific member of the GLFG family, NUP116. An additional peptide is highly homologous to a second sequence found in NUP116 and other members of the yeast GLFG family. A monoclonal antibody to the GLFG domain cross-reacts with a major Xenopus protein of 97 kD and polyclonal antiserum to p97 recognizes the yeast GLFG nucleoporin family. The p97 antiserum was used to immunodeplete Xenopus egg cytosol and p97-deficient nuclei were reconstituted. The p97-depleted nuclei remained largely competent for nuclear protein import. However, in contrast to control nuclei, nuclei deficient in p97 fail to grow in size over time and do not replicate their chromosomal DNA. ssDNA replication in such extracts remains unaffected. Addition of the N-acetylglucosaminylated nuclear proteins of Xenopus or rat reverses these replication and growth defects. The possible role(s) of p97 in these nuclear functions is discussed.

Indexed as

Nuclear Pore Complex ProteinsSaccharomyces cerevisiae ProteinsAmino Acid SequenceAnimalsBiological TransportCell NucleusChromosomesDNA ReplicationFemaleFluorescent Antibody TechniqueFungal ProteinsMembrane ProteinsMolecular Sequence DataNuclear EnvelopeNuclear ProteinsRepetitive Sequences, Nucleic AcidFungal ProteinsMembrane ProteinsNuclear Pore Complex Proteinsnuclear pore protein p97Nuclear ProteinsNUP100 protein, S cerevisiaeNUP116 protein, S cerevisiaeNUP145 protein, S cerevisiaeRNA-Binding ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID7876300
PMCPMC2120401
OpenAlexW2098238189

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.