Evidence map›Paper›PMID 11029043›Full record

ArticleMolecular biology of the cell2000

Identification of a new vertebrate nucleoporin, Nup188, with the use of a novel organelle trap assay.

B R Miller, M Powers, M Park, W Fischer, D J Forbes

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

26 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. A rare cause of steroid-resistant nephrotic syndrome - a case report.Central-European journal of immunology · 2023
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  4. Review
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  12. Article
  13. The nuclear pore complex and nuclear transport.Cold Spring Harbor perspectives in biology · 2010
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. ELYS is a dual nucleoporin/kinetochore protein required for nuclear pore assembly and proper cell division.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  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

5 authors at 3 institutions in 1 country.

B R MillerDepartment of Biology, University of California at San Diego, La Jolla, California 92093, USA.
M Powers
M Park
W Fischer
D J Forbes
Salk Institute for Biological Studies · USUniversity of California, San Diego · USEmory University · US

Funding

FUNCTIONAL STUDY OF NATIVE AND SYNTHETIC NUCLEIR01GM033279 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI FORBES, DOUGLASS JANE · 1985 to 2015
$7.0M
PROTEIN SEQUENCER SYSTEMS10RR011404 · NCRR · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI FISCHER, WOLFGANG H · 1997 to 1997
–
NCRR NIH HHS S10 RR 11404-01A1NIGMS NIH HHS R01 GM033279NIGMS NIH HHS R01 GM33279
6 · The paper itself

Abstract

The study of the nuclear pore in vertebrates would benefit from a strategy to directly identify new nucleoporins and interactions between those nucleoporins. We have developed a novel two-step "organelle trap" assay involving affinity selection and in vitro pore assembly. In the first step, soluble proteins derived from Xenopus egg extracts are applied to a column containing a ligand of interest. The bound proteins are then tagged by biotinylation and eluted. In the second step, potential nucleoporins are selected for by virtue of their ability to assemble into annulate lamellae, a cytoplasmic mimic of nuclear pores. The incorporated proteins are then recognized by their biotin tag. Here we use the lectin wheat germ agglutinin (WGA) as ligand; WGA inhibits nuclear transport and has been shown to directly bind three known nucleoporins from Xenopus extract, Nup62, Nup98, and Nup214, all of which contain N-acetylglucosamine residues. Under reduced-stringency conditions, three additional proteins bind to WGA-Sepharose and are revealed by the organelle trap assay. We identified all three as partner nucleoporins. Two were discovered to be Xenopus Nup93 and Nup205. The third is a novel vertebrate nucleoporin, Nup188. This new vertebrate protein, Xenopus Nup188, exists in a complex with xNup93 and xNup205. The Nup93-Nup188-Nup205 complex does not bind directly to WGA but binds indirectly via the N-acetylglucosamine-modified nucleoporins. A gene encoding human Nup188 was also identified. The discovery of vertebrate Nup188, related to a yeast nucleoporin, and its novel protein-protein interactions illustrates the power of the two-step organelle trap assay and identifies new building blocks for constructing the nuclear pore.

Indexed as

Nuclear Pore Complex ProteinsSaccharomyces cerevisiae ProteinsXenopus ProteinsAcetylglucosamineAmino Acid SequenceAnimalsChromatography, AffinityFemaleFungal ProteinsLigandsMolecular Sequence DataMolecular WeightNuclear PoreNuclear ProteinsOvumPorinsAcetylglucosamineFungal ProteinsLigandsNuclear Pore Complex ProteinsNuclear ProteinsNUP188 protein, S cerevisiaeNup188 protein, XenopusPorinsSaccharomyces cerevisiae ProteinsWheat Germ AgglutininsXenopus Proteins

Identifiers

PMID11029043
PMCPMC15000
OpenAlexW2159577341

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.