Evidence map›Paper›PMID 19805193›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Structure of a trimeric nucleoporin complex reveals alternate oligomerization states.

Vivien Nagy, Kuo-Chiang Hsia, Erik W Debler, Martin Kampmann, Andrew M Davenport, Günter Blobel, André Hoelz

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed.

  1. Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026
    Review
  2. Structure and Function of the Nuclear Pore Complex.Cold Spring Harbor perspectives in biology · 2022
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. The Structure of the Nuclear Pore Complex (An Update).Annual review of biochemistry · 2019
    Review
  9. Evolutionary divergence of the nuclear pore complex from fungi to metazoans.Protein science : a publication of the Protein Society · 2019
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Atomic structure of the Y complex of the nuclear pore.Nature structural & molecular biology · 2015
    Article
  17. Article
  18. Article
  19. Article
  20. Evidence for an evolutionary relationship between the large adaptor nucleoporin Nup192 and karyopherins.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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

7 authors.

Vivien NagyLaboratory of Cell Biology, Howard Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA.
Kuo-Chiang Hsia
Erik W Debler
Martin Kampmann
Andrew M Davenport
Günter Blobel
André Hoelz

Funding

Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
Molecular Basis of mRNA ExportR01GM117360 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI Andre Hoelz · 2016 to 2026
$2.6M
Howard Hughes Medical InstituteNIBIB NIH HHS P30 EB009998NIGMS NIH HHS R01 GM117360
6 · The paper itself

Abstract

The heptameric Nup84 complex constitutes an evolutionarily conserved building block of the nuclear pore complex. Here, we present the crystal structure of the heterotrimeric Sec13 x Nup145C x Nup84 complex, the centerpiece of the heptamer, at 3.2-A resolution. Nup84 forms a U-shaped alpha-helical solenoid domain, topologically similar to two other members of the heptamer, Nup145C and Nup85. The interaction between Nup84 and Nup145C is mediated via a hydrophobic interface located in the kink regions of the two solenoids that is reinforced by additional interactions of two long Nup84 loops. The Nup84 binding site partially overlaps with the homo-dimerization interface of Nup145C, suggesting competing binding events. Fitting of the elongated Z-shaped heterotrimer into electron microscopy (EM) envelopes of the heptamer indicates that structural changes occur at the Nup145C x Nup84 interface. Docking the crystal structures of all heptamer components into the EM envelope constitutes a major advance toward the completion of the structural characterization of the Nup84 complex.

Indexed as

Binding, CompetitiveBinding SitesCrystallography, X-RayModels, MolecularMultiprotein ComplexesNuclear PoreNuclear Pore Complex ProteinsProtein Interaction Domains and MotifsProtein Structure, QuaternarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsMultiprotein ComplexesNuclear Pore Complex ProteinsNUP145 protein, S cerevisiaeNUP84 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSEC13 protein, S cerevisiae

Identifiers

PMID19805193
PMCPMC2764879

What OpenQuestion holds

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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.