Evidence map›Paper›PMID 19576787›Full record

ArticleStructure (London, England : 1993)2009

The structure of the scaffold nucleoporin Nup120 reveals a new and unexpected domain architecture.

Nina C Leksa, Stephen G Brohawn, Thomas U Schwartz

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

40 citing papers in PubMed, 62 citations in OpenAlex.

  1. Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026
    Review
  2. Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025
    Review
  3. Structure and Function of the Nuclear Pore Complex.Cold Spring Harbor perspectives in biology · 2022
    Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. The Structure of the Nuclear Pore Complex (An Update).Annual review of biochemistry · 2019
    Review
  13. Evolutionary divergence of the nuclear pore complex from fungi to metazoans.Protein science : a publication of the Protein Society · 2019
    Article
  14. Modeling of the mechano-chemical behaviour of the nuclear pore complex: current research and perspectives.Integrative biology : quantitative biosciences from nano to macro · 2016
    Review
  15. Review
  16. The Structure Inventory of the Nuclear Pore Complex.Journal of molecular biology · 2016
    Review
  17. Atomic structure of the Y complex of the nuclear pore.Nature structural & molecular biology · 2015
    Article
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Nina C LeksaDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Stephen G Brohawn
Thomas U Schwartz
Massachusetts Institute of Technology · US

Funding

High Resolution Assembly Structure of The Nuclear Pore ComplexR01GM077537 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SCHWARTZ, THOMAS · 2007 to 2019
$4.3M
NIGMS NIH HHS GM77537NIGMS NIH HHS R01 GM077537
6 · The paper itself

Abstract

Nucleocytoplasmic transport is mediated by nuclear pore complexes (NPCs), enormous protein assemblies residing in circular openings in the nuclear envelope. The NPC is modular, with transient and stable components. The stable core is essentially built from two multiprotein complexes, the Y-shaped heptameric Nup84 complex and the Nic96 complex, arranged around an eightfold axis. We present the crystal structure of Nup120(1-757), one of the two short arms of the Y-shaped Nup84 complex. The protein adopts a compact oval shape built around a novel bipartite alpha-helical domain intimately integrated with a beta-propeller domain. The domain arrangement is substantially different from the Nup85*Seh1 complex, which forms the other short arm of the Y. With the data presented here, we establish that all three branches of the Y-shaped Nup84 complex are tightly connected by helical interactions and that the beta-propellers likely form interaction site(s) to neighboring complexes.

Indexed as

Protein Structure, TertiaryChromatography, GelCrystallizationCrystallography, X-RayGreen Fluorescent ProteinsHumansMicroscopy, FluorescenceModels, MolecularMultiprotein ComplexesMutationNuclear PoreNuclear Pore Complex ProteinsNuclear ProteinsProtein BindingProtein FoldingProtein Structure, SecondaryGreen Fluorescent ProteinsMultiprotein ComplexesNuclear Pore Complex ProteinsNuclear ProteinsNUP120 protein, S cerevisiaeNUP145 protein, S cerevisiaeNUP160 protein, humanNUP85 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID19576787
PMCPMC2743489
OpenAlexW2068160472

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.