Evidence map›Paper›PMID 23499022›Full record

ArticleStructure (London, England : 1993)2013

Structural and functional studies of the 252 kDa nucleoporin ELYS reveal distinct roles for its three tethered domains.

Silvija Bilokapic, Thomas U Schwartz

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.9field-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

30 citing papers in PubMed, 43 citations in OpenAlex.

  1. Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025
    Review
  2. Article
  3. Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023
    Review
  4. eLife · 2023
    Article
  5. Structure and Function of the Nuclear Pore Complex.Cold Spring Harbor perspectives in biology · 2022
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. The Journal of biological chemistry · 2020
    Article
  14. Article
  15. The Structure of the Nuclear Pore Complex (An Update).Annual review of biochemistry · 2019
    Review
  16. Article
  17. Evolutionary divergence of the nuclear pore complex from fungi to metazoans.Protein science : a publication of the Protein Society · 2019
    Article
  18. Article
  19. Genetic Analyses ofG3 (Bethesda, Md.) · 2018
    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

2 authors at 1 institution in 1 country.

Silvija BilokapicDepartment of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.
Thomas U Schwartz
Massachusetts Institute of Technology · US

Funding

Y-FAMILY POLYMERASES AND CO-FACTORS IN TRANSLESION REPLICATIONP41RR015301 · NCRR · CORNELL UNIVERSITY ITHACA · PI EISENBERG, DAVID · 2001 to 2011
$28.2M
High Resolution Assembly Structure of The Nuclear Pore ComplexR01GM077537 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SCHWARTZ, THOMAS · 2007 to 2019
$4.3M
Acquisition of Automated Nanoscale Crystallization EquipmentS10RR024526 · NCRR · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SCHWARTZ, THOMAS · 2009 to 2009
$489k
NCRR NIH HHS P41 RR015301NCRR NIH HHS S10 RR024526NIGMS NIH HHS GM077537NIGMS NIH HHS R01 GM077537
6 · The paper itself

Abstract

In metazoa, the nuclear envelope (NE), together with the embedded nuclear pore complexes (NPCs), breaks down and reassembles during cell division. It is suggested that ELYS, a nucleoporin, binds to chromatin in an initial step of postmitotic NPC assembly and subsequently recruits the essential Y-subcomplex, the major scaffolding unit of the NPC. Here, we show that ELYS contains three domains: an N-terminal β-propeller domain, a central α-helical domain, and a C-terminal disordered region. While the disordered region is responsible for the interactions with chromatin, the two preceding domains synergistically mediate tethering to the NPC. We present the crystal structure of the seven-bladed β-propeller domain at 1.9 Å resolution. Analysis of the β-propeller surface reveals the regions that are required for NPC anchorage. We discuss the possible roles of ELYS in the context of the NPC scaffold architecture.

Indexed as

Models, MolecularProtein ConformationProtein Interaction Domains and MotifsCell LineChromatinCrystallizationDNA-Binding ProteinsHumansNuclear PoreNuclear Pore Complex ProteinsTranscription FactorsX-Ray DiffractionAHCTF1 protein, humanChromatinDNA-Binding ProteinsNuclear Pore Complex ProteinsTranscription Factors

Identifiers

PMID23499022
PMCPMC4077343
OpenAlexW2138786561

What OpenQuestion holds

Textmetadata
LicenceTDM
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.