Evidence map›Paper›PMID 22171326›Full record

ArticleMolecular biology of the cell2012

The C-terminal domain of Nup93 is essential for assembly of the structural backbone of nuclear pore complexes.

Ruchika Sachdev, Cornelia Sieverding, Matthias Flötenmeyer, Wolfram Antonin

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2012. 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
–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

40 citing papers in PubMed.

  1. Article
  2. NNature cell biology · 2026
    Article
  3. Inheriting chromosome conformation.Nature cell biology · 2026
    Article
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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.

Ruchika SachdevFriedrich Miescher Laboratory of the Max Planck Society, 72076 Tuebingen, Germany.
Cornelia Sieverding
Matthias Flötenmeyer
Wolfram Antonin

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nuclear pore complexes (NPCs) are large macromolecular assemblies that control all transport across the nuclear envelope. They are formed by about 30 nucleoporins (Nups), which can be roughly categorized into those forming the structural skeleton of the pore and those creating the central channel and thus providing the transport and gating properties of the NPC. Here we show that the conserved nucleoporin Nup93 is essential for NPC assembly and connects both portions of the NPC. Although the C-terminal domain of the protein is necessary and sufficient for the assembly of a minimal structural backbone, full-length Nup93 is required for the additional recruitment of the Nup62 complex and the establishment of transport-competent NPCs.

Indexed as

AnimalsCells, CulturedMembrane GlycoproteinsNuclear PoreNuclear Pore Complex ProteinsProtein Structure, TertiaryProtein TransportXenopusXenopus ProteinsMembrane GlycoproteinsNuclear Pore Complex Proteinsnuclear pore protein p62Nup93 protein, XenopusXenopus Proteins

Identifiers

PMID22171326
PMCPMC3279400

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.