Evidence map›Paper›PMID 28202688›Full record

ArticleJournal of cell science2017

Super-resolution mapping of scaffold nucleoporins in the nuclear pore complex.

Jiong Ma, Joseph M Kelich, Samuel L Junod, Weidong Yang

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

15 citing papers in PubMed, 22 citations in OpenAlex.

  1. HIV-1 capsid interactions with Nuclear Pore Complex components support nuclear entry via affinity gradient.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. O-GlcNAc modulation of nuclear pore complexes orchestrates mRNA export efficiency.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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 at 2 institutions in 2 countries.

Jiong MaDepartment of Biology, Temple University, 1900 N. 12th Street, Philadelphia, PA, 19122, USA.
Joseph M KelichDepartment of Biology, Temple University, 1900 N. 12th Street, Philadelphia, PA, 19122, USA.
Samuel L JunodDepartment of Biology, Temple University, 1900 N. 12th Street, Philadelphia, PA, 19122, USA.
Weidong YangDepartment of Biology, Temple University, 1900 N. 12th Street, Philadelphia, PA, 19122, USA weidong.yang@temple.edu.ORCID 0000-0002-3554-3035
Temple University · USFudan University · CN

Funding

Super-resolution Microscopy Study of Molecular Transport MechanismsR35GM122552 · NIGMS · TEMPLE UNIV OF THE COMMONWEALTH · PI Weidong Yang · 2017 to 2026
$4.5M
Structure and Function of the Ciliary Pore ComplexR01GM116204 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI VERHEY, KRISTEN J., YANG, WEIDONG · 2015 to 2018
$2.1M
Three-Dimensional Super-Resolution Microscopy Study of Nuclear TransportR01GM097037 · NIGMS · TEMPLE UNIV OF THE COMMONWEALTH · PI YANG, WEIDONG · 2011 to 2015
$1.3M
Single-Molecule Three-Dimensional Snapshots of Nuclear TransportR15GM094041 · NIGMS · BOWLING GREEN STATE UNIVERSITY · PI YANG, WEIDONG · 2010 to 2010
$348k
NIGMS NIH HHS R01 GM097037NIGMS NIH HHS R01 GM116204NIGMS NIH HHS R15 GM094041NIGMS NIH HHS R35 GM122552
6 · The paper itself

Abstract

The nuclear pore complex (NPC), composed of ∼30 different nucleoporins (Nups), is one of the largest supramolecular structures in eukaryotic cells. Its octagonal ring scaffold perforates the nuclear envelope and features a unique molecular machinery that regulates nucleocytoplasmic transport. However, the precise copy number and the spatial location of each Nup in the native NPC remain obscure due to the inherent difficulty of counting and localizing proteins inside of the sub-micrometer supramolecular complex. Here, we combined super-resolution single-point edge-excitation subdiffraction (SPEED) microscopy and nanobody-specific labeling to reveal the spatial distribution of scaffold Nups within three separate layers in the native NPC with a precision of ∼3 nm. Our data reveal both the radial and axial spatial distributions for Pom121, Nup37 and Nup35 and provide evidence for their copy numbers of 8, 32 and 16, respectively, per NPC. This approach can help pave the path for mapping the entirety of Nups in native NPCs and also other structural components of macromolecular complexes.

Indexed as

Gene DosageHeLa CellsHumansMicroscopyNuclear PoreNuclear Pore Complex ProteinsNuclear Pore Complex ProteinsNanobodyNuclear pore complexSuper resolution

Identifiers

PMID28202688
PMCPMC5399779
OpenAlexW2589016295

What OpenQuestion holds

Textmetadata
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.