Evidence map›Paper›PMID 31839259›Full record

ArticleBiophysical journal2020

Nanocompartmentalization of the Nuclear Pore Lumen.

Kai Huang, Mario Tagliazucchi, Sung Hyun Park, Yitzhak Rabin, Igal Szleifer

Abstract read
In one paragraph

Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  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. Integrative mapping reveals molecular features underlying the mechanism of nucleocytoplasmic transport.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Review
  6. Molecular Crowing in Nuclear Pore.Sub-cellular biochemistry · 2025
    Review
  7. Review
  8. Article
  9. Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Self-regulation of the nuclear pore complex enables clogging-free crowded transport.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Multi-scale dynamics of heterochromatin repair.Current opinion in genetics & development · 2021
    Review
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

5 authors.

Kai HuangDepartment of Biomedical Engineering, Northwestern University, Evanston, Illinois.
Mario TagliazucchiDQIAQF and INQUIMAE, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Pab. II, Ciudad Autónoma de Buenos Aires, Argentina.
Sung Hyun ParkDepartment of Biomedical Engineering, Northwestern University, Evanston, Illinois.
Yitzhak RabinDepartment of Physics and Institute for Nanotechnology and Advanced Materials, Bar-Ilan University, Ramat-Gan, Israel.
Igal SzleiferDepartment of Biomedical Engineering, Northwestern University, Evanston, Illinois; Department of Chemistry, and Chemistry of Life Processes Institute, Northwestern University, Evanston, Illinois. Electronic address: igalsz@northwestern.edu.

Funding

Reducing Cancer Transcriptional Heterogeneity through Regulation of Chromatin StructureR01CA228272 · NCI · NORTHWESTERN UNIVERSITY · PI BACKMAN, VADIM, ROY, HEMANT K. · 2018 to 2022
$3.2M
NCI NIH HHS R01 CA228272
6 · The paper itself

Abstract

The nuclear pore complex (NPC) employs the intrinsically disordered regions (IDRs) from a family of phenylalanine-glycine-rich nucleoporins (FG-Nups) to control nucleocytoplasmic transport. It has been a long-standing mystery how the IDR-mediated mass exchange can be rapid yet selective. Here, we use a computational microscope to show that nanocompartmentalization of IDR subdomains leads to a remarkably elaborate gating structure as programmed by the amino acid sequences. In particular, we reveal a heterogeneous permeability barrier that combines an inner ring barrier with two vestibular condensates. Throughout the NPC, we find a polarized electrostatic potential and a diffuse thermoreversible FG network featuring mosaic FG territories with low FG-FG pairing fraction. Our theoretical anatomy of the central transporter sheds light into the sequence-structure-function relationship of the FG-Nups and provides a picture of nucleocytoplasmic mass exchange that allows a reconciliation of transport efficiency and specificity.

Indexed as

Models, MolecularNanostructuresNuclear PoreStatic Electricity

Identifiers

PMID31839259
PMCPMC6952220

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.