Evidence map›Paper›PMID 29927350›Full record

ArticleMolecular biology of the cell2018

Correlation of CRM1-NES affinity with nuclear export activity.

Szu-Chin Fu, Ho Yee Joyce Fung, Tolga Cağatay, Jordan Baumhardt, Yuh Min Chook

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

35 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Characterizing Optogenetic Tools for Use in Synthetic Gene Circuits.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  6. Article
  7. Review
  8. Nanobodies targeting hnRNPA2/B1 and tau.bioRxiv : the preprint server for biology · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. The CRM1-dependent NESVeterinary research · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023
    Review
  19. Review
  20. Karyopherin-mediated nucleocytoplasmic transport.Nature reviews. Molecular cell biology · 2022
    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 at 1 institution in 1 country.

Szu-Chin FuDepartment of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390.
Ho Yee Joyce FungDepartment of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390.
Tolga CağatayDepartment of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390.
Jordan BaumhardtDepartment of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390.
Yuh Min ChookDepartment of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390.
The University of Texas Southwestern Medical Center · US

Funding

Structures and Mechanisms of Nuclear Import and ExportR01GM069909 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI CHOOK, YUH MIN · 2004 to 2020
$5.8M
NIGMS NIH HHS R01 GM069909
6 · The paper itself

Abstract

CRM1 (Exportin1/XPO1) exports hundreds of broadly functioning protein cargoes out of the cell nucleus by binding to their classical nuclear export signals (NESs). The 8- to 15-amino-acid-long NESs contain four to five hydrophobic residues and are highly diverse in both sequence and CRM1-bound structure. Here we examine the relationship between nuclear export activities of 24 different NES peptides in cells and their CRM1-NES affinities. We found that binding affinity and nuclear export activity are linearly correlated for NESs with dissociation constants ( K

Indexed as

Nuclear Export SignalsActive Transport, Cell NucleusAmino Acid SequenceCell NucleusCell SurvivalCrystallography, X-RayExportin 1 ProteinHeLa CellsHumansKaryopherinsPeptidesProtein BindingReceptors, Cytoplasmic and NuclearStructure-Activity RelationshipViral ProteinsExportin 1 ProteinKaryopherinsNuclear Export SignalsPeptidesReceptors, Cytoplasmic and NuclearViral Proteins

Identifiers

PMID29927350
PMCPMC6232958
OpenAlexW2809240511

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.