Evidence map›Paper›PMID 41016879›Full record

ReviewTrends in biochemical sciences2025

The nuclear export receptor CRM1/XPO1 and its diverse cargoes.

Ralph H Kehlenbach, Yuh Min Chook

Abstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. 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

2 authors.

Ralph H KehlenbachDepartment of Molecular Biology, Faculty of Medicine, GZMB, Georg-August-University Göttingen, Humboldtallee 23, 37073 Göttingen, Germany. Electronic address: rkehlen@gwdg.de.
Yuh Min ChookDepartment of Pharmacology, University of Texas Southwestern Medical Center, 6001 Forest Park Road, Dallas, TX 75390-9041, USA. Electronic address: yuhmin.chook@utsouthwestern.edu.

Funding

Biochemical and cellular functions of Karyopherins - Revision - 2R35GM141461 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI Yuh Min Chook · 2021 to 2026
$2.8M
NIGMS NIH HHS R35 GM141461NIGMS NIH HHS R35GM144137
6 · The paper itself

Abstract

CRM1 (Exportin 1, XPO1), the best-characterized nuclear export receptor, exports hundreds of proteins and various RNA species. Its broad cargo repertoire necessitates versatile binding modes for diverse interaction partners, including nuclear export signal/sequence (NES)-containing cargoes, the GTPase Ran, nucleoporins that line nuclear pore complexes, and accessory proteins that facilitate export complex assembly or disassembly. We review the current knowledge of CRM1's protein and RNA cargoes and examine its modes of interactions in the context of the basic mechanism of nuclear export - NES recognition, recent structural studies that reveal how CRM1 engages cargoes beyond NESs, and allosteric regulation. Finally, we touch on the state of NES/cargo prediction, CRM1's interactions with nucleoporins, and its emerging roles beyond nuclear export.

Indexed as

KaryopherinsReceptors, Cytoplasmic and NuclearActive Transport, Cell NucleusAnimalsCell NucleusExportin 1 ProteinHumansNuclear Export SignalsNuclear Pore Complex ProteinsProtein Bindingran GTP-Binding ProteinExportin 1 ProteinKaryopherinsNuclear Export SignalsNuclear Pore Complex Proteinsran GTP-Binding ProteinReceptors, Cytoplasmic and NuclearallosteryCRM1exportin 1 (XPO1)nuclear pore complex (NPC)nuclear transportRNA export

Identifiers

PMID41016879
PMCPMC13532322

What OpenQuestion holds

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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.