ReviewBiochimica et biophysica acta2011
Nuclear import by karyopherin-βs: recognition and inhibition.
Review in Biochimica et biophysica acta, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 238 papers.
What it found
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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.
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.
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Who cites it
238 citing papers in PubMed, 377 citations in OpenAlex.
- Troponin: biology, molecular mechanisms, and multidimensional clinical applications.Molecular biomedicine · 2026Review
- Signal recognition particle 14 binds to importin α in Plasmodium falciparum.Molecular biology reports · 2026Article
- 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 · 2026Article
- Importin 7 mediates the nuclear import of HIV-1 integrase via a specific interacting interface.FEBS open bio · 2026Article
- Multiple roads between the nucleus and the cytoplasm: classes of linear NLSs and NESs and their receptors.Current opinion in structural biology · 2026Review
- Bound for the nucleus: defining the molecular principles of cargo selection by importin 9.bioRxiv : the preprint server for biology · 2026Article
- Nuclear translocation of mitochondrial ferredoxin reductase is regulated by AKT-mediated phosphorylation.The Biochemical journal · 2026Article
- Importin-9 recognizes the winged-helix fold of ETS transcription factors to mediate nuclear import.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Exploration of the proxiOME of large subunit ribosomal proteins reveals Acl1 and Bcl1 as cooperating dedicated chaperones of Rpl1.Nucleic acids research · 2026Article
- Hallmarks of nuclear metabolism: implications for genome integrity, nuclear signaling, and therapeutic targeting.npj metabolic health and disease · 2026Review
- Importins recognize the winged-helix fold of ETS transcription factors to mediate nuclear import.bioRxiv : the preprint server for biology · 2026Article
- Nanoscale biointerfaces in inter-organelle communication: membrane contact sites, organelle trafficking, and cell fate control.Frontiers in cell and developmental biology · 2026Review
- Translocation of HIV capsid core through the Nuclear Pore Complex by affinity gradient.bioRxiv : the preprint server for biology · 2025Article
- Visualizing developmental dynamics of nuclear morphology and transport machinery in Drosophila.Developmental biology · 2025Article
- High-throughput behavioural phenotyping of 25 C. elegans disease models including patient-specific mutations.BMC biology · 2025Article
- A revised model of nuclear actin import: Importin 9 competes with cofilin, profilin, and RanGTP for actin binding.bioRxiv : the preprint server for biology · 2025Article
- Article
- Structural basis of phosphorylation-independent nuclear import of CIRBP by TNPO3.Nature communications · 2025Article
- The Sequence [RRKLPVGRS] Is a Nuclear Localization Signal for Importin 8 Binding (NLS8): A Chemical Biology and Bioinformatics Study.International journal of molecular sciences · 2025Article
- PCV2 Cap protein nuclear import via importin α/β receptor: molecular insights and antiviral potential.Frontiers in microbiology · 2025Article
178 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Proteins in the karyopherin-β family mediate the majority of macromolecular transport between the nucleus and the cytoplasm. Eleven of the 19 known human karyopherin-βs and 10 of the 14S. cerevisiae karyopherin-βs mediate nuclear import through recognition of nuclear localization signals or NLSs in their cargos. This receptor-mediated process is essential to cellular viability as proteins are translated in the cytoplasm but many have functional roles in the nucleus. Many known karyopherin-β-cargo interactions were discovered through studies of the individual cargos rather than the karyopherins, and this information is thus widely scattered in the literature. We consolidate information about cargos that are directly recognized by import-karyopherin-βs and review common characteristics or lack thereof among cargos of different import pathways. Knowledge of karyopherin-β-cargo interactions is also critical for the development of nuclear import inhibitors and the understanding of their mechanisms of inhibition. This article is part of a Special Issue entitled: Regulation of Signaling and Cellular Fate through Modulation of Nuclear Protein Import.
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Registered trials
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.