ReviewBiochemical Society transactions2020
Multifunctionality of F-rich nucleoporins.
Review in Biochemical Society transactions, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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
12 citing papers in PubMed.
- The role of phase separation for RNA and protein transport through the nuclear pore complex.Journal of experimental botany · 2026Review
- Cytoplasmic nucleoporin assemblage: the cellular artwork in physiology and disease.Nucleus (Austin, Tex.) · 2024Review
- Evolutionary trajectory for nuclear functions of ciliary transport complex proteins.Microbiology and molecular biology reviews : MMBR · 2024Review
- Impact of distinct FG nucleoporin repeats on Nup98 self-association.Nature communications · 2024Article
- Article
- Nuclear-import receptors as gatekeepers of pathological phase transitions in ALS/FTD.Molecular neurodegeneration · 2024Review
- Improving the hole picture: towards a consensus on the mechanism of nuclear transport.Biochemical Society transactions · 2023Article
- Article
- Spelling out the roles of individual nucleoporins in nuclear export of mRNA.Nucleus (Austin, Tex.) · 2022Review
- Molecular interactions of FG nucleoporin repeats at high resolution.Nature chemistry · 2022Article
- New Activities of the Nuclear Pore Complexes.Cells · 2021Article
- DNA-Origami NanoTrap for Studying the Selective Barriers Formed by Phenylalanine-Glycine-Rich Nucleoporins.Journal of the American Chemical Society · 2021Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Nucleoporins (Nups) represent a range of proteins most known for composing the macromolecular assembly of the nuclear pore complex (NPC). Among them, the family of intrinsically disordered proteins (IDPs) phenylalanine-glycine (FG) rich Nups, form the permeability barrier and coordinate the high-speed nucleocytoplasmic transport in a selective way. Those FG-Nups have been demonstrated to participate in various biological processes besides nucleocytoplasmic transport. The high number of accessible hydrophobic motifs of FG-Nups potentially gives rise to this multifunctionality, enabling them to form unique microenvironments. In this review, we discuss the multifunctionality of disordered and F-rich Nups and the diversity of their localizations, emphasizing the important roles of those Nups in various regulatory and metabolic processes.
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Registered trials
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