ArticleCell reports2018
Two Differential Binding Mechanisms of FG-Nucleoporins and Nuclear Transport Receptors.
Article in Cell reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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.
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.
Who cites it
33 citing papers in PubMed, 50 citations in OpenAlex.
- Targeting Exportin-1 in Cancer: From Nuclear Export to Oncogenic Transcriptional Hubs.JMA journal · 2026Review
- Mechanoresponsive modulation of nuclear pore complex structure and function bybioRxiv : the preprint server for biology · 2026Article
- An Nrf2-Nup214 positive feedback loop sustains the antioxidant response and promotes microbial infection in ticks.bioRxiv : the preprint server for biology · 2026Article
- Cooperative multivalency converts disorder into rods, resolving a paradox in cellular architecture.bioRxiv : the preprint server for biology · 2026Article
- The nuclear export receptor CRM1/XPO1 and its diverse cargoes.Trends in biochemical sciences · 2025Review
- O-GlcNAc modulation of nuclear pore complexes orchestrates mRNA export efficiency.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Therapeutic targeting of exportin-1 beyond nuclear export.Trends in pharmacological sciences · 2025Review
- Deciphering the intrinsically disordered characteristics of the FG-Nups through the lens of polymer physics.Nucleus (Austin, Tex.) · 2024Review
- Regulating transport efficiency through the nuclear pore complex: The role of binding affinity with FG-Nups.Molecular biology of the cell · 2024Article
- Nucleocytoplasmic transport rates are regulated by cellular processes that modulate GTP availability.The Journal of cell biology · 2024Article
- Nucleocytoplasmic transport rates are regulated by cellular processes that modulate GTP availability.bioRxiv : the preprint server for biology · 2023Article
- Recognition and coacervation of G-quadruplexes by a multifunctional disordered region in RECQ4 helicase.Nature communications · 2023Article
- Nucleoporin foci are stress-sensitive condensates dispensable for C. elegans nuclear pore assembly.The EMBO journal · 2023Article
- Article
- Protein Binding: A Fuzzy Concept.Life (Basel, Switzerland) · 2023Article
- Unveiling the complexity: assessing models describing the structure and function of the nuclear pore complex.Frontiers in cell and developmental biology · 2023Review
- Sequence-based Prediction of the Cellular Toxicity Associated with Amyloid Aggregation within Protein Condensates.Biochemistry · 2022Article
- Structure, Maintenance, and Regulation of Nuclear Pore Complexes: The Gatekeepers of the Eukaryotic Genome.Cold Spring Harbor perspectives in biology · 2022Review
- Synergies of Single Molecule Fluorescence and NMR for the Study of Intrinsically Disordered Proteins.Biomolecules · 2021Review
- Non-genetic and genetic rewiring underlie adaptation to hypomorphic alleles of an essential gene.The EMBO journal · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Phenylalanine-glycine-rich nucleoporins (FG-Nups) are intrinsically disordered proteins, constituting the selective barrier of the nuclear pore complex (NPC). Previous studies showed that nuclear transport receptors (NTRs) were found to interact with FG-Nups by forming an "archetypal-fuzzy" complex through the rapid formation and breakage of interactions with many individual FG motifs. Here, we use single-molecule studies combined with atomistic simulations to show that, in sharp contrast, FG-Nup214 undergoes a coupled reconfiguration-binding mechanism when interacting with the export receptor CRM1. Association and dissociation rate constants are more than an order of magnitude lower than in the archetypal-fuzzy complex between FG-Nup153 and NTRs. Unexpectedly, this behavior appears not to be encoded selectively into CRM1 but rather into the FG-Nup214 sequence. The same distinct binding mechanisms are unperturbed in O-linked β-N-acetylglucosamine-modified FG-Nups. Our results have implications for differential roles of distinctly spatially distributed FG-Nup⋅NTR interactions in the cell.
Indexed as
Identifiers
What OpenQuestion holds
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.