ArticleNature chemistry2022
Molecular interactions of FG nucleoporin repeats at high resolution.
Article in Nature chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 39 citations in OpenAlex.
- Accurate interdomain contacts in a mixed folded protein from NMR-guided coarse-grained simulations.Physical chemistry chemical physics : PCCP · 2026Article
- Exon junction complex and nuclear pore complex components preferentially govern the nuclear export of spliced lncRNAs.Cell death discovery · 2026Article
- NUP62 promotes breast cancer progression and inhibits ferroptosis by stabilizing NRF2 in a KEAP1-dependent way.iScience · 2026Article
- Chiral inversion mutagenesis identifies geometrically constrained residues within self-associating low-complexity domains.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Preferential formation of NUP98-KDM5A condensates at specific H3K4me3-rich loci drives leukemogenic gene expression.bioRxiv : the preprint server for biology · 2026Article
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- Chiral inversion mutagenesis identifies geometrically constrained residues within self-associating low-complexity domains.bioRxiv : the preprint server for biology · 2025Article
- Effects of Nanopore Confinement on the Conformational, Dynamical, and Self-Assembly Properties of an FG-Repeat Peptide.The journal of physical chemistry. B · 2025Article
- Effects of Nanopore Confinement on the Conformational, Dynamical, and Self-Assembly Properties of an FG-Repeat Peptide.bioRxiv : the preprint server for biology · 2025Article
- Leveraging structure-informed machine learning for fast steric zipper propensity prediction across whole proteomes.PLoS computational biology · 2025Article
- Off-pore Nup98 condensates mobilize heterochromatic breaks and exclude Rad51.Molecular cell · 2025Article
- The molecular mechanism of temperature-dependent phase separation of heat shock factor 1.Nature chemical biology · 2025Article
- A low-complexity linker as a driver of intra- and intermolecular interactions in DNAJB chaperones.Nature communications · 2025Article
- A simple method for mapping the location of cross-β-forming regions within protein domains of low sequence complexity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Transcription regulation by biomolecular condensates.Nature reviews. Molecular cell biology · 2025Review
- Molecular Crowing in Nuclear Pore.Sub-cellular biochemistry · 2025Review
- Regulating transport efficiency through the nuclear pore complex: The role of binding affinity with FG-Nups.Molecular biology of the cell · 2024Article
- Nuclear pore dysfunction and disease: a complex opportunity.Nucleus (Austin, Tex.) · 2024Review
- Protein folding and quality control during nuclear transport.Current opinion in cell biology · 2024Review
- Interdependence between Nuclear Pore Gatekeepers and Genome Caretakers: Cues from Genome Instability Syndromes.International journal of molecular sciences · 2024Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins that contain repeat phenylalanine-glycine (FG) residues phase separate into oncogenic transcription factor condensates in malignant leukaemias, form the permeability barrier of the nuclear pore complex and mislocalize in neurodegenerative diseases. Insights into the molecular interactions of FG-repeat nucleoporins have, however, remained largely elusive. Using a combination of NMR spectroscopy and cryoelectron microscopy, we have identified uniformly spaced segments of transient β-structure and a stable preformed α-helix recognized by messenger RNA export factors in the FG-repeat domain of human nucleoporin 98 (Nup98). In addition, we have determined at high resolution the molecular organization of reversible FG-FG interactions in amyloid fibrils formed by a highly aggregation-prone segment in Nup98. We have further demonstrated that amyloid-like aggregates of the FG-repeat domain of Nup98 have low stability and are reversible. Our results provide critical insights into the molecular interactions underlying the self-association and phase separation of FG-repeat nucleoporins in physiological and pathological cell activities.
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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.