ArticleThe Journal of biological chemistry2018
Thermodynamic characterization of the multivalent interactions underlying rapid and selective translocation through the nuclear pore complex.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 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
37 citing papers in PubMed, 63 citations in OpenAlex.
- Topology-Encoded Charge Polarity Governs Multiphase Organization in Intrinsically Disordered Protein Polymer Condensates.Small (Weinheim an der Bergstrasse, Germany) · 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
- Affinity Enhancement in Discrete Multivalent MegaMolecules.Chembiochem : a European journal of chemical biology · 2026Article
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025Review
- Integrative mapping reveals molecular features underlying the mechanism of nucleocytoplasmic transport.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Translocation of HIV capsid core through the Nuclear Pore Complex by affinity gradient.bioRxiv : the preprint server for biology · 2025Article
- Role of charges in a dynamic disordered complex between an IDP and a folded domain.Nature communications · 2025Article
- Allovalent scavenging of activation domains in the transcription factor ANAC013 gears transcriptional regulation.Nucleic acids research · 2025Article
- The low complexity linker of DNAJB6b is key to its anti-amyloid function.QRB discovery · 2025Article
- Deciphering the intrinsically disordered characteristics of the FG-Nups through the lens of polymer physics.Nucleus (Austin, Tex.) · 2024Review
- From molecular descriptions to cellular functions of intrinsically disordered protein regions.Biophysics reviews · 2024Review
- Protein folding and quality control during nuclear transport.Current opinion in cell biology · 2024Review
- Role of charge in enhanced nuclear transport and retention of graphene quantum dots.Scientific reports · 2024Article
- A survey of the specificity and mechanism of 1,6 hexanediol-induced disruption of nuclear transport.Nucleus (Austin, Tex.) · 2023Article
- Improving the hole picture: towards a consensus on the mechanism of nuclear transport.Biochemical Society transactions · 2023Article
- Dynamic molecular mechanism of the nuclear pore complex permeability barrier.bioRxiv : the preprint server for biology · 2023Article
- Article
- The return of the rings: Evolutionary convergence of aromatic residues in the intrinsically disordered regions of RNA-binding proteins for liquid-liquid phase separation.Protein science : a publication of the Protein Society · 2022Article
- On the nuclear pore complex and its emerging role in cellular mechanotransduction.APL bioengineering · 2022Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Intrinsically disordered proteins (IDPs) play important roles in many biological systems. Given the vast conformational space that IDPs can explore, the thermodynamics of the interactions with their partners is closely linked to their biological functions. Intrinsically disordered regions of Phe-Gly nucleoporins (FG Nups) that contain multiple phenylalanine-glycine repeats are of particular interest, as their interactions with transport factors (TFs) underlie the paradoxically rapid yet also highly selective transport of macromolecules mediated by the nuclear pore complex. Here, we used NMR and isothermal titration calorimetry to thermodynamically characterize these multivalent interactions. These analyses revealed that a combination of low per-FG motif affinity and the enthalpy-entropy balance prevents high-avidity interaction between FG Nups and TFs, whereas the large number of FG motifs promotes frequent FG-TF contacts, resulting in enhanced selectivity. Our thermodynamic model underlines the importance of functional disorder of FG Nups. It helps explain the rapid and selective translocation of TFs through the nuclear pore complex and further expands our understanding of the mechanisms of "fuzzy" interactions involving IDPs.
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.