ArticleeLife2016
Simple biophysics underpins collective conformations of the intrinsically disordered proteins of the Nuclear Pore Complex.
Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 78 citations in OpenAlex.
- Deciphering the intrinsically disordered characteristics of the FG-Nups through the lens of polymer physics.Nucleus (Austin, Tex.) · 2024Review
- Kinetic cooperativity resolves bidirectional clogging within the nuclear pore complex.Biophysical journal · 2024Article
- The Burgeoning Significance of Liquid-Liquid Phase Separation in the Pathogenesis and Therapeutics of Cancers.International journal of biological sciences · 2024Review
- Dynamic molecular mechanism of the nuclear pore complex permeability barrier.bioRxiv : the preprint server for biology · 2023Article
- Self-regulation of the nuclear pore complex enables clogging-free crowded transport.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Effects of Sequence Composition, Patterning and Hydrodynamics on the Conformation and Dynamics of Intrinsically Disordered Proteins.International journal of molecular sciences · 2023Article
- Morphology of Polymer Brushes in the Presence of Attractive Nanoparticles: Effects of Temperature.International journal of molecular sciences · 2023Article
- Organelle-targeted therapies: a comprehensive review on system design for enabling precision oncology.Signal transduction and targeted therapy · 2022Review
- A simple thermodynamic description of phase separation of Nup98 FG domains.Nature communications · 2022Article
- Percolation transition prescribes protein size-specific barrier to passive transport through the nuclear pore complex.Nature communications · 2022Article
- Karyopherin enrichment and compensation fortifies the nuclear pore complex against nucleocytoplasmic leakage.The Journal of cell biology · 2022Article
- Function of the Nuclear Transport Machinery in Maintaining the Distinctive Compositions of the Nucleus and Cytoplasm.International journal of molecular sciences · 2022Review
- Crowding-induced phase separation of nuclear transport receptors in FG nucleoporin assemblies.eLife · 2022Article
- Structure and dynamics of nanoconfined water and aqueous solutions.The European physical journal. E, Soft matter · 2021Review
- Characterizing Binding Interactions That Are Essential for Selective Transport through the Nuclear Pore Complex.International journal of molecular sciences · 2021Article
- Physics of the Nuclear Pore Complex: Theory, Modeling and Experiment.Physics reports · 2021Article
- Recapitulation of selective nuclear import and export with a perfectly repeated 12mer GLFG peptide.Nature communications · 2021Article
- Physical modeling of multivalent interactions in the nuclear pore complex.Biophysical journal · 2021Article
- Theoretical Modeling of Chemical Equilibrium in Weak Polyelectrolyte Layers on Curved Nanosystems.Polymers · 2020Review
- A Method to Quantify Molecular Diffusion within Thin Solvated Polymer Films: A Case Study on Films of Natively Unfolded Nucleoporins.ACS nano · 2020Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nuclear Pore Complexes (NPCs) are key cellular transporter that control nucleocytoplasmic transport in eukaryotic cells, but its transport mechanism is still not understood. The centerpiece of NPC transport is the assembly of intrinsically disordered polypeptides, known as FG nucleoporins, lining its passageway. Their conformations and collective dynamics during transport are difficult to assess in vivo. In vitro investigations provide partially conflicting results, lending support to different models of transport, which invoke various conformational transitions of the FG nucleoporins induced by the cargo-carrying transport proteins. We show that the spatial organization of FG nucleoporin assemblies with the transport proteins can be understood within a first principles biophysical model with a minimal number of key physical variables, such as the average protein interaction strengths and spatial densities. These results address some of the outstanding controversies and suggest how molecularly divergent NPCs in different species can perform essentially the same function.
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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.