ArticlePLoS computational biology2008
Intramolecular cohesion of coils mediated by phenylalanine--glycine motifs in the natively unfolded domain of a nucleoporin.
Article in PLoS computational biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 53 citations in OpenAlex.
- Diversity of hydrodynamic radii of intrinsically disordered proteins.European biophysics journal : EBJ · 2023Article
- GermlineInternational journal of molecular sciences · 2023Article
- Atomic resolution dynamics of cohesive interactions in phase-separated Nup98 FG domains.Nature communications · 2022Article
- Investigating Intrinsically Disordered Proteins With Brownian Dynamics.Frontiers in molecular biosciences · 2022Article
- New Family Members of FG Repeat Proteins and Their Unexplored Roles During Phase Separation.Frontiers in cell and developmental biology · 2021Review
- Enhanced Nucleocytoplasmic Transport due to Competition for Elastic Binding Sites.Biophysical journal · 2018Article
- Article
- The Multiple Faces of Disordered Nucleoporins.Journal of molecular biology · 2016Review
- Energetics of Transport through the Nuclear Pore Complex.PloS one · 2016Article
- Evolutionarily Conserved Sequence Features Regulate the Formation of the FG Network at the Center of the Nuclear Pore Complex.Scientific reports · 2015Article
- Parametrization of Backbone Flexibility in a Coarse-Grained Force Field for Proteins (COFFDROP) Derived from All-Atom Explicit-Solvent Molecular Dynamics Simulations of All Possible Two-Residue Peptides.Journal of chemical theory and computation · 2015Article
- Probing the disordered domain of the nuclear pore complex through coarse-grained molecular dynamics simulations.Biophysical journal · 2014Article
- Classification of intrinsically disordered regions and proteins.Chemical reviews · 2014Review
- Nuclear pore complex protein sequences determine overall copolymer brush structure and function.Biophysical journal · 2014Article
- NMR based solvent exchange experiments to understand the conformational preference of intrinsically disordered proteins using FG-nucleoporin peptide as a model.Biopolymers · 2014Article
- Single-molecule analysis of the recognition forces underlying nucleo-cytoplasmic transport.Angewandte Chemie (International ed. in English) · 2013Article
- Identification of minimally interacting modules in an intrinsically disordered protein.Biophysical journal · 2012Article
- Nucleocytoplasmic transport: a role for nonspecific competition in karyopherin-nucleoporin interactions.Molecular & cellular proteomics : MCP · 2012Article
- The yeast nuclear pore complex and transport through it.Genetics · 2012Article
- Validating clustering of molecular dynamics simulations using polymer models.BMC bioinformatics · 2011Article
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Authors and funding
7 authors at 5 institutions in 1 country.
Funding
Abstract
The nuclear pore complex (NPC) provides the sole aqueous conduit for macromolecular exchange between the nucleus and the cytoplasm of cells. Its diffusion conduit contains a size-selective gate formed by a family of NPC proteins that feature large, natively unfolded domains with phenylalanine-glycine repeats (FG domains). These domains of nucleoporins play key roles in establishing the NPC permeability barrier, but little is known about their dynamic structure. Here we used molecular modeling and biophysical techniques to characterize the dynamic ensemble of structures of a representative FG domain from the yeast nucleoporin Nup116. The results showed that its FG motifs function as intramolecular cohesion elements that impart order to the FG domain and compact its ensemble of structures into native premolten globular configurations. At the NPC, the FG motifs of nucleoporins may exert this cohesive effect intermolecularly as well as intramolecularly to form a malleable yet cohesive quaternary structure composed of highly flexible polypeptide chains. Dynamic shifts in the equilibrium or competition between intra- and intermolecular FG motif interactions could facilitate the rapid and reversible structural transitions at the NPC conduit needed to accommodate passing karyopherin-cargo complexes of various shapes and sizes while simultaneously maintaining a size-selective gate against protein diffusion.
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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.