ArticlePloS one2013
Physical motif clustering within intrinsically disordered nucleoporin sequences reveals universal functional features.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Role of pore dilation in molecular transport through the nuclear pore complex: Insights from polymer scaling theory.PLoS computational biology · 2025Article
- Regulating transport efficiency through the nuclear pore complex: The role of binding affinity with FG-Nups.Molecular biology of the cell · 2024Article
- Deciphering the intrinsically disordered characteristics of the FG-Nups through the lens of polymer physics.Nucleus (Austin, Tex.) · 2024Review
- Function of the Nuclear Transport Machinery in Maintaining the Distinctive Compositions of the Nucleus and Cytoplasm.International journal of molecular sciences · 2022Review
- Nucleoporins' exclusive amino acid sequence features regulate their transient interaction with and selectivity of cargo complexes in the nuclear pore.Molecular biology of the cell · 2021Article
- Free energy calculations shed light on the nuclear pore complex's selective barrier nature.Biophysical journal · 2021Article
- FG nucleoporins feature unique patterns that distinguish them from other IDPs.Biophysical journal · 2021Article
- Physics of the Nuclear Pore Complex: Theory, Modeling and Experiment.Physics reports · 2021Article
- Extra-Low-Frequency Pulse Stimulated Conformational Change in Blood-Cell Proteins and Consequent Immune Activity Transformation.IEEE journal of translational engineering in health and medicine · 2020Article
- The Role of Cohesiveness in the Permeability of the Spatial Assemblies of FG Nucleoporins.Biophysical journal · 2019Article
- Two Differential Binding Mechanisms of FG-Nucleoporins and Nuclear Transport Receptors.Cell reports · 2018Article
- Charge Influences Substrate Recognition and Self-Assembly of Hydrophobic FG Sequences.Biophysical journal · 2017Article
- Article
- The selective permeability barrier in the nuclear pore complex.Nucleus (Austin, Tex.) · 2016Review
- Tau mediates microtubule bundle architectures mimicking fascicles of microtubules found in the axon initial segment.Nature communications · 2016Article
- Dynamic Protein Interaction Networks and New Structural Paradigms in Signaling.Chemical reviews · 2016Review
- The Multiple Faces of Disordered Nucleoporins.Journal of molecular biology · 2016Review
- Article
- Evolutionarily Conserved Sequence Features Regulate the Formation of the FG Network at the Center of the Nuclear Pore Complex.Scientific reports · 2015Article
- Nucleoporin's Like Charge Regions Are Major Regulators of FG Coverage and Dynamics Inside the Nuclear Pore Complex.PloS one · 2015Article
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Authors and funding
4 authors.
Funding
Abstract
Bioinformatics of disordered proteins is especially challenging given high mutation rates for homologous proteins and that functionality may not be strongly related to sequence. Here we have performed a novel bioinformatic analysis, based on the spatial clustering of physically relevant features such as binding motifs and charges within disordered proteins, on thousands of Nuclear Pore Complex (NPC) FG motif containing proteins (FG nups). The biophysical mechanism by which FG nups regulate nucleocytoplasmic transport has remained elusive. Our analysis revealed a set of highly conserved spatial features in the sequence structure of individual FG nups, such as the separation, localization, and ordering of FG motifs and charged residues along the protein chain. These functionally conserved features provide insight into the particular biophysical mechanisms responsible for regulation of nucleocytoplasmic traffic in the NPC, strongly constraining current models. Additionally this method allows us to identify potentially functionally analogous disordered proteins across distantly related species.
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