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Abstract The nuclear pore complex (NPC) regulates molecular traffic between nucleus and cytoplasm1,2. Its permeability barrier is formed by intrinsically disordered phenylalanine-glycine-rich nucleoporins (FG-NUPs), whose physical state has long been debated3,4,5,6,7,8,9,10,11,12,13. Deciphering how FG-NUPs behave inside living cells is crucial for understanding how NPCs achieve both selective and rapid transport.
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