Proteins that contain repeat phenylalanine-glycine (FG) residues phase separate into oncogenic transcription factor condensates in malignant leukaemias, form the permeability barrier of the nuclear pore complex and mislocalize in neurodegenerative diseases. Insights into the molecular interactions of FG-repeat nucleoporins have, however, remained largely elusive. Using a combination of NMR spectroscopy and cryoelectron microscopy, we have identified uniformly spaced segments of transient β-structure and a stable preformed α-helix recognized by messenger RNA export factors in the FG-repeat domain of human nucleoporin 98 (Nup98). In addition, we have determined at high resolution the molecular organization of reversible FG–FG interactions in ...
Nuclear pore complexes (NPCs) are highly selective gates that mediate the exchange of all proteins a...
Nucleocytoplasmic transport is mediated by nuclear pore complexes (NPCs) embedded in the nuclear env...
Bioinformatics of disordered proteins is especially challenging given high mutation rates for homolo...
AbstractNucleoporins (Nups), which are intrinsically disordered, form a selectivity filter inside th...
The condensation and compartmentalization of biomacromolecules in the cell are driven by the process...
A eukaryotic cell\u27s genetic material is stored in the nucleus, surrounded and protected by the nu...
Nucleoporins (Nups) build highly organized nuclear pore complexes (NPCs) at the nuclear envelope (NE...
Nuclear pore complexes (NPCs) are ∼100 MDa transport channels assembled from multiple copies of ∼30 ...
The 62 kDa FG repeat domain of the nucleoporin Nsp1p forms a hydrogel-based, sieve-like permeability...
The nuclear pore complex (NPC) is an immense structure which functions as a primary gateway for tran...
The nuclear pore complex (NPC) provides the sole aqueous conduit for macromolecular exchange between...
The nuclear pore complex (NPC) is the portal for bidirectional transportation of cargos between the ...
AbstractSelective transport through the nuclear pore complex (NPC) requires nucleoporins containing ...
Nucleocytoplasmic traffic of nucleic acids and proteins across the nuclear envelop via the nuclear p...
Liquid–liquid phase separation (LLPS) of proteins enables the formation of non-membrane-bound organe...
Nuclear pore complexes (NPCs) are highly selective gates that mediate the exchange of all proteins a...
Nucleocytoplasmic transport is mediated by nuclear pore complexes (NPCs) embedded in the nuclear env...
Bioinformatics of disordered proteins is especially challenging given high mutation rates for homolo...
AbstractNucleoporins (Nups), which are intrinsically disordered, form a selectivity filter inside th...
The condensation and compartmentalization of biomacromolecules in the cell are driven by the process...
A eukaryotic cell\u27s genetic material is stored in the nucleus, surrounded and protected by the nu...
Nucleoporins (Nups) build highly organized nuclear pore complexes (NPCs) at the nuclear envelope (NE...
Nuclear pore complexes (NPCs) are ∼100 MDa transport channels assembled from multiple copies of ∼30 ...
The 62 kDa FG repeat domain of the nucleoporin Nsp1p forms a hydrogel-based, sieve-like permeability...
The nuclear pore complex (NPC) is an immense structure which functions as a primary gateway for tran...
The nuclear pore complex (NPC) provides the sole aqueous conduit for macromolecular exchange between...
The nuclear pore complex (NPC) is the portal for bidirectional transportation of cargos between the ...
AbstractSelective transport through the nuclear pore complex (NPC) requires nucleoporins containing ...
Nucleocytoplasmic traffic of nucleic acids and proteins across the nuclear envelop via the nuclear p...
Liquid–liquid phase separation (LLPS) of proteins enables the formation of non-membrane-bound organe...
Nuclear pore complexes (NPCs) are highly selective gates that mediate the exchange of all proteins a...
Nucleocytoplasmic transport is mediated by nuclear pore complexes (NPCs) embedded in the nuclear env...
Bioinformatics of disordered proteins is especially challenging given high mutation rates for homolo...