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UnknownCharge of karyopherins and nuclear FG-Nups are key ingredients of nucleocytoplasmic transport.
Not available
S-EPMC11788480 | biostudies-literature
UnknownDeciphering the intrinsically disordered characteristics of the FG-Nups through the lens of polymer physics.
Not available
S-EPMC11407397 | biostudies-literature
ProteomicsNucleoporin Nsp1 surveils the phase state of FG-Nups
Transport through the NPC relies on intrinsically disordered FG-Nups forming a selective barrier. Away from the NPC, FG-Nups readily form condensates and aggregates, and we address how this behavior is surveilled in cells. FG-Nups, including Nsp1, together with nuclear transport receptor Kap95, form...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2025-01-27 | PXD041710 | Pride
Liquid-liquid phase-separation Nuclear pore complex Chaperones Condensate Aging Protein homeostasis Intrinsically disordered protein Nsp1 Fg-nucleoporin Kap95 
GenomicsChEC-seq2 profiling of Crm1, Nucleoporins (nups), and RNA Pol II from budding yeast grown in SDC
Nuclear pore proteins (Nups) physically interact with hundreds of chromosomal sites, impacting transcription. In yeast, transcription factors mediate interactions between Nups and enhancers and promoters. To define the molecular basis of this mechanism, we exploited a separation-of-function mutation...
ORGANISM(S): Saccharomyces cerevisiae 
2025-03-24 | GSE288515 | GEO
GenomicsNucleoporin Nup153 Regulates Stem Cell Pluripotency through Gene Silencing
Nucleoporins (Nups) are a family of proteins best known as the constituent building blocks of nuclear pore complexes (NPCs), the transport channels that mediate nuclear transport. Recent evidence suggest that several Nups have additional roles in controlling the activation and silencing of developme...
ORGANISM(S): Mus musculus 
2015-06-19 | E-GEOD-64008 | biostudies-arrayexpress
GenomicsSaccharomyces cerevisiae
Crm1, Nucleoporins (nups), and RNA Pol II binding patterns from budding yeast grown in synthetic complete medium containing glucose (SDC)
PRJNA1109451 | ENA
ProteomicsTurboID identification of evolutionarily divergent components of the nuclear pore complex in the malaria model Plasmodium berghei
Twenty years since publication of the Plasmodium falciparum and P. berghei genomes one-third of their protein-coding genes lack functional annotation. In the absence of sequence and structural homology, protein-protein interactions can facilitate functional prediction of such orphan genes by mapping...
ORGANISM(S): Plasmodium 
2022-08-21 | PXD034491 | Pride
Plasmodium Malaria Turboid Nup Bioid Proximity-labeling Nucleoporins Nuclear pore complex 
ProteomicsAn Amphipathic Helix in Brl1 is Required for Nuclear Pore Complex Biogenesis in S. cerevisiae – targeted analysis of cell lysate (PRM)
The project was aimed at assessing the metabolic labeling of NUPs in the full lysate upon SILAC labeling of growing yeast cultures, 90 min post labeling. This experiment was performed to exclude that the systematic labeling differences that we observed in KARMA assays with Brl1 bait were present alr...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2022-08-17 | PXD032016 | Pride
Cell lysate Prm 
TranscriptomicsMis-regulation of Nucleoporins 98 and 96 leads to translational stress that promotes hallmarks of tumorigenesis.
Compromising Nups 98 and 96 triggers cell death and compensatory proliferation via JNK and TNF signaling that becomes tumorigenic when apoptosis is blocked.
ORGANISM(S): Drosophila melanogaster 
2020-09-01 | GSE152679 | GEO
GenomicsChEC-seq2 profiling of Crm1 and Nup2 during degradation of Nup2 or inhibition/degradation of Crm1, respectively
Nuclear pore proteins (Nups) physically interact with hundreds of chromosomal sites, impacting transcription. In yeast, transcription factors mediate interactions between Nups and enhancers and promoters. To define the molecular basis of this mechanism, we exploited a separation-of-function mutation...
ORGANISM(S): Saccharomyces cerevisiae 
2025-03-24 | GSE288549 | GEO
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