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Slx9 is a newly discovered type of RanGTP-binding protein required for Crm1-mediated nuclear export.

Length-dependent interference of arginine-containing dipeptide repeat proteins with multiple components of the nucleocytoplasmic transport machinery is a potential mechanistic pathway of C9orf72 amyotrophic lateral sclerosis or frontotemporal dementia toxicity.

Biomimetic nanopores reveal that the sequence-dependent spatial distribution of intrinsically disordered proteins plays a crucial role in establishing the selective permeability barrier of the nuclear pore complex.

Advanced microscopy techniques reveal unique biological features that distinguish androgen receptor variant 7 (AR-V7) from the canonical AR, including high intranuclear mobility and rapid nuclear import that occurs independently of importin-α/β.

Nuclear pore complex mimics based on solid-state nanopores show significant selectivity below a diameter of 55 nm, which decreases gradually for larger pore diameters.

NMR spectroscopy has been used to explain a central unresolved issue of nuclear transport, namely how it can be both fast and specific.

Animal RanBP1 nuclear export and cargo dissociation mechanisms are surprisingly different from yeast, due to mutations of critical residues, leading to greater nuclear transport efficiency and higher energy cost.

β-adrenergic receptors at the Golgi apparatus activate a local signaling pathway, not accessed by cell surface receptors, to drive cardiac hypertrophy and could represent a target for heart failure therapy.

Ligand capture by cell surface receptor complexes sets the shape of the Nodal signaling pattern in zebrafish.

Dopamine D1 receptor signaling from the Golgi apparatus in murine striatal medium spiny neurons is regulated by monoamine transporter OCT2.