The Journal of Cell Biology · 2000 · 1.4K citations · 66 references
Yeast NpcBiochemistryProtein FoldingNatural SciencesMolecular BiologyNuclear Pore ComplexYeastNuclear OrganizationMembrane BiologyProtein TransportCellular StructureCellular BiochemistryMedicineSecretory PathwayStructural BiologyNpc Fraction
An understanding of how the nuclear pore complex (NPC) mediates nucleocytoplasmic exchange requires a comprehensive inventory of the molecular components of the NPC and a knowledge of how each component contributes to the overall structure of this large molecular translocation machine. Therefore, we have taken a comprehensive approach to classify all components of the yeast NPC (nucleoporins). This involved identifying all the proteins present in a highly enriched NPC fraction, determining which of these proteins were nucleoporins, and localizing each nucleoporin within the NPC. Using these data, we present a map of the molecular architecture of the yeast NPC and provide evidence for a Brownian affinity gating mechanism for nucleocytoplasmic transport.
66
CRM1 Is an Export Receptor for Leucine-Rich Nuclear Export Signals
Maarten Fornerod, Mutsuhito Ohno, Minoru Yoshida et al. · Cell · 1997 · 2.1K citations · Full text
Marcelo O. Magnasco · Physical Review Letters · 1993 · 1.2K citations
Philip L. Paine, Leonard C. Moore, Samuel B. Horowitz · Nature · 1975 · 819 citations