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.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
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.
|
| skos:exactMatch | |
| uniprot:name |
J. Cell Biol.
|
| uniprot:author |
Aitchison J.D.,
Chait B.T.,
Hjertaas K.,
Rout M.P.,
Suprapto A.,
Zhao Y.
|
| uniprot:date |
2000
|
| uniprot:pages |
635-651
|
| uniprot:title |
The yeast nuclear pore complex: composition, architecture, and transport mechanism.
|
| uniprot:volume |
148
|
| dc-term:identifier |
doi:10.1083/jcb.148.4.635
|