Deconstructing transport-distribution reconstruction in the nuclear-pore complex
| dc.contributor.author | Tu, Li-Chun | |
| dc.contributor.author | Huisman, Maximiliaan | |
| dc.contributor.author | Chung, Yu-Chieh | |
| dc.contributor.author | Smith, Carlas | |
| dc.contributor.author | Grunwald, David | |
| dc.date | 2022-08-11T08:10:52.000 | |
| dc.date.accessioned | 2022-08-23T17:22:54Z | |
| dc.date.available | 2022-08-23T17:22:54Z | |
| dc.date.issued | 2018-12-05 | |
| dc.date.submitted | 2019-06-03 | |
| dc.identifier.citation | <p>Nat Struct Mol Biol. 2018 Dec;25(12):1061-1062. doi: 10.1038/s41594-018-0161-2. Epub 2018 Dec 5. <a href="https://doi.org/10.1038/s41594-018-0161-2">Link to article on publisher's site</a></p> | |
| dc.identifier.issn | 1545-9985 (Linking) | |
| dc.identifier.doi | 10.1038/s41594-018-0161-2 | |
| dc.identifier.pmid | 30518848 | |
| dc.identifier.uri | http://hdl.handle.net/20.500.14038/48845 | |
| dc.description.abstract | Nuclear-pore complexes (NPCs) span the nuclear envelope and mediate bidirectional transport between the nucleus and cytoplasm. Macromolecules (>40 kDa) require transport receptors to transit the NPC efficiently, whereas smaller molecules diffuse through the NPC passively. The mechanism through which the semipermeable barrier at the center of the NPC regulates selective transport is unknown. Aiming to elucidate this mechanism, Yang and colleagues have investigated spatial cargo distribution within the NPC2 by using single-point edge-excitation subdiffraction (SPEED) microscopy. | |
| dc.language.iso | en_US | |
| dc.relation | <p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=30518848&dopt=Abstract">Link to Article in PubMed</a></p> | |
| dc.relation.url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6481291/ | |
| dc.subject | Amino Acids, Peptides, and Proteins | |
| dc.subject | Biochemistry, Biophysics, and Structural Biology | |
| dc.title | Deconstructing transport-distribution reconstruction in the nuclear-pore complex | |
| dc.type | Letter to the Editor | |
| dc.source.journaltitle | Nature structural and molecular biology | |
| dc.source.volume | 25 | |
| dc.source.issue | 12 | |
| dc.identifier.legacycoverpage | https://escholarship.umassmed.edu/rti_pubs/53 | |
| dc.identifier.contextkey | 14647625 | |
| html.description.abstract | <p>Nuclear-pore complexes (NPCs) span the nuclear envelope and mediate bidirectional transport between the nucleus and cytoplasm. Macromolecules (>40 kDa) require transport receptors to transit the NPC efficiently, whereas smaller molecules diffuse through the NPC passively. The mechanism through which the semipermeable barrier at the center of the NPC regulates selective transport is unknown. Aiming to elucidate this mechanism, Yang and colleagues have investigated spatial cargo distribution within the NPC<sup><a href="https://www.nature.com/articles/s41594-018-0161-2#ref-CR2" id="x-x-x-ref-link-section-d6026e455" title="Ma, J., Goryaynov, A. & Yang, W. Nat. Struct. Mol. Biol. 23, 239–247 (2016).">2</a></sup> by using single-point edge-excitation subdiffraction (SPEED) microscopy.</p> | |
| dc.identifier.submissionpath | rti_pubs/53 | |
| dc.contributor.department | Graduate School of Biomedical Sciences | |
| dc.contributor.department | RNA Therapeutics Institute | |
| dc.source.pages | 1061-1062 |