Nuclear export signals: small domains with large impact
Engelsma, D.H.
Citation
Engelsma, D. H. (2008, October 16). Nuclear export signals: small domains with large impact. Retrieved from https://hdl.handle.net/1887/13258
Version: Corrected Publisher’s Version
License: Licence agreement concerning inclusion of doctoral thesis in the Institutional Repository of the University of Leiden
Downloaded from: https://hdl.handle.net/1887/13258
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Stellingen
1. Nup358 is a disassembly site of CRM1‐cargo‐RanGTP complexes (this thesis)
2. Nuclear export signals evolve away from biochemically optimal binding to CRM1 to assure biologically optimal export (this thesis)
3. Ribosomal and MVM viral capsid export from the nucleus are mechanistically similar (this thesis)
4. Supraphysiological NESs are important for viral pathogenicity and identify possible modes of intervention (this thesis).
5. Large particles use multiple transport receptors and benefit from
supraphysiological NESs to pass the NPC (this thesis and Bradatsch et al.
2007)
6. The binding of CRM1 to Survivin is not required for proper mitotic function.
(Knauer 2006, Stauber 2007, Knauer and Colnaghi 2006)
7. The center of the NPC is not filled by repulsive bristles but is formed by a gelatinous meshwork.
8 The most noticable sub‐cellular localizations of proteins are often the least interesting.
9 The scientist’s brain is the most overrated organ (adapted from Woody Allen).
10 De overstap van virologie naar vinologie is ogenschijnlijk klein.
11 Het valt te onderzoeken of wijn tijdens vatrijping azijnsteek kan krijgen, immers ‘wat in het vat zit verzuurt niet’.
