Intrinsically disordered nuclear pore proteins show ideal-polymer morphologies and dynamics
Author:
Funder
Engineering and Physical Sciences Research Council
Royal Society
Publisher
American Physical Society (APS)
Link
http://harvest.aps.org/v2/journals/articles/10.1103/PhysRevE.101.022420/fulltext
Reference54 articles.
1. Protein Transport by the Nuclear Pore Complex: Simple Biophysics of a Complex Biomachine
2. Floppy but not sloppy: Interaction mechanism of FG-nucleoporins and nuclear transport receptors
3. Biomechanics of the transport barrier in the nuclear pore complex
4. The Permeability of Reconstituted Nuclear Pores Provides Direct Evidence for the Selective Phase Model
5. A Bimodal Distribution of Two Distinct Categories of Intrinsically Disordered Structures with Separate Functions in FG Nucleoporins
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