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Assembly of Nsp1 Nucleoporins Provides Insight into Nuclear Pore Complex Gating

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  • Ramya Gamini
  • Wei Han
  • John E Stone
  • Klaus Schulten

Abstract

Nuclear pore complexes (NPCs) form gateways for material transfer across the nuclear envelope of eukaryotic cells. Disordered proteins, rich in phenylalanine-glycine repeat motifs (FG-nups), form the central transport channel. Understanding how nups are arranged in the interior of the NPC may explain how NPC functions as a selectivity filter for transport of large molecules and a sieve-like filter for diffusion of small molecules (

Suggested Citation

  • Ramya Gamini & Wei Han & John E Stone & Klaus Schulten, 2014. "Assembly of Nsp1 Nucleoporins Provides Insight into Nuclear Pore Complex Gating," PLOS Computational Biology, Public Library of Science, vol. 10(3), pages 1-14, March.
    • Handle: RePEc:plo:pcbi00:1003488
    DOI: 10.1371/journal.pcbi.1003488
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    1. Frank Alber & Svetlana Dokudovskaya & Liesbeth M. Veenhoff & Wenzhu Zhang & Julia Kipper & Damien Devos & Adisetyantari Suprapto & Orit Karni-Schmidt & Rosemary Williams & Brian T. Chait & Andrej Sali, 2007. "The molecular architecture of the nuclear pore complex," Nature, Nature, vol. 450(7170), pages 695-701, November.
    2. Ruhollah Moussavi-Baygi & Yousef Jamali & Reza Karimi & Mohammad R K Mofrad, 2011. "Brownian Dynamics Simulation of Nucleocytoplasmic Transport: A Coarse-Grained Model for the Functional State of the Nuclear Pore Complex," PLOS Computational Biology, Public Library of Science, vol. 7(6), pages 1-16, June.
    3. Frank Alber & Svetlana Dokudovskaya & Liesbeth M. Veenhoff & Wenzhu Zhang & Julia Kipper & Damien Devos & Adisetyantari Suprapto & Orit Karni-Schmidt & Rosemary Williams & Brian T. Chait & Michael P. , 2007. "Determining the architectures of macromolecular assemblies," Nature, Nature, vol. 450(7170), pages 683-694, November.
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