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Research Article
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Atomic force microscopy reveals structural variability amongst nuclear pore complexes

George J Stanley, Ariberto Fassati, View ORCID ProfileBart W Hoogenboom  Correspondence email
George J Stanley
1London Centre for Nanotechnology, University College London, London, UK
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Ariberto Fassati
2Division of Infection and Immunity, University College London, London, UK
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Bart W Hoogenboom
1London Centre for Nanotechnology, University College London, London, UK
3Department of Physics and Astronomy, University College London, London, UK
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  • ORCID record for Bart W Hoogenboom
  • For correspondence: b.hoogenboom@ucl.ac.uk
Published 20 August 2018. DOI: 10.26508/lsa.201800142
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Structural variability of nuclear pore complexes
George J Stanley, Ariberto Fassati, Bart W Hoogenboom
Life Science Alliance Aug 2018, 1 (4) e201800142; DOI: 10.26508/lsa.201800142

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Structural variability of nuclear pore complexes
George J Stanley, Ariberto Fassati, Bart W Hoogenboom
Life Science Alliance Aug 2018, 1 (4) e201800142; DOI: 10.26508/lsa.201800142
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Volume 1, No. 4
August 2018
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Cited By...

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  • TopoStats - a program for automated tracing of biomolecules from AFM images
  • Nuclear pores constrict upon energy depletion
  • Structure of the yeast Nup84-Nup133 complex details flexibility and reveals universal conservation of the membrane anchoring ALPS motif
  • A nanobody suite for yeast scaffold nucleoporins provides details of the Nuclear Pore Complex structure
  • Quantification of biomolecular dynamics inside real and synthetic nuclear pore complexes using time-resolved atomic force microscopy
  • Molecular model of the nuclear pore complex reveals a thermoreversible FG-network with distinct territories occupied by different FG motifs
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