Related references
Note: Only part of the references are listed.The liquid state of FG-nucleoporins mimics permeability barrier properties of nuclear pore complexes
Giorgia Celetti et al.
JOURNAL OF CELL BIOLOGY (2020)
FUS pathology in ALS is linked to alterations in multiple ALS-associated proteins and rescued by drugs stimulating autophagy
Lara Marrone et al.
ACTA NEUROPATHOLOGICA (2019)
Friend or foePost-translational modifications as regulators of phase separation and RNP granule dynamics
Mario Hofweber et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2019)
Nuclear-Import Receptors Reverse Aberrant Phase Transitions of RNA-Binding Proteins with Prion-like Domains
Lin Guo et al.
CELL (2018)
Floppy but not sloppy: Interaction mechanism of FG-nucleoporins and nuclear transport receptors
Iker Valle Aramburu et al.
SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY (2017)
Plasticity of an Ultrafast Interaction between Nucleoporins and Nuclear Transport Receptors
Sigrid Milles et al.
CELL (2015)
A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation
Avinash Patel et al.
CELL (2015)
Inhibition of amyloid-β plaque formation by α-synuclein
Teresa Bachhuber et al.
NATURE MEDICINE (2015)
Amyloid-like interactions within nucleoporin FG hydrogels
Christian Ader et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2010)
A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes
Steffen Frey et al.
CELL (2007)
Kinetic analysis of translocation through nuclear pore complexes
K Ribbeck et al.
EMBO JOURNAL (2001)