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8 Å structure of the outer rings of the Xenopus laevis nuclear pore complex obtained by cryo-EM and AI. , Tai L., Protein Cell. October 1, 2022; 13 (10): 760-777.
ZC3HC1 Is a Novel Inherent Component of the Nuclear Basket, Resident in a State of Reciprocal Dependence with TPR. , Gunkel P., Cells. July 30, 2021; 10 (8):
Structure of the cytoplasmic ring of the Xenopus laevis nuclear pore complex by cryo-electron microscopy single particle analysis. , Huang G., Cell Res. June 1, 2020; 30 (6): 520-531.
Nup98 FG domains from diverse species spontaneously phase-separate into particles with nuclear pore-like permselectivity. , Schmidt HB., Elife. January 6, 2015; 4
Nanobodies: site-specific labeling for super-resolution imaging, rapid epitope-mapping and native protein complex isolation. , Pleiner T., Elife. January 6, 2015; 4 e11349.
Systematic analysis of barrier-forming FG hydrogels from Xenopus nuclear pore complexes. , Labokha AA., EMBO J. January 23, 2013; 32 (2): 204-18.
Dimerization and direct membrane interaction of Nup53 contribute to nuclear pore complex assembly. , Vollmer B., EMBO J. October 17, 2012; 31 (20): 4072-84.
The permeability of reconstituted nuclear pores provides direct evidence for the selective phase model. , Hülsmann BB., Cell. August 17, 2012; 150 (4): 738-51.
Structural organization of the nuclear pore permeability barrier. , Liashkovich I., J Control Release. June 28, 2012; 160 (3): 601-8.
The C-terminal domain of Nup93 is essential for assembly of the structural backbone of nuclear pore complexes. , Sachdev R., Mol Biol Cell. February 1, 2012; 23 (4): 740-9.
Domain topology of nucleoporin Nup98 within the nuclear pore complex. , Chatel G., J Struct Biol. January 1, 2012; 177 (1): 81-9.
POM121 and Sun1 play a role in early steps of interphase NPC assembly. , Talamas JA., J Cell Biol. July 11, 2011; 194 (1): 27-37.
Nup98 regulates bipolar spindle assembly through association with microtubules and opposition of MCAK. , Cross MK., Mol Biol Cell. March 1, 2011; 22 (5): 661-72.
The nucleoporin Nup188 controls passage of membrane proteins across the nuclear pore complex. , Theerthagiri G., J Cell Biol. June 28, 2010; 189 (7): 1129-42.
The cytoplasmic filaments of the nuclear pore complex are dispensable for selective nuclear protein import. , Walther TC., J Cell Biol. July 8, 2002; 158 (1): 63-77.
Interference with the cytoplasmic tail of gp210 disrupts "close apposition" of nuclear membranes and blocks nuclear pore dilation. , Drummond SP., J Cell Biol. July 8, 2002; 158 (1): 53-62.
Cofactor requirements for nuclear export of Rev response element (RRE)- and constitutive transport element (CTE)-containing retroviral RNAs. An unexpected role for actin. , Hofmann W., J Cell Biol. March 5, 2001; 152 (5): 895-910.
The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates. , Bachi A., RNA. January 1, 2000; 6 (1): 136-58.
RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98 motif at the nuclear pore complex through multiple domains. , Pritchard CE., J Cell Biol. April 19, 1999; 145 (2): 237-54.
Nup116p and nup100p are interchangeable through a conserved motif which constitutes a docking site for the mRNA transport factor gle2p. , Bailer SM., EMBO J. February 16, 1998; 17 (4): 1107-19.