Papers associated with left (and nup214)

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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.
	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.
	Nucleoporin gene expression in Xenopus tropicalis embryonic development., Reza N., Int J Dev Biol. January 1, 2016; 60 (4-6): 181-8.
	Systematic analysis of barrier-forming FG hydrogels from Xenopus nuclear pore complexes., Labokha AA., EMBO J. January 23, 2013; 32 (2): 204-18.
	The permeability of reconstituted nuclear pores provides direct evidence for the selective phase model., Hülsmann BB., Cell. August 17, 2012; 150 (4): 738-51.
	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.
	Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export., Vasu S., J Cell Biol. October 29, 2001; 155 (3): 339-54.
	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.
	Major binding sites for the nuclear import receptor are the internal nucleoporin Nup153 and the adjacent nuclear filament protein Tpr., Shah S., J Cell Biol. April 6, 1998; 141 (1): 31-49.

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