Papers associated with left (and nup98)

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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.
	Conservation and divergence of protein pathways in the vertebrate heart., Federspiel JD., PLoS Biol. September 6, 2019; 17 (9): e3000437.
	Xenopus as a model organism for birth defects-Congenital heart disease and heterotaxy., Duncan AR., Semin Cell Dev Biol. March 1, 2016; 51 73-9.
	Nucleoporin gene expression in Xenopus tropicalis embryonic development., Reza N., Int J Dev Biol. January 1, 2016; 60 (4-6): 181-8.
	The NIMA-like kinase Nek2 is a key switch balancing cilia biogenesis and resorption in the development of left-right asymmetry., Endicott SJ., Development. December 1, 2015; 142 (23): 4068-79.
	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.
	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.
	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.
	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.
	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.
	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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