???pagination.result.count???
???pagination.result.page???
1
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.
Cryo-EM structure of the inner ring from the Xenopus laevis nuclear pore complex. , Huang G., Cell Res. May 1, 2022; 32 (5): 451-460.
Nucleoporin NUP205 plays a critical role in cilia and congenital disease. , Marquez J ., Dev Biol. January 1, 2021; 469 46-53.
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.
A self-inhibitory interaction within Nup155 and membrane binding are required for nuclear pore complex formation. , De Magistris P., J Cell Sci. January 4, 2018; 131 (1):
Congenital Heart Disease Genetics Uncovers Context-Dependent Organization and Function of Nucleoporins at Cilia. , Del Viso F., Dev Cell. September 12, 2016; 38 (5): 478-92.
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.
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.