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Summary Anatomy Item Literature (235) Expression Attributions Wiki
XB-ANAT-3742

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Pharmacological profile of NPC 12626, a novel, competitive N-methyl-D-aspartate receptor antagonist., Ferkany JW., J Pharmacol Exp Ther. July 1, 1989; 250 (1): 100-9.


Interactions and structure of the nuclear pore complex revealed by cryo-electron microscopy., Akey CW., J Cell Biol. September 1, 1989; 109 (3): 955-70.


Protein import through the nuclear pore complex is a multistep process., Akey CW., J Cell Biol. September 1, 1989; 109 (3): 971-82.


Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components., Reichelt R., J Cell Biol. April 1, 1990; 110 (4): 883-94.


Functional expression of B2 bradykinin receptors from Balb/c cell mRNA in Xenopus oocytes., Mahan LC., Mol Pharmacol. June 1, 1990; 37 (6): 785-9.


Cytoplasmic transport of ribosomal subunits microinjected into the Xenopus laevis oocyte nucleus: a generalized, facilitated process., Bataillé N., J Cell Biol. October 1, 1990; 111 (4): 1571-82.


Probing the structure and function of the nuclear pore complex., Akey CW., Semin Cell Biol. June 1, 1991; 2 (3): 167-77.


Toward a more complete 3-D structure of the nuclear pore complex., Jarnik M., J Struct Biol. December 1, 1991; 107 (3): 291-308.


The use of field emission in-lens scanning electron microscopy to study the steps of assembly of the nuclear envelope in vitro., Goldberg MW., J Struct Biol. January 1, 1992; 108 (3): 257-68.


High resolution scanning electron microscopy of the nuclear envelope: demonstration of a new, regular, fibrous lattice attached to the baskets of the nucleoplasmic face of the nuclear pores., Goldberg MW, Goldberg MW., J Cell Biol. December 1, 1992; 119 (6): 1429-40.


High-resolution field emission scanning electron microscope imaging of internal cell structures after Epon extraction from sections: a new approach to correlative ultrastructural and immunocytochemical studies., Ris H., J Struct Biol. January 1, 1993; 111 (2): 148-57.


Pharmacological profile of NPC 17742 [2R,4R,5S-(2-amino-4,5-(1, 2-cyclohexyl)-7-phosphonoheptanoic acid)], a potent, selective and competitive N-methyl-D-aspartate receptor antagonist., Ferkany JW., J Pharmacol Exp Ther. January 1, 1993; 264 (1): 256-64.


Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy., Akey CW., J Cell Biol. July 1, 1993; 122 (1): 1-19.


The nuclear pore complex: three-dimensional surface structure revealed by field emission, in-lens scanning electron microscopy, with underlying structure uncovered by proteolysis., Goldberg MW., J Cell Sci. September 1, 1993; 106 ( Pt 1) 261-74.


Nup180, a novel nuclear pore complex protein localizing to the cytoplasmic ring and associated fibrils., Wilken N., J Cell Biol. December 1, 1993; 123 (6 Pt 1): 1345-54.


Intranuclear filaments containing a nuclear pore complex protein., Cordes VC., J Cell Biol. December 1, 1993; 123 (6 Pt 1): 1333-44.


Mutation of aspartate residues in the third extracellular loop of the rat B2 bradykinin receptor decreases affinity for bradykinin., Novotny EA., Biochem Biophys Res Commun. June 15, 1994; 201 (2): 523-30.


Interactions and three-dimensional localization of a group of nuclear pore complex proteins., Panté N., J Cell Biol. August 1, 1994; 126 (3): 603-17.


Exploring nuclear pore complex structure and function in molecular detail., Panté N., J Cell Sci Suppl. January 1, 1995; 19 1-11.


The nuclear pore complex., Davis LI., Annu Rev Biochem. January 1, 1995; 64 865-96.


Structural plasticity of the nuclear pore complex., Akey CW., J Mol Biol. April 28, 1995; 248 (2): 273-93.


Nucleocytoplasmic transport: factors and mechanisms., Simos G., FEBS Lett. August 1, 1995; 369 (1): 107-12.


High content of a nuclear pore complex protein in cytoplasmic annulate lamellae of Xenopus oocytes., Cordes VC., Eur J Cell Biol. November 1, 1995; 68 (3): 240-55.


Protein import into the nucleus., Schlenstedt G., FEBS Lett. June 24, 1996; 389 (1): 75-9.


Sequential binding of import ligands to distinct nucleopore regions during their nuclear import., Panté N., Science. September 20, 1996; 273 (5282): 1729-32.


Conformational states of the nuclear pore complex induced by depletion of nuclear Ca2+ stores., Perez-Terzic C., Science. September 27, 1996; 273 (5283): 1875-7.


Identification of different roles for RanGDP and RanGTP in nuclear protein import., Görlich D., EMBO J. October 15, 1996; 15 (20): 5584-94.


A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex., Matunis MJ., J Cell Biol. December 1, 1996; 135 (6 Pt 1): 1457-70.


Molecular mechanisms of nuclear protein transport., Moroianu J., Crit Rev Eukaryot Gene Expr. January 1, 1997; 7 (1-2): 61-72.


Identification of protein p270/Tpr as a constitutive component of the nuclear pore complex-attached intranuclear filaments., Cordes VC., J Cell Biol. February 10, 1997; 136 (3): 515-29.                  


Dominant-negative mutants of importin-beta block multiple pathways of import and export through the nuclear pore complex., Kutay U., EMBO J. March 17, 1997; 16 (6): 1153-63.


Three-dimensional visualization of the route of protein import: the role of nuclear pore complex substructures., Rutherford SA., Exp Cell Res. April 10, 1997; 232 (1): 146-60.


Visualizing nuclear export of different classes of RNA by electron microscopy., Panté N., RNA. May 1, 1997; 3 (5): 498-513.


A novel class of RanGTP binding proteins., Görlich D., J Cell Biol. July 14, 1997; 138 (1): 65-80.                    


Mediators of nuclear protein import target karyophilic proteins to pore complexes of cytoplasmic annulate lamellae., Cordes VC., Exp Cell Res. December 15, 1997; 237 (2): 419-33.


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.


ATP-Induced shape change of nuclear pores visualized with the atomic force microscope., Rakowska A., J Membr Biol. May 15, 1998; 163 (2): 129-36.


Regulated expression of neurogenic basic helix-loop-helix transcription factors during differentiation of the immortalized neuronal progenitor cell line HC2S2 into neurons., Ohtsuka T., Cell Tissue Res. July 1, 1998; 293 (1): 23-9.


Interaction of the human immunodeficiency virus type 1 Vpr protein with the nuclear pore complex., Fouchier RA., J Virol. July 1, 1998; 72 (7): 6004-13.


The role of the ran GTPase in nuclear assembly and DNA replication: characterisation of the effects of Ran mutants., Hughes M., J Cell Sci. October 1, 1998; 111 ( Pt 20) 3017-26.


Molecular architecture of the yeast nuclear pore complex: localization of Nsp1p subcomplexes., Fahrenkrog B., J Cell Biol. November 2, 1998; 143 (3): 577-88.              


Molecular segments of protein Tpr that confer nuclear targeting and association with the nuclear pore complex., Cordes VC., Exp Cell Res. November 25, 1998; 245 (1): 43-56.


Calcium-mediated structural changes of native nuclear pore complexes monitored by time-lapse atomic force microscopy., Stoffler D., J Mol Biol. April 9, 1999; 287 (4): 741-52.


CRM1-mediated recycling of snurportin 1 to the cytoplasm., Paraskeva E., J Cell Biol. April 19, 1999; 145 (2): 255-64.              


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.                  


Conformational changes of the in situ nuclear pore complex., Wang H., Biophys J. July 1, 1999; 77 (1): 241-7.


Permeability of single nuclear pores., Keminer O., Biophys J. July 1, 1999; 77 (1): 217-28.


Dbp5, a DEAD-box protein required for mRNA export, is recruited to the cytoplasmic fibrils of nuclear pore complex via a conserved interaction with CAN/Nup159p., Schmitt C., EMBO J. August 2, 1999; 18 (15): 4332-47.


Optical recording of signal-mediated protein transport through single nuclear pore complexes., Keminer O., Proc Natl Acad Sci U S A. October 12, 1999; 96 (21): 11842-7.


Nuclear hourglass technique: an approach that detects electrically open nuclear pores in Xenopus laevis oocyte., Danker T., Proc Natl Acad Sci U S A. November 9, 1999; 96 (23): 13530-5.

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