scholarly journals Correlative super-resolution fluorescence and electron microscopy of the nuclear pore complex with molecular resolution

2014 ◽  
Vol 127 (20) ◽  
pp. 4351-4355 ◽  
Author(s):  
Anna Löschberger ◽  
Christian Franke ◽  
Georg Krohne ◽  
Sebastian van de Linde ◽  
Markus Sauer
Keyword(s):  
Electron Microscopy ◽  
Nuclear Pore Complex ◽  
Super Resolution ◽  
Nuclear Pore ◽  
Fluorescence And Electron Microscopy

scholarly journals Comparative Spatial Localization of Protein-A-Tagged and Authentic Yeast Nuclear Pore Complex Proteins by Immunogold Electron Microscopy

2000 ◽  
Vol 129 (2-3) ◽  
pp. 295-305 ◽  
Author(s):  
Birthe Fahrenkrog ◽  
John P. Aris ◽  
Eduard C. Hurt ◽  
Nelly Panté ◽  
Ueli Aebi
Keyword(s):  
Electron Microscopy ◽  
Nuclear Pore Complex ◽  
Protein A ◽  
Spatial Localization ◽  
Immunogold Electron Microscopy ◽  
Nuclear Pore

scholarly journals Super-resolution mapping of scaffold nucleoporins in the nuclear pore complex

2017 ◽  
Vol 130 (7) ◽  
pp. 1299-1306 ◽  
Author(s):  
Jiong Ma ◽  
Joseph M. Kelich ◽  
Samuel L. Junod ◽  
Weidong Yang
Keyword(s):  
Nuclear Pore Complex ◽  
Super Resolution ◽  
Nuclear Pore ◽  
Resolution Mapping ◽  
Super Resolution Mapping

scholarly journals Super-resolution 3D tomography of interactions and competition in the nuclear pore complex

2016 ◽  
Vol 23 (3) ◽  
pp. 239-247 ◽  
Author(s):  
Jiong Ma ◽  
Alexander Goryaynov ◽  
Weidong Yang
Keyword(s):  
Nuclear Pore Complex ◽  
Super Resolution ◽  
Nuclear Pore ◽  
3D Tomography

scholarly journals Isolation of the yeast nuclear pore complex.

1993 ◽  
Vol 123 (4) ◽  
pp. 771-783 ◽  
Author(s):  
M P Rout ◽  
G Blobel
Keyword(s):  
Electron Microscopy ◽  
Image Reconstruction ◽  
Nuclear Pore Complex ◽  
Sedimentation Coefficient ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Negative Stain ◽  
Negative Stain Electron Microscopy ◽  
Pore Complexes

Nuclear pore complexes (NPCs) have been isolated from the yeast Saccharomyces. Negative stain electron microscopy of the isolated NPCs and subsequent image reconstruction revealed the octagonal symmetry and many of the ultrastructural features characteristic of vertebrate NPCs. The overall dimensions of the yeast NPC, both in its isolated form as well as in situ, are smaller than its vertebrate counterpart. However, the diameter of the central structures are similar. The isolated yeast NPC has a sedimentation coefficient of approximately 310 S and an M(r) of approximately 66 MD. It retains all but one of the eight known NPC proteins. In addition it contains as many as 80 uncharacterized proteins that are candidate NPC proteins.

scholarly journals Super-Resolution by Feedback Imaging: Mechanisms of Translocation through the Nuclear Pore Complex

2013 ◽  
Vol 104 (2) ◽  
pp. 120a
Author(s):  
Francesco Cardarelli ◽  
Luca Lanzano ◽  
Enrico Gratton
Keyword(s):  
Nuclear Pore Complex ◽  
Super Resolution ◽  
Nuclear Pore ◽  
Imaging Mechanisms

scholarly journals A Cyclometalated Iridium (III) Complex as a Microtubule Probe for Correlative Super‐Resolution Fluorescence and Electron Microscopy

2020 ◽  
Vol 32 (39) ◽  
pp. 2003901
Author(s):  
Xiaohe Tian ◽  
Cesare De Pace ◽  
Lorena Ruiz‐Perez ◽  
Bo Chen ◽  
Rina Su ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Super Resolution ◽  
Fluorescence And Electron Microscopy

scholarly journals The role of the integral membrane nucleoporins Ndc1p and Pom152p in nuclear pore complex assembly and function

2006 ◽  
Vol 173 (3) ◽  
pp. 361-371 ◽  
Author(s):  
Alexis S. Madrid ◽  
Joel Mancuso ◽  
W. Zacheus Cande ◽  
Karsten Weis
Keyword(s):  
Electron Microscopy ◽  
Saccharomyces Cerevisiae ◽  
Nuclear Envelope ◽  
Lipid Bilayers ◽  
Nuclear Pore Complex ◽  
Transmembrane Proteins ◽  
Nuclear Pore ◽  
Large Channel ◽  
And Function

The nuclear pore complex (NPC) is a large channel that spans the two lipid bilayers of the nuclear envelope and mediates transport events between the cytoplasm and the nucleus. Only a few NPC components are transmembrane proteins, and the role of these proteins in NPC function and assembly remains poorly understood. We investigate the function of the three integral membrane nucleoporins, which are Ndc1p, Pom152p, and Pom34p, in NPC assembly and transport in Saccharomyces cerevisiae. We find that Ndc1p is important for the correct localization of nuclear transport cargoes and of components of the NPC. However, the role of Ndc1p in NPC assembly is partially redundant with Pom152p, as cells lacking both of these proteins show enhanced NPC disruption. Electron microscopy studies reveal that the absence of Ndc1p and Pom152p results in aberrant pores that have enlarged diameters and lack proteinaceous material, leading to an increased diffusion between the cytoplasm and the nucleus.

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