Literature DB >> 9262022

High-resolution field-emission scanning electron microscopy of nuclear pore complex.

H Ris1.   

Abstract

The nuclear pore complex (NPC) is a large macromolecular assembly inserted into the nuclear envelope (NE). It controls the traffic of proteins, RNA, and RNA proteins between nucleus and cytoplasm. It chemical composition and function are now intensively investigated in many organisms. To understand this unique membrane transport system, we must know the supramolecular organization of the NPC. In recent years, high-resolution field-emission scanning electron microscopy has made important contributions to our knowledge of NPC structure. It provided the first images of the complex and beautiful fish trap-like structure of its intranuclear surface, documented in this review. It also has provided the first images of a new intranuclear structure, a system of branching hollow cables connecting the nuclear interior with the NPCs at the nuclear surface. Most likely this is an intranuclear transport system, assuring efficient exchange between the nuclear interior and the NE, especially in large nuclei.

Mesh:

Year:  1997        PMID: 9262022     DOI: 10.1002/sca.4950190504

Source DB:  PubMed          Journal:  Scanning        ISSN: 0161-0457            Impact factor:   1.932


  19 in total

1.  Amino acid substitutions of coiled-coil protein Tpr abrogate anchorage to the nuclear pore complex but not parallel, in-register homodimerization.

Authors:  M E Hase; N V Kuznetsov; V C Cordes
Journal:  Mol Biol Cell       Date:  2001-08       Impact factor: 4.138

Review 2.  Versatility at the nuclear pore complex: lessons learned from the nucleoporin Nup153.

Authors:  Jennifer R Ball; Katharine S Ullman
Journal:  Chromosoma       Date:  2005-11-12       Impact factor: 4.316

3.  From the trap to the basket: getting to the bottom of the nuclear pore complex.

Authors:  Roderick Y H Lim; Ueli Aebi; Daniel Stoffler
Journal:  Chromosoma       Date:  2006-01-10       Impact factor: 4.316

Review 4.  Route of glucocorticoid-induced macromolecules across the nuclear envelope as viewed by atomic force microscopy.

Authors:  Victor Shahin
Journal:  Pflugers Arch       Date:  2006-05-31       Impact factor: 3.657

Review 5.  The Tpr protein: linking structure and function in the nuclear interior?

Authors:  M R Paddy
Journal:  Am J Hum Genet       Date:  1998-08       Impact factor: 11.025

6.  The nucleoporin Nup98 associates with the intranuclear filamentous protein network of TPR.

Authors:  B M Fontoura; S Dales; G Blobel; H Zhong
Journal:  Proc Natl Acad Sci U S A       Date:  2001-03-13       Impact factor: 11.205

Review 7.  Beyond lamins other structural components of the nucleoskeleton.

Authors:  Zhixia Zhong; Katherine L Wilson; Kris Noel Dahl
Journal:  Methods Cell Biol       Date:  2010       Impact factor: 1.441

8.  Protein Tpr is required for establishing nuclear pore-associated zones of heterochromatin exclusion.

Authors:  Sandra Krull; Julia Dörries; Björn Boysen; Sonja Reidenbach; Lars Magnius; Helene Norder; Johan Thyberg; Volker C Cordes
Journal:  EMBO J       Date:  2010-04-20       Impact factor: 11.598

9.  Depletion of a single nucleoporin, Nup107, prevents the assembly of a subset of nucleoporins into the nuclear pore complex.

Authors:  Thomas Boehmer; Jost Enninga; Samuel Dales; Gunter Blobel; Hualin Zhong
Journal:  Proc Natl Acad Sci U S A       Date:  2003-01-27       Impact factor: 11.205

10.  Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket.

Authors:  Sandra Krull; Johan Thyberg; Birgitta Björkroth; Hans-Richard Rackwitz; Volker C Cordes
Journal:  Mol Biol Cell       Date:  2004-06-30       Impact factor: 4.138

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