Dimerization and direct membrane interaction of Nup53 contribute to nuclear pore complex assembly-Reference-Cited by-同舟云学术

Dimerization and direct membrane interaction of Nup53 contribute to nuclear pore complex assembly

Published:2012-09-07 Issue:20 Volume:31 Page:4072-4084
ISSN:0261-4189
Container-title:The EMBO Journal
language:en
Short-container-title:

Author:

Vollmer Benjamin¹,Schooley Allana¹,Sachdev Ruchika¹,Eisenhardt Nathalie¹,Schneider Anna M²,Sieverding Cornelia¹,Madlung Johannes³,Gerken Uwe⁴,Macek Boris³,Antonin Wolfram¹

Affiliation:

1. Friedrich Miescher Laboratory of the Max Planck Society; Tübingen Germany

2. Max Planck Institute for Developmental Biology, Department of Biochemistry; Tübingen Germany

3. Proteome Center Tübingen, University of Tübingen; Tübingen Germany

4. Institute of Microbiology, University of Hohenheim; Stuttgart Germany

Publisher

Wiley

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology,General Neuroscience

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4. Nuclear pore complex assembly through the cell cycle: regulation and membrane organization;Antonin;FEBS Lett,2008

5. The integral membrane nucleoporin pom121 functionally links nuclear pore complex assembly and nuclear envelope formation;Antonin;Mol Cell,2005

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