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The Journal of Biological Chemistry|December 25, 2012
Several phenylalanine-glycine motives in the nucleoporin Nup214 are essential for binding of the nuclear export receptor CRM1Stephanie Roloff, Christiane Spillner, Ralph H Kehlenbach
Methods in Enzymology|October 11, 2022
RAPIDS, a method for sub-compartmental identification of protein interactomesChristina James, Christof Lenz, Ralph H Kehlenbach
The Journal of Biological Chemistry|July 27, 2007
Nuclear import of c-Jun is mediated by multiple transport receptorsInga Waldmann, Sarah Wälde, Ralph H Kehlenbach
International Review of Cell and Molecular Biology|November 29, 2015
Nuclear Pore Complexes and Nucleocytoplasmic Transport: From Structure to Function to DiseaseAchim Dickmanns, Ralph H Kehlenbach, Birthe Fahrenkrog
International Journal of Molecular Sciences|December 24, 2021
Sequestosome 1 Is Part of the Interaction Network of VAPBChristina James, Christof Lenz, Henning Urlaub, et al.
The Biochemical Journal|January 9, 2020
Into the basket and beyond: the journey of mRNA through the nuclear pore complexAsaf Ashkenazy-Titelman, Yaron Shav-Tal, Ralph H Kehlenbach
Molecular Biology of the Cell|February 29, 2008
The Nup358-RanGAP complex is required for efficient importin alpha/beta-dependent nuclear importSaskia Hutten, Annette Flotho, Frauke Melchior, et al.
The Journal of Biological Chemistry|January 13, 2006
Transportin is a major nuclear import receptor for c-Fos: a novel mode of cargo interactionMarc Arnold, Annegret Nath, Daniel Wohlwend, et al.
Methods in Cell Biology|May 27, 2014
Analysis of nucleocytoplasmic transport in digitonin-permeabilized cells under different cellular conditionsMaiko Furuta, Shingo Kose, Ralph H Kehlenbach, et al.
Biological Chemistry|May 21, 2023
Interaction of nucleoporins with nuclear transport receptors: a structural perspectiveRalph H Kehlenbach, Piotr Neumann, Ralf Ficner, et al.
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