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  Identification of Two novel RanGTP-binding proteins belonging to the importin β superfamily.

Kutay, U., Hartmann, E., Treichel, N., Calado, A., Carmo-Fonseca, M., Prehn, S., et al. (2000). Identification of Two novel RanGTP-binding proteins belonging to the importin β superfamily. The Journal of Biological Chemistry, 275(51), 40163-40168. doi:10.1074/jbc.M006242200.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0015-3D4E-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-E4DE-7
Genre: Journal Article

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1932930.pdf (Publisher version), 716KB
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 Creators:
Kutay, U., Author
Hartmann, E., Author
Treichel, N., Author
Calado, A., Author
Carmo-Fonseca, M., Author
Prehn, S., Author
Kraft, R., Author
Görlich, D.1, Author              
Bischoff, F. R., Author
Affiliations:
1Department of Cellular Logistics, MPI for biophysical chemistry, Max Planck Society, ou_578574              

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 Abstract: Nucleo-cytoplasmic transport comprises a large number of distinct pathways, many of which are defined by members of the importin β superfamily of nuclear transport receptors. These transport receptors all directly interact with RanGTP to modulate the compartment-specific binding of their transport substrates. To identify new members of the importin β family, we used affinity chromatography on immobilized RanGTP and isolated Ran-binding protein (RanBP) 16 from HeLa cell extracts. RanBP16 and its close human homologue, RanBP17, are distant members of the importin β family. Like the other members of the transport receptor superfamily, RanBP16 interacts with the nuclear pore complex and is able to enter the nucleus independent of energy and additional nuclear transport receptors.

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Language(s): eng - English
 Dates: 2000-10-062000-12-22
 Publication Status: Published in print
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1074/jbc.M006242200
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Title: The Journal of Biological Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 275 (51) Sequence Number: - Start / End Page: 40163 - 40168 Identifier: -