ERK nuclear translocation is dimerization-independent but controlled by the 
rate of phosphorylation.

Lidke, D. S.; Huang, F.; Post, J. N.; Rieger, B.; Wilsbacher, J.; Thomas, J. L.; Pouyssegur, J.; Jovin, T. M.; Lenormand, P.

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ERK nuclear translocation is dimerization-independent but controlled by the rate of phosphorylation.

Lidke, D. S., Huang, F., Post, J. N., Rieger, B., Wilsbacher, J., Thomas, J. L., et al. (2010). ERK nuclear translocation is dimerization-independent but controlled by the rate of phosphorylation. The Journal of Biological Chemistry, 285, 3092-3102. Retrieved from http://www.jbc.org/content/285/5/3092.full.pdf+html.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0012-D640-8 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0027-F275-2

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Creators:
Lidke, D. S.¹, Author
Huang, F., Author
Post, J. N.¹, Author
Rieger, B.¹, Author
Wilsbacher, J., Author
Thomas, J. L., Author
Pouyssegur, J., Author
Jovin, T. M.², Author
Lenormand, P., Author

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1Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society, ou_578628
2Max Planck Society, ou_persistent13

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Language(s): eng - English

Dates: Date issued: 2010-01-29

Publication Status: Issued

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Identifiers: eDoc: 439528
URI: http://www.jbc.org/content/285/5/3092.full.pdf+html

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Title: The Journal of Biological Chemistry

Source Genre: Journal

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Pages: - Volume / Issue: 285 Sequence Number: - Start / End Page: 3092 - 3102 Identifier: -