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Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons78394

Messerschmidt,  A.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78347

Macieira,  Sofia
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78826

Velarde,  Milko
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

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Messerschmidt, A., Macieira, S., Velarde, M., Badeker, M., Benda, C., Jestel, A., et al. (2005). Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif. Journal of Molecular Biology, 352(4), 918-931.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-6576-A
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