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

Messerschmidt, A.; Macieira, Sofia; Velarde, Milko; Badeker, M.; Benda, C.; Jestel, A.; Brandstetter, H.; Neuefeind, T.; Blaesse, M.

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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

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

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

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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., Brandstetter, H., Neuefeind, T., & Blaesse, M. (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.

引用: https://hdl.handle.net/11858/00-001M-0000-0010-6576-A

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