Ceramide kinase profiling by mass spectrometry reveals a conserved phosphorylation pattern downstream of the catalytic site.

MLA

Chen, Wei-Qiang, et al. “Ceramide Kinase Profiling by Mass Spectrometry Reveals a Conserved Phosphorylation Pattern Downstream of the Catalytic Site.” Journal of Proteome Research, vol. 9, no. 1, Jan. 2010, pp. 420–29. EBSCOhost, https://doi.org/10.1021/pr900763z.

APA

Chen, W.-Q., Graf, C., Zimmel, D., Rovina, P., Krapfenbauer, K., Jaritz, M., Parker, P. J., Lubec, G., & Bornancin, F. (2010). Ceramide kinase profiling by mass spectrometry reveals a conserved phosphorylation pattern downstream of the catalytic site. Journal of Proteome Research, 9(1), 420–429. https://doi.org/10.1021/pr900763z

Chicago

Chen, Wei-Qiang, Christine Graf, David Zimmel, Philipp Rovina, Kurt Krapfenbauer, Markus Jaritz, Peter J Parker, Gert Lubec, and Frédéric Bornancin. 2010. “Ceramide Kinase Profiling by Mass Spectrometry Reveals a Conserved Phosphorylation Pattern Downstream of the Catalytic Site.” Journal of Proteome Research 9 (1): 420–29. doi:10.1021/pr900763z.