APA

Lee J., Han K. C., Kang J. H., Pearce L. L., Lewin N. E., Yan S., Benzaria S., Nicklaus M. C., Blumberg P. M. & Marquez V. E. (20020107). Conformationally constrained analogues of diacylglycerol. 18. The incorporation of a hydroxamate moiety into diacylglycerol-lactones reduces lipophilicity and helps discriminate between sn-1 and sn-2 binding modes to protein kinase C (PK-C). Implications for isozyme specificity. : Journal of medicinal chemistry.

Chicago

Lee J, Han K C, Kang J H, Pearce L L, Lewin N E, Yan S, Benzaria S, Nicklaus M C, Blumberg P M and Marquez V E. 20020107. Conformationally constrained analogues of diacylglycerol. 18. The incorporation of a hydroxamate moiety into diacylglycerol-lactones reduces lipophilicity and helps discriminate between sn-1 and sn-2 binding modes to protein kinase C (PK-C). Implications for isozyme specificity. : Journal of medicinal chemistry.

Harvard

Lee J., Han K. C., Kang J. H., Pearce L. L., Lewin N. E., Yan S., Benzaria S., Nicklaus M. C., Blumberg P. M. and Marquez V. E. (20020107). Conformationally constrained analogues of diacylglycerol. 18. The incorporation of a hydroxamate moiety into diacylglycerol-lactones reduces lipophilicity and helps discriminate between sn-1 and sn-2 binding modes to protein kinase C (PK-C). Implications for isozyme specificity. : Journal of medicinal chemistry.

MLA

Lee J, Han K C, Kang J H, Pearce L L, Lewin N E, Yan S, Benzaria S, Nicklaus M C, Blumberg P M and Marquez V E. Conformationally constrained analogues of diacylglycerol. 18. The incorporation of a hydroxamate moiety into diacylglycerol-lactones reduces lipophilicity and helps discriminate between sn-1 and sn-2 binding modes to protein kinase C (PK-C). Implications for isozyme specificity. : Journal of medicinal chemistry. 20020107.