APA

Fujita-Yamaguchi Y., Kathuria S., Xu Q. Y., McDonald J. M., Nakano H. & Kamata T. (19891109). In vitro tyrosine phosphorylation studies on RAS proteins and calmodulin suggest that polylysine-like basic peptides or domains may be involved in interactions between insulin receptor kinase and its substrate. : Proceedings of the National Academy of Sciences of the United States of America.

Chicago

Fujita-Yamaguchi Y, Kathuria S, Xu Q Y, McDonald J M, Nakano H and Kamata T. 19891109. In vitro tyrosine phosphorylation studies on RAS proteins and calmodulin suggest that polylysine-like basic peptides or domains may be involved in interactions between insulin receptor kinase and its substrate. : Proceedings of the National Academy of Sciences of the United States of America.

Harvard

Fujita-Yamaguchi Y., Kathuria S., Xu Q. Y., McDonald J. M., Nakano H. and Kamata T. (19891109). In vitro tyrosine phosphorylation studies on RAS proteins and calmodulin suggest that polylysine-like basic peptides or domains may be involved in interactions between insulin receptor kinase and its substrate. : Proceedings of the National Academy of Sciences of the United States of America.

MLA

Fujita-Yamaguchi Y, Kathuria S, Xu Q Y, McDonald J M, Nakano H and Kamata T. In vitro tyrosine phosphorylation studies on RAS proteins and calmodulin suggest that polylysine-like basic peptides or domains may be involved in interactions between insulin receptor kinase and its substrate. : Proceedings of the National Academy of Sciences of the United States of America. 19891109.