APA aipamena

Kong, R. C. K., Petrie, E. J., Mohanty, B., Ling, J., Lee, J. C. Y., Gooley, P. R., & Bathgate, R. A. D. (2013). The Relaxin Receptor (RXFP1) Utilizes Hydrophobic Moieties on a Signaling Surface of Its N-terminal Low Density Lipoprotein Class A Module to Mediate Receptor Activation. American Society for Biochemistry and Molecular Biology.

Chicago Style aipamena

Kong, Roy C. K., Emma J. Petrie, Biswaranjan Mohanty, Jason Ling, Jeremy C. Y. Lee, Paul R. Gooley, and Ross A. D. Bathgate. The Relaxin Receptor (RXFP1) Utilizes Hydrophobic Moieties On a Signaling Surface of Its N-terminal Low Density Lipoprotein Class A Module to Mediate Receptor Activation. American Society for Biochemistry and Molecular Biology, 2013.

MLA aipamena

Kong, Roy C. K., et al. The Relaxin Receptor (RXFP1) Utilizes Hydrophobic Moieties On a Signaling Surface of Its N-terminal Low Density Lipoprotein Class A Module to Mediate Receptor Activation. American Society for Biochemistry and Molecular Biology, 2013.