Adenosine monophosphate (AMP) is a nucleotide, consisting of a phosphate group, the sugar ribose, and the nucleobase adenine. AMP is an activator of several enzymes in the tissues. In the glycolytic pathway, the enzyme phosphofructokinase is inhibited by ATP but the inhibition is reversed by AMP, the deciding factor for the reaction being the ratio between ATP and AMP. In medicine, AMP is used mainly as an alternative to adenosine for treatment of ischemia and as a tool compound to measure hyperresponsiveness of airways.

α,β-methylene adenosine 5′-diphosphate (AOPCP, adenosine-5′-O-[(phosphonomethyl)phosphonic acid] or α,β-methylene-ADP) is an analog of adenosine 5′-diphosphate (ADP). It acts as a CD73/ecto-5′-nucleotidase inhibitor. Blocks ecto-5'-nucleotidase-mediated adenosine production by preventing the conversion of AMP to adenosine.

Cyclic adenosine monophosphate (cAMP, cyclic AMP or 3'-5'-cyclic adenosine monophosphate) is a molecule that is important in many biological processes; it is derived from adenosine triphosphate (ATP) by adenylate cyclase located on the inner side of the plasma membrane and anchored at various locations in the interior of the cell. Around 1960 Earl W. Sutherland, Jr. showed that cyclic adenosine monophosphate (cAMP) serves as the secondary messenger within the cell. Cyclic AMP works by activating protein kinase A (PKA, or cAMP-dependent protein kinase). PKA is normally inactive as a tetrameric holoenzyme, consisting of two catalytic and two regulatory units with the regulatory units blocking the catalytic centers of the catalytic units. Cyclic AMP binds to specific locations on the regulatory units of the protein kinase, and causes dissociation between the regulatory and catalytic subunits, thus enabling those catalytic units to phosphorylate substrate proteins. It was discovered, that melanocytes require the RAS/RAF/MEK/ERK and the cyclic AMP (cAMP) signaling pathways to maintain the fine balance between proliferation and differentiation. cAMP suppressed CRAF activity in melanocytes and that was essential to suppress the oncogenic potential of CRAF in the cells. When RAS was mutated in melanoma, the cells switched their signaling from BRAF to CRAF. That switch was accompanied by dysregulated cAMP signaling, a step that was necessary to allow CRAF to signal to MEK. Thus, a fundamental switch in RAF isoform usage occurs when RAS was mutated in melanoma, and that occurs in the context of disrupted cAMP signaling. These data have important implications for the development of therapeutic strategies to treat this life-threatening disease.