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A\u03b2 inhibits protein phosphatases in a dose-dependent manner, thus it is expected that the phosphorylation state of specific proteins would be altered in response to A\u03b2. In fact several Alzheimer\u2019s disease related proteins, such as APP and TAU, exhibit pathology associated hyperphosphorylated states. A systems biology approach was adopted and the phosphoproteome, of primary cortical neuronal cells exposed to A\u03b2, was evaluated. Phosphorylated proteins were recovered and those whose recovery increased or decreased, upon A\u03b2 exposure across experimental sets, were identified. Significant differences were evident for 141 proteins and investigation of their interactors revealed key protein clusters responsive to A\u03b2 treatment. Of these, 73 phosphorylated proteins increased and 68 decreased upon A\u03b2 addition. 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