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Extracellular phosphorylation of a receptor tyrosine kinase controls synaptic localization of NMDA receptors and regulates pathological pain

Modification of protein function by phosphorylation controls many aspects of cellular function and signaling. Interestingly, the first evidence for phosphoproteins came from the observation that the secreted milk protein, casein, contained phosphate, suggesting that phosphorylation can occur in the extracellular space.

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Extracellular phosphorylation of a receptor tyrosine kinase controls synaptic localization of NMDA receptors and regulates pathological pain

Modification of protein function by phosphorylation controls many aspects of cellular function and signaling. Interestingly, the first evidence for phosphoproteins came from the observation that the secreted milk protein, casein, contained phosphate, suggesting that phosphorylation can occur in the extracellular space.

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Extracellular phosphorylation of a receptor tyrosine kinase controls synaptic localization of NMDA receptors and regulates pathological pain

Modification of protein function by phosphorylation controls many aspects of cellular function and signaling. Interestingly, the first evidence for phosphoproteins came from the observation that the secreted milk protein, casein, contained phosphate, suggesting that phosphorylation can occur in the extracellular space.

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