Hartings AU Phosphorylation Lab

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We are synthesizing novel ruthenium-modified adenosine triphosphate (ATP) analogues. These molecules are being designed so that they can be used by kinases to phosphorylate protein-substrates with a ruthenium-modified phosphate group. Additionally, the ruthenated-phosphate group must be inaccessible to phosphatases such that once the protein-substrate is irreversibly phosphorylated. We plan to use these molecules to study and disrupt intracellular communication with a specific focus on cancerous cells. (The image above shows that one of the ruthenium-modified ATP molecules will look like (left) as well as a rendering of a protein structure with a tyrosine that has been phosphorylated with our modified ATP (right)). You can find more information on this lab at our group [http://hartingslab.com/research/phosphorylation website].<br>
We are synthesizing novel ruthenium-modified adenosine triphosphate (ATP) analogues. These molecules are being designed so that they can be used by kinases to phosphorylate protein-substrates with a ruthenium-modified phosphate group. Additionally, the ruthenated-phosphate group must be inaccessible to phosphatases such that once the protein-substrate is irreversibly phosphorylated. We plan to use these molecules to study and disrupt intracellular communication with a specific focus on cancerous cells. (The image above shows that one of the ruthenium-modified ATP molecules will look like (left) as well as a rendering of a protein structure with a tyrosine that has been phosphorylated with our modified ATP (right)). You can find more information on this lab at our group [http://hartingslab.com/research/phosphorylation website].<br>
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Current revision



We are synthesizing novel ruthenium-modified adenosine triphosphate (ATP) analogues. These molecules are being designed so that they can be used by kinases to phosphorylate protein-substrates with a ruthenium-modified phosphate group. Additionally, the ruthenated-phosphate group must be inaccessible to phosphatases such that once the protein-substrate is irreversibly phosphorylated. We plan to use these molecules to study and disrupt intracellular communication with a specific focus on cancerous cells. (The image above shows that one of the ruthenium-modified ATP molecules will look like (left) as well as a rendering of a protein structure with a tyrosine that has been phosphorylated with our modified ATP (right)). You can find more information on this lab at our group website.


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