Key result
Differential proteomics identified several proteins that change in abundance upon platelet activation, implicating novel pathomechanisms and potential therapeutic targets for platelet inhibition.
Highlights the utility of differential proteomics in discovering novel mechanisms and therapeutic targets for platelet inhibition.
In this issue of Blood, Schulz and colleagues report promising findings using differential proteomics as a discovery tool to identify functionally important proteins in platelet activation. The authors identify several proteins that change in abundance upon platelet activation. These findings implicate several novel pathomechanisms relevant to platelet activation and identify novel potential therapeutic targets for platelet inhibition.1
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Karlheinz Peter (2010) conducted an editorial in Platelet activation. Differential proteomics was evaluated on Proteins that change in abundance upon platelet activation. Differential proteomics identified several proteins that change in abundance upon platelet activation, implicating novel pathomechanisms and potential therapeutic targets for platelet inhibition.
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