Abstract
This article has no abstract.
Highlights
Renewed appreciation for the power of small organic molecules to address questions in cell biology has fueled an explosion of interest in chemical biology[1]
This strategy has been used in S. cerevisiae to probe the role of the kinase Cdc[28], which is the primary cyclin-dependent kinase (CDK) that controls the cell cycle in budding yeast[2]
The expectation was that treatment of the strain carrying only an inhibitor-sensitive Cdc[28] would show an identical G1/S transition arrest point
Summary
Using small molecules to perturb protein function has many advantages including: the effects of drugs are (1) rapid, potentially diffusion-limited, (2) often reversible due to metabolism/clearing, (3) tunable, allowing for graded phenotypes by varying concentration, and (4) conditional, since they can be introduced at any point in development. Despite these advantages, the use of small molecules to probe cellular signaling has lagged behind that of genetic or biochemical methods. Our lab has developed a combined chemical genetic method to inhibit protein kinases[2]. The active site of protein kinases is well conserved and makes specific inhibition of a desired kinase challenging
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