Abstract
Photocaging of a tight-binding bisubstrate inhibitor of cAMP-dependent protein kinase (PKA) with a nitrodibenzofuran-based group fully abolished its inhibitory potency. The affinity difference between the photocaged and the active inhibitor was over 5 orders of magnitude. The photocaged inhibitor disrupted the PKA holoenzyme in cell lysates upon photolysis under a 398 nm LED.
MeSH terms
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Animals
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CHO Cells
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Cricetulus
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Cyclic AMP-Dependent Protein Kinases / metabolism*
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Dibenzofurans / chemical synthesis
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Dibenzofurans / chemistry
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Dibenzofurans / pharmacology*
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Dibenzofurans / radiation effects
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Humans
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Molecular Structure
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Protein Kinase Inhibitors / chemical synthesis
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Protein Kinase Inhibitors / chemistry
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Protein Kinase Inhibitors / pharmacology*
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Protein Kinase Inhibitors / radiation effects
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Purines / chemical synthesis
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Purines / chemistry
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Purines / pharmacology*
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Purines / radiation effects
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Ultraviolet Rays
Substances
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Dibenzofurans
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Protein Kinase Inhibitors
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Purines
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Cyclic AMP-Dependent Protein Kinases