6-Bnz-cAMP is a membrane permeable and selective cAMP-dependent protein kinase (PKA) activator. For preferential stimulation of cAK type I, a combination with the site B selective analog 8-HA-cAMP or 8-AHA-cAMP can be used.
6-Bnz-cAMP is a membrane-permeable and selective cAMP-dependent protein kinase (PKA) activator.
Features and Benefits
This compound is featured on the PKA & PKG page of the Handbook of Receptor Classification and Signal Transduction. To browse other handbook pages, click here.
Biochemical and biophysical research communications, 152(3), 1504-1510 (1988-05-16)
The levels of mRNA for cellular retinol binding protein (CRBP) were studied in primary rat Sertoli cell cultures treated with cAMP analogues and retinol. In the presence of cyclic AMP analogues a dose- and time-dependent reduction (70-90%) of the levels
The Journal of biological chemistry, 268(34), 25343-25349 (1993-12-05)
The interaction of high density lipoprotein with its putative receptor stimulates translocation and efflux of intracellular sterols by a process involving activation of protein kinase C. This study shows that activation of cAMP-dependent protein kinase also stimulates efflux of intracellular
Proceedings of the National Academy of Sciences of the United States of America, 86(17), 6812-6815 (1989-09-01)
The suprachiasmatic nuclei (SCN) of mammals contain a circadian clock that synchronizes behavioral and physiological rhythms to the daily cycle of light and darkness. We have been probing the biochemical substrates of this endogenous pacemaker by examining the ability of
Critical reviews in oral biology and medicine : an official publication of the American Association of Oral Biologists, 4(3-4), 443-448 (1993-01-01)
A series of cAMP analogs that have different specificities for the two different binding sites on the regulatory subunit of type I and type II cAMP-dependent protein kinase (PKA) were used to determine whether selective activation of type I or
The Journal of biological chemistry, 271(44), 27630-27636 (1996-11-01)
The guanidinium groups of conserved arginines in the two intrachain cAMP-binding sites of regulatory (R) subunit of cAMP-dependent protein kinase have been implicated in the allosteric interactions by which cAMP binding leads to kinase activation. We have investigated the functional
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