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The Journal of Biological Chemistry|May 25, 1980
Studies on functional domains of the regulatory subunit of bovine heart adenosine 3':5'-monophosphate-dependent protein kinaseD A Flockhart, D M Watterson, J D Corbin
The Journal of Biological Chemistry|July 25, 1985
cAMP-dependent protein kinase activation lowers hepatocyte cAMPJ D Corbin, S J Beebe, P F Blackmore
The American Journal of Physiology|April 1, 1988
An assessment of phosphodiesterase activity in situ after treatment of hepatocytes with hormonesT W Gettys, P F Blackmore, J D Corbin
The Journal of Biological Chemistry|March 25, 1984
Two classes of cAMP analogs which are selective for the two different cAMP-binding sites of type II protein kinase demonstrate synergism when added together to intact adipocytesS J Beebe, R Holloway, S R Rannels, et al.
The Journal of Biological Chemistry|December 25, 1991
Mutating protein kinase cAMP-binding sites into cGMP-binding sites. Mechanism of cGMP selectivityJ B Shabb, B D Buzzeo, L Ng, et al.
Biochemical and Biophysical Research Communications|July 31, 1985
Regulatory subunit of cAMP-dependent protein kinase inhibits phosphoprotein phosphataseB S Khatra, R Printz, C E Cobb, et al.
The Journal of Biological Chemistry|March 15, 1987
Studies on the interactions between the cyclic nucleotide-binding sites of cGMP-dependent protein kinaseS O Døskeland, O K Vintermyr, J D Corbin, et al.
The Journal of Biological Chemistry|August 5, 1989
Expression and characterization of mutant forms of the type I regulatory subunit of cAMP-dependent protein kinase. The effect of defective cAMP binding on holoenzyme activationT A Woodford, L A Correll, G S McKnight, et al.
Advances in Cyclic Nucleotide Research|January 1, 1975
Hormonal regulation of adenosine 3',5'-monophosphate-dependent protein kinaseJ D Corbin, S L Keely, T R Soderling, et al.
The Journal of Biological Chemistry|July 25, 1988
Activation of the particulate low Km phosphodiesterase of adipocytes by addition of cAMP-dependent protein kinaseT W Gettys, A J Vine, M F Simonds, et al.
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