The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Activation of adenylate cyclase by the diterpene forskolin does not require the guanine nucleotide regulatory protein.
Open accessAbstract
Forskolin, a novel diterpene activator of adenylate cyclase in membranes and intact cells, activates the enzyme in membranes from mutant cyc-S49 murine lymphoma cells and the soluble enzyme from rat testes. Each of these enzymes consists only of the catalytic subunit and does not have a functional guanine nucleotide-binding protein. In both cases forskolin converts the manganese-dependent enzymes to a form which does not require manganese for activity. Forskolin can also stimulate a detergent-solubilized preparation of adenylate cyclase from rat cerebral cortex. Activation of adenylate cyclase by forskolin is therefore not dependent on a perturbation of membrane structure nor does it require a functional guanine nucleotide-binding subunit.
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Cites
Forskolin: unique diterpene activator of adenylate cyclase in membranes and in intact cells.
Seamon, K. B., Padgett, W., & Daly, J. W. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.6.3363 · Cited by 1,658
Self-citation
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Metadata
- Authors
- Seamon, K., & Daly, J. W.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1981-10
- Volume
- 256
- Issue
- 19
- Pages
- 9799-9801
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1576014737
- Cited by
- 738
- References
- 1
- FWCI
- 23.18
- Type
- journal article
- Language
- en
- Open access
- hybrid
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