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Two distinct adenosine-sensitive sites on adenylate cyclase.
Open accessAbstract
The effects of adenosine and adenosine analogs on adenylate cyclases from several tissues have been examined. Two adenosine-reactive sites have been identified: (i) the "R" site, occupancy of which usually leads to activation of cyclase and which requires integrity of the ribose ring for activity, and (ii) the "P" site, which mediates inhibition and requires integrity of the purine ring for activity. Biphasic effects of adenosine are explained by the presence of both sites on a single adenylate cyclase. Comparison of these data with those in the literature indicates that adenosine-reactive "P" and "R" sites are present generally.
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Cited by
Nomenclature and classification of purinoceptors.
Fredholm, B. B., Abbracchio, M. P., Burnstock, G., Daly, J. W., Harden, T. K., Jacobson, K. A., Leff, P., & Williams, M. (1994) · Pharmacological Reviews · doi:10.1016/s0031-6997(25)06782-1 · Cited by 1,585
Complexity and Diversity of Mammalian Adenylyl Cyclases
Sunahara, R. K., Dessauer, C. W., & Gilman, A. G. (1996) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.36.040196.002333 · Cited by 874
Isoforms of Mammalian Adenylyl Cyclase: Multiplicities of Signaling
Sunahara, R. K. (2002) · Molecular Interventions · doi:10.1124/mi.2.3.168 · Cited by 406
Caffeine analogs: biomedical impact
Daly, J. W. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7051-9 · Cited by 256
Islet-activating protein. A modifier of receptor-mediated regulation of rat islet adenylate cyclase.
Katada, T., & Ui, M. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68845-9 · Cited by 253
Metadata
- Authors
- Londos, C., & Wolff, J.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1977-12
- Volume
- 74
- Issue
- 12
- Pages
- 5482-5486
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2068447507
- Cited by
- 574
- References
- 0
- FWCI
- 12.34
- Type
- journal article
- Language
- en
- Open access
- green
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