The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.
Rising behind NO: cGMP-dependent protein kinases
Abstract
Over the past few years, a wealth of biochemical and functional data has been gathered on mammalian cGMP-dependent protein kinases (cGKs). In mammals, three different kinases are encoded by two genes. Mutant and chimeric cGMP kinase proteins generated by molecular biology techniques have yielded important biochemical knowledge, such as the function of the N-terminal domains of cGKI and cGKII, the identity of the cGMP-binding sites of cGKI, the substrate specificity of the enzymes and structural details of the catalytic center. Genetic approaches have proved to be especially useful for the analysis of the biological function of cGKs. Recently, some of the in vivo targets and mechanisms leading to smooth muscle relaxation have been identified. In vivo targets are the myosin-binding subunit of myosin phosphatase (PP1M), a member of the protein phosphatase 1, the calcium-activated maxi K+ channel and a new protein named IRAG that forms a complex with the inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) receptor and cGKI. Phosphorylation of PP1M by cGKIα activates myosin phosphatase, whereas phosphorylation of IRAG by cGKIβ decreases Ins(1,4,5)P3-induced calcium release. cGKII regulates in vivo intestinal fluid secretion by phosphorylation of the cystic fibrosis transmembrane conductance regulator (CFTR), bone growth and renal renin secretion by phosphorylation of unknown proteins.
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Cites
Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor
Palmer, R. M. J., Ferrige, A. G., & Moncada, S. (1987) · Nature · doi:10.1038/327524a0 · Cited by 10,704
Regulation of Myosin Phosphatase by Rho and Rho-Associated Kinase (Rho-Kinase)
Kimura, K., Ito, M., Amano, M., Chihara, K., Fukata, Y., Nakafuku, M., Yamamori, B., Feng, J., Nakano, T., Okawa, K., et al. (1996) · Science · doi:10.1126/science.273.5272.245 · Cited by 2,884
Garg, U. C., & Hassid, A. (1989) · Journal of Clinical Investigation · doi:10.1172/jci114081 · Cited by 2,155
Ignarro, L. J., Byrns, R. E., Buga, G. M., & Wood, K. S. (1987) · Circulation Research · doi:10.1161/01.res.61.6.866 · Cited by 1,179
Nitric Oxide as a Signaling Molecule in the Vascular System: An Overview
Ignarro, L. J., Cirino, G., Casini, A., & Napoli, C. (1999) · Journal of Cardiovascular Pharmacology · doi:10.1097/00005344-199912000-00016 · Cited by 763
Katsuki, S., Arnold, W. P., Mittal, C. K., & Murad, F. (1977) · PubMed · Cited by 700
Natural Behavior Polymorphism Due to a cGMP-Dependent Protein Kinase of Drosophila
Osborne, K. A., Robichon, A., Burgess, E., Butland, S., Shaw, R. A., Coulthard, A., Pereira, H. S., Greenspan, R. J., & Sokolowski, M. B. (1997) · Science · doi:10.1126/science.277.5327.834 · Cited by 536
Regulation of Myosin Phosphatase by a Specific Interaction with cGMP- Dependent Protein Kinase Iα
Surks, H. K., Mochizuki, N., Kasai, Y., Georgescu, S. P., Tang, K. M., Ito, M., Lincoln, T. M., & Mendelsohn, M. E. (1999) · Science · doi:10.1126/science.286.5444.1583 · Cited by 527
Defective smooth muscle regulation in cGMP kinase I-deficient mice
Pfeifer, A. (1998) · The EMBO Journal · doi:10.1093/emboj/17.11.3045 · Cited by 497
Calderone, A., Thaik, C. M., Takahashi, N., Chang, D. L., & Colucci, W. S. (1998) · Journal of Clinical Investigation · doi:10.1172/jci119883 · Cited by 490
Cited by
Mollnau, H., Wendt, M., Szöcs, K., Lassègue, B., Schulz, E., Oelze, M., Li, H., Bodenschatz, M., August, M., Kleschyov, A. L., et al. (2002) · Circulation Research · doi:10.1161/01.res.0000012569.55432.02 · Cited by 676
Regulation of Nitric Oxide-Sensitive Guanylyl Cyclase
Friebe, A., & Koesling, D. (2003) · Circulation Research · doi:10.1161/01.res.0000082524.34487.31 · Cited by 508
Rho/Rho-kinase mediated signaling in physiology and pathophysiology
Wettschureck, N., & Offermanns, S. (2002) · Journal of Molecular Medicine · doi:10.1007/s00109-002-0370-2 · Cited by 334
Münzel, T., Feil, R., Mülsch, A., Lohmann, S. M., Hofmann, F., & Walter, U. (2003) · Circulation · doi:10.1161/01.cir.0000094403.78467.c3 · Cited by 316
Self-citationTrebicka, J., Hennenberg, M., Laleman, W., Shelest, N., Biecker, E., Schepke, M., Nevens, F., Sauerbruch, T., & Heller, J. (2007) · Hepatology · doi:10.1002/hep.21673 · Cited by 305
Metadata
- Authors
- Hofmann, F., Ammendola, A., & Schlossmann, J.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2000-05-15
- Volume
- 113
- Issue
- 10
- Pages
- 1671-1676
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W1902300865
- Cited by
- 340
- References
- 49
- FWCI
- 9.24
- Type
- journal article
- Language
- en
- Open access
- closed
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