Journal articles: 'Cyclic GMP'

1

Sager, Georg. "Cyclic GMP transporters." Neurochemistry International 45, no. 6 (November 2004): 865–73. http://dx.doi.org/10.1016/j.neuint.2004.03.017.

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2

Takemoto, Dolores J., Karen Gonzalez, Igor Udovichenko, and Jess Cunnick. "Cyclic GMP-regulated cyclic nucleotide phosphodiesterases." Cellular Signalling 5, no. 5 (September 1993): 549–53. http://dx.doi.org/10.1016/0898-6568(93)90050-v.

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3

Souness, J. E., B. K. Diocee, W. Martin, and S. A. Moodie. "Pig aortic endothelial-cell cyclic nucleotide phosphodiesterases. Use of phosphodiesterase inhibitors to evaluate their roles in regulating cyclic nucleotide levels in intact cells." Biochemical Journal 266, no. 1 (February 15, 1990): 127–32. http://dx.doi.org/10.1042/bj2660127.

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Two cyclic nucleotide phosphodiesterase (PDE) activities were identified in pig aortic endothelial cells, a cyclic GMP-stimulated PDE and a cyclic AMP PDE. Cyclic GMP-stimulated PDE had Km values of 367 microM for cyclic AMP and 24 microM for cyclic GMP, and low concentrations (1 microM) of cyclic GMP increased the affinity of the enzyme for cyclic AMP (Km = 13 microM) without changing the Vmax. This isoenzyme was inhibited by trequinsin [IC50 (concn. giving 50% inhibition of substrate hydrolysis) = 0.6 microM for cyclic AMP hydrolysis in the presence of cyclic GMP; IC50 = 0.6 microM for cyclic GMP hydrolysis] and dipyridamole (IC50 = 5 microM for cyclic AMP hydrolysis in the presence of cyclic GMP; IC50 = 3 microM for cyclic GMP hydrolysis). Cyclic AMP PDE exhibited a Km of 2 microM for cyclic AMP and did not hydrolyse cyclic GMP. This activity was inhibited by trequinsin (IC50 = 0.2 microM), dipyridamole (IC50 = 6 microM) and, selectively, by rolipram (IC50 = 3 microM). Inhibitors of cyclic GMP PDE (M&B 22948) and of low Km (Type III) cyclic AMP PDE (SK&F 94120) only weakly inhibited the two endothelial PDEs. Incubation of intact cells with trequinsin and dipyridamole induced large increases in cyclic GMP, which were completely blocked by LY-83583. Rolipram, SK&F 94120 and M&B 22948 did not significantly influence cyclic GMP accumulation. Dipyridamole enhanced the increase in cyclic GMP induced by sodium nitroprusside. Cyclic AMP accumulation was stimulated by dipyridamole and trequinsin with and without forskolin. Rolipram, although without effect alone, increased cyclic AMP in the presence of forskolin, whereas M&B 22948 and SK&F 94120 had no effects on resting or forskolin-stimulated levels. These results suggest that cyclic GMP-stimulated PDE regulates cyclic GMP levels and that both endothelial PDE isoenzymes contribute to the control of cyclic AMP.

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4

Srivastava, D., D. A. Fox, and R. L. Hurwitz. "Effects of magnesium on cyclic GMP hydrolysis by the bovine retinal rod cyclic GMP phosphodiesterase." Biochemical Journal 308, no. 2 (June 1, 1995): 653–58. http://dx.doi.org/10.1042/bj3080653.

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Knowledge of the kinetics of the rod cyclic GMP phosphodiesterase is essential for understanding the kinetics and gain of the light response. Therefore, the interactions between Mg2+, cyclic GMP, and purified, trypsin-activated bovine rod cyclic GMP phosphodiesterase (EC 3.1.4.17) were examined. The effects of Mg2+ and of cyclic GMP on the rod phosphodiesterase activity were mutually concentration-dependent. Formation of a free Mg-cyclic GMP complex is unlikely due to its high dissociation constant (Kd = 19 mM). Plots of 1/velocity versus 1/[cyclic GMP] as a function of [Mg2+] and 1/velocity versus 1/[Mg2+] as a function of [cyclic GMP] intersected to the left of the 1/velocity axis. This is consistent with the formation of a ternary complex between the phosphodiesterase, Mg2+, and cyclic GMP. A competitive inhibitor of the phosphodiesterase relative to cyclic GMP, 3-isobutyl-1-methylxanthine, non-competitively inhibited the enzyme relative to Mg2+, Pb2+, a competitive inhibitor of the phosphodiesterase relative to Mg2+ [D. Srivastava, R.L. Hurwitz and D. A. Fox (1995) Toxicol. Appl. Pharmacol, in the press] non-competitively inhibited the enzyme relative to cyclic GMP. Collectively these results are suggestive of a rapid equilibrium random binding order of Mg2+ and cyclic GMP to the rod phosphodiesterase.

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5

Wahler, Gordon M., Nancy J. Rusch, and Nicholas Sperelakis. "8-Bromo-cyclic GMP inhibits the calcium channel current in embryonic chick ventricular myocytes." Canadian Journal of Physiology and Pharmacology 68, no. 4 (April 1, 1990): 531–34. http://dx.doi.org/10.1139/y90-076.

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Superfusion with 8-bromo-cyclic GMP or intracellular injection of cyclic GMP inhibits calcium-dependent slow action potentials in embryonic chick or guinea pig ventricular cells, suggesting that cyclic GMP inhibits calcium currents. Recently, cyclic GMP has been shown to reduce cyclic AMP-stimulated calcium currents in voltage-clamped ventricular myocytes. Since earlier results in intact cells had suggested that cyclic GMP might inhibit basal (i.e., unstimulated by cyclic AMP) calcium currents, we directly investigated the effect of 8-bromo-cyclic GMP on basal calcium channel currents (using barium as the charge carrier) in voltage-clamped ventricular myocytes isolated from embryonic chick hearts. Superfusion with 1 mM 8-bromo-cyclic GMP (without prior cyclic AMP elevation) progressively decreased peak calcium channel currents (−68% at 15 min after the onset of drug exposure). In contrast, the currents were unchanged during 15 min superfusion with control solution, or 1 mM 8-bromo-GMP (the noncyclic inactive analog of 8-bromo-cyclic GMP). The present results in voltage-clamped embryonic chick heart cells indicate that cyclic GMP can inhibit basal calcium channel currents, apparently through a cyclic AMP-independent mechanism.Key words: cyclic GMP, calcium channels, calcium current, heart.

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6

Houslay, Miles D. "Renaissance for cyclic GMP?" Trends in Biochemical Sciences 10, no. 12 (December 1985): 465–66. http://dx.doi.org/10.1016/0968-0004(85)90199-9.

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7

Okada, D. "Cyclic GMP binding regulates the catalytic activity of cyclic GMP-specific phosphodiesterase." Neuroscience Research 38 (2000): S48. http://dx.doi.org/10.1016/s0168-0102(00)81135-9.

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8

Zhang, Qihang, Michael Lazar, Lin Yan, Yiqi He, James Tse, Harvey R. Weiss, and Peter M. Scholz. "Cyclic GMP Reduces Myocardial Stunning Through Non-Cyclic GMP Protein Kinase Mechanisms." Journal of Cardiovascular Pharmacology 44, no. 2 (August 2004): 235–43. http://dx.doi.org/10.1097/00005344-200408000-00014.

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9

Biswas, Kabir H., and Sandhya S. Visweswariah. "Distinct Allostery Induced in the Cyclic GMP-binding, Cyclic GMP-specific Phosphodiesterase (PDE5) by Cyclic GMP, Sildenafil, and Metal Ions." Journal of Biological Chemistry 286, no. 10 (December 29, 2010): 8545–54. http://dx.doi.org/10.1074/jbc.m110.193185.

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10

Miller, Herman T., W. Yesus, T. Cooper, and S. Harwell. "Cyclic AMP and cyclic GMP in hyperresponsiveness." Life Sciences 43, no. 24 (January 1988): 1991–97. http://dx.doi.org/10.1016/0024-3205(88)90572-3.

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11

Villegas, Sonia, and Laurence L. Brunton. "Separation of Cyclic GMP and Cyclic AMP." Analytical Biochemistry 235, no. 1 (March 1996): 102–3. http://dx.doi.org/10.1006/abio.1996.0097.

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12

Thakkar, Jayanti, Shu-Ben Tang, Nicholas Sperelakis, and Gordon M. Wahler. "Inhibition of cardiac slow action potentials by 8-bromo-cyclic GMP occurs independent of changes in cyclic AMP levels." Canadian Journal of Physiology and Pharmacology 66, no. 8 (August 1, 1988): 1092–95. http://dx.doi.org/10.1139/y88-178.

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Cyclic GMP inhibits the slow inward Ca current of cardiac cells. This effect could be due to a cyclic GMP-mediated phosphorylation of the Ca channel (or some protein modifying Ca channel activity), or alternatively, to enhanced degradation of cyclic AMP owing to stimulation of a phosphodiesterase by cyclic GMP. To test the latter possibility, we examined the effect of extracellular 8-bromo-cyclic GMP on cyclic AMP levels in guinea pig papillary muscles, in parallel with electrophysiological experiments. Isoproterenol (10−6 M) significantly increased the cyclic AMP levels and induced Ca-dependent slow action potentials. Superfusion with 8-bromo-cyclic GMP (10−3 M) inhibited the slow action potentials induced by isoproterenol. However, muscles superfused with 8-bromo-cyclic GMP had cyclic AMP levels identical to those of muscles superfused with isoproterenol alone. Similarly, 8-bromo-cyclic GMP had no effect on the increase in cyclic AMP levels of muscles treated with forskolin (10−6 M) or histamine (10−6 M). We conclude that the inhibitory effect of cyclic GMP on slow Ca channels in guinea pig ventricular cells is not due to a decrease in the cyclic AMP levels. We hypothesize that a cyclic GMP-mediated phosphorylation is the most likely explanation for the Ca channel inhibition observed in this preparation.

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13

Sagnella, G. A., N. D. Markandu, M. G. Buckley, D. R. J. Singer, and G. A. MacGregor. "Atrial Natriuretic Peptide-Cyclic Gmp Relationships in Normal Humans: Effects of Dietary Sodium Intake." Clinical Science 85, no. 1 (July 1, 1993): 13–17. http://dx.doi.org/10.1042/cs0850013.

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1. The present study was designed to investigate the relationships between circulating atrial natriuretic peptide, plasma and urinary cyclic GMP and sodium excretion under basal conditions and in response to changes in dietary sodium intake. 2. Measurements of plasma atrial natriuretic peptide and plasma and urinary (24 h collections) cyclic GMP, sodium and creatinine were made in (i) 30 normotensive subjects on their normal sodium intake and (ii) 12 subjects on the 5th day of a low and on the 5th day of a high sodium intake. 3. Plasma cyclic GMP, urinary cyclic GMP and fractional excretion of cyclic GMP in 30 normotensive subjects on their normal sodium intake were (means ± SEM) 5.4 ± 0.5 pmol/ml, 434.5 ± 31.8 pmol/min and 86.9 ± 8.6%, respectively. There were significant correlations between urinary cyclic GMP and its corresponding filtered load (r = 0.55) and between the renal clearance of cyclic GMP and that of creatinine (r = 0.44), but there were no significant associations between circulating atrial natriuretic peptide and plasma cyclic GMP or the fractional excretion of cyclic GMP or between urinary sodium and the fractional excretion of cyclic GMP. 5. Plasma atrial natriuretic peptide was significantly raised on the 5th day of the high sodium intake compared with the low sodium intake (10.6 ± 1.6 versus 4.2 ± 0.9 pg/ml; P <0.05). Similarly, there were increases in urinary cyclic GMP excretion (692.3 ± 43.4 versus 427.4 ± 41.9 pmol/min, P <0.05), but there were no significant differences in the fractional excretion of cyclic GMP. 6. As neither plasma nor urinary cyclic GMP was strongly associated with circulating levels of atrial natriuretic peptide, the present study suggests that other factors may be more important than circulating atrial natriuretic peptide as determinants of extracellular cyclic GMP.

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14

Light, Douglas B., Jackie D. Corbin, and Bruce A. Stanton. "Dual ion-channel regulation by cyclic GMP and cyclic GMP-dependent protein kinase." Nature 344, no. 6264 (March 1990): 336–39. http://dx.doi.org/10.1038/344336a0.

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15

Keller, Heiko, A. Katharina Weickhmann, Thomas Bock, and Jens Wöhnert. "Adenine protonation enables cyclic-di-GMP binding to cyclic-GAMP sensing riboswitches." RNA 24, no. 10 (July 13, 2018): 1390–402. http://dx.doi.org/10.1261/rna.067470.118.

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16

Newell, Peter C. "Signal transduction and motility of Dictyostelium." Bioscience Reports 15, no. 6 (December 1, 1995): 445–62. http://dx.doi.org/10.1007/bf01204348.

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This review is concerned with the roles of cyclic GMP and Ca2+ ions in signal transduction for chemotaxis of Dictyostelium. These molecules are involved in signalling between the cell surface cyclic AMP receptors and cytoskeletal myosin II involved in chemotactic cell movement. Evidence is presented for uptake and/or eflux of Ca2+ being regulated by cyclic GMP. The link between Ca2+, cyclic GMP and chemotactic cell movement has been explored using “streamer F” mutants whose primary defect is in the structural gene for the cyclic GMP-specific phosphodiesterase. This mutation causes the mutants to produce an abnormally prolonged peak of cyclic GMP accumulation in response to stimulation with the chemoattractant cyclic AMP. The production and relay of cyclic AMP signals is normal in these mutants, but certain events associated with movement are (like the cyclic GMP response) abnormally prolonged in the mutants. These events include Ca2+ uptake, myosin II association with the cytoskeleton and regulation of both myosin heavy and light chain phosphorylation. These changes can be correlated with changes in the shape of the amoebae after chemotactic stimulation. Other mutants in which the accumulation of cyclic GMP in response to cyclic AMP stimulation was absent produced no myosin II responses.A model is described in which cyclic GMP (directly or indirectly via Ca2+) regulates accumulation of myosin II on the cytoskeleton by regulating phosphorylation of the myosin heavy and light chain kinases.

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17

Wyatt, Todd. "Cyclic GMP and Cilia Motility." Cells 4, no. 3 (July 31, 2015): 315–30. http://dx.doi.org/10.3390/cells4030315.

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18

Stryer, L. "Cyclic GMP Cascade of Vision." Annual Review of Neuroscience 9, no. 1 (March 1986): 87–119. http://dx.doi.org/10.1146/annurev.ne.09.030186.000511.

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19

Krawutschke, Christian, Doris Koesling, and Michael Russwurm. "Cyclic GMP in Vascular Relaxation." Arteriosclerosis, Thrombosis, and Vascular Biology 35, no. 9 (September 2015): 2011–19. http://dx.doi.org/10.1161/atvbaha.115.306133.

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20

OPPENHEIM, RONALD W. "Cyclic GMP and neurone death." Nature 313, no. 5999 (January 1985): 248. http://dx.doi.org/10.1038/313248a0.

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21

Lolley, Richard N., and Rehwa H. Lee. "Cyclic GMP and photoreceptor function." FASEB Journal 4, no. 12 (September 1990): 3001–8. http://dx.doi.org/10.1096/fasebj.4.12.1697545.

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22

Lincoln, Thomas M., and Trudy L. Cornwell. "Intracellular cyclic GMP receptor proteins." FASEB Journal 7, no. 2 (February 1993): 328–38. http://dx.doi.org/10.1096/fasebj.7.2.7680013.

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23

Deschepper, Christian F. "Cardioprotective Actions of Cyclic GMP." Hypertension 55, no. 2 (February 2010): 453–58. http://dx.doi.org/10.1161/hypertensionaha.109.145235.

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24

Miller, W. H. "Cyclic GMP controls rod phototransduction." Neuroscience Research Supplements 2 (January 1985): S127—S132. http://dx.doi.org/10.1016/0921-8696(85)90012-x.

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25

Lewko, Barbara, and Jan Stepinski. "Cyclic GMP signaling in podocytes." Microscopy Research and Technique 57, no. 4 (May 7, 2002): 232–35. http://dx.doi.org/10.1002/jemt.10080.

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26

Frame, Mhairi J., Rothwelle Tate, David R. Adams, Keith M. Morgan, M. D. Houslay, Peter Vandenabeele, and Nigel J. Pyne. "Interaction of caspase-3 with the cyclic GMP binding cyclic GMP specific phosphodiesterase (PDE5a1)." European Journal of Biochemistry 270, no. 5 (September 10, 2003): 962–70. http://dx.doi.org/10.1046/j.1432-1033.2003.03464.x.

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27

Diamond, Jack, and Evelyn B. Chu. "A novel cyclic GMP-lowering agent, LY83583, blocks carbachol-indiiced cyclic GMP elevation in rabbit atrial strips without blocking the negative inotropic effects of carbachol." Canadian Journal of Physiology and Pharmacology 63, no. 8 (August 1, 1985): 908–11. http://dx.doi.org/10.1139/y85-150.

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A novel cyclic GMP-lowering agent, LY83583(6-anilino-5,8-quinolinedkme), was used to investigate the possibility that increases in myocardial cyclic GMP levels are responsible for the negative inotropic effects of cholinergic agonists. Concentrations of carbachol from 0.3 to 3 μM elevated cyclic GMP levels in electrically paced rabbit atrial strips by 75 to 200% and decreased contractile force in the strips by 30 to 60%. Pretreatment of the muscles for 10 min with 10 μM LY83583 significantly lowered resting cyclic GMP levels and completely blocked the elevation of cyclic GMP by these concentrations of carbachol. However, the negative inotropic effects of carbachol were not blocked by the LY83583. These results indicate that the negative inotropic effects of carbachol in rabbit atrium are not mediated by increases in tissue levels of cyclic GMP.

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28

Eckstein, Hans. "Evidence for Cyclic GMP in the Yeast Saccharomyces cerevisiae, and Studies on Its Possible Role in Growth." Zeitschrift für Naturforschung C 43, no. 5-6 (June 1, 1988): 386–96. http://dx.doi.org/10.1515/znc-1988-5-611.

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The yeast Saccharomyces cerevisiae is shown to be equipped with cyclic GMP, the level of which ranges from 6 pmol/109 cells with pressed baker’s yeast to 21 pmol/109 cells with exponentially growing cells. In extracts from synchronized growing yeast, cyclic GMP increases stepwise, being doubled at the time of each mitosis. Theophylline and 3-isobutyl-1-methylxanthine induce a rapid increase of cyclic GMP, followed by a premature formation of the septal cell wall between mother cell and bud. The effects of 3-isobutyl-1-methylxanthine are reversible. Dibutyryl-cyclic GMP, and, after a pronounced lag, also dibutyryl-cyclic AMP, induce a premature cell division, too. Cholera toxin induces premature cell divisions without a preceding increase in cyclic GMP. Neither theophylline nor 3-isobutyl-1-methylxanthine, cholera toxin or one of the dibutyryl-cyclic nucleotides modify the growth rate of the culture. None of the agents has significant effects on the level of cyclic AMP. The results suggest that cyclic GMP possibly controls an early step of mitosis, whereas ADP-ribosylation might govern a subsequent event.

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29

Rybtke, Morten T., Bradley R. Borlee, Keiji Murakami, Yasuhiko Irie, Morten Hentzer, Thomas E. Nielsen, Michael Givskov, Matthew R. Parsek, and Tim Tolker-Nielsen. "Fluorescence-Based Reporter for Gauging Cyclic Di-GMP Levels in Pseudomonas aeruginosa." Applied and Environmental Microbiology 78, no. 15 (May 11, 2012): 5060–69. http://dx.doi.org/10.1128/aem.00414-12.

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ABSTRACTThe increased tolerance toward the host immune system and antibiotics displayed by biofilm-formingPseudomonas aeruginosaand other bacteria in chronic infections such as cystic fibrosis bronchopneumonia is of major concern. Targeting of biofilm formation is believed to be a key aspect in the development of novel antipathogenic drugs that can augment the effect of classic antibiotics by decreasing antimicrobial tolerance. The second messenger cyclic di-GMP is a positive regulator of biofilm formation, and cyclic di-GMP signaling is now regarded as a potential target for the development of antipathogenic compounds. Here we describe the development of fluorescent monitors that can gauge the cellular level of cyclic di-GMP inP. aeruginosa. We have created cyclic di-GMP level reporters by transcriptionally fusing the cyclic di-GMP-responsivecdrApromoter to genes encoding green fluorescent protein. We show that the reporter constructs give a fluorescent readout of the intracellular level of cyclic di-GMP inP. aeruginosastrains with different levels of cyclic di-GMP. Furthermore, we show that the reporters are able to detect increased turnover of cyclic di-GMP mediated by treatment ofP. aeruginosawith the phosphodiesterase inducer nitric oxide. Considering that biofilm formation is a necessity for the subsequent development of a chronic infection and therefore a pathogenicity trait, the reporters display a significant potential for use in the identification of novel antipathogenic compounds targeting cyclic di-GMP signaling, as well as for use in research aiming at understanding the biofilm biology ofP. aeruginosa.

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30

Truman, J., J. Ewer, and E. Ball. "Dynamics of cyclic GMP levels in identified neurones during ecdysis behaviour in the locust Locusta migratoria." Journal of Experimental Biology 199, no. 4 (April 1, 1996): 749–58. http://dx.doi.org/10.1242/jeb.199.4.749.

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A grasshopper hatches from its egg, which is laid in soil, as a vermiform larva. This larva continues the stereotyped hatching behaviour as it digs through the egg pod, which provides a passageway to the soil surface. Once at the surface, shedding, or ecdysis, of the vermiform cuticle is initiated. When this process is complete, the first-instar cuticle is expanded to assume the form of the first-instar hopper. We have demonstrated, using immunocytochemical techniques, that these behaviour patterns are associated with dramatic increases in intracellular levels of cyclic GMP in sets of identified neurones in the ventral central nervous system. The most prominent cyclic-GMP-expressing cells are 34 neurones that appear to contain crustacean cardioactive peptide (CCAP). These CCAP cells show no detectable cyclic GMP at hatching or while the vermiform larva digs through the soil. Upon reaching the surface and freeing itself, the larva initiates ecdysis and associated air-swallowing and tracheal filling within about 1 min. These changes are immediately preceded by the appearance of cyclic GMP in the CCAP cells. Cyclic GMP levels in these neurones peak by 5 min and then decline back to basal levels by 20-30 min. Conditions that cause ecdysing animals to resume digging prolong the elevation of cyclic GMP levels. Once animals have assumed their 'hopper' form, however, external stimuli can no longer affect the time course of the cyclic GMP response. The neurones containing elevated cyclic GMP levels probably influence the air-swallowing, tracheal filling and circulatory changes that are associated with ecdysis behaviour. Pairs of descending midline neurones in abdominal segments 2-4 also become cyclic-GMP-immunoreactive, but they show peak expression after cyclic GMP levels in the CCAP cells have declined. Also, neurones in the caudolateral region of the abdominal ganglia often become cyclic-GMP-immunoreactive when ecdysing animals are forced to resume digging for an extended period.

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31

Diamond, Jack. "Effects of LY83583, nordihydroguaiaretic acid, and quinacrine on cyclic GMP elevation and inhibition of tension by muscarinic agonists in rabbit aorta and left atrium." Canadian Journal of Physiology and Pharmacology 65, no. 9 (September 1, 1987): 1913–17. http://dx.doi.org/10.1139/y87-297.

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Elevation of cyclic GMP by muscarinic agonists has been suggested to be responsible for the negative inotropic effects of these agents in cardiac muscle, and for the endothelium-dependent relaxation caused by these agents in vascular smooth muscle. These relationships were studied by monitoring the effects of muscarinic agonists on tension and cyclic GMP levels in rabbit left atrial strips and aortic rings, in the presence and absence of the cyclic GMP lowering agent, LY83583. LY83583 completely blocked both the cyclic GMP increase and the relaxation caused by acetylcholine in rabbit aortic rings with intact endothelial cells. Acetylcholine-induced cyclic GMP elevation and relaxation in these preparations were also blocked by quinacrine and nordihydroguaiaretic acid (NDGA), but neither response was blocked by the 5-lipoxygenase inhibitor U-60257. In the experiments with rabbit left atrium, LY83583 blocked the acetylcholine-induced cyclic GMP elevation but did not block the negative inotropic effects of the drug. Quinacrine, NDGA, and a guanylate cyclase inhibitor, methylene blue, failed to block either the cyclic GMP increase or the decrease in contractile force caused by carbachol in atrial strips. These results support the suggestion that an increase in cyclic GMP may be responsible for the endothelium-dependent relaxation of rabbit aorta by muscarinic agonists, but not for the direct negative inotropic effects of these drugs in rabbit atrium. Muscarinic agents appear to increase cyclic GMP levels in rabbit atrium and aorta by different mechanisms. Although both are blocked by LY83583, they differ not only in their requirements for endothelial cells, but also in their susceptibility to other blocking agents.

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32

Kumar, Vinod D., and Irene T. Weber. "Molecular model of the cyclic GMP-binding domain of the cyclic GMP-gated ion channel." Biochemistry 31, no. 19 (May 19, 1992): 4643–49. http://dx.doi.org/10.1021/bi00134a015.

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33

Epstein, Lynn, Richard C. Staples, and Harvey C. Hoch. "Cyclic AMP, cyclic GMP, and bean rust uredospore germlings." Experimental Mycology 13, no. 1 (March 1989): 100–104. http://dx.doi.org/10.1016/0147-5975(89)90013-3.

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34

Weiss, Harvey R., Gary X. Gong, Michaela Straznicka, Lin Yan, James Tse, and Peter M. Scholz. "Cyclic GMP and cyclic AMP induced changes in control and hypertrophic cardiac myocyte function interact through cyclic GMP affected cyclic-AMP phosphodiesterases." Canadian Journal of Physiology and Pharmacology 77, no. 6 (July 1, 1999): 422–31. http://dx.doi.org/10.1139/y99-039.

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We tested the hypothesis that the negative functional effects of cyclic GMP (cGMP) would be greater after increasing cyclic AMP (cAMP), because of the action of cGMP-affected cAMP phosphodiesterases in cardiac myocytes and that this effect would be altered in left ventricular hypertrophy (LVH) produced by aortic valve plication. Myocyte shortening data were collected using a video edge detector, and O2 consumption was measured by O2 electrodes during stimulation (5 ms, 1 Hz, in 2 mM Ca2+) from control (n = 7) and LVH (n = 7) dog ventricular myocytes. cAMP and cGMP were determined by a competitive binding assay. cAMP was increased by forskolin and milrinone (10-6 M). cGMP was increased with zaprinast and decreased by 1H-[1,2,4]oxadiazolo[4,3-a]quinoxilin-1-one (ODQ) both at 10-6 and 10-4 M, with and without forskolin or forskolin + milrinone. Zaprinast significantly decreased percent shortening in control (9 ± 1 to 7 ± 1%) and LVH (10 ± 1 to 7 ± 1%) myocytes. It increased cGMP in control (36 ± 5 to 52 ± 7 fmol/105 myocytes) and from the significantly higher baseline value in LVH (71 ± 12 to 104 ± 18 fmol/105 myocytes). ODQ increased myocyte function and decreased cGMP levels in control and LVH myocytes. Forskolin + milrinone increased cAMP levels in control (6 ± 1 to 15 ± 2 pmol/105 myocytes) and LVH (8 ± 1 to 18 ± 2 pmol/105 myocytes) myocytes, as did forskolin alone. They also significantly increased percent shortening. There were significant negative functional effects of zaprinast after forskolin + milrinone in control (15 ± 2 to 9 ± 1%), which were greater than zaprinast alone, and LVH (12 ± 1 to 9 ± 1%). This was associated with an increase in cGMP and a reduction in the increased cAMP induced by forskolin or milrinone. ODQ did not further increase function after forskolin or milrinone in control myocytes, despite lowering cGMP. However, it prevented the forskolin and milrinone induced increase in cAMP. In hypertrophy, ODQ lowered cGMP and increased function after forskolin. ODQ did not affect cAMP after forskolin and milrinone in LVH. Thus, the level of cGMP was inversely correlated with myocyte function. When cAMP levels were elevated, cGMP was still inversely correlated with myocyte function. This was, in part, related to alterations in cAMP. The interaction between cGMP and cAMP was altered in LVH myocytes.Key words: second messengers, cyclic AMP, cyclic GMP, cardiac myocyte function, cyclic GMP dependent cyclic-AMP phosphodiesterases, left ventricular hypertrophy, dog.

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35

Mukhopadhyay, A. K., M. Schumacher, and F. A. Leidenberger. "Steroidogenic effect of atrial natriuretic factor in isolated mouse Leydig cells is mediated by cyclic GMP." Biochemical Journal 239, no. 2 (October 15, 1986): 463–67. http://dx.doi.org/10.1042/bj2390463.

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The effects of different atrial natriuretic peptides on cyclic GMP formation and steroidogenesis have been studied in Percoll-purified mouse Leydig cells. Rat atrial peptides rANP (rat atrial natriuretic peptide), rAP-I (rat atriopeptin I) and rAP-II (rat atriopeptin II), in the presence of a phosphodiesterase inhibitor, stimulated cyclic GMP formation in a concentration-dependent manner. In the presence of saturating concentrations of the peptides, a 400-600 fold stimulation of cyclic GMP accumulation was observed. Among the peptides, rAP-II appeared to be the most potent. ED50 values (concentration causing half-maximal effect) for rAP-II, rANP and rAP-I were 1 × 10(-9) M, 2 × 10(-9) M and 2 × 10(-8) M respectively. A parallel stimulation of cyclic GMP formation and testosterone production by the cells was observed after incubation of the cells with various concentrations of rAP-II. In the presence of a saturating concentration of rAP-II (2 × 10(-8) M), maximum stimulation of intracellular cyclic GMP content was obtained within 5 min of incubation. Testosterone production by mouse Leydig cells could be stimulated by 8-bromo cyclic GMP in a concentration-related manner. At a 10 mM concentration of the cyclic nucleotide, steroidogenesis was stimulated to a similar extent as that obtained with a saturating concentration of human chorionic gonadotrophin (5 ng/ml). On the basis of these results we conclude that cyclic GMP acts as a second messenger in atrial-peptide-stimulated steroidogenesis in mouse Leydig cells. The steroidogenic effect of atrial peptides appears to be species-specific, since none of these peptides stimulated testosterone production by purified Leydig cells of rats, though in these cells a 40-60-fold stimulation of cyclic GMP formation in response to each of the three peptides was observed. However, 8-bromo cyclic GMP could stimulate testosterone production in rat Leydig cells. Therefore we conclude that the lack of steroidogenic response in rat Leydig cells to atrial-natriuretic-factor-stimulation results from an insufficient formation of cyclic GMP in these cells. This species difference would appear to result from a lower guanylate cyclase activity in rat Leydig cells.

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36

Lacey, Melissa M., Jonathan D. Partridge, and Jeffrey Green. "Escherichia coli K-12 YfgF is an anaerobic cyclic di-GMP phosphodiesterase with roles in cell surface remodelling and the oxidative stress response." Microbiology 156, no. 9 (September 1, 2010): 2873–86. http://dx.doi.org/10.1099/mic.0.037887-0.

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The Escherichia coli K-12 yfgF gene encodes a protein with domains associated with cyclic di-GMP signalling: GGDEF (associated with diguanylate cyclase activity) and EAL (associated with cyclic di-GMP phosphodiesterase activity). Here, it is shown that yfgF is expressed under anaerobic conditions from a class II FNR (regulator of fumarate and nitrate reduction)-dependent promoter. Anaerobic expression of yfgF is greatest in stationary phase, and in cultures grown at 28 °C, suggesting that low growth rates promote yfgF expression. Mutation of yfgF resulted in altered cell surface properties and enhanced sensitivity when anaerobic cultures were exposed to peroxides. The purified YfgF GGDEF-EAL (YfgFGE) and EAL (YfgFE) domains possessed cyclic di-GMP-specific phosphodiesterase activity, but lacked diguanylate cyclase activity. However, the catalytically inactive GGDEF domain was required for YfgFGE dimerization and enhanced cyclic di-GMP phosphodiesterase activity in the presence of physiological concentrations of Mg2+. The cyclic di-GMP phosphodiesterase activity of YfgFGE and YfgFE was inhibited by the product of the reaction, 5′-phosphoguanylyl-(3′–5′)-guanosine (pGpG). Thus, it is shown that the yfgF gene encodes an anaerobic cyclic di-GMP phosphodiesterase that is involved in remodelling the cell surface of E. coli K-12 and in the response to peroxide shock, with implications for integrating three global regulatory networks, i.e. oxygen regulation, cyclic di-GMP signalling and the oxidative stress response.

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37

Leitman, D. C., V. L. Agnost, J. J. Tuan, J. W. Andresen, and F. Murad. "Atrial natriuretic factor and sodium nitroprusside increase cyclic GMP in cultured rat lung fibroblasts by activating different forms of guanylate cyclase." Biochemical Journal 244, no. 1 (May 15, 1987): 69–74. http://dx.doi.org/10.1042/bj2440069.

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We used cultured rat lung fibroblasts to evaluate the role of particulate and soluble guanylate cyclase in the atrial natriuretic factor (ANF)-induced stimulation of cyclic GMP. ANF receptors were identified by binding of 125I-ANF to confluent cells at 37 degrees C. Specific ANF binding was rapid and saturable with increasing concentrations of ANF. The equilibrium dissociation constant (KD) was 0.66 +/- 0.077 nM and the Bmax. was 216 +/- 33 fmol bound/10(6) cells, which corresponds to 130,000 +/- 20,000 sites/cell. The molecular characteristics of ANF binding sites were examined by affinity cross-linking of 125I-ANF to intact cells with disuccinimidyl suberate. ANF specifically labelled two sites with molecular sizes of 66 and 130 kDa, which we have identified in other cultured cells. ANF and sodium nitroprusside produced a time- and concentration-dependent increase in intracellular cyclic GMP. An increase in cyclic GMP by ANF was detected at 1 nM, and at 100 nM an approx. 100-fold increase in cyclic GMP was observed. Nitroprusside stimulated cyclic GMP at 10 nM and at 1 mM a 500-600-fold increase in cyclic GMP occurred. The simultaneous addition of 100 nM-ANF and 10 microM-nitroprusside to cells resulted in cyclic GMP levels that were additive. ANF increased the activity of particulate guanylate cyclase by about 10-fold, but had no effect on soluble guanylate cyclase. In contrast, nitroprusside did not alter the activity of particulate guanylate cyclase, but increased the activity of soluble guanylate cyclase by 17-fold. These results demonstrate that rat lung fibroblasts contain ANF receptors and suggest that the ANF-induced stimulation of cyclic GMP is mediated entirely by particulate guanylate cyclase.

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38

Karaolis, David K. R., Mohammed H. Rashid, Rajanna Chythanya, Wensheng Luo, Mamoru Hyodo, and Yoshihiro Hayakawa. "c-di-GMP (3′-5′-Cyclic Diguanylic Acid) Inhibits Staphylococcus aureus Cell-Cell Interactions and Biofilm Formation." Antimicrobial Agents and Chemotherapy 49, no. 3 (March 2005): 1029–38. http://dx.doi.org/10.1128/aac.49.3.1029-1038.2005.

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ABSTRACT Staphylococcus aureus is an important pathogen of humans and animals, and antibiotic resistance is a public health concern. Biofilm formation is essential in virulence and pathogenesis, and the ability to resist antibiotic treatment results in difficult-to-treat and persistent infections. As such, novel antimicrobial approaches are of great interest to the scientific, medical, and agriculture communities. We recently proposed that modulating levels of the cyclic dinucleotide signaling molecule, c-di-GMP (cyclic diguanylate [3′,5′-cyclic diguanylic acid], cGpGp), has utility in regulating phenotypes of prokaryotes. We report that extracellular c-di-GMP shows activity against human clinical and bovine intramammary mastitis isolates of S. aureus, including methicillin-resistant S. aureus (MRSA) isolates. We show that chemically synthesized c-di-GMP is soluble and stable in water and physiological saline and stable following boiling and exposure to acid and alkali. Treatment of S. aureus with extracellular c-di-GMP inhibited cell-to-cell (intercellular) adhesive interactions in liquid medium and reduced (>50%) biofilm formation in human and bovine isolates compared to untreated controls. c-di-GMP inhibited the adherence of S. aureus to human epithelial HeLa cells. The cyclic nucleotide analogs cyclic GMP and cyclic AMP had a lesser inhibitory effect on biofilms, while 5′-GMP had no major effect. We propose that cyclic dinucleotides such as c-di-GMP, used either alone or in combination with other antimicrobial agents, represent a novel and attractive approach in the development of intervention strategies for the prevention of biofilms and the control and treatment of infection.

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39

Huggins, J. P., E. A. Cook, J. R. Piggott, T. J. Mattinsley, and P. J. England. "Phospholamban is a good substrate for cyclic GMP-dependent protein kinase in vitro, but not in intact cardiac or smooth muscle." Biochemical Journal 260, no. 3 (June 15, 1989): 829–35. http://dx.doi.org/10.1042/bj2600829.

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1. Cyclic GMP-dependent protein kinase phosphorylates purified phospholamban. It also phosphorylates phospholamban present in vesicles of cardiac sarcoplasmic reticulum and smooth muscle microsomal fractions, and in transformants of Escherichia coli which contain a plasmid into which a gene encoding phospholamban has been inserted. 2. In vitro the phospholamban present in cardiac sarcoplasmic reticulum membranes is a better substrate for cyclic GMP-dependent protein kinase than for cyclic AMP-dependent protein kinase. 3. Studies using [32P]Pi to label the cellular ATP in intact cardiac or smooth muscle failed to demonstrate that phosphorylation of phospholamban occurs in response to stimuli which increase intracellular cyclic GMP. Possible reasons for this functional separation between increased cyclic GMP and phosphorylation of phospholamban are discussed.

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40

Bonini, N. M., and D. L. Nelson. "Phosphoproteins associated with cyclic nucleotide stimulation of ciliary motility in Paramecium." Journal of Cell Science 95, no. 2 (February 1, 1990): 219–30. http://dx.doi.org/10.1242/jcs.95.2.219.

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Permeabilized, MgATP-reactivated cells of Paramecium (models) respond to cyclic AMP and cyclic GMP by increasing forward swimming speed. In association with the motile response, cyclic AMP and 8-bromo-cyclic GMP (8-Br-cyclic GMP) stimulated protein phosphorylation. Cyclic AMP addition to permeabilized cells reproducibly stimulated the phosphorylation of 10 proteins, ranging in molecular weight from 15 to 110K (K = 10(3) Mr). 8-Br-cyclic GMP, which selectively activates the cyclic GMP-dependent protein kinase of Paramecium, stimulated the phosphorylation of a subset of the proteins phosphorylated by cyclic AMP. Ca2+ addition caused backward swimming and stimulated the phosphorylation of four substrates, including a 25K target that may also be phosphorylated in response to cyclic nucleotide addition. Ba2+ and Sr2+ also induced backward swimming, but did not cause detectable phosphorylation. To identify ciliary targets of cyclic nucleotide-dependent protein kinase activity, permeabilized cells were deciliated following reactivation of motility with Mg-[gamma-32P]ATP in the presence or absence of cyclic nucleotide. Soluble proteins of the deciliation supernatant were enriched in 15 cyclic AMP-stimulated phosphoproteins, ranging in molecular weight from 15 to 95K. Most of the ciliary substrates were axonemal and could be released by high salt solution. A 29K protein that copurified in sucrose gradients with the 22S dynein, and a high molecular weight protein (greater than 300K) in the 19 S region were phosphorylated when cyclic AMP was added to permeabilized, motile cells. These data suggest that regulation of ciliary motility by cyclic AMP may include phosphorylation of dynein-associated proteins.

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41

PARISSENTI, A. M., and M. B. COUKELL. "Identification of a Nucleic Acid-Regulated Cyclic GMP-Binding Activity in Dictyostelium Discoideum." Journal of Cell Science 92, no. 2 (February 1, 1989): 291–301. http://dx.doi.org/10.1242/jcs.92.2.291.

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Using ion-exchange chromatography, we have identified and isolated two forms of a cyclic GMP-specific binding activity in filter-broken cell extracts of Dictyostelium discoideum. Upon addition of excess cold ligand, one form (S-type) released bound 3H-labelled cyclic GMP very slowly (t½ ≈ 68 min), while the other form (F-type) released the cyclic GMP in <1 min. After photoaffinity labelling with 32P-labelled cyclic GMP, both forms revealed a major 160x103Mr band (and a few bands of lower molecular weight) on autoradiograms of sodium dodecyl sulphate-polyacrylamide gels. Addition of 500 mM-NaCl to S-type activity converted the activity to a fast-dissociating form indistinguishable from F-type, and this conversion was reversed by dialysis. Salt treatment or dialysis had no appreciable effect on the association/dissociation kinetics of F-type activity. When crude S-type activity was heated (to destroy cyclic GMP binding) and then added to F-type activity, the latter activity acquired slow-dissociating properties identical to S-type. This result suggested that the cells possess a ‘factor’ that can dramatically alter binding properties of this cyclic GMP-binding protein. Crude preparations of this factor were by boiling or proteases, but were sensitive to RNase A. Further studies revealed that acids (in particular, DNA) could effectively mimic the factor in its ability to modulate the binding kinetics of the cyclic GMP-binding activity.

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42

Kuhn, Michaela. "It's cold, mom! It's cyclic GMP." EMBO Journal 34, no. 3 (January 2, 2015): 270–72. http://dx.doi.org/10.15252/embj.201490639.

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43

Forte, L. R., R. H. Freeman, W. J. Krause, and R. M. London. "Guanylin peptides: cyclic GMP signaling mechanisms." Brazilian Journal of Medical and Biological Research 32, no. 11 (November 1999): 1329–36. http://dx.doi.org/10.1590/s0100-879x1999001100002.

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44

MacFarland, R. Trevor. "Molecular Aspects of Cyclic GMP Signaling." Zoological Science 12, no. 2 (April 1995): 151–63. http://dx.doi.org/10.2108/zsj.12.151.

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45

Wang, Hsien-yu. "WNT-frizzled signaling via cyclic GMP." Frontiers in Bioscience 9, no. 1-3 (2004): 1043. http://dx.doi.org/10.2741/1310.

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46

McDonald, L. J., and F. Murad. "Nitric Oxide and Cyclic GMP Signaling." Experimental Biology and Medicine 211, no. 1 (January 1, 1996): 1–6. http://dx.doi.org/10.3181/00379727-211-43950a.

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47

WEILL, CHERYL L. "Cyclic GMP and neurone death (reply)." Nature 313, no. 5999 (January 1985): 248. http://dx.doi.org/10.1038/313248b0.

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48

Jenal, Urs, Alberto Reinders, and Christian Lori. "Cyclic di-GMP: second messenger extraordinaire." Nature Reviews Microbiology 15, no. 5 (February 6, 2017): 271–84. http://dx.doi.org/10.1038/nrmicro.2016.190.

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49

Somlyo, Avril V. "Cyclic GMP Regulation of Myosin Phosphatase." Circulation Research 101, no. 7 (September 28, 2007): 645–47. http://dx.doi.org/10.1161/circresaha.107.161893.

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50

Haddad, Elie, Roger A. Johns, and Thomas N. Pajewski. "Sevoflurane MAC and Cerebellar Cyclic GMP." Anesthesiology 90, no. 5 (May 1, 1999): 1487. http://dx.doi.org/10.1097/00000542-199905000-00038.

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Journal articles on the topic 'Cyclic GMP'

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