| Name | calmodulin |
|---|---|
| Synonyms | CALM; CAM; CALM 1; CALM 2; CALM 3; CALM1; CALM2; CALM3… |
| Name | anthraquinone |
|---|---|
| CAS | 9,10-anthracenedione |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 2155616 | Matsuda Y, Nakanishi S, Nagasawa K, Kase H: Inhibition by new anthraquinone compounds, K-259-2 and KS-619-1, of calmodulin-dependent cyclic nucleotide phosphodiesterase. Biochem Pharmacol. 1990 Mar 1;39(5):841-9. K-259-2 and KS-619-1, novel anionic anthraquinone metabolites isolated from culture broth of microorganisms, inhibited activation of bovine brain phosphodiesterase induced by calmodulin (CaM), or limited proteolysis with almost equal potency. |
113(1,2,2,3) | Details |
| 3680022 | Matsuda Y, Kase H: KS-619-1, a new inhibitor of Ca2+ and calmodulin-dependent cyclic nucleotide phosphodiesterase from Streptomyces californicus. J Antibiot. 1987 Aug;40(8):1104-10. KS-619-1 has an anthraquinone moiety. |
4(0,0,0,4) | Details |
| 3680021 | Yasuzawa T, Yoshida M, Shirahata K, Sano H: Structure of a novel Ca2+ and calmodulin-dependent cyclic nucleotide phosphodiesterase inhibitor K-259-2. J Antibiot. 1987 Aug;40(8):1101-3. The structure of K-259-2, a potent inhibitor of Ca2+ and calmodulin-dependent cyclic nucleotide phosphodiesterase, was determined to be 3-(2Z-2-ethyl-2-butenyl)-1,6,8-trihydroxy-anthraquinone-2-carboxyl ic acid by chemical conversion and spectral studies. |
32(0,1,1,2) | Details |
| 3680020 | Matsuda Y, Asano K, Kawamoto I, Kase H: K-259-2, a new inhibitor of Ca2+ and calmodulin-dependent cyclic nucleotide phosphodiesterase from Micromonospora olivasterospora. J Antibiot. 1987 Aug;40(8):1092-100. K-259-2 has an anthraquinone moiety in its structure. |
4(0,0,0,4) | Details |
| 1466788 | Jinsart W, Ternai B, Polya GM: Inhibition of myosin light chain kinase, cAMP-dependent protein kinase, protein kinase C and of plant Ca (2+)-dependent protein kinase by anthraquinones. Biol Chem Hoppe Seyler. 1992 Sep;373(9):903-10. A variety of anthraquinone (anthracene-9,10-dione) derivatives inhibits rat brain Ca (2+)- and phospholipid-activated protein kinase C (PKC) of which the most potent inhibitors are mitoxantrone (1,4-dihydroxy-5,8-bis [2-(hydroxyethylamino)-ethylamino]-9,10- anthracenedione) (IC50 4 microM) and quinalizarin (1,2,5,8-tetrahydroxy-anthraquinone (IC50 4 microM). Ca (2+)-calmodulin-dependent myosin light chain kinase (MLCK) is inhibited by a range of di-, tri- and tetrahydroxylated anthraquinones (IC50 values 2 to 53 microM), the most potent inhibitors being the more polar compounds, namely mitoxantrone (IC50 2 microM) and emodin (1,3,8-trihydroxy-6-methylanthraquinone) (IC50 8 microM). |
2(0,0,0,2) | Details |
| 16386736 | Zhang HL, Tang ZY, Yang JX, Zhang Y, Li Y, Lin Y: Bi-directional regulation of emodin and on smooth muscle myosin of gizzard. FEBS Lett. 2006 Jan 23;580(2):469-73. Epub 2005 Dec 22. This study is to reveal the characteristics of bidirectional regulation of emodin (1,3,8-trihydroxy-6-methyl-anthraquinone) and on gizzard smooth muscle myosin. Our results indicate that: (a) emodin demonstrates stimulatory effects, and produces inhibitory effects on myosin phosphorylation and Mg (2+)-ATPase activities of Ca (2+)/calmodulin-dependent phosphorylated myosin in a dose-dependent manner; (b) a combination of emodin and enhances phosphorylation and Mg (2+)-ATPase activities for partially phosphorylated myosin and inhibits those activities for fully phosphorylated myosin; (c) 1-(5-Chloronaphthalene-1-sulfonyl)-1H2-hexahydro-1,4-diazepine inhibits myosin phosphorylation in the presence of emodin and/or |
1(0,0,0,1) | Details |
| 9625728 | Kumagai Y, Nakajima H, Midorikawa K, Homma-Takeda S, Shimojo N: Inhibition of formation by neuronal synthase by quinones: synthase as a quinone reductase. Chem Res Toxicol. 1998 Jun;11(6):608-13. Reductase activity of PQ by purified nNOS required CaCl2/calmodulin and was markedly suppressed by the flavoprotein inhibitor diphenyleneiodonium but not by l-nitroarginine which is a specific inhibitor for NO formation. nNOS effectively reduced the quinones as well as PQ causing a marked decrease in the production of NO from while 1, 4- 9,10-anthraquinone, mitomycin C, and lapachol, which show negligible inhibitory action on nNOS activity, were poor substrates for the enzyme on reduction. |
0(0,0,0,0) | Details |