High impact information on Purealin

• These results suggest that purealin modulates the ATPase activities of dephosphorylated gizzard myosin by enhancing the stability of myosin filaments against the disassembling action of ATP [1].
• Purealin and some of the analogues inhibited the microtubule-stimulated ATPase activity of recombinant cytoplasmic dynein heavy chain motor domain [2].
• Synthesis and biological evaluation of purealin and analogues as cytoplasmic dynein heavy chain inhibitors [2].
• Purealin, a novel bioactive principle of a sea sponge Psammaplysilla purea, blocked the motility of Triton-demembranated sea urchin sperm flagella within 5 min at concentrations above 20 microM [3].
• The calmodulin-stimulated phosphodiesterase activity was inhibited by purealin (IC50, 7 microM) at concentrations very close to those that inhibit myosin phosphorylation [4].

Biological context of Purealin

• The mechanism of inhibition of light-chain phosphorylation by purealin in chicken gizzard myosin [4].
• Some modulators of the function of myosin (purealin, etc.) and actin (goniodomin A, etc.) have been demonstrated to be important chemical probes for understanding the physiological roles of the contractile proteins in structural changes and their interaction in muscle contraction [5].

Anatomical context of Purealin

• In contrast, purealin had little effect on the ATPase activities of phosphorylated gizzard myosin [1].
• Purealin, a novel stabilizer of smooth muscle myosin filaments that modulates ATPase activity of dephosphorylated myosin [1].
• Purealin, a novel activator of skeletal muscle actomyosin ATPase and myosin EDTA-ATPase that enhanced the superprecipitation of actomyosin [6].
• Enhancement of the actin-activated ATPase activity of myosin from canine cardiac ventricle by purealin [7].

Gene context of Purealin

• Taken together, our results suggest that purealin-sensitive ATPase activity of the dynein arms plays an essential role in generating the sliding movement of flagellar axonemes [3].
• Purealin inhibited the phosphorylation of myosin light chains caused by MLCK and calmodulin (IC50, 5 microM) [4].

Analytical, diagnostic and therapeutic context of Purealin

• Upon ultracentrifugation, dephosphorylated myosin sedimented as two components, the 10 S species and myosin filaments, in the solution containing 0.18 M KCl and 1 mM Mg X ATP in the presence of 60 microM purealin [1].

References