منابع مشابه
Recent advances into vanadyl, vanadate and decavanadate interactions with actin.
Although the number of papers about "vanadium" has doubled in the last decade, the studies about "vanadium and actin" are scarce. In the present review, the effects of vanadyl, vanadate and decavanadate on actin structure and function are compared. Decavanadate (51)V NMR signals, at -516 ppm, broadened and decreased in intensity upon actin titration, whereas no effects were observed for vanadat...
متن کاملTemplated polymerizations on solid supports mediated by complementary nucleoside interactions†
Template-directed radical polymerizations on solid supports are presented, which take advantage of complementary nucleoside interactions in non-polar solvents. The templates are prepared through copper-mediated living radical polymerization allowing control over the length and dispersity of the polymer bound to the support. We report a degree of control over subsequent polymerization of a compl...
متن کاملPharmacokinetic drug interactions with non-nucleoside reverse transcriptase inhibitors.
Non-nucleoside reverse transcriptase inhibitors (NNRTIs) are a diverse group of compounds that inhibit HIV Type 1 reverse transcriptase. Although possessing a common mechanism of action, the approved NNRTIs, delavirdine, efavirenz and nevirapine, differ in structural and pharmacokinetic characteristics. Each of the NNRTIs undergoes biotransformation by the cytochrome P450 (CYP) enzyme system, t...
متن کاملEffect of sodium vanadate
Platelet-activating factor (1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine, AGEPC) and sodium vanadate (a phosphotyrosine phosphatase inhibitor) induced a timeand concentration-dependent increase in phosphotyrosine in several proteins and stimulated prostaglandin (PG) E2 production in cultured rat Kupffer cells. In addition, vanadate induced a decrease in the surface expression of AGEPC recepto...
متن کاملA characterization of vanadate interactions with the (Na,K)-ATPase. Mechanistic and regulatory implications.
The interaction of vanadium in the +5 oxidation state (vanadate) with purified dog kidney Na+ and K+-stimulated adenosine trlphosphatase [(Na,K)-ATPase] has been studied using equilibrium binding, steady state kinetics, and measurements of relaxation kinetics. Vanadate binds to one high affinity site (Kl = 4 no) and one low afinity site (Kz = 0.5 pM) per enzyme molecule (Le. per ouabain binding...
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ژورنال
عنوان ژورنال: Acta Chemica Scandinavica
سال: 1992
ISSN: 0904-213X
DOI: 10.3891/acta.chem.scand.46-1170