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Filtros: Autor is Aureliano, Manuel  [Clear All Filters]
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Ramos S, Moura JJG, Aureliano M. Actin as a potential target for decavanadate. J Inorg Biochem. 2010;104(12):1234-9. doi:10.1016/j.jinorgbio.2010.08.001
Tiago T, Martel P, Gutiérrez-Merino C, Aureliano M. Binding modes of decavanadate to myosin and inhibition of the actomyosin ATPase activity. Biochim Biophys Acta. 2007;1774(4):474-80. doi:10.1016/j.bbapap.2007.02.004
Fraqueza G, de Carvalho LAEBatist, M Marques PM, et al. Decavanadate, decaniobate, tungstate and molybdate interactions with sarcoplasmic reticulum Ca(2+)-ATPase: quercetin prevents cysteine oxidation by vanadate but does not reverse ATPase inhibition. Dalton Trans. 2012;41(41):12749-58. doi:10.1039/c2dt31688a
Ramos S, Duarte RO, Moura JJG, Aureliano M. Decavanadate interactions with actin: cysteine oxidation and vanadyl formation. Dalton Trans. 2009;(38):7985-94. doi:10.1039/b906255f
Ramos S, Manuel M, Tiago T, et al. Decavanadate interactions with actin: Inhibition of G-actin polymerization and stabilization of decameric vanadate. Journal of Inorganic Biochemistry. 2006;100(11):1734 - 1743. doi:10.1016/j.jinorgbio.2006.06.007
Aureliano M, Crans DC. Decavanadate (V10 O28 6-) and oxovanadates: oxometalates with many biological activities. J Inorg Biochem. 2009;103(4):536-46. doi:10.1016/j.jinorgbio.2008.11.010
Tiago T, Marques-da-Silva D, Samhan-Arias AK, Aureliano M, Gutiérrez-Merino C. Early disruption of the actin cytoskeleton in cultured cerebellar granule neurons exposed to 3-morpholinosydnonimine-oxidative stress is linked to alterations of the cytosolic calcium concentration. Cell Calcium. 2011;49(3):174-83. doi:10.1016/j.ceca.2011.01.009
Matos E, Silva TS, Tiago T, Aureliano M, Dinis MTeresa, Dias J. Effect of harvesting stress and storage conditions on protein degradation in fillets of farmed gilthead seabream (Sparus aurata): A differential scanning calorimetry study. Food Chemistry. 2011;126(1):270 - 276. doi:10.1016/j.foodchem.2010.11.017
Pereira MJoão, Carvalho E, Eriksson JW, Crans DC, Aureliano M. Effects of decavanadate and insulin enhancing vanadium compounds on glucose uptake in isolated rat adipocytes. J Inorg Biochem. 2009;103(12):1687-92. doi:10.1016/j.jinorgbio.2009.09.015
Pereira MJ, Palming J, Rizell M, et al. The immunosuppressive agents rapamycin, cyclosporin A and tacrolimus increase lipolysis, inhibit lipid storage and alter expression of genes involved in lipid metabolism in human adipose tissue. Mol Cell Endocrinol. 2013;365(2):260-9. doi:10.1016/j.mce.2012.10.030
Tiago DM, Laizé V, M. Cancela L, Aureliano M. Impairment of mineralization by metavanadate and decavanadate solutions in a fish bone-derived cell line. Cell Biol Toxicol. 2008;24(3):253-63. doi:10.1007/s10565-007-9034-x
Ramos S, Almeida RM, Moura JJG, Aureliano M. Implications of oxidovanadium(IV) binding to actin. J Inorg Biochem. 2011;105(6):777-83. doi:10.1016/j.jinorgbio.2011.02.010
Fraqueza G, Fuentes J, Krivosudský L, et al. Inhibition of Na+/K+- and Ca2+-ATPase activities by phosphotetradecavanadate. Journal of Inorganic Biochemistry. 2019;197:110700. doi:10.1016/j.jinorgbio.2019.110700
Aureliano M, Fraqueza G, C Ohlin A. Ion pumps as biological targets for decavanadate. Dalton Trans. 2013;42(33):11770-7. doi:10.1039/c3dt50462j
Pereira MJ, Palming J, Rizell M, et al. mTOR inhibition with rapamycin causes impaired insulin signalling and glucose uptake in human subcutaneous and omental adipocytes. Mol Cell Endocrinol. 2012;355(1):96-105. doi:10.1016/j.mce.2012.01.024
Laizé V, Tiago DM, Aureliano M, M. Cancela L. New insights into mineralogenic effects of vanadate. Cell Mol Life Sci. 2009;66(24):3831-6. doi:10.1007/s00018-009-0137-9
Tiago T, Ramos S, Aureliano M, Gutiérrez-Merino C. Peroxynitrite induces F-actin depolymerization and blockade of myosin ATPase stimulation. Biochem Biophys Res Commun. 2006;342(1):44-9. doi:10.1016/j.bbrc.2006.01.112
Tiago T, Palma PS, Gutiérrez-Merino C, Aureliano M. Peroxynitrite-mediated oxidative modifications of myosin and implications on structure and function. Free Radic Res. 2010;44(11):1317-27. doi:10.3109/10715762.2010.502170
Gumerova N, Krivosudský L, Fraqueza G, et al. The P-type ATPase inhibiting potential of polyoxotungstates. Metallomics. 2018;10(2):287 - 295. doi:10.1039/C7MT00279C
Fraqueza G, C Ohlin A, Casey WH, Aureliano M. Sarcoplasmic reticulum calcium ATPase interactions with decaniobate, decavanadate, vanadate, tungstate and molybdate. J Inorg Biochem. 2012;107(1):82-9. doi:10.1016/j.jinorgbio.2011.10.010
Aureliano M, Henao F, Tiago T, et al. Sarcoplasmic reticulum calcium ATPase is inhibited by organic vanadium coordination compounds: pyridine-2,6-dicarboxylatodioxovanadium(V), BMOV, and an amavadine analogue. Inorg Chem. 2008;47(13):5677-84. doi:10.1021/ic702405d
Soares SSofia, Henao F, Aureliano M, Gutiérrez-Merino C. Vanadate induces necrotic death in neonatal rat cardiomyocytes through mitochondrial membrane depolarization. Chem Res Toxicol. 2008;21(3):607-18. doi:10.1021/tx700204r
Tiago DM, M. Cancela L, Aureliano M, Laizé V. Vanadate proliferative and anti-mineralogenic effects are mediated by MAPK and PI-3K/Ras/Erk pathways in a fish chondrocyte cell line. FEBS Lett. 2008;582(9):1381-5. doi:10.1016/j.febslet.2008.03.025