TY  - JOUR
AU  - Bošnjaković-Pavlović, Nada
AU  - Xu, Xiao
AU  - Krstić, Danijela Z.
AU  - Gillet, Jean-Michel
AU  - Wei, Yongge
AU  - Wu, Pingfan
AU  - Čolović, Mirjana B.
AU  - Spasojević-de Bire, Anne
PY  - 2019
UR  - https://linkinghub.elsevier.com/retrieve/pii/S0162013418306998
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/8355
AB  - The influence of three functionalized hexavanadates (V6): Na2 [V6O13{(OCH2)3CCH3}2], [H2]2 [V6O13{(OCH2)3CCH2OCOCH2CH3}2] and [(C4H9)4N]2 [V6O13{(OCH2)3CCH2OOC(CH3)2-COOH}2 on Na+/K+-ATPase activity, was investigated in vitro. Including compounds already tested by Xu et al. (Journal of Inorganic Biochemistry 161 (2016) 27–36), all functionalized hexavanadates inhibit the activity of Na+/K+-ATPase in a dose-dependent manner but with different inhibitory potencies. Na2 [V6O13{(OCH2)3CCH3}2] was found to have the best inhibition properties - showing 50% inhibition IC50 = 5.50 × 10−5 M, while [(C4H9)4N]2 [V6O13{(OCH2)3CCH2OOC(CH3)2-COOH}2] showed the lowest inhibitory power, IC50 = 1.31 × 10−4 M. In order to understand the bioactivity of functionalized hexavanadates series, we have also used a combined theoretical approach: determination of electrostatic potential from ab initio theoretical calculations and computation of the molecular interaction field (MIF) surface. © 2019
T2  - Journal of Inorganic Biochemistry
T1  - Experimental and theoretical insights of functionalized hexavanadates on Na+/K+-ATPase activity; molecular interaction field, ab initio calculations and in vitro assays
VL  - 198
SP  - 110720
DO  - 10.1016/j.jinorgbio.2019.110720
ER  - 

@article{
author = "Bošnjaković-Pavlović, Nada and Xu, Xiao and Krstić, Danijela Z. and Gillet, Jean-Michel and Wei, Yongge and Wu, Pingfan and Čolović, Mirjana B. and Spasojević-de Bire, Anne",
year = "2019",
abstract = "The influence of three functionalized hexavanadates (V6): Na2 [V6O13{(OCH2)3CCH3}2], [H2]2 [V6O13{(OCH2)3CCH2OCOCH2CH3}2] and [(C4H9)4N]2 [V6O13{(OCH2)3CCH2OOC(CH3)2-COOH}2 on Na+/K+-ATPase activity, was investigated in vitro. Including compounds already tested by Xu et al. (Journal of Inorganic Biochemistry 161 (2016) 27–36), all functionalized hexavanadates inhibit the activity of Na+/K+-ATPase in a dose-dependent manner but with different inhibitory potencies. Na2 [V6O13{(OCH2)3CCH3}2] was found to have the best inhibition properties - showing 50% inhibition IC50 = 5.50 × 10−5 M, while [(C4H9)4N]2 [V6O13{(OCH2)3CCH2OOC(CH3)2-COOH}2] showed the lowest inhibitory power, IC50 = 1.31 × 10−4 M. In order to understand the bioactivity of functionalized hexavanadates series, we have also used a combined theoretical approach: determination of electrostatic potential from ab initio theoretical calculations and computation of the molecular interaction field (MIF) surface. © 2019",
journal = "Journal of Inorganic Biochemistry",
title = "Experimental and theoretical insights of functionalized hexavanadates on Na+/K+-ATPase activity; molecular interaction field, ab initio calculations and in vitro assays",
volume = "198",
pages = "110720",
doi = "10.1016/j.jinorgbio.2019.110720"
}

Bošnjaković-Pavlović, N., Xu, X., Krstić, D. Z., Gillet, J., Wei, Y., Wu, P., Čolović, M. B.,& Spasojević-de Bire, A.. (2019). Experimental and theoretical insights of functionalized hexavanadates on Na+/K+-ATPase activity; molecular interaction field, ab initio calculations and in vitro assays. in Journal of Inorganic Biochemistry, 198, 110720.
https://doi.org/10.1016/j.jinorgbio.2019.110720

Bošnjaković-Pavlović N, Xu X, Krstić DZ, Gillet J, Wei Y, Wu P, Čolović MB, Spasojević-de Bire A. Experimental and theoretical insights of functionalized hexavanadates on Na+/K+-ATPase activity; molecular interaction field, ab initio calculations and in vitro assays. in Journal of Inorganic Biochemistry. 2019;198:110720.
doi:10.1016/j.jinorgbio.2019.110720 .

Bošnjaković-Pavlović, Nada, Xu, Xiao, Krstić, Danijela Z., Gillet, Jean-Michel, Wei, Yongge, Wu, Pingfan, Čolović, Mirjana B., Spasojević-de Bire, Anne, "Experimental and theoretical insights of functionalized hexavanadates on Na+/K+-ATPase activity; molecular interaction field, ab initio calculations and in vitro assays" in Journal of Inorganic Biochemistry, 198 (2019):110720,
https://doi.org/10.1016/j.jinorgbio.2019.110720 . .

TY  - JOUR
AU  - Xu, Xiao
AU  - Spasojević-de Bire, Anne
AU  - Ghermani, Nour Eddine
AU  - Wei, Yongge
AU  - Novaković, Slađana B.
AU  - Bošnjaković-Pavlović, Nada
AU  - Wu, Pingfan
PY  - 2017
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/1649
AB  - A high resolution X-ray diffraction study has been carried out on [(C4H9)(4)N](2) [V6O13{(OCH2)(3)CCH2OCCH2CH3}(2)] (V6-C3) at 100 K. The V6 core possesses a negative charge, leading to a strong polarization of the anion. A nucleophilic region localized near the organic moiety and an electrophilic region in the vicinity of the V6 core provide an overall description of charge-transfer behavior.
T2  - Physical Chemistry Chemical Physics
T1  - Experimental evidence of charge transfer in a functionalized hexavanadate: a high resolution X-ray diffraction study
VL  - 19
IS  - 28
SP  - 18162
EP  - 18166
DO  - 10.1039/c7cp01840a
ER  - 

@article{
author = "Xu, Xiao and Spasojević-de Bire, Anne and Ghermani, Nour Eddine and Wei, Yongge and Novaković, Slađana B. and Bošnjaković-Pavlović, Nada and Wu, Pingfan",
year = "2017",
abstract = "A high resolution X-ray diffraction study has been carried out on [(C4H9)(4)N](2) [V6O13{(OCH2)(3)CCH2OCCH2CH3}(2)] (V6-C3) at 100 K. The V6 core possesses a negative charge, leading to a strong polarization of the anion. A nucleophilic region localized near the organic moiety and an electrophilic region in the vicinity of the V6 core provide an overall description of charge-transfer behavior.",
journal = "Physical Chemistry Chemical Physics",
title = "Experimental evidence of charge transfer in a functionalized hexavanadate: a high resolution X-ray diffraction study",
volume = "19",
number = "28",
pages = "18162-18166",
doi = "10.1039/c7cp01840a"
}

Xu, X., Spasojević-de Bire, A., Ghermani, N. E., Wei, Y., Novaković, S. B., Bošnjaković-Pavlović, N.,& Wu, P.. (2017). Experimental evidence of charge transfer in a functionalized hexavanadate: a high resolution X-ray diffraction study. in Physical Chemistry Chemical Physics, 19(28), 18162-18166.
https://doi.org/10.1039/c7cp01840a

Xu X, Spasojević-de Bire A, Ghermani NE, Wei Y, Novaković SB, Bošnjaković-Pavlović N, Wu P. Experimental evidence of charge transfer in a functionalized hexavanadate: a high resolution X-ray diffraction study. in Physical Chemistry Chemical Physics. 2017;19(28):18162-18166.
doi:10.1039/c7cp01840a .

Xu, Xiao, Spasojević-de Bire, Anne, Ghermani, Nour Eddine, Wei, Yongge, Novaković, Slađana B., Bošnjaković-Pavlović, Nada, Wu, Pingfan, "Experimental evidence of charge transfer in a functionalized hexavanadate: a high resolution X-ray diffraction study" in Physical Chemistry Chemical Physics, 19, no. 28 (2017):18162-18166,
https://doi.org/10.1039/c7cp01840a . .

TY  - JOUR
AU  - Xu, Xiao
AU  - Bošnjaković-Pavlović, Nada
AU  - Čolović, Mirjana B.
AU  - Krstić, Danijela Z.
AU  - Vasić, Vesna M.
AU  - Gillet, Jean-Michel
AU  - Wu, Pingfan
AU  - Wei, Yongge
AU  - Spasojević-de Bire, Anne
PY  - 2016
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/1158
AB  - In vitro influence of five synthesized functionalized hexavanadates (V-6) on commercial porcine cerebral cortex Na+/K+-ATPase activity has been studied. Dose dependent Na+/K+-ATPase inhibition was obtained for all investigated compounds. Calculated half maximal inhibitory concentration IC50 values, in mol/L, for Na+/K+-ATPase were 7.6 x 10(-5), 1.8 x 10(-5), 2.9 x 10(-5), 5.5 x 10(-5) for functionalized hexavanadates (V-6) with tetrabutylammonium (TBA) [V-6-CH3][TBA](2), [V-6-NO2][TBA](2), [V-6-OH][TBA](2) and [V-6-C-3][TBA](2) respectively. [V-6-OH][Na](2) inhibited Na+/K+-ATPase activity up to 30% at maximal investigated concentration 1 x 10(-3) mol/L. This reactivity has been interpreted using a study of the non-covalent interactions of functionalized hexavanadate hybrids through Cambridge Structural Database (CSD) analysis. Bibliographic searching has led to 18 different structures and 99 contacts. We have observed that C-H center dot center dot center dot O contacts consolidate the structures. We have also performed density functional theory (DFT) calculations and have determined electrostatic potential values at the molecular surface on a series of functionalized V-6. These results enlightened their chemical reactivity and their potential biological applications such as the inhibition of the ATPase. (C) 2016 Elsevier Inc. All rights reserved.
T2  - Journal of Inorganic Biochemistry
T1  - A combined crystallographic analysis and ab initio calculations to interpret the reactivity of functionalized hexavanadates and their inhibitor potency toward Na+/K+-ATPase
VL  - 161
SP  - 27
EP  - 36
DO  - 10.1016/j.jinorgbio.2016.04.029
ER  - 

@article{
author = "Xu, Xiao and Bošnjaković-Pavlović, Nada and Čolović, Mirjana B. and Krstić, Danijela Z. and Vasić, Vesna M. and Gillet, Jean-Michel and Wu, Pingfan and Wei, Yongge and Spasojević-de Bire, Anne",
year = "2016",
abstract = "In vitro influence of five synthesized functionalized hexavanadates (V-6) on commercial porcine cerebral cortex Na+/K+-ATPase activity has been studied. Dose dependent Na+/K+-ATPase inhibition was obtained for all investigated compounds. Calculated half maximal inhibitory concentration IC50 values, in mol/L, for Na+/K+-ATPase were 7.6 x 10(-5), 1.8 x 10(-5), 2.9 x 10(-5), 5.5 x 10(-5) for functionalized hexavanadates (V-6) with tetrabutylammonium (TBA) [V-6-CH3][TBA](2), [V-6-NO2][TBA](2), [V-6-OH][TBA](2) and [V-6-C-3][TBA](2) respectively. [V-6-OH][Na](2) inhibited Na+/K+-ATPase activity up to 30% at maximal investigated concentration 1 x 10(-3) mol/L. This reactivity has been interpreted using a study of the non-covalent interactions of functionalized hexavanadate hybrids through Cambridge Structural Database (CSD) analysis. Bibliographic searching has led to 18 different structures and 99 contacts. We have observed that C-H center dot center dot center dot O contacts consolidate the structures. We have also performed density functional theory (DFT) calculations and have determined electrostatic potential values at the molecular surface on a series of functionalized V-6. These results enlightened their chemical reactivity and their potential biological applications such as the inhibition of the ATPase. (C) 2016 Elsevier Inc. All rights reserved.",
journal = "Journal of Inorganic Biochemistry",
title = "A combined crystallographic analysis and ab initio calculations to interpret the reactivity of functionalized hexavanadates and their inhibitor potency toward Na+/K+-ATPase",
volume = "161",
pages = "27-36",
doi = "10.1016/j.jinorgbio.2016.04.029"
}

Xu, X., Bošnjaković-Pavlović, N., Čolović, M. B., Krstić, D. Z., Vasić, V. M., Gillet, J., Wu, P., Wei, Y.,& Spasojević-de Bire, A.. (2016). A combined crystallographic analysis and ab initio calculations to interpret the reactivity of functionalized hexavanadates and their inhibitor potency toward Na+/K+-ATPase. in Journal of Inorganic Biochemistry, 161, 27-36.
https://doi.org/10.1016/j.jinorgbio.2016.04.029

Xu X, Bošnjaković-Pavlović N, Čolović MB, Krstić DZ, Vasić VM, Gillet J, Wu P, Wei Y, Spasojević-de Bire A. A combined crystallographic analysis and ab initio calculations to interpret the reactivity of functionalized hexavanadates and their inhibitor potency toward Na+/K+-ATPase. in Journal of Inorganic Biochemistry. 2016;161:27-36.
doi:10.1016/j.jinorgbio.2016.04.029 .

Xu, Xiao, Bošnjaković-Pavlović, Nada, Čolović, Mirjana B., Krstić, Danijela Z., Vasić, Vesna M., Gillet, Jean-Michel, Wu, Pingfan, Wei, Yongge, Spasojević-de Bire, Anne, "A combined crystallographic analysis and ab initio calculations to interpret the reactivity of functionalized hexavanadates and their inhibitor potency toward Na+/K+-ATPase" in Journal of Inorganic Biochemistry, 161 (2016):27-36,
https://doi.org/10.1016/j.jinorgbio.2016.04.029 . .

TY  - JOUR
AU  - Čolović, Mirjana B.
AU  - Bajuk-Bogdanović, Danica V.
AU  - Avramović, Nataša
AU  - Holclajtner-Antunović, Ivanka D.
AU  - Bošnjaković-Pavlović, Nada
AU  - Vasić, Vesna M.
AU  - Krstić, Danijela Z.
PY  - 2011
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/4558
AB  - C. The in vitro influence of Keggin structure polyoxotungstates, 12-tungstosilicic acid, H4SiW12O40 (WSiA) and 12-tungstophosphoric acid, H3PW12O40 (WPA), and monomer Na2WO4 x 2H(2)O on rat synaptic plasma membrane (SPM) Na+/K+-ATPase and E-NTPDase activity was studied, whereas the commercial porcine cerebral cortex Na+/K+-ATPase served as a reference. Dose-dependent Na+/K+-ATPase inhibition was obtained for all investigated compounds. Calculated IC50 (10 min) values, in mol/l, for SPM/commercial Na+/K+-ATPase, were: 3.4 x 10(-6)/4.3 x 10(-6), 2.9 x 10(-6)/3.1 x 10(-6) and 1.3 x 10(-3)/1.5 x 10(-3) for WSiA, WPA and Na2WO4 x 2H(2)O, respectively. In the case of E-NTPDase, increasing concentrations of WSiA and WPA induced its activity reduction, while Na2WO4 x 2H(2)O did not noticeably affect the enzyme activity at all investigated concentrations (up to 1 x 10(-3) mol/l). IC50 (10 min) values, obtained from the inhibition curves, were (in mol/l): 4.1 x 10(-6) for WSiA and 1.6 x 10(-6) for WPA. Monolacunary Keggin anion was found as the main active molecular species present under physiological conditions (in the enzyme assays, pH 7.4), for the both polyoxotungstates solutions (1 mmol/l), using Fourier transform infrared (FT-IR) and micro-Raman spectroscopy. Additionally, commercial porcine cerebral cortex Na+/K+-ATPase was exposed to the mixture of Na2WO4 x 2H(2)O and WSiA at different concentrations. Additive inhibition effect was achieved for lower concentrations of Na2WO4 x 2H(2)O/WSiA ( LT = 1 x 10(-3)/ 4 x 10(-6) mol/l), while antagonistic effect was obtained for all higher concentrations of the inhibitors. (C) 2011 Elsevier Ltd. All rights reserved.
T2  - Bioorganic and Medicinal Chemistry
T1  - Inhibition of rat synaptic membrane Na+/K+-ATPase and ecto-nucleoside triphosphate diphosphohydrolases by 12-tungstosilicic and 12-tungstophosphoric acid
VL  - 19
IS  - 23
SP  - 7063
EP  - 7069
DO  - 10.1016/j.bmc.2011.10.008
ER  - 

@article{
author = "Čolović, Mirjana B. and Bajuk-Bogdanović, Danica V. and Avramović, Nataša and Holclajtner-Antunović, Ivanka D. and Bošnjaković-Pavlović, Nada and Vasić, Vesna M. and Krstić, Danijela Z.",
year = "2011",
abstract = "C. The in vitro influence of Keggin structure polyoxotungstates, 12-tungstosilicic acid, H4SiW12O40 (WSiA) and 12-tungstophosphoric acid, H3PW12O40 (WPA), and monomer Na2WO4 x 2H(2)O on rat synaptic plasma membrane (SPM) Na+/K+-ATPase and E-NTPDase activity was studied, whereas the commercial porcine cerebral cortex Na+/K+-ATPase served as a reference. Dose-dependent Na+/K+-ATPase inhibition was obtained for all investigated compounds. Calculated IC50 (10 min) values, in mol/l, for SPM/commercial Na+/K+-ATPase, were: 3.4 x 10(-6)/4.3 x 10(-6), 2.9 x 10(-6)/3.1 x 10(-6) and 1.3 x 10(-3)/1.5 x 10(-3) for WSiA, WPA and Na2WO4 x 2H(2)O, respectively. In the case of E-NTPDase, increasing concentrations of WSiA and WPA induced its activity reduction, while Na2WO4 x 2H(2)O did not noticeably affect the enzyme activity at all investigated concentrations (up to 1 x 10(-3) mol/l). IC50 (10 min) values, obtained from the inhibition curves, were (in mol/l): 4.1 x 10(-6) for WSiA and 1.6 x 10(-6) for WPA. Monolacunary Keggin anion was found as the main active molecular species present under physiological conditions (in the enzyme assays, pH 7.4), for the both polyoxotungstates solutions (1 mmol/l), using Fourier transform infrared (FT-IR) and micro-Raman spectroscopy. Additionally, commercial porcine cerebral cortex Na+/K+-ATPase was exposed to the mixture of Na2WO4 x 2H(2)O and WSiA at different concentrations. Additive inhibition effect was achieved for lower concentrations of Na2WO4 x 2H(2)O/WSiA ( LT = 1 x 10(-3)/ 4 x 10(-6) mol/l), while antagonistic effect was obtained for all higher concentrations of the inhibitors. (C) 2011 Elsevier Ltd. All rights reserved.",
journal = "Bioorganic and Medicinal Chemistry",
title = "Inhibition of rat synaptic membrane Na+/K+-ATPase and ecto-nucleoside triphosphate diphosphohydrolases by 12-tungstosilicic and 12-tungstophosphoric acid",
volume = "19",
number = "23",
pages = "7063-7069",
doi = "10.1016/j.bmc.2011.10.008"
}

Čolović, M. B., Bajuk-Bogdanović, D. V., Avramović, N., Holclajtner-Antunović, I. D., Bošnjaković-Pavlović, N., Vasić, V. M.,& Krstić, D. Z.. (2011). Inhibition of rat synaptic membrane Na+/K+-ATPase and ecto-nucleoside triphosphate diphosphohydrolases by 12-tungstosilicic and 12-tungstophosphoric acid. in Bioorganic and Medicinal Chemistry, 19(23), 7063-7069.
https://doi.org/10.1016/j.bmc.2011.10.008

Čolović MB, Bajuk-Bogdanović DV, Avramović N, Holclajtner-Antunović ID, Bošnjaković-Pavlović N, Vasić VM, Krstić DZ. Inhibition of rat synaptic membrane Na+/K+-ATPase and ecto-nucleoside triphosphate diphosphohydrolases by 12-tungstosilicic and 12-tungstophosphoric acid. in Bioorganic and Medicinal Chemistry. 2011;19(23):7063-7069.
doi:10.1016/j.bmc.2011.10.008 .

Čolović, Mirjana B., Bajuk-Bogdanović, Danica V., Avramović, Nataša, Holclajtner-Antunović, Ivanka D., Bošnjaković-Pavlović, Nada, Vasić, Vesna M., Krstić, Danijela Z., "Inhibition of rat synaptic membrane Na+/K+-ATPase and ecto-nucleoside triphosphate diphosphohydrolases by 12-tungstosilicic and 12-tungstophosphoric acid" in Bioorganic and Medicinal Chemistry, 19, no. 23 (2011):7063-7069,
https://doi.org/10.1016/j.bmc.2011.10.008 . .

TY  - CONF
AU  - Krstić, Danijela Z.
AU  - Čolović, Mirjana B.
AU  - Bajuk-Bogdanović, Danica V.
AU  - Bošnjaković-Pavlović, Nada
AU  - Holclajtner-Antunović, Ivanka D.
AU  - Vasić, Vesna M.
PY  - 2010
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9317
AB  - The in vitro influence of 12-tungstosilicic acid (WSiA) and 12-tungstophosporic
acid (WPA) on Na+/K+_ATPase activity, using rat synaptic plasma membrane
(SPM) as a model system was investigated. The half-maximum inhibition (IC50) of
the enzyme activity was achieved with 5.80⋅ 10-5mol/L of WPA and 1.17⋅10-4
mol/L of WSiA. The both examined compounds showed a dose-dependent
inhibitory effect on the enzyme activity in the concentration higher than 1 μmol/L.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2010 : 10th international conference on fundamental and applied aspects of physical chemistry
T1  - Influence of heteropoly acids on rat synaptic plasma membrane atp -ase activity
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9317
ER  - 

@conference{
author = "Krstić, Danijela Z. and Čolović, Mirjana B. and Bajuk-Bogdanović, Danica V. and Bošnjaković-Pavlović, Nada and Holclajtner-Antunović, Ivanka D. and Vasić, Vesna M.",
year = "2010",
abstract = "The in vitro influence of 12-tungstosilicic acid (WSiA) and 12-tungstophosporic
acid (WPA) on Na+/K+_ATPase activity, using rat synaptic plasma membrane
(SPM) as a model system was investigated. The half-maximum inhibition (IC50) of
the enzyme activity was achieved with 5.80⋅ 10-5mol/L of WPA and 1.17⋅10-4
mol/L of WSiA. The both examined compounds showed a dose-dependent
inhibitory effect on the enzyme activity in the concentration higher than 1 μmol/L.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2010 : 10th international conference on fundamental and applied aspects of physical chemistry",
title = "Influence of heteropoly acids on rat synaptic plasma membrane atp -ase activity",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9317"
}

Krstić, D. Z., Čolović, M. B., Bajuk-Bogdanović, D. V., Bošnjaković-Pavlović, N., Holclajtner-Antunović, I. D.,& Vasić, V. M.. (2010). Influence of heteropoly acids on rat synaptic plasma membrane atp -ase activity. in Physical chemistry 2010 : 10th international conference on fundamental and applied aspects of physical chemistry
Society of Physical Chemists of Serbia..
https://hdl.handle.net/21.15107/rcub_vinar_9317

Krstić DZ, Čolović MB, Bajuk-Bogdanović DV, Bošnjaković-Pavlović N, Holclajtner-Antunović ID, Vasić VM. Influence of heteropoly acids on rat synaptic plasma membrane atp -ase activity. in Physical chemistry 2010 : 10th international conference on fundamental and applied aspects of physical chemistry. 2010;.
https://hdl.handle.net/21.15107/rcub_vinar_9317 .

Krstić, Danijela Z., Čolović, Mirjana B., Bajuk-Bogdanović, Danica V., Bošnjaković-Pavlović, Nada, Holclajtner-Antunović, Ivanka D., Vasić, Vesna M., "Influence of heteropoly acids on rat synaptic plasma membrane atp -ase activity" in Physical chemistry 2010 : 10th international conference on fundamental and applied aspects of physical chemistry (2010),
https://hdl.handle.net/21.15107/rcub_vinar_9317 .

TY  - JOUR
AU  - Krstić, Danijela Z.
AU  - Čolović, Mirjana B.
AU  - Bošnjaković-Pavlović, Nada
AU  - Spasojević-de Bire, Anne
AU  - Vasić, Vesna M.
PY  - 2009
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3840
AB  - The in vitro influence of decameric vanadate species on Na(+)/K(+)-ATPase, plasma membrane Ca(2+)-ATPase (PMCA)-calcium pump and ecto-ATPase activity, using rat synaptic plasma membrane (SPM) as model system was investigated, whereas the commercial porcine cerebral cortex Na(+)/K(+)-ATPase served as a reference. The thermal behaviour of the synthesized decavanadate (V(10)) has been studied by differential scanning calorimetry and thermogravimetric analysis, while the type of polyvanadate anion was identified using the IR spectroscopy. The concentration-dependent responses to V(10) of all enzymes were obtained. The half-maximum inhibitory concentration (IC(50)) of the enzyme activity was achieved at (4.74 +/- 1.15) x 10(-7) mol/l for SPM Na(+)/K(+)-ATPase, (1.30 +/- 0.10) x 10(-6) mol/l for commercial Na(+)/K(+)-ATPase and (3.13 +/- 1.70) x 10(-8) mol/l for Ca(2+)-ATPase, while ecto-ATPase is significantly less sensitive toward V(10) (IC(50) = (1.05 +/- 0.10) x 10(-4) mol/l) than investigated P-type ATPases. Kinetic analysis showed that V(10) inhibited Na(+)/K(+)-ATPase by reducing the maximum enzymatic velocity and apparent affinity for ATP (increasing K(m) value), implying a mixed mode of interaction between V(10) and P-type ATPases.
T2  - General Physiology and Biophysics
T1  - Influence of decavanadate on rat synaptic plasma membrane ATPases activity
VL  - 28
IS  - 3
SP  - 302
EP  - 308
DO  - 10.4149/gpb_2009_03_302
ER  - 

@article{
author = "Krstić, Danijela Z. and Čolović, Mirjana B. and Bošnjaković-Pavlović, Nada and Spasojević-de Bire, Anne and Vasić, Vesna M.",
year = "2009",
abstract = "The in vitro influence of decameric vanadate species on Na(+)/K(+)-ATPase, plasma membrane Ca(2+)-ATPase (PMCA)-calcium pump and ecto-ATPase activity, using rat synaptic plasma membrane (SPM) as model system was investigated, whereas the commercial porcine cerebral cortex Na(+)/K(+)-ATPase served as a reference. The thermal behaviour of the synthesized decavanadate (V(10)) has been studied by differential scanning calorimetry and thermogravimetric analysis, while the type of polyvanadate anion was identified using the IR spectroscopy. The concentration-dependent responses to V(10) of all enzymes were obtained. The half-maximum inhibitory concentration (IC(50)) of the enzyme activity was achieved at (4.74 +/- 1.15) x 10(-7) mol/l for SPM Na(+)/K(+)-ATPase, (1.30 +/- 0.10) x 10(-6) mol/l for commercial Na(+)/K(+)-ATPase and (3.13 +/- 1.70) x 10(-8) mol/l for Ca(2+)-ATPase, while ecto-ATPase is significantly less sensitive toward V(10) (IC(50) = (1.05 +/- 0.10) x 10(-4) mol/l) than investigated P-type ATPases. Kinetic analysis showed that V(10) inhibited Na(+)/K(+)-ATPase by reducing the maximum enzymatic velocity and apparent affinity for ATP (increasing K(m) value), implying a mixed mode of interaction between V(10) and P-type ATPases.",
journal = "General Physiology and Biophysics",
title = "Influence of decavanadate on rat synaptic plasma membrane ATPases activity",
volume = "28",
number = "3",
pages = "302-308",
doi = "10.4149/gpb_2009_03_302"
}

Krstić, D. Z., Čolović, M. B., Bošnjaković-Pavlović, N., Spasojević-de Bire, A.,& Vasić, V. M.. (2009). Influence of decavanadate on rat synaptic plasma membrane ATPases activity. in General Physiology and Biophysics, 28(3), 302-308.
https://doi.org/10.4149/gpb_2009_03_302

Krstić DZ, Čolović MB, Bošnjaković-Pavlović N, Spasojević-de Bire A, Vasić VM. Influence of decavanadate on rat synaptic plasma membrane ATPases activity. in General Physiology and Biophysics. 2009;28(3):302-308.
doi:10.4149/gpb_2009_03_302 .

Krstić, Danijela Z., Čolović, Mirjana B., Bošnjaković-Pavlović, Nada, Spasojević-de Bire, Anne, Vasić, Vesna M., "Influence of decavanadate on rat synaptic plasma membrane ATPases activity" in General Physiology and Biophysics, 28, no. 3 (2009):302-308,
https://doi.org/10.4149/gpb_2009_03_302 . .

TY  - CONF
AU  - Krstić, Danijela Z.
AU  - Čolović, Mirjana B.
AU  - Bošnjaković-Pavlović, Nada
AU  - Spasojević-de Bire, Anne
AU  - Vasić, Vesna M.
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9369
AB  - The in vitro influence of decameric vanadate species on Na+/K+_ATPase, plasma membrane Ca2+-ATPase (PMCA)-calcium pump and ecto-ATPase activity, using rat synaptic plasma membrane (SPM) as a model system was investigated. The concentration-dependent responses to decavanadate of these enzymes were obtained. The half-maximum inhibition (IC50) of the enzyme activity was achieved at (4.74 ± 1.15) x 10-7mol/l for Na+/K+_ATPase and (3.13 ± 1.70) x 10-8 mol/l for Ca2+-ATPase, while ecto-ATPase is significantly less sensitive toward decavanadate (IC50- (1.05 ± 0.10) x 10-4 mol/l) than investigated P-type ATPases.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry
T1  - Influence of decavanadate on rat synaptic plasma membrane atpases activity
VL  - 1
SP  - 363
EP  - 365
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9369
ER  - 

@conference{
author = "Krstić, Danijela Z. and Čolović, Mirjana B. and Bošnjaković-Pavlović, Nada and Spasojević-de Bire, Anne and Vasić, Vesna M.",
year = "2008",
abstract = "The in vitro influence of decameric vanadate species on Na+/K+_ATPase, plasma membrane Ca2+-ATPase (PMCA)-calcium pump and ecto-ATPase activity, using rat synaptic plasma membrane (SPM) as a model system was investigated. The concentration-dependent responses to decavanadate of these enzymes were obtained. The half-maximum inhibition (IC50) of the enzyme activity was achieved at (4.74 ± 1.15) x 10-7mol/l for Na+/K+_ATPase and (3.13 ± 1.70) x 10-8 mol/l for Ca2+-ATPase, while ecto-ATPase is significantly less sensitive toward decavanadate (IC50- (1.05 ± 0.10) x 10-4 mol/l) than investigated P-type ATPases.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry",
title = "Influence of decavanadate on rat synaptic plasma membrane atpases activity",
volume = "1",
pages = "363-365",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9369"
}

Krstić, D. Z., Čolović, M. B., Bošnjaković-Pavlović, N., Spasojević-de Bire, A.,& Vasić, V. M.. (2008). Influence of decavanadate on rat synaptic plasma membrane atpases activity. in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry
Society of Physical Chemists of Serbia., 1, 363-365.
https://hdl.handle.net/21.15107/rcub_vinar_9369

Krstić DZ, Čolović MB, Bošnjaković-Pavlović N, Spasojević-de Bire A, Vasić VM. Influence of decavanadate on rat synaptic plasma membrane atpases activity. in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry. 2008;1:363-365.
https://hdl.handle.net/21.15107/rcub_vinar_9369 .

Krstić, Danijela Z., Čolović, Mirjana B., Bošnjaković-Pavlović, Nada, Spasojević-de Bire, Anne, Vasić, Vesna M., "Influence of decavanadate on rat synaptic plasma membrane atpases activity" in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry, 1 (2008):363-365,
https://hdl.handle.net/21.15107/rcub_vinar_9369 .

TY  - CONF
AU  - Bošnjaković-Pavlović, Nada
AU  - Ghermani, Nour Eddine
AU  - Spasojević-de Bire, Anne
AU  - Bogdanović, Goran A.
AU  - Mioč, Ubavka B.
PY  - 2004
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9575
AB  - The X-ray structure of ammonium decavanadate hexahydrate, (NH4)6V10O28·6H2O, was redetermined at low temperature (100 K) in order to locate the hydrogen sites. A kappa refinement was performed to estimate the experimental atomic charges. Comparisons with previous theoretical calculation results were discussed.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry
T1  - Crystal structure redetermination and atomic charges of ammonium decavanadate hexahydrate based on a low temperature x-ray experiment
VL  - 2
SP  - 544
EP  - 546
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9575
ER  - 

@conference{
author = "Bošnjaković-Pavlović, Nada and Ghermani, Nour Eddine and Spasojević-de Bire, Anne and Bogdanović, Goran A. and Mioč, Ubavka B.",
year = "2004",
abstract = "The X-ray structure of ammonium decavanadate hexahydrate, (NH4)6V10O28·6H2O, was redetermined at low temperature (100 K) in order to locate the hydrogen sites. A kappa refinement was performed to estimate the experimental atomic charges. Comparisons with previous theoretical calculation results were discussed.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry",
title = "Crystal structure redetermination and atomic charges of ammonium decavanadate hexahydrate based on a low temperature x-ray experiment",
volume = "2",
pages = "544-546",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9575"
}

Bošnjaković-Pavlović, N., Ghermani, N. E., Spasojević-de Bire, A., Bogdanović, G. A.,& Mioč, U. B.. (2004). Crystal structure redetermination and atomic charges of ammonium decavanadate hexahydrate based on a low temperature x-ray experiment. in Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry
Society of Physical Chemists of Serbia., 2, 544-546.
https://hdl.handle.net/21.15107/rcub_vinar_9575

Bošnjaković-Pavlović N, Ghermani NE, Spasojević-de Bire A, Bogdanović GA, Mioč UB. Crystal structure redetermination and atomic charges of ammonium decavanadate hexahydrate based on a low temperature x-ray experiment. in Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry. 2004;2:544-546.
https://hdl.handle.net/21.15107/rcub_vinar_9575 .

Bošnjaković-Pavlović, Nada, Ghermani, Nour Eddine, Spasojević-de Bire, Anne, Bogdanović, Goran A., Mioč, Ubavka B., "Crystal structure redetermination and atomic charges of ammonium decavanadate hexahydrate based on a low temperature x-ray experiment" in Physical chemistry 2004: 7th international conference on fundemental and applied aspract of physical chemistry, 2 (2004):544-546,
https://hdl.handle.net/21.15107/rcub_vinar_9575 .