TY  - JOUR
AU  - Sevaljevic, L
AU  - Isenović, Esma R.
AU  - Vulović, Mojca D.
AU  - Mačvanin, Mirjana
AU  - Žakula, Zorica
AU  - Kanazir, Dušan T.
AU  - Ribarac-Stepić, Nevena B.
PY  - 2001
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2450
AB  - The responses of liver glucocorticoid receptor (GR) and genes coding for a glucocorticoid-inducible tyrosine aminotransferase (TAT) and two acute-phase proteins (APP) [alpha (2)-macroglobulin (alpha (2)-M) and gamma -fibrinogen (Fb)] to changes in glucocorticoid (GC) and proinflammatory (AP) cytokine contents have been examined in rats after single or combined treatments with turpentine oil, dexamethasone (Dex) and adrenalectomy. Activation of two APP genes in turpentine-induced inflammation was accompanied by an increase in the level of GR mRNA and a preferential translocation of GR-GC complexes to the nucleoplasm, while the expression of TAT remained unaltered. Dex alone caused a decrease in the levels of GR and Fb mRNAs, activation of TAT and alpha (2)-M genes, a decrease in the affinity of hormone binding sites and redistribution of translocated GR-Dex complexes within the nuclei. Inflammation potentiated the effect which Dex alone exerted on the GIR content and the number of GR binding sites but counteracted its influence on the affinity of GR binding sites and nuclear distribution of GR-Dex complexes.
T2  - Biological Signals and Receptors
T1  - The responses of rat liver glucocorticoid receptors and genes for tyrosine aminotransferase, alpha-2-macroglobulin and gamma-fibrinogen to adrenalectomy-, dexamethasone- and inflammation-induced changes in the levels of glucocorticoids and proinflammatory cytokines
VL  - 10
IS  - 5
SP  - 299
EP  - 309
UR  - https://hdl.handle.net/21.15107/rcub_vinar_2450
ER  - 

@article{
author = "Sevaljevic, L and Isenović, Esma R. and Vulović, Mojca D. and Mačvanin, Mirjana and Žakula, Zorica and Kanazir, Dušan T. and Ribarac-Stepić, Nevena B.",
year = "2001",
abstract = "The responses of liver glucocorticoid receptor (GR) and genes coding for a glucocorticoid-inducible tyrosine aminotransferase (TAT) and two acute-phase proteins (APP) [alpha (2)-macroglobulin (alpha (2)-M) and gamma -fibrinogen (Fb)] to changes in glucocorticoid (GC) and proinflammatory (AP) cytokine contents have been examined in rats after single or combined treatments with turpentine oil, dexamethasone (Dex) and adrenalectomy. Activation of two APP genes in turpentine-induced inflammation was accompanied by an increase in the level of GR mRNA and a preferential translocation of GR-GC complexes to the nucleoplasm, while the expression of TAT remained unaltered. Dex alone caused a decrease in the levels of GR and Fb mRNAs, activation of TAT and alpha (2)-M genes, a decrease in the affinity of hormone binding sites and redistribution of translocated GR-Dex complexes within the nuclei. Inflammation potentiated the effect which Dex alone exerted on the GIR content and the number of GR binding sites but counteracted its influence on the affinity of GR binding sites and nuclear distribution of GR-Dex complexes.",
journal = "Biological Signals and Receptors",
title = "The responses of rat liver glucocorticoid receptors and genes for tyrosine aminotransferase, alpha-2-macroglobulin and gamma-fibrinogen to adrenalectomy-, dexamethasone- and inflammation-induced changes in the levels of glucocorticoids and proinflammatory cytokines",
volume = "10",
number = "5",
pages = "299-309",
url = "https://hdl.handle.net/21.15107/rcub_vinar_2450"
}

Sevaljevic, L., Isenović, E. R., Vulović, M. D., Mačvanin, M., Žakula, Z., Kanazir, D. T.,& Ribarac-Stepić, N. B.. (2001). The responses of rat liver glucocorticoid receptors and genes for tyrosine aminotransferase, alpha-2-macroglobulin and gamma-fibrinogen to adrenalectomy-, dexamethasone- and inflammation-induced changes in the levels of glucocorticoids and proinflammatory cytokines. in Biological Signals and Receptors, 10(5), 299-309.
https://hdl.handle.net/21.15107/rcub_vinar_2450

Sevaljevic L, Isenović ER, Vulović MD, Mačvanin M, Žakula Z, Kanazir DT, Ribarac-Stepić NB. The responses of rat liver glucocorticoid receptors and genes for tyrosine aminotransferase, alpha-2-macroglobulin and gamma-fibrinogen to adrenalectomy-, dexamethasone- and inflammation-induced changes in the levels of glucocorticoids and proinflammatory cytokines. in Biological Signals and Receptors. 2001;10(5):299-309.
https://hdl.handle.net/21.15107/rcub_vinar_2450 .

Sevaljevic, L, Isenović, Esma R., Vulović, Mojca D., Mačvanin, Mirjana, Žakula, Zorica, Kanazir, Dušan T., Ribarac-Stepić, Nevena B., "The responses of rat liver glucocorticoid receptors and genes for tyrosine aminotransferase, alpha-2-macroglobulin and gamma-fibrinogen to adrenalectomy-, dexamethasone- and inflammation-induced changes in the levels of glucocorticoids and proinflammatory cytokines" in Biological Signals and Receptors, 10, no. 5 (2001):299-309,
https://hdl.handle.net/21.15107/rcub_vinar_2450 .

TY  - JOUR
AU  - Banjac, Ana
AU  - Nedeljković, N.
AU  - Horvat, Anica
AU  - Kanazir, Dušan T.
AU  - Nikezić, Gordana S.
PY  - 2001
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2455
AB  - An ontogenetic study of ecto-ATPase activity and the content of enzyme proteins was assessed in the caudate nucleus and hippocampal synaptic plasma membranes isolated from rats at various ages (15, 30, 90, 180 and 365 days). The ontogenetic profile revealed that the enzyme activities in both brain areas were the highest on day 30 and 365, while the ecto-ATPase protein abundance was the highest on day 15 after birth. Possible explanation for obtained ontogenetic profile and the discrepancy between activity and abundance may reside in the fact that ecto-ATPase during development could exert additional roles other than those related to metabolism of ATP. It is likely that ecto-ATPase, regulating the concentration of ATP and adenosine in synaptic cleft, has important role in the processes of brain development and aging.
T2  - Physiological Research
T1  - Ontogenetic profile of ecto-ATPase activity in rat hippocampal and caudate nucleus synaptic plasma membrane fractions
VL  - 50
IS  - 4
SP  - 411
EP  - 417
UR  - https://hdl.handle.net/21.15107/rcub_vinar_2455
ER  - 

@article{
author = "Banjac, Ana and Nedeljković, N. and Horvat, Anica and Kanazir, Dušan T. and Nikezić, Gordana S.",
year = "2001",
abstract = "An ontogenetic study of ecto-ATPase activity and the content of enzyme proteins was assessed in the caudate nucleus and hippocampal synaptic plasma membranes isolated from rats at various ages (15, 30, 90, 180 and 365 days). The ontogenetic profile revealed that the enzyme activities in both brain areas were the highest on day 30 and 365, while the ecto-ATPase protein abundance was the highest on day 15 after birth. Possible explanation for obtained ontogenetic profile and the discrepancy between activity and abundance may reside in the fact that ecto-ATPase during development could exert additional roles other than those related to metabolism of ATP. It is likely that ecto-ATPase, regulating the concentration of ATP and adenosine in synaptic cleft, has important role in the processes of brain development and aging.",
journal = "Physiological Research",
title = "Ontogenetic profile of ecto-ATPase activity in rat hippocampal and caudate nucleus synaptic plasma membrane fractions",
volume = "50",
number = "4",
pages = "411-417",
url = "https://hdl.handle.net/21.15107/rcub_vinar_2455"
}

Banjac, A., Nedeljković, N., Horvat, A., Kanazir, D. T.,& Nikezić, G. S.. (2001). Ontogenetic profile of ecto-ATPase activity in rat hippocampal and caudate nucleus synaptic plasma membrane fractions. in Physiological Research, 50(4), 411-417.
https://hdl.handle.net/21.15107/rcub_vinar_2455

Banjac A, Nedeljković N, Horvat A, Kanazir DT, Nikezić GS. Ontogenetic profile of ecto-ATPase activity in rat hippocampal and caudate nucleus synaptic plasma membrane fractions. in Physiological Research. 2001;50(4):411-417.
https://hdl.handle.net/21.15107/rcub_vinar_2455 .

Banjac, Ana, Nedeljković, N., Horvat, Anica, Kanazir, Dušan T., Nikezić, Gordana S., "Ontogenetic profile of ecto-ATPase activity in rat hippocampal and caudate nucleus synaptic plasma membrane fractions" in Physiological Research, 50, no. 4 (2001):411-417,
https://hdl.handle.net/21.15107/rcub_vinar_2455 .

TY  - JOUR
AU  - Nikezić, Gordana S.
AU  - Horvat, Anica
AU  - Nedeljković, N.
AU  - Todorović, S.
AU  - Nikolić, Vladimir M.
AU  - Kanazir, Dušan T.
AU  - Vujisić Lj.
AU  - Kopečni Miroslav
PY  - 1998
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2146
AB  - The neurotoxicity of pyridine and urea was investigated in respect to their ability to alter the activity of synaptosomal membrane Na+/K+-ATPase and Mg2+-ATPase. In vitro treatment with pyridine and urea stimulated Na+/K+-ATPase activity in a dose-dependent manner up to 40% and 60%, respectively. Mg2+-ATPase activity increased up to 40% after pyridine treatment, while urea had no effect at all. The neuroactive potencies of pyridine and urea were evaluated by estimating parameters K-m and Delta V-max for enzyme stimulation, as well as Hill coefficient to estimate the levels of cooperativity for pyridine and urea binding. The results suggest that pyridine stimulates both enzymes, probably by interacting with some neuronal membrane components, and altering the lipid micro-environment of the ATPases. In contrast, urea stimulates the Na+/K+-ATPase only, assumingly by acting on it directly or via some other regulatory mechanism. Stimulation of Na+/K+-ATPase and Mg2+-ATPase by the substances tested and subsequent alteration of neuronal cell functioning could contribute to the CNS dysfunction upon chronic exposure to pyridine and urea.
T2  - General Physiology and Biophysics
T1  - Influence of pyridine and urea on the rat brain ATPase activity
VL  - 17
IS  - 1
SP  - 15
EP  - 23
UR  - https://hdl.handle.net/21.15107/rcub_vinar_2146
ER  - 

@article{
author = "Nikezić, Gordana S. and Horvat, Anica and Nedeljković, N. and Todorović, S. and Nikolić, Vladimir M. and Kanazir, Dušan T. and Vujisić Lj. and Kopečni Miroslav",
year = "1998",
abstract = "The neurotoxicity of pyridine and urea was investigated in respect to their ability to alter the activity of synaptosomal membrane Na+/K+-ATPase and Mg2+-ATPase. In vitro treatment with pyridine and urea stimulated Na+/K+-ATPase activity in a dose-dependent manner up to 40% and 60%, respectively. Mg2+-ATPase activity increased up to 40% after pyridine treatment, while urea had no effect at all. The neuroactive potencies of pyridine and urea were evaluated by estimating parameters K-m and Delta V-max for enzyme stimulation, as well as Hill coefficient to estimate the levels of cooperativity for pyridine and urea binding. The results suggest that pyridine stimulates both enzymes, probably by interacting with some neuronal membrane components, and altering the lipid micro-environment of the ATPases. In contrast, urea stimulates the Na+/K+-ATPase only, assumingly by acting on it directly or via some other regulatory mechanism. Stimulation of Na+/K+-ATPase and Mg2+-ATPase by the substances tested and subsequent alteration of neuronal cell functioning could contribute to the CNS dysfunction upon chronic exposure to pyridine and urea.",
journal = "General Physiology and Biophysics",
title = "Influence of pyridine and urea on the rat brain ATPase activity",
volume = "17",
number = "1",
pages = "15-23",
url = "https://hdl.handle.net/21.15107/rcub_vinar_2146"
}

Nikezić, G. S., Horvat, A., Nedeljković, N., Todorović, S., Nikolić, V. M., Kanazir, D. T., Vujisić Lj.,& Kopečni Miroslav. (1998). Influence of pyridine and urea on the rat brain ATPase activity. in General Physiology and Biophysics, 17(1), 15-23.
https://hdl.handle.net/21.15107/rcub_vinar_2146

Nikezić GS, Horvat A, Nedeljković N, Todorović S, Nikolić VM, Kanazir DT, Vujisić Lj., Kopečni Miroslav. Influence of pyridine and urea on the rat brain ATPase activity. in General Physiology and Biophysics. 1998;17(1):15-23.
https://hdl.handle.net/21.15107/rcub_vinar_2146 .

Nikezić, Gordana S., Horvat, Anica, Nedeljković, N., Todorović, S., Nikolić, Vladimir M., Kanazir, Dušan T., Vujisić Lj., Kopečni Miroslav, "Influence of pyridine and urea on the rat brain ATPase activity" in General Physiology and Biophysics, 17, no. 1 (1998):15-23,
https://hdl.handle.net/21.15107/rcub_vinar_2146 .

TY  - JOUR
AU  - Počuča, Nataša
AU  - Ruždijić, Sabera
AU  - Demonacos, Constantinos
AU  - Kanazir, Dušan T.
AU  - Krstić-Demonacos, Marija
PY  - 1998
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2188
AB  - The glucocorticoid receptor (GR) is a phosphoprotein and a member of the steroid/thyroid receptor superfamily of ligand dependent transcription factors. When the glucocorticoid receptor is expressed in yeast (Saccharomyces cerevisiae), it is competent for signal transduction and transcriptional regulation. We have studied the glucocorticoid receptor phosphorylation in yeast and demonstrated that the receptor is phosphorylated in both the absence and presence of hormone, on serine and threonine residues. This phosphorylation occurs within 15 min upon addition of radioactivity in both hormone treated and untreated cells. As reported for mammalian cells, additional phosphorylation occurs upon hormone binding and this phosphorylation is dependent on the type of the ligand. We have followed the hormone dependent receptor phosphorylation by electrophoretic mobility shift assay, and have shown that this mobility change is sensitive to phosphatase treatment. In addition, the appearance of hormone dependent phosphoisoforms of the receptor depends on the potency of the agonist used. Using this method we show that the residues contributing to the hormone dependent mobility shift are localized in one of the transcriptional activation domains, between amino acids 130-247. We altered the phosphorylation sites within this domain that correspond to the amino acids phosphorylated in mouse hormone treated cells. Using phosphopeptide maps we show that hormone changes the peptide pattern of metabolically labelled receptor, and we identify peptides which are phosphorylated in hormone dependent manner. Then we determine that phosphorylation of residues S224 and S232 is increased in the presence of hormone, whereas phosphorylation of residues T171 and S246 is constitutive. Finally, we show that in both yeast and mammalian cells the same residues on the glucocorticoid receptor are phosphorylated. Our results suggest that yeast cells would be a suitable system to study glucocorticoid receptor phosphorylation. The genetic manipulability of yeast cells, together with conservation of the phosphorylation of GR in yeast and mammalian cells and identification of hormone dependent phosphorylation, would facilitate the isolation of molecules involved in the glucocorticoid receptor phosphorylation pathway and further our understanding of this process. (C) 1998 Elsevier Science Ltd. All rights reserved.
T2  - Journal of Steroid Biochemistry and Molecular Biology
T1  - Using yeast to study glucocorticoid receptor phosphorylation
VL  - 66
IS  - 5-6
SP  - 303
EP  - 318
DO  - 10.1016/S0960-0760(98)00057-0
ER  - 

@article{
author = "Počuča, Nataša and Ruždijić, Sabera and Demonacos, Constantinos and Kanazir, Dušan T. and Krstić-Demonacos, Marija",
year = "1998",
abstract = "The glucocorticoid receptor (GR) is a phosphoprotein and a member of the steroid/thyroid receptor superfamily of ligand dependent transcription factors. When the glucocorticoid receptor is expressed in yeast (Saccharomyces cerevisiae), it is competent for signal transduction and transcriptional regulation. We have studied the glucocorticoid receptor phosphorylation in yeast and demonstrated that the receptor is phosphorylated in both the absence and presence of hormone, on serine and threonine residues. This phosphorylation occurs within 15 min upon addition of radioactivity in both hormone treated and untreated cells. As reported for mammalian cells, additional phosphorylation occurs upon hormone binding and this phosphorylation is dependent on the type of the ligand. We have followed the hormone dependent receptor phosphorylation by electrophoretic mobility shift assay, and have shown that this mobility change is sensitive to phosphatase treatment. In addition, the appearance of hormone dependent phosphoisoforms of the receptor depends on the potency of the agonist used. Using this method we show that the residues contributing to the hormone dependent mobility shift are localized in one of the transcriptional activation domains, between amino acids 130-247. We altered the phosphorylation sites within this domain that correspond to the amino acids phosphorylated in mouse hormone treated cells. Using phosphopeptide maps we show that hormone changes the peptide pattern of metabolically labelled receptor, and we identify peptides which are phosphorylated in hormone dependent manner. Then we determine that phosphorylation of residues S224 and S232 is increased in the presence of hormone, whereas phosphorylation of residues T171 and S246 is constitutive. Finally, we show that in both yeast and mammalian cells the same residues on the glucocorticoid receptor are phosphorylated. Our results suggest that yeast cells would be a suitable system to study glucocorticoid receptor phosphorylation. The genetic manipulability of yeast cells, together with conservation of the phosphorylation of GR in yeast and mammalian cells and identification of hormone dependent phosphorylation, would facilitate the isolation of molecules involved in the glucocorticoid receptor phosphorylation pathway and further our understanding of this process. (C) 1998 Elsevier Science Ltd. All rights reserved.",
journal = "Journal of Steroid Biochemistry and Molecular Biology",
title = "Using yeast to study glucocorticoid receptor phosphorylation",
volume = "66",
number = "5-6",
pages = "303-318",
doi = "10.1016/S0960-0760(98)00057-0"
}

Počuča, N., Ruždijić, S., Demonacos, C., Kanazir, D. T.,& Krstić-Demonacos, M.. (1998). Using yeast to study glucocorticoid receptor phosphorylation. in Journal of Steroid Biochemistry and Molecular Biology, 66(5-6), 303-318.
https://doi.org/10.1016/S0960-0760(98)00057-0

Počuča N, Ruždijić S, Demonacos C, Kanazir DT, Krstić-Demonacos M. Using yeast to study glucocorticoid receptor phosphorylation. in Journal of Steroid Biochemistry and Molecular Biology. 1998;66(5-6):303-318.
doi:10.1016/S0960-0760(98)00057-0 .

Počuča, Nataša, Ruždijić, Sabera, Demonacos, Constantinos, Kanazir, Dušan T., Krstić-Demonacos, Marija, "Using yeast to study glucocorticoid receptor phosphorylation" in Journal of Steroid Biochemistry and Molecular Biology, 66, no. 5-6 (1998):303-318,
https://doi.org/10.1016/S0960-0760(98)00057-0 . .

TY  - JOUR
AU  - Nikezić, Gordana S.
AU  - Nedeljković, N.
AU  - Horvat, Anica
AU  - Kanazir, Dušan T.
AU  - Martinović, Jelena
PY  - 1997
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2108
AB  - Membrane vesicles loaded with [Na+], prepared from synaptosomal plasma membranes (SPM) of whole brains (WE), hippocampi (Hip) and caudate nuclei (NC) of female rats, were used to study Na+-dependent Ca2+ transport across SPM vesicles under the influence of 17 beta-estradiol (E-2) in vitro. In concentrations near to physiologic, E-2 significantly increased Ca-45(2+) uptake by SPM vesicles from all the brain tissues investigated. The maximum increase was observed for WE (21%) and Hip (33%) at 10(-9) mol/l, and for NC (31%) at 5 x 10(-9) mol/l of E-2. These results (a) confirm our earlier finding that E, in vitro modulates Na+-dependent Ca2+ transport across synaptosomal membrane in rat brain regions, and (b) suggest Na+/Ca2+ exchange as principal mechanism of the E-2-stimulated Na+-dependent Ca2+ uptake by membrane vesicles. The involvement of any ATPases as possible mediators is discussed. (C) 1997, Editrice Kurtis.
T2  - Journal of Endocrinological Investigation
T1  - Estradiol in vitro modulates Na+-dependent Ca2+ uptake by synaptic plasma membrane vesicles of rat brain regions
VL  - 20
IS  - 11
SP  - 664
EP  - 668
DO  - 10.1007/BF03348028
ER  - 

@article{
author = "Nikezić, Gordana S. and Nedeljković, N. and Horvat, Anica and Kanazir, Dušan T. and Martinović, Jelena",
year = "1997",
abstract = "Membrane vesicles loaded with [Na+], prepared from synaptosomal plasma membranes (SPM) of whole brains (WE), hippocampi (Hip) and caudate nuclei (NC) of female rats, were used to study Na+-dependent Ca2+ transport across SPM vesicles under the influence of 17 beta-estradiol (E-2) in vitro. In concentrations near to physiologic, E-2 significantly increased Ca-45(2+) uptake by SPM vesicles from all the brain tissues investigated. The maximum increase was observed for WE (21%) and Hip (33%) at 10(-9) mol/l, and for NC (31%) at 5 x 10(-9) mol/l of E-2. These results (a) confirm our earlier finding that E, in vitro modulates Na+-dependent Ca2+ transport across synaptosomal membrane in rat brain regions, and (b) suggest Na+/Ca2+ exchange as principal mechanism of the E-2-stimulated Na+-dependent Ca2+ uptake by membrane vesicles. The involvement of any ATPases as possible mediators is discussed. (C) 1997, Editrice Kurtis.",
journal = "Journal of Endocrinological Investigation",
title = "Estradiol in vitro modulates Na+-dependent Ca2+ uptake by synaptic plasma membrane vesicles of rat brain regions",
volume = "20",
number = "11",
pages = "664-668",
doi = "10.1007/BF03348028"
}

Nikezić, G. S., Nedeljković, N., Horvat, A., Kanazir, D. T.,& Martinović, J.. (1997). Estradiol in vitro modulates Na+-dependent Ca2+ uptake by synaptic plasma membrane vesicles of rat brain regions. in Journal of Endocrinological Investigation, 20(11), 664-668.
https://doi.org/10.1007/BF03348028

Nikezić GS, Nedeljković N, Horvat A, Kanazir DT, Martinović J. Estradiol in vitro modulates Na+-dependent Ca2+ uptake by synaptic plasma membrane vesicles of rat brain regions. in Journal of Endocrinological Investigation. 1997;20(11):664-668.
doi:10.1007/BF03348028 .

Nikezić, Gordana S., Nedeljković, N., Horvat, Anica, Kanazir, Dušan T., Martinović, Jelena, "Estradiol in vitro modulates Na+-dependent Ca2+ uptake by synaptic plasma membrane vesicles of rat brain regions" in Journal of Endocrinological Investigation, 20, no. 11 (1997):664-668,
https://doi.org/10.1007/BF03348028 . .

TY  - JOUR
AU  - Ristić-Fira, Aleksandra
AU  - Đorđević Marković, R.
AU  - Radojčić, Marija
AU  - Ribarac-Stepić, Nevena B.
AU  - Kanazir, Dušan T.
PY  - 1996
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/2031
T2  - Jugoslovenska Medicinska Biohemija
T1  - Glucocorticoid effects on B16/F10 and B16/C3 mouse melanoma cell growth
VL  - 15
IS  - 4
SP  - 320
EP  - 321
UR  - https://hdl.handle.net/21.15107/rcub_vinar_2031
ER  - 

@article{
author = "Ristić-Fira, Aleksandra and Đorđević Marković, R. and Radojčić, Marija and Ribarac-Stepić, Nevena B. and Kanazir, Dušan T.",
year = "1996",
journal = "Jugoslovenska Medicinska Biohemija",
title = "Glucocorticoid effects on B16/F10 and B16/C3 mouse melanoma cell growth",
volume = "15",
number = "4",
pages = "320-321",
url = "https://hdl.handle.net/21.15107/rcub_vinar_2031"
}

Ristić-Fira, A., Đorđević Marković, R., Radojčić, M., Ribarac-Stepić, N. B.,& Kanazir, D. T.. (1996). Glucocorticoid effects on B16/F10 and B16/C3 mouse melanoma cell growth. in Jugoslovenska Medicinska Biohemija, 15(4), 320-321.
https://hdl.handle.net/21.15107/rcub_vinar_2031

Ristić-Fira A, Đorđević Marković R, Radojčić M, Ribarac-Stepić NB, Kanazir DT. Glucocorticoid effects on B16/F10 and B16/C3 mouse melanoma cell growth. in Jugoslovenska Medicinska Biohemija. 1996;15(4):320-321.
https://hdl.handle.net/21.15107/rcub_vinar_2031 .

Ristić-Fira, Aleksandra, Đorđević Marković, R., Radojčić, Marija, Ribarac-Stepić, Nevena B., Kanazir, Dušan T., "Glucocorticoid effects on B16/F10 and B16/C3 mouse melanoma cell growth" in Jugoslovenska Medicinska Biohemija, 15, no. 4 (1996):320-321,
https://hdl.handle.net/21.15107/rcub_vinar_2031 .