Ilić, Vesna

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orcid::0000-0003-1119-1343
  • Ilić, Vesna (4)
  • Llić, Vesna (1)

Author's Bibliography

Selectivity of polyclonal repertoire of anti-microbial IgA and its subclasses in saliva and serum in humans

Nikodijević, Slavomir; Blagojević, Veljko; Ćuruvija, Ivana; Kosanović, Dejana; Đukić, Tamara; Đorđević, Brižita; Ilić, Vesna; Minić, Rajna

(John Wiley and Sons Inc, 2022)

TY  - JOUR
AU  - Nikodijević, Slavomir
AU  - Blagojević, Veljko
AU  - Ćuruvija, Ivana
AU  - Kosanović, Dejana
AU  - Đukić, Tamara
AU  - Đorđević, Brižita
AU  - Ilić, Vesna
AU  - Minić, Rajna
PY  - 2022
UR  - https://farfar.pharmacy.bg.ac.rs/handle/123456789/4294
AB  - Increased interest in microbiota calls for the thorough analysis of antibody reactivity to different microorganisms. As salivary IgA represents the first line of defence against microorganisms contacting mucosal surfaces, we explored the binding and specificity of salivary IgA by testing the binding of purified, FITC-labelled salivary IgA to different microorganisms in flow cytometry and conclude that this kind of analysis enables the differentiation of species/strains with high IgA binding capacity, which should be corroborated on a larger sample size. Further we compare, with in-house ELISA, the binding of polyclonal salivary IgA with the binding of polyclonal serum IgA from the same individuals to whole microbial cells and to purified microbial components. High correlations were obtained in total salivary IgA binding to Lactobacillus rhamnosus and Escherichia coli, very distant bacterial species, as well as to isolated bacterial components (r =.70–.97). The binding of total salivary IgA resembled the binding of both salivary IgA1 and IgA2, with IgA2 predominating. For serum polyclonal IgA repertoire, substantially higher specificity was obtained. Serum IgA binding to E. coli correlated best with serum IgA binding to lipopolysaccharide (r =.86), and serum IgA against L. rhamnosus correlated best with the anti-peptidoglycan IgA levels (r =.88). We have also detected that total serum IgA response is governed by either IgA1 or IgA2 response, depending on the nature of the antigen/s. We conclude that steady state salivary IgA repertoire, unlike serum IgA repertoire, consists of polyreactive antibodies with innate specificity, questioning its capacity to select resident microbiota.
PB  - John Wiley and Sons Inc
T2  - Scandinavian Journal of Immunology
T1  - Selectivity of polyclonal repertoire of anti-microbial IgA and its subclasses in saliva and serum in humans
VL  - 96
IS  - 6
DO  - 10.1111/sji.13223
ER  - 
@article{
author = "Nikodijević, Slavomir and Blagojević, Veljko and Ćuruvija, Ivana and Kosanović, Dejana and Đukić, Tamara and Đorđević, Brižita and Ilić, Vesna and Minić, Rajna",
year = "2022",
abstract = "Increased interest in microbiota calls for the thorough analysis of antibody reactivity to different microorganisms. As salivary IgA represents the first line of defence against microorganisms contacting mucosal surfaces, we explored the binding and specificity of salivary IgA by testing the binding of purified, FITC-labelled salivary IgA to different microorganisms in flow cytometry and conclude that this kind of analysis enables the differentiation of species/strains with high IgA binding capacity, which should be corroborated on a larger sample size. Further we compare, with in-house ELISA, the binding of polyclonal salivary IgA with the binding of polyclonal serum IgA from the same individuals to whole microbial cells and to purified microbial components. High correlations were obtained in total salivary IgA binding to Lactobacillus rhamnosus and Escherichia coli, very distant bacterial species, as well as to isolated bacterial components (r =.70–.97). The binding of total salivary IgA resembled the binding of both salivary IgA1 and IgA2, with IgA2 predominating. For serum polyclonal IgA repertoire, substantially higher specificity was obtained. Serum IgA binding to E. coli correlated best with serum IgA binding to lipopolysaccharide (r =.86), and serum IgA against L. rhamnosus correlated best with the anti-peptidoglycan IgA levels (r =.88). We have also detected that total serum IgA response is governed by either IgA1 or IgA2 response, depending on the nature of the antigen/s. We conclude that steady state salivary IgA repertoire, unlike serum IgA repertoire, consists of polyreactive antibodies with innate specificity, questioning its capacity to select resident microbiota.",
publisher = "John Wiley and Sons Inc",
journal = "Scandinavian Journal of Immunology",
title = "Selectivity of polyclonal repertoire of anti-microbial IgA and its subclasses in saliva and serum in humans",
volume = "96",
number = "6",
doi = "10.1111/sji.13223"
}
Nikodijević, S., Blagojević, V., Ćuruvija, I., Kosanović, D., Đukić, T., Đorđević, B., Ilić, V.,& Minić, R.. (2022). Selectivity of polyclonal repertoire of anti-microbial IgA and its subclasses in saliva and serum in humans. in Scandinavian Journal of Immunology
John Wiley and Sons Inc., 96(6).
https://doi.org/10.1111/sji.13223
Nikodijević S, Blagojević V, Ćuruvija I, Kosanović D, Đukić T, Đorđević B, Ilić V, Minić R. Selectivity of polyclonal repertoire of anti-microbial IgA and its subclasses in saliva and serum in humans. in Scandinavian Journal of Immunology. 2022;96(6).
doi:10.1111/sji.13223 .
Nikodijević, Slavomir, Blagojević, Veljko, Ćuruvija, Ivana, Kosanović, Dejana, Đukić, Tamara, Đorđević, Brižita, Ilić, Vesna, Minić, Rajna, "Selectivity of polyclonal repertoire of anti-microbial IgA and its subclasses in saliva and serum in humans" in Scandinavian Journal of Immunology, 96, no. 6 (2022),
https://doi.org/10.1111/sji.13223 . .
1

ELLSA based profiling of surface glycosylation in microorganisms reveals that ß-glucan rich yeasts’ surfaces are selectively recognized with recombinant banana lectin

Dragačević, Luka; Đorđević, Brižita; Gavrović-Jankulović, Marija; Ilić, Vesna; Kanazir, Danijela; Minić, Rajna

(Springer Nature, 2020)

TY  - JOUR
AU  - Dragačević, Luka
AU  - Đorđević, Brižita
AU  - Gavrović-Jankulović, Marija
AU  - Ilić, Vesna
AU  - Kanazir, Danijela
AU  - Minić, Rajna
PY  - 2020
UR  - https://farfar.pharmacy.bg.ac.rs/handle/123456789/3531
AB  - The surface of microorganisms is covered with polysaccharide structures which are in immediate contact with receptor structures on host’s cells and antibodies. The interaction between microorganisms and their host is dependent on surface glycosylation and in this study we have tested the interaction of plant lectins with different microorganisms. Enzyme-linked lectin sorbent assay - ELLSA was used to test the binding of recombinant Musa acuminata lectin - BL to 27 selected microorganisms and 7 other lectins were used for comparison: Soy bean agglutinin - SBA, Lens culinaris lectin - LCA, Wheat germ agglutinin - WGA, RCA120 - Ricinus communis agglutinin, Con A - from Canavalia ensiformis, Sambucus nigra agglutinin - SNA I and Maackia amurensis agglutinin - MAA. The goal was to define the microorganisms’ surface glycosylation by means of interaction with the selected plant lectins and to make a comparison with BL. Among the tested lectins most selective binding was observed for RCA120 which preferentially bound Lactobacillus casei DG. Recombinant banana lectin showed specific binding to all of the tested fungal species. The binding of BL to Candida albicans was further tested with fluorescence microscopy and flow cytometry and it was concluded that this lectin can differentiate ß-glucan rich surfaces. The binding of BL to S. boulardii could be inhibited with ß-glucan from yeast with IC50 1.81 μg mL−1 and to P. roqueforti with 1.10 μg mL−1. This unique specificity of BL could be exploited for screening purposes and potentially for the detection of ß-glucan in solutions.
PB  - Springer Nature
T2  - Glycoconjugate Journal
T1  - ELLSA based profiling of surface glycosylation in microorganisms reveals that ß-glucan rich yeasts’ surfaces are selectively recognized with recombinant banana lectin
VL  - 37
IS  - 1
SP  - 95
EP  - 105
DO  - 10.1007/s10719-019-09898-8
ER  - 
@article{
author = "Dragačević, Luka and Đorđević, Brižita and Gavrović-Jankulović, Marija and Ilić, Vesna and Kanazir, Danijela and Minić, Rajna",
year = "2020",
abstract = "The surface of microorganisms is covered with polysaccharide structures which are in immediate contact with receptor structures on host’s cells and antibodies. The interaction between microorganisms and their host is dependent on surface glycosylation and in this study we have tested the interaction of plant lectins with different microorganisms. Enzyme-linked lectin sorbent assay - ELLSA was used to test the binding of recombinant Musa acuminata lectin - BL to 27 selected microorganisms and 7 other lectins were used for comparison: Soy bean agglutinin - SBA, Lens culinaris lectin - LCA, Wheat germ agglutinin - WGA, RCA120 - Ricinus communis agglutinin, Con A - from Canavalia ensiformis, Sambucus nigra agglutinin - SNA I and Maackia amurensis agglutinin - MAA. The goal was to define the microorganisms’ surface glycosylation by means of interaction with the selected plant lectins and to make a comparison with BL. Among the tested lectins most selective binding was observed for RCA120 which preferentially bound Lactobacillus casei DG. Recombinant banana lectin showed specific binding to all of the tested fungal species. The binding of BL to Candida albicans was further tested with fluorescence microscopy and flow cytometry and it was concluded that this lectin can differentiate ß-glucan rich surfaces. The binding of BL to S. boulardii could be inhibited with ß-glucan from yeast with IC50 1.81 μg mL−1 and to P. roqueforti with 1.10 μg mL−1. This unique specificity of BL could be exploited for screening purposes and potentially for the detection of ß-glucan in solutions.",
publisher = "Springer Nature",
journal = "Glycoconjugate Journal",
title = "ELLSA based profiling of surface glycosylation in microorganisms reveals that ß-glucan rich yeasts’ surfaces are selectively recognized with recombinant banana lectin",
volume = "37",
number = "1",
pages = "95-105",
doi = "10.1007/s10719-019-09898-8"
}
Dragačević, L., Đorđević, B., Gavrović-Jankulović, M., Ilić, V., Kanazir, D.,& Minić, R.. (2020). ELLSA based profiling of surface glycosylation in microorganisms reveals that ß-glucan rich yeasts’ surfaces are selectively recognized with recombinant banana lectin. in Glycoconjugate Journal
Springer Nature., 37(1), 95-105.
https://doi.org/10.1007/s10719-019-09898-8
Dragačević L, Đorđević B, Gavrović-Jankulović M, Ilić V, Kanazir D, Minić R. ELLSA based profiling of surface glycosylation in microorganisms reveals that ß-glucan rich yeasts’ surfaces are selectively recognized with recombinant banana lectin. in Glycoconjugate Journal. 2020;37(1):95-105.
doi:10.1007/s10719-019-09898-8 .
Dragačević, Luka, Đorđević, Brižita, Gavrović-Jankulović, Marija, Ilić, Vesna, Kanazir, Danijela, Minić, Rajna, "ELLSA based profiling of surface glycosylation in microorganisms reveals that ß-glucan rich yeasts’ surfaces are selectively recognized with recombinant banana lectin" in Glycoconjugate Journal, 37, no. 1 (2020):95-105,
https://doi.org/10.1007/s10719-019-09898-8 . .
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5

Profiling of microorganism-binding serum antibody specificities in professional athletes

Minić, Rajna; Papić, Zlatko; Đorđević, Brižita; Michalickova, Danica; Llić, Vesna; Mathiesen, Geir; Živković, Irena; Pantić, Višnja; Dimitrijević, Ljiljana

(Public Library Science, San Francisco, 2018)

TY  - JOUR
AU  - Minić, Rajna
AU  - Papić, Zlatko
AU  - Đorđević, Brižita
AU  - Michalickova, Danica
AU  - Llić, Vesna
AU  - Mathiesen, Geir
AU  - Živković, Irena
AU  - Pantić, Višnja
AU  - Dimitrijević, Ljiljana
PY  - 2018
UR  - https://farfar.pharmacy.bg.ac.rs/handle/123456789/3199
AB  - The goal of this work was to elucidate similarities between microorganisms from the perspective of the humoral immune system reactivity in professional athletes. The reactivity of serum IgG of 14 young, individuals was analyzed to 23 selected microorganisms as antigens by use of the in house ELISA. Serum IgM and IgA reactivity was also analyzed and a control group of sex and age matched individuals was used for comparison. The obtained absorbance levels were used as a string of values to correlate the reactivity to different microorganisms. IgM was found to be the most cross reactive antibody class, Pearson's r = 0.7 +/- 0.92, for very distant bacterial species such as Lactobacillus and E. coli. High correlation in IgG levels was found for Gammaproteobacteria and LPS (from E. coli) (r = 0.77 for LPS vs. P. aeruginosa to r = 0.98 for LPS vs. E. coli), whereas this correlation was lower in the control group (r = 0.49 for LPS vs. P. aeruginosa to r = 0.66 for LPS vs. E. coli). The correlation was also analyzed between total IgG and IgG subclasses specific for the same microorganism, and IgG2 was identified as the main subclass recognising different microorganisms, as well as recognising LPS. Upon correlation of IgG with IgA for the same microorganism absence of or negative correlation was found between bacteria-specific IgA and IgG in case of Lactobacillus and Staphylococcusgeni, whereas correlation was absent or positive for Candida albicans, Enterococcusfaecalis, Streptococcus species tested in professional athletes. Opposite results were obtained for the control group. Outlined here is a simple experimental procedure and data analysis which yields functional significance and which can be used for determining the similarities between microorganisms from the aspect of the humoral immune system, for determining the main IgG subclass involved in an immune response as well as for the analysis of different target populations.
PB  - Public Library Science, San Francisco
T2  - PLoS One
T1  - Profiling of microorganism-binding serum antibody specificities in professional athletes
VL  - 13
IS  - 9
DO  - 10.1371/journal.pone.0203665
ER  - 
@article{
author = "Minić, Rajna and Papić, Zlatko and Đorđević, Brižita and Michalickova, Danica and Llić, Vesna and Mathiesen, Geir and Živković, Irena and Pantić, Višnja and Dimitrijević, Ljiljana",
year = "2018",
abstract = "The goal of this work was to elucidate similarities between microorganisms from the perspective of the humoral immune system reactivity in professional athletes. The reactivity of serum IgG of 14 young, individuals was analyzed to 23 selected microorganisms as antigens by use of the in house ELISA. Serum IgM and IgA reactivity was also analyzed and a control group of sex and age matched individuals was used for comparison. The obtained absorbance levels were used as a string of values to correlate the reactivity to different microorganisms. IgM was found to be the most cross reactive antibody class, Pearson's r = 0.7 +/- 0.92, for very distant bacterial species such as Lactobacillus and E. coli. High correlation in IgG levels was found for Gammaproteobacteria and LPS (from E. coli) (r = 0.77 for LPS vs. P. aeruginosa to r = 0.98 for LPS vs. E. coli), whereas this correlation was lower in the control group (r = 0.49 for LPS vs. P. aeruginosa to r = 0.66 for LPS vs. E. coli). The correlation was also analyzed between total IgG and IgG subclasses specific for the same microorganism, and IgG2 was identified as the main subclass recognising different microorganisms, as well as recognising LPS. Upon correlation of IgG with IgA for the same microorganism absence of or negative correlation was found between bacteria-specific IgA and IgG in case of Lactobacillus and Staphylococcusgeni, whereas correlation was absent or positive for Candida albicans, Enterococcusfaecalis, Streptococcus species tested in professional athletes. Opposite results were obtained for the control group. Outlined here is a simple experimental procedure and data analysis which yields functional significance and which can be used for determining the similarities between microorganisms from the aspect of the humoral immune system, for determining the main IgG subclass involved in an immune response as well as for the analysis of different target populations.",
publisher = "Public Library Science, San Francisco",
journal = "PLoS One",
title = "Profiling of microorganism-binding serum antibody specificities in professional athletes",
volume = "13",
number = "9",
doi = "10.1371/journal.pone.0203665"
}
Minić, R., Papić, Z., Đorđević, B., Michalickova, D., Llić, V., Mathiesen, G., Živković, I., Pantić, V.,& Dimitrijević, L.. (2018). Profiling of microorganism-binding serum antibody specificities in professional athletes. in PLoS One
Public Library Science, San Francisco., 13(9).
https://doi.org/10.1371/journal.pone.0203665
Minić R, Papić Z, Đorđević B, Michalickova D, Llić V, Mathiesen G, Živković I, Pantić V, Dimitrijević L. Profiling of microorganism-binding serum antibody specificities in professional athletes. in PLoS One. 2018;13(9).
doi:10.1371/journal.pone.0203665 .
Minić, Rajna, Papić, Zlatko, Đorđević, Brižita, Michalickova, Danica, Llić, Vesna, Mathiesen, Geir, Živković, Irena, Pantić, Višnja, Dimitrijević, Ljiljana, "Profiling of microorganism-binding serum antibody specificities in professional athletes" in PLoS One, 13, no. 9 (2018),
https://doi.org/10.1371/journal.pone.0203665 . .
8
6
4
6

Selected Microorganisms from an Antibody Binding Perspective in Professional Athletes

Minić, Rajna; Papić, Zlatko; Đorđević, Brižita; Michalickova, Danica; Ilić, Vesna; Mathiesen, Geir; Živković, Irena; Dimitrijević, Ljiljana

(Lippincott Williams & Wilkins, Philadelphia, 2018)

TY  - CONF
AU  - Minić, Rajna
AU  - Papić, Zlatko
AU  - Đorđević, Brižita
AU  - Michalickova, Danica
AU  - Ilić, Vesna
AU  - Mathiesen, Geir
AU  - Živković, Irena
AU  - Dimitrijević, Ljiljana
PY  - 2018
UR  - https://farfar.pharmacy.bg.ac.rs/handle/123456789/3121
PB  - Lippincott Williams & Wilkins, Philadelphia
C3  - Journal of Clinical Gastroenterology
T1  - Selected Microorganisms from an Antibody Binding Perspective in Professional Athletes
VL  - 52
UR  - https://hdl.handle.net/21.15107/rcub_farfar_3121
ER  - 
@conference{
author = "Minić, Rajna and Papić, Zlatko and Đorđević, Brižita and Michalickova, Danica and Ilić, Vesna and Mathiesen, Geir and Živković, Irena and Dimitrijević, Ljiljana",
year = "2018",
publisher = "Lippincott Williams & Wilkins, Philadelphia",
journal = "Journal of Clinical Gastroenterology",
title = "Selected Microorganisms from an Antibody Binding Perspective in Professional Athletes",
volume = "52",
url = "https://hdl.handle.net/21.15107/rcub_farfar_3121"
}
Minić, R., Papić, Z., Đorđević, B., Michalickova, D., Ilić, V., Mathiesen, G., Živković, I.,& Dimitrijević, L.. (2018). Selected Microorganisms from an Antibody Binding Perspective in Professional Athletes. in Journal of Clinical Gastroenterology
Lippincott Williams & Wilkins, Philadelphia., 52.
https://hdl.handle.net/21.15107/rcub_farfar_3121
Minić R, Papić Z, Đorđević B, Michalickova D, Ilić V, Mathiesen G, Živković I, Dimitrijević L. Selected Microorganisms from an Antibody Binding Perspective in Professional Athletes. in Journal of Clinical Gastroenterology. 2018;52.
https://hdl.handle.net/21.15107/rcub_farfar_3121 .
Minić, Rajna, Papić, Zlatko, Đorđević, Brižita, Michalickova, Danica, Ilić, Vesna, Mathiesen, Geir, Živković, Irena, Dimitrijević, Ljiljana, "Selected Microorganisms from an Antibody Binding Perspective in Professional Athletes" in Journal of Clinical Gastroenterology, 52 (2018),
https://hdl.handle.net/21.15107/rcub_farfar_3121 .

Investigation of metabolic properties and effects of 17 beta-carboxamide glucocorticoids on human peripheral blood leukocytes

Dobričić, Vladimir; Drvenica, Ivana; Stancić, Ana; Mihailović, Marija; Čudina, Olivera; Bugarski, Diana; Ilić, Vesna

(Wiley-VCH Verlag GMBH, Weinheim, 2018)

TY  - JOUR
AU  - Dobričić, Vladimir
AU  - Drvenica, Ivana
AU  - Stancić, Ana
AU  - Mihailović, Marija
AU  - Čudina, Olivera
AU  - Bugarski, Diana
AU  - Ilić, Vesna
PY  - 2018
UR  - https://farfar.pharmacy.bg.ac.rs/handle/123456789/3162
AB  - The biological activity of three previously synthesized 17 beta-carboxamide glucocorticoids (BG, BEG, and MPEA) was tested in vitro on mitogen stimulated and non-stimulated peripheral blood mononuclear cells (MNCs) and granulocytes from human healthy donors, and the results were compared to the conventional glucocorticoid dexamethasone. The tested 17 beta-carboxamide glucocorticoids did not induce decreases in MNC viability and proliferation, while modulation of reactive oxygen species (ROS) synthesis in granulocytes was dependent on the cell donor. The obtained results indicate the possibility of avoidance of strong lymphocyte suppression, which is generally recognized during administration of conventional glucocorticoids. Furthermore, the metabolism of the tested derivatives was predicted in silico. The predicted metabolites were synthesized and the in silico results were confirmed by in vitro evaluation of the metabolism of BG, BEG, and MPEA in human serum and in cultures of peripheral blood MNCs. The results of the biological activity and metabolism evaluation and of previous in vivo evaluations of biological activity indicate the soft drug nature of BG, BEG, and MPEA. In order to be fully considered as soft glucocorticoids, further investigations on the toxicity and activity of the formed metabolites are required.
PB  - Wiley-VCH Verlag GMBH, Weinheim
T2  - Archiv der Pharmazie
T1  - Investigation of metabolic properties and effects of 17 beta-carboxamide glucocorticoids on human peripheral blood leukocytes
VL  - 351
IS  - 5
DO  - 10.1002/ardp.201700371
ER  - 
@article{
author = "Dobričić, Vladimir and Drvenica, Ivana and Stancić, Ana and Mihailović, Marija and Čudina, Olivera and Bugarski, Diana and Ilić, Vesna",
year = "2018",
abstract = "The biological activity of three previously synthesized 17 beta-carboxamide glucocorticoids (BG, BEG, and MPEA) was tested in vitro on mitogen stimulated and non-stimulated peripheral blood mononuclear cells (MNCs) and granulocytes from human healthy donors, and the results were compared to the conventional glucocorticoid dexamethasone. The tested 17 beta-carboxamide glucocorticoids did not induce decreases in MNC viability and proliferation, while modulation of reactive oxygen species (ROS) synthesis in granulocytes was dependent on the cell donor. The obtained results indicate the possibility of avoidance of strong lymphocyte suppression, which is generally recognized during administration of conventional glucocorticoids. Furthermore, the metabolism of the tested derivatives was predicted in silico. The predicted metabolites were synthesized and the in silico results were confirmed by in vitro evaluation of the metabolism of BG, BEG, and MPEA in human serum and in cultures of peripheral blood MNCs. The results of the biological activity and metabolism evaluation and of previous in vivo evaluations of biological activity indicate the soft drug nature of BG, BEG, and MPEA. In order to be fully considered as soft glucocorticoids, further investigations on the toxicity and activity of the formed metabolites are required.",
publisher = "Wiley-VCH Verlag GMBH, Weinheim",
journal = "Archiv der Pharmazie",
title = "Investigation of metabolic properties and effects of 17 beta-carboxamide glucocorticoids on human peripheral blood leukocytes",
volume = "351",
number = "5",
doi = "10.1002/ardp.201700371"
}
Dobričić, V., Drvenica, I., Stancić, A., Mihailović, M., Čudina, O., Bugarski, D.,& Ilić, V.. (2018). Investigation of metabolic properties and effects of 17 beta-carboxamide glucocorticoids on human peripheral blood leukocytes. in Archiv der Pharmazie
Wiley-VCH Verlag GMBH, Weinheim., 351(5).
https://doi.org/10.1002/ardp.201700371
Dobričić V, Drvenica I, Stancić A, Mihailović M, Čudina O, Bugarski D, Ilić V. Investigation of metabolic properties and effects of 17 beta-carboxamide glucocorticoids on human peripheral blood leukocytes. in Archiv der Pharmazie. 2018;351(5).
doi:10.1002/ardp.201700371 .
Dobričić, Vladimir, Drvenica, Ivana, Stancić, Ana, Mihailović, Marija, Čudina, Olivera, Bugarski, Diana, Ilić, Vesna, "Investigation of metabolic properties and effects of 17 beta-carboxamide glucocorticoids on human peripheral blood leukocytes" in Archiv der Pharmazie, 351, no. 5 (2018),
https://doi.org/10.1002/ardp.201700371 . .