TY  - JOUR
AU  - Protić-Rosić, Isidora
AU  - Nešić, Andrijana N.
AU  - Lukić, Ivana
AU  - Miljković, Radmila
AU  - Popović, Dragan M.
AU  - Atanasković-Marković, Marina
AU  - Stojanović, Marijana M.
AU  - Gavrović-Jankulović, Marija
PY  - 2021
UR  - https://www.sciencedirect.com/science/article/pii/S0161589021001905
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4604
AB  - Allergen-specific immunotherapy (AIT) is a desensitizing treatment for allergic diseases that corrects the underlined pathological immune response to innocuous protein antigens, called allergens. Recombinant allergens employed in the AIT allowed the production of well-defined formulations that possessed consistent quality but were often less efficient than natural allergen extracts. Combining recombinant allergens with an adjuvant or immunomodulatory agent could improve AIT efficacy. This study aimed to perform structural and functional characterization of newly designed recombinant chimera composed of the Bet v 1, the major birch pollen allergen, and Banana Lectin (BanLec), TLR2, and CD14 binding protein, for the application in AIT. rBet v 1-BanLec chimera was designed in silico and expressed as a soluble fraction in Escherichia coli. Purified rBet v 1-BanLec (33.4 kDa) retained BanLec-associated biological activity of carbohydrate-binding and preserved IgE reactive epitopes of Bet v 1. The chimera revealed secondary structures with predominant β sheets. The immunomodulatory capacity of rBet v 1-BanLec tested on macrophages showed changes in myeloperoxidase activity, reduced NO production, and significant alterations in the production of cytokines when compared to both rBanLec and rBet v 1. Comparing to rBet v 1, rBet v 1-BanLec was demonstrated to be more efficient promoter of IL-10 production as well as weaker inducer of NO production and secretion of pro-inflammatory cytokines TNFα, and IL-6. The ability of rBet v 1-BanLec to promote IL-10 in together with the preserved 3D structure of Bet v 1 part implies that the construct might exert a beneficial effect in the allergen-specific immunotherapy.
PB  - Elsevier
T2  - Molecular Immunology
T2  - Molecular ImmunologyMolecular Immunology
T1  - Recombinant Bet v 1-BanLec chimera modulates functional characteristics of peritoneal murine macrophages by promoting IL-10 secretion
VL  - 138
SP  - 58
EP  - 67
DO  - 10.1016/j.molimm.2021.06.015
ER  - 

@article{
author = "Protić-Rosić, Isidora and Nešić, Andrijana N. and Lukić, Ivana and Miljković, Radmila and Popović, Dragan M. and Atanasković-Marković, Marina and Stojanović, Marijana M. and Gavrović-Jankulović, Marija",
year = "2021",
abstract = "Allergen-specific immunotherapy (AIT) is a desensitizing treatment for allergic diseases that corrects the underlined pathological immune response to innocuous protein antigens, called allergens. Recombinant allergens employed in the AIT allowed the production of well-defined formulations that possessed consistent quality but were often less efficient than natural allergen extracts. Combining recombinant allergens with an adjuvant or immunomodulatory agent could improve AIT efficacy. This study aimed to perform structural and functional characterization of newly designed recombinant chimera composed of the Bet v 1, the major birch pollen allergen, and Banana Lectin (BanLec), TLR2, and CD14 binding protein, for the application in AIT. rBet v 1-BanLec chimera was designed in silico and expressed as a soluble fraction in Escherichia coli. Purified rBet v 1-BanLec (33.4 kDa) retained BanLec-associated biological activity of carbohydrate-binding and preserved IgE reactive epitopes of Bet v 1. The chimera revealed secondary structures with predominant β sheets. The immunomodulatory capacity of rBet v 1-BanLec tested on macrophages showed changes in myeloperoxidase activity, reduced NO production, and significant alterations in the production of cytokines when compared to both rBanLec and rBet v 1. Comparing to rBet v 1, rBet v 1-BanLec was demonstrated to be more efficient promoter of IL-10 production as well as weaker inducer of NO production and secretion of pro-inflammatory cytokines TNFα, and IL-6. The ability of rBet v 1-BanLec to promote IL-10 in together with the preserved 3D structure of Bet v 1 part implies that the construct might exert a beneficial effect in the allergen-specific immunotherapy.",
publisher = "Elsevier",
journal = "Molecular Immunology, Molecular ImmunologyMolecular Immunology",
title = "Recombinant Bet v 1-BanLec chimera modulates functional characteristics of peritoneal murine macrophages by promoting IL-10 secretion",
volume = "138",
pages = "58-67",
doi = "10.1016/j.molimm.2021.06.015"
}

Protić-Rosić, I., Nešić, A. N., Lukić, I., Miljković, R., Popović, D. M., Atanasković-Marković, M., Stojanović, M. M.,& Gavrović-Jankulović, M.. (2021). Recombinant Bet v 1-BanLec chimera modulates functional characteristics of peritoneal murine macrophages by promoting IL-10 secretion. in Molecular Immunology
Elsevier., 138, 58-67.
https://doi.org/10.1016/j.molimm.2021.06.015

Protić-Rosić I, Nešić AN, Lukić I, Miljković R, Popović DM, Atanasković-Marković M, Stojanović MM, Gavrović-Jankulović M. Recombinant Bet v 1-BanLec chimera modulates functional characteristics of peritoneal murine macrophages by promoting IL-10 secretion. in Molecular Immunology. 2021;138:58-67.
doi:10.1016/j.molimm.2021.06.015 .

Protić-Rosić, Isidora, Nešić, Andrijana N., Lukić, Ivana, Miljković, Radmila, Popović, Dragan M., Atanasković-Marković, Marina, Stojanović, Marijana M., Gavrović-Jankulović, Marija, "Recombinant Bet v 1-BanLec chimera modulates functional characteristics of peritoneal murine macrophages by promoting IL-10 secretion" in Molecular Immunology, 138 (2021):58-67,
https://doi.org/10.1016/j.molimm.2021.06.015 . .

TY  - JOUR
AU  - Atanasković-Marković, Marina
AU  - Janković, Jelena
AU  - Tmušić, Vladimir
AU  - Gavrović-Jankulović, Marija
AU  - Ćirković-Veličković, Tanja
AU  - Nikolić, Dimitrije
AU  - Škorić, Dejan
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3704
AB  - Background: Antiepileptic drugs (AEDs) can cause hypersensitivity reactions in children. These reactions are mainly cutaneous, self-limiting, and benign, but life-threatening severe cutaneous adverse reactions can occur. Infections can lead to skin eruptions and mimic drug hypersensitivity reactions, if a drug is taken at the same time. The aims of our study were to confirm or rule out the diagnosis of hypersensitivity reactions to AEDs in children and to detect an infection which mimics these reactions. Methods: A prospective survey was conducted in a group of 100 children with histories of hypersensitivity reactions to AEDs by performing patch tests, delayed-reading intradermal test, and, in case of negative results, challenge test. In all children, a study was performed to detect infections by viruses or Mycoplasma pneumoniae. Results: Maculopapular exanthema and delayed-appearing urticaria were the most reported hypersensitivity reactions to AEDs. Sixty-six (66%) of 100 children had confirmed hypersensitivity reactions to AEDs. Fifty-nine children had positive patch test. No children had positive challenge tests. The most common AEDs causing hypersensitivity reactions were carbamazepine (45.4%) and lamotrigine (43.6%). Thirty-two children had positive tests for viruses or M pneumoniae, and nine of them had also a positive allergy work-up. Conclusion: Considering that there are no specific tests to distinguish between a viral infection and hypersensitivity reactions to AEDs in the acute phase, a diagnostic work-up should be performed in all children with suspected hypersensitivity reactions to AEDs, as well as infectious agent study, to remove a false label of hypersensitivity.
PB  - John Wiley and Sons Ltd.
T2  - Pediatric Allergy and Immunology
T1  - Hypersensitivity reactions to antiepileptic drugs in children
VL  - 30
IS  - 5
SP  - 547
EP  - 552
DO  - 10.1111/pai.13055
ER  - 

@article{
author = "Atanasković-Marković, Marina and Janković, Jelena and Tmušić, Vladimir and Gavrović-Jankulović, Marija and Ćirković-Veličković, Tanja and Nikolić, Dimitrije and Škorić, Dejan",
year = "2019",
abstract = "Background: Antiepileptic drugs (AEDs) can cause hypersensitivity reactions in children. These reactions are mainly cutaneous, self-limiting, and benign, but life-threatening severe cutaneous adverse reactions can occur. Infections can lead to skin eruptions and mimic drug hypersensitivity reactions, if a drug is taken at the same time. The aims of our study were to confirm or rule out the diagnosis of hypersensitivity reactions to AEDs in children and to detect an infection which mimics these reactions. Methods: A prospective survey was conducted in a group of 100 children with histories of hypersensitivity reactions to AEDs by performing patch tests, delayed-reading intradermal test, and, in case of negative results, challenge test. In all children, a study was performed to detect infections by viruses or Mycoplasma pneumoniae. Results: Maculopapular exanthema and delayed-appearing urticaria were the most reported hypersensitivity reactions to AEDs. Sixty-six (66%) of 100 children had confirmed hypersensitivity reactions to AEDs. Fifty-nine children had positive patch test. No children had positive challenge tests. The most common AEDs causing hypersensitivity reactions were carbamazepine (45.4%) and lamotrigine (43.6%). Thirty-two children had positive tests for viruses or M pneumoniae, and nine of them had also a positive allergy work-up. Conclusion: Considering that there are no specific tests to distinguish between a viral infection and hypersensitivity reactions to AEDs in the acute phase, a diagnostic work-up should be performed in all children with suspected hypersensitivity reactions to AEDs, as well as infectious agent study, to remove a false label of hypersensitivity.",
publisher = "John Wiley and Sons Ltd.",
journal = "Pediatric Allergy and Immunology",
title = "Hypersensitivity reactions to antiepileptic drugs in children",
volume = "30",
number = "5",
pages = "547-552",
doi = "10.1111/pai.13055"
}

Atanasković-Marković, M., Janković, J., Tmušić, V., Gavrović-Jankulović, M., Ćirković-Veličković, T., Nikolić, D.,& Škorić, D.. (2019). Hypersensitivity reactions to antiepileptic drugs in children. in Pediatric Allergy and Immunology
John Wiley and Sons Ltd.., 30(5), 547-552.
https://doi.org/10.1111/pai.13055

Atanasković-Marković M, Janković J, Tmušić V, Gavrović-Jankulović M, Ćirković-Veličković T, Nikolić D, Škorić D. Hypersensitivity reactions to antiepileptic drugs in children. in Pediatric Allergy and Immunology. 2019;30(5):547-552.
doi:10.1111/pai.13055 .

Atanasković-Marković, Marina, Janković, Jelena, Tmušić, Vladimir, Gavrović-Jankulović, Marija, Ćirković-Veličković, Tanja, Nikolić, Dimitrije, Škorić, Dejan, "Hypersensitivity reactions to antiepileptic drugs in children" in Pediatric Allergy and Immunology, 30, no. 5 (2019):547-552,
https://doi.org/10.1111/pai.13055 . .

TY  - CONF
AU  - Radosavljević, Jelena
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Atanasković-Marković, Marina
AU  - Burazer, Lidija M.
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2176
PB  - Wiley, Hoboken
C3  - FEBS OPEN BIO
T1  - Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes
VL  - 8
SP  - 257
EP  - 257
UR  - https://hdl.handle.net/21.15107/rcub_cherry_2176
ER  - 

@conference{
author = "Radosavljević, Jelena and Apostolović, Danijela and Mihailović-Vesić, Jelena and Atanasković-Marković, Marina and Burazer, Lidija M. and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
publisher = "Wiley, Hoboken",
journal = "FEBS OPEN BIO",
title = "Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes",
volume = "8",
pages = "257-257",
url = "https://hdl.handle.net/21.15107/rcub_cherry_2176"
}

Radosavljević, J., Apostolović, D., Mihailović-Vesić, J., Atanasković-Marković, M., Burazer, L. M., van Hage, M.,& Ćirković-Veličković, T.. (2018). Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes. in FEBS OPEN BIO
Wiley, Hoboken., 8, 257-257.
https://hdl.handle.net/21.15107/rcub_cherry_2176

Radosavljević J, Apostolović D, Mihailović-Vesić J, Atanasković-Marković M, Burazer LM, van Hage M, Ćirković-Veličković T. Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes. in FEBS OPEN BIO. 2018;8:257-257.
https://hdl.handle.net/21.15107/rcub_cherry_2176 .

Radosavljević, Jelena, Apostolović, Danijela, Mihailović-Vesić, Jelena, Atanasković-Marković, Marina, Burazer, Lidija M., van Hage, Marianne, Ćirković-Veličković, Tanja, "Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes" in FEBS OPEN BIO, 8 (2018):257-257,
https://hdl.handle.net/21.15107/rcub_cherry_2176 .

TY  - JOUR
AU  - Nikolić, Jasna
AU  - Nešić, Andrijana N.
AU  - Čavić, Milena
AU  - Đorđević, Neda O.
AU  - Anđelković, Uroš
AU  - Atanasković-Marković, Marina
AU  - Drakulić, Branko J.
AU  - Gavrović-Jankulović, Marija
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2384
AB  - Background: Protein oxidation can occur as a consequence of lipid peroxidation during food processing. The aim of this work was to explore the effect of malondialdehyde (MDA) modification of ovalbumin (OVA) on its interaction with T84 intestinal cells. Methods: Molecular dynamics simulation was employed for the prediction of MDA modification in the OVA, while introduced structural changes were evaluated by measurement of carbonyl group content, fluorescence spectra, MS/MS analysis, and IgE reactivity. Effects of MDA modified OVA on T84 epithelial cells were analyzed by gene expression for pro-inflammatory cytokines and protein secretion. Results: Out of 9 predicted, five modified Lys residues were confirmed by MS/MS analysis: (51)TQINKVVR(58), (85)DILNQITKPNDVYSFSLASR(104), (111)YPILPEYLQCVKELYR(126), (187)AFKDEDTQAMPFR(99), (KIKVYLPR284)-K-277, and (IKVYLPR284)-I-278. The introduced MDA modifications influenced profile of IgE reactivity to OVA. Treatment of T84 epithelial cells with OVA and OVA modified with 1 mM MDA, induced up-regulation of pro-inflammatory cytokines (IL-1 beta,IL-25, IL-33, TSLP and TNF alpha), while OVA modification with 10 mM MDA induced down regulation of the cytokine expression profile, except for IL-1 beta. OVA and OVA modified with 1 mM MDA induced secretion of epithelial cells specific cytokine IL-33. Conclusions: This finding indicated that OVA and its MDA modified form have the potential to trigger the innate immunity by inducing up-regulation and secretion of pro-allergenic IL-33 in T84 intestinal epithelial cells. General significance: Interactions of ovalbumin and its MDA modified form with intestinal epithelial cells can induce a specific immunological priming necessary for the downstream activation of innate immunity. (C) 2016 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Biochimica et Biophysica Acta: General Subjects
T1  - Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells
VL  - 1861
IS  - 2
SP  - 126
EP  - 134
DO  - 10.1016/j.bbagen.2016.11.021
ER  - 

@article{
author = "Nikolić, Jasna and Nešić, Andrijana N. and Čavić, Milena and Đorđević, Neda O. and Anđelković, Uroš and Atanasković-Marković, Marina and Drakulić, Branko J. and Gavrović-Jankulović, Marija",
year = "2017",
abstract = "Background: Protein oxidation can occur as a consequence of lipid peroxidation during food processing. The aim of this work was to explore the effect of malondialdehyde (MDA) modification of ovalbumin (OVA) on its interaction with T84 intestinal cells. Methods: Molecular dynamics simulation was employed for the prediction of MDA modification in the OVA, while introduced structural changes were evaluated by measurement of carbonyl group content, fluorescence spectra, MS/MS analysis, and IgE reactivity. Effects of MDA modified OVA on T84 epithelial cells were analyzed by gene expression for pro-inflammatory cytokines and protein secretion. Results: Out of 9 predicted, five modified Lys residues were confirmed by MS/MS analysis: (51)TQINKVVR(58), (85)DILNQITKPNDVYSFSLASR(104), (111)YPILPEYLQCVKELYR(126), (187)AFKDEDTQAMPFR(99), (KIKVYLPR284)-K-277, and (IKVYLPR284)-I-278. The introduced MDA modifications influenced profile of IgE reactivity to OVA. Treatment of T84 epithelial cells with OVA and OVA modified with 1 mM MDA, induced up-regulation of pro-inflammatory cytokines (IL-1 beta,IL-25, IL-33, TSLP and TNF alpha), while OVA modification with 10 mM MDA induced down regulation of the cytokine expression profile, except for IL-1 beta. OVA and OVA modified with 1 mM MDA induced secretion of epithelial cells specific cytokine IL-33. Conclusions: This finding indicated that OVA and its MDA modified form have the potential to trigger the innate immunity by inducing up-regulation and secretion of pro-allergenic IL-33 in T84 intestinal epithelial cells. General significance: Interactions of ovalbumin and its MDA modified form with intestinal epithelial cells can induce a specific immunological priming necessary for the downstream activation of innate immunity. (C) 2016 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Biochimica et Biophysica Acta: General Subjects",
title = "Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells",
volume = "1861",
number = "2",
pages = "126-134",
doi = "10.1016/j.bbagen.2016.11.021"
}

Nikolić, J., Nešić, A. N., Čavić, M., Đorđević, N. O., Anđelković, U., Atanasković-Marković, M., Drakulić, B. J.,& Gavrović-Jankulović, M.. (2017). Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells. in Biochimica et Biophysica Acta: General Subjects
Elsevier Science Bv, Amsterdam., 1861(2), 126-134.
https://doi.org/10.1016/j.bbagen.2016.11.021

Nikolić J, Nešić AN, Čavić M, Đorđević NO, Anđelković U, Atanasković-Marković M, Drakulić BJ, Gavrović-Jankulović M. Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells. in Biochimica et Biophysica Acta: General Subjects. 2017;1861(2):126-134.
doi:10.1016/j.bbagen.2016.11.021 .

Nikolić, Jasna, Nešić, Andrijana N., Čavić, Milena, Đorđević, Neda O., Anđelković, Uroš, Atanasković-Marković, Marina, Drakulić, Branko J., Gavrović-Jankulović, Marija, "Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells" in Biochimica et Biophysica Acta: General Subjects, 1861, no. 2 (2017):126-134,
https://doi.org/10.1016/j.bbagen.2016.11.021 . .

TY  - JOUR
AU  - Nikolić, Jasna
AU  - Nešić, Andrijana N.
AU  - Čavić, Milena
AU  - Đorđević, Neda O.
AU  - Anđelković, Uroš
AU  - Atanasković-Marković, Marina
AU  - Drakulić, Branko J.
AU  - Gavrović-Jankulović, Marija
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2384
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2954
AB  - ackground: Protein oxidation can occur as a consequence of lipid peroxidation during food processing. The aim of this work was to explore the effect of malondialdehyde (MDA) modification of ovalbumin (OVA) on its interaction with T84 intestinal cells. Methods: Molecular dynamics simulation was employed for the prediction of MDA modification in the OVA, while introduced structural changes were evaluated by measurement of carbonyl group content, fluorescence spectra, MS/MS analysis, and IgE reactivity. Effects of MDA modified OVA on T84 epithelial cells were analyzed by gene expression for pro-inflammatory cytokines and protein secretion. Results: Out of 9 predicted, five modified Lys residues were confirmed by MS/MS analysis: (51)TQINKVVR(58), (85)DILNQITKPNDVYSFSLASR(104), (111)YPILPEYLQCVKELYR(126), (187)AFKDEDTQAMPFR(99), (KIKVYLPR284)-K-277, and (IKVYLPR284)-I-278. The introduced MDA modifications influenced profile of IgE reactivity to OVA. Treatment of T84 epithelial cells with OVA and OVA modified with 1 mM MDA, induced up-regulation of pro-inflammatory cytokines (IL-1 beta,IL-25, IL-33, TSLP and TNF alpha), while OVA modification with 10 mM MDA induced down regulation of the cytokine expression profile, except for IL-1 beta. OVA and OVA modified with 1 mM MDA induced secretion of epithelial cells specific cytokine IL-33. Conclusions: This finding indicated that OVA and its MDA modified form have the potential to trigger the innate immunity by inducing up-regulation and secretion of pro-allergenic IL-33 in T84 intestinal epithelial cells. General significance: Interactions of ovalbumin and its MDA modified form with intestinal epithelial cells can induce a specific immunological priming necessary for the downstream activation of innate immunity. (C) 2016 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Biochimica et Biophysica Acta: General Subjects
T1  - Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells
VL  - 1861
IS  - 2
SP  - 126
EP  - 134
DO  - 10.1016/j.bbagen.2016.11.021
ER  - 

@article{
author = "Nikolić, Jasna and Nešić, Andrijana N. and Čavić, Milena and Đorđević, Neda O. and Anđelković, Uroš and Atanasković-Marković, Marina and Drakulić, Branko J. and Gavrović-Jankulović, Marija",
year = "2017",
abstract = "ackground: Protein oxidation can occur as a consequence of lipid peroxidation during food processing. The aim of this work was to explore the effect of malondialdehyde (MDA) modification of ovalbumin (OVA) on its interaction with T84 intestinal cells. Methods: Molecular dynamics simulation was employed for the prediction of MDA modification in the OVA, while introduced structural changes were evaluated by measurement of carbonyl group content, fluorescence spectra, MS/MS analysis, and IgE reactivity. Effects of MDA modified OVA on T84 epithelial cells were analyzed by gene expression for pro-inflammatory cytokines and protein secretion. Results: Out of 9 predicted, five modified Lys residues were confirmed by MS/MS analysis: (51)TQINKVVR(58), (85)DILNQITKPNDVYSFSLASR(104), (111)YPILPEYLQCVKELYR(126), (187)AFKDEDTQAMPFR(99), (KIKVYLPR284)-K-277, and (IKVYLPR284)-I-278. The introduced MDA modifications influenced profile of IgE reactivity to OVA. Treatment of T84 epithelial cells with OVA and OVA modified with 1 mM MDA, induced up-regulation of pro-inflammatory cytokines (IL-1 beta,IL-25, IL-33, TSLP and TNF alpha), while OVA modification with 10 mM MDA induced down regulation of the cytokine expression profile, except for IL-1 beta. OVA and OVA modified with 1 mM MDA induced secretion of epithelial cells specific cytokine IL-33. Conclusions: This finding indicated that OVA and its MDA modified form have the potential to trigger the innate immunity by inducing up-regulation and secretion of pro-allergenic IL-33 in T84 intestinal epithelial cells. General significance: Interactions of ovalbumin and its MDA modified form with intestinal epithelial cells can induce a specific immunological priming necessary for the downstream activation of innate immunity. (C) 2016 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Biochimica et Biophysica Acta: General Subjects",
title = "Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells",
volume = "1861",
number = "2",
pages = "126-134",
doi = "10.1016/j.bbagen.2016.11.021"
}

Nikolić, J., Nešić, A. N., Čavić, M., Đorđević, N. O., Anđelković, U., Atanasković-Marković, M., Drakulić, B. J.,& Gavrović-Jankulović, M.. (2017). Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells. in Biochimica et Biophysica Acta: General Subjects
Elsevier Science Bv, Amsterdam., 1861(2), 126-134.
https://doi.org/10.1016/j.bbagen.2016.11.021

Nikolić J, Nešić AN, Čavić M, Đorđević NO, Anđelković U, Atanasković-Marković M, Drakulić BJ, Gavrović-Jankulović M. Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells. in Biochimica et Biophysica Acta: General Subjects. 2017;1861(2):126-134.
doi:10.1016/j.bbagen.2016.11.021 .

Nikolić, Jasna, Nešić, Andrijana N., Čavić, Milena, Đorđević, Neda O., Anđelković, Uroš, Atanasković-Marković, Marina, Drakulić, Branko J., Gavrović-Jankulović, Marija, "Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells" in Biochimica et Biophysica Acta: General Subjects, 1861, no. 2 (2017):126-134,
https://doi.org/10.1016/j.bbagen.2016.11.021 . .

TY  - JOUR
AU  - Zivanovic, Mirjana
AU  - Atanasković-Marković, Marina
AU  - Međo, Biljana
AU  - Gavrović-Jankulović, Marija
AU  - Smiljanić, Katarina
AU  - Tmušić, Vladimir
AU  - Đurić, Vojislav
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2469
AB  - IgE-mediated food allergy affects 6-8% of children. Our study aimed to define the correlations between the results obtained with skin prick tests (SPTs) using commercial extracts and fresh foods, and the correlations between these result and those obtained with specific IgE (sIgE) and/or challenge. Children aged from 2 months to 6 years were recruited prospectively. Overall 571 children were positive to one food. In all children we performed SPT using commercial extracts of suspected food and fresh foods and sIgE. If SPT and sIgE test results did not correspond to the history, we performed open oral food challenge. Sensitivity of SPT with commercial extracts for all tested food was poor (3-35%), while sensitivity of fresh food skin prick tests (FFSPT) was excellent (50-100%), and showed correlation with open oral food challenge (p lt 0.001). Our results suggest that fresh food extracts are more effective in detecting sensitization and with levels of sIgE greater than class 3 could predict clinical reactivity, without the need for potentially hazardous food challenges.
PB  - Iranian Scientific Society Medical Entomology, Tehran
T2  - Iranian Journal of Allergy Asthma and Immunology
T1  - Evaluation of Food Allergy in Children by Skin Prick Tests with Commercial Extracts and Fresh Foods, Specific IgE and, Open Oral Food Challenge: Our Five Years Experience in Food Allergy Work-up
VL  - 16
IS  - 2
SP  - 127
EP  - 132
UR  - https://hdl.handle.net/21.15107/rcub_cherry_2469
ER  - 

@article{
author = "Zivanovic, Mirjana and Atanasković-Marković, Marina and Međo, Biljana and Gavrović-Jankulović, Marija and Smiljanić, Katarina and Tmušić, Vladimir and Đurić, Vojislav",
year = "2017",
abstract = "IgE-mediated food allergy affects 6-8% of children. Our study aimed to define the correlations between the results obtained with skin prick tests (SPTs) using commercial extracts and fresh foods, and the correlations between these result and those obtained with specific IgE (sIgE) and/or challenge. Children aged from 2 months to 6 years were recruited prospectively. Overall 571 children were positive to one food. In all children we performed SPT using commercial extracts of suspected food and fresh foods and sIgE. If SPT and sIgE test results did not correspond to the history, we performed open oral food challenge. Sensitivity of SPT with commercial extracts for all tested food was poor (3-35%), while sensitivity of fresh food skin prick tests (FFSPT) was excellent (50-100%), and showed correlation with open oral food challenge (p lt 0.001). Our results suggest that fresh food extracts are more effective in detecting sensitization and with levels of sIgE greater than class 3 could predict clinical reactivity, without the need for potentially hazardous food challenges.",
publisher = "Iranian Scientific Society Medical Entomology, Tehran",
journal = "Iranian Journal of Allergy Asthma and Immunology",
title = "Evaluation of Food Allergy in Children by Skin Prick Tests with Commercial Extracts and Fresh Foods, Specific IgE and, Open Oral Food Challenge: Our Five Years Experience in Food Allergy Work-up",
volume = "16",
number = "2",
pages = "127-132",
url = "https://hdl.handle.net/21.15107/rcub_cherry_2469"
}

Zivanovic, M., Atanasković-Marković, M., Međo, B., Gavrović-Jankulović, M., Smiljanić, K., Tmušić, V.,& Đurić, V.. (2017). Evaluation of Food Allergy in Children by Skin Prick Tests with Commercial Extracts and Fresh Foods, Specific IgE and, Open Oral Food Challenge: Our Five Years Experience in Food Allergy Work-up. in Iranian Journal of Allergy Asthma and Immunology
Iranian Scientific Society Medical Entomology, Tehran., 16(2), 127-132.
https://hdl.handle.net/21.15107/rcub_cherry_2469

Zivanovic M, Atanasković-Marković M, Međo B, Gavrović-Jankulović M, Smiljanić K, Tmušić V, Đurić V. Evaluation of Food Allergy in Children by Skin Prick Tests with Commercial Extracts and Fresh Foods, Specific IgE and, Open Oral Food Challenge: Our Five Years Experience in Food Allergy Work-up. in Iranian Journal of Allergy Asthma and Immunology. 2017;16(2):127-132.
https://hdl.handle.net/21.15107/rcub_cherry_2469 .

Zivanovic, Mirjana, Atanasković-Marković, Marina, Međo, Biljana, Gavrović-Jankulović, Marija, Smiljanić, Katarina, Tmušić, Vladimir, Đurić, Vojislav, "Evaluation of Food Allergy in Children by Skin Prick Tests with Commercial Extracts and Fresh Foods, Specific IgE and, Open Oral Food Challenge: Our Five Years Experience in Food Allergy Work-up" in Iranian Journal of Allergy Asthma and Immunology, 16, no. 2 (2017):127-132,
https://hdl.handle.net/21.15107/rcub_cherry_2469 .

TY  - JOUR
AU  - Mrkić, Ivan
AU  - Minić, Rajna
AU  - Bulat, Tanja
AU  - Aradska, Jana
AU  - Atanasković-Marković, Marina
AU  - Drakulić, Branko J.
AU  - Gavrović-Jankulović, Marija
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2472
AB  - BACKGROUND: Group 1 and group 2 allergens from house dust mite are the major elicitors of respiratory allergic diseases and the main candidates for immunotherapy. RESULTS: The potential therapeutic role of a chimera composed of recombinant Der p 2 (D2) linked to Influenza A virus hemagglutinin 1 (H1) for intranasal application was created, expressed and tested in a mouse model. H1D2 and D2 were produced by genetic engineering in Escherichia coli and their primary structure was confirmed by mass fingerprint. Both antigens preserved IgE reactivity in immunoblot with serum from seven house dust mite allergic persons. Balb/c mice were sensitized with D2 allergen in alum and subsequently received H1D2 or D2, intranasally. The reduced levels of serum D2 specific IgE, together with the increased serum specific IgG and IgA were detected in both groups which received H1D2 and D2 intranasally. A higher level of effector CD4+CD25+ spleen lymphocytes was found only in the group of mice which received i.n. H1D2. CONCLUSION: H1D2 chimera can have therapeutic potential in Der p 2 allergic persons as dual vaccine which, beside protective allergen specific, can provide protective antibodies against Influenza A virus hemagglutinin 1. (C) 2016 Society of Chemical Industry
PB  - Wiley, Hoboken
T2  - Journal of Chemical Technology and Biotechnology
T1  - Modulation of the specific immune response in Balb/cmice by intranasal application of recombinant H1D2 chimera
VL  - 92
IS  - 6
SP  - 1328
EP  - 1335
DO  - 10.1002/jctb.5127
ER  - 

@article{
author = "Mrkić, Ivan and Minić, Rajna and Bulat, Tanja and Aradska, Jana and Atanasković-Marković, Marina and Drakulić, Branko J. and Gavrović-Jankulović, Marija",
year = "2017",
abstract = "BACKGROUND: Group 1 and group 2 allergens from house dust mite are the major elicitors of respiratory allergic diseases and the main candidates for immunotherapy. RESULTS: The potential therapeutic role of a chimera composed of recombinant Der p 2 (D2) linked to Influenza A virus hemagglutinin 1 (H1) for intranasal application was created, expressed and tested in a mouse model. H1D2 and D2 were produced by genetic engineering in Escherichia coli and their primary structure was confirmed by mass fingerprint. Both antigens preserved IgE reactivity in immunoblot with serum from seven house dust mite allergic persons. Balb/c mice were sensitized with D2 allergen in alum and subsequently received H1D2 or D2, intranasally. The reduced levels of serum D2 specific IgE, together with the increased serum specific IgG and IgA were detected in both groups which received H1D2 and D2 intranasally. A higher level of effector CD4+CD25+ spleen lymphocytes was found only in the group of mice which received i.n. H1D2. CONCLUSION: H1D2 chimera can have therapeutic potential in Der p 2 allergic persons as dual vaccine which, beside protective allergen specific, can provide protective antibodies against Influenza A virus hemagglutinin 1. (C) 2016 Society of Chemical Industry",
publisher = "Wiley, Hoboken",
journal = "Journal of Chemical Technology and Biotechnology",
title = "Modulation of the specific immune response in Balb/cmice by intranasal application of recombinant H1D2 chimera",
volume = "92",
number = "6",
pages = "1328-1335",
doi = "10.1002/jctb.5127"
}

Mrkić, I., Minić, R., Bulat, T., Aradska, J., Atanasković-Marković, M., Drakulić, B. J.,& Gavrović-Jankulović, M.. (2017). Modulation of the specific immune response in Balb/cmice by intranasal application of recombinant H1D2 chimera. in Journal of Chemical Technology and Biotechnology
Wiley, Hoboken., 92(6), 1328-1335.
https://doi.org/10.1002/jctb.5127

Mrkić I, Minić R, Bulat T, Aradska J, Atanasković-Marković M, Drakulić BJ, Gavrović-Jankulović M. Modulation of the specific immune response in Balb/cmice by intranasal application of recombinant H1D2 chimera. in Journal of Chemical Technology and Biotechnology. 2017;92(6):1328-1335.
doi:10.1002/jctb.5127 .

Mrkić, Ivan, Minić, Rajna, Bulat, Tanja, Aradska, Jana, Atanasković-Marković, Marina, Drakulić, Branko J., Gavrović-Jankulović, Marija, "Modulation of the specific immune response in Balb/cmice by intranasal application of recombinant H1D2 chimera" in Journal of Chemical Technology and Biotechnology, 92, no. 6 (2017):1328-1335,
https://doi.org/10.1002/jctb.5127 . .

TY  - DATA
AU  - Stanić-Vučinić, Dragana
AU  - Stojadinović, Marija M.
AU  - Mirkov, Ivana
AU  - Apostolović, Danijela
AU  - Burazer, Lidija M.
AU  - Atanasković-Marković, Marina
AU  - Kataranovski, Milena
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3528
PB  - Royal Soc Chemistry, Cambridge
T2  - RSC Advances
T1  - Supplementary data for the article: Stanic-Vucinic, D.; Stojadinovic, M.; Mirkov, I.; Apostolovic, D.; Burazer, L.; Atanaskovic-Markovic, M.; Kataranovski, M.; Cirkovic Velickovic, T. Hypoallergenic Acid-Sensitive Modification Preserves Major Mugwort Allergen Fold and Delivers Full Repertoire of MHC Class II-Binding Peptides during Endolysosomal Degradation. RSC Advances 2016, 6 (91), 88216–88228. https://doi.org/10.1039/c6ra17261j
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3528
ER  - 

@misc{
author = "Stanić-Vučinić, Dragana and Stojadinović, Marija M. and Mirkov, Ivana and Apostolović, Danijela and Burazer, Lidija M. and Atanasković-Marković, Marina and Kataranovski, Milena and Ćirković-Veličković, Tanja",
year = "2016",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "RSC Advances",
title = "Supplementary data for the article: Stanic-Vucinic, D.; Stojadinovic, M.; Mirkov, I.; Apostolovic, D.; Burazer, L.; Atanaskovic-Markovic, M.; Kataranovski, M.; Cirkovic Velickovic, T. Hypoallergenic Acid-Sensitive Modification Preserves Major Mugwort Allergen Fold and Delivers Full Repertoire of MHC Class II-Binding Peptides during Endolysosomal Degradation. RSC Advances 2016, 6 (91), 88216–88228. https://doi.org/10.1039/c6ra17261j",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3528"
}

Stanić-Vučinić, D., Stojadinović, M. M., Mirkov, I., Apostolović, D., Burazer, L. M., Atanasković-Marković, M., Kataranovski, M.,& Ćirković-Veličković, T.. (2016). Supplementary data for the article: Stanic-Vucinic, D.; Stojadinovic, M.; Mirkov, I.; Apostolovic, D.; Burazer, L.; Atanaskovic-Markovic, M.; Kataranovski, M.; Cirkovic Velickovic, T. Hypoallergenic Acid-Sensitive Modification Preserves Major Mugwort Allergen Fold and Delivers Full Repertoire of MHC Class II-Binding Peptides during Endolysosomal Degradation. RSC Advances 2016, 6 (91), 88216–88228. https://doi.org/10.1039/c6ra17261j. in RSC Advances
Royal Soc Chemistry, Cambridge..
https://hdl.handle.net/21.15107/rcub_cherry_3528

Stanić-Vučinić D, Stojadinović MM, Mirkov I, Apostolović D, Burazer LM, Atanasković-Marković M, Kataranovski M, Ćirković-Veličković T. Supplementary data for the article: Stanic-Vucinic, D.; Stojadinovic, M.; Mirkov, I.; Apostolovic, D.; Burazer, L.; Atanaskovic-Markovic, M.; Kataranovski, M.; Cirkovic Velickovic, T. Hypoallergenic Acid-Sensitive Modification Preserves Major Mugwort Allergen Fold and Delivers Full Repertoire of MHC Class II-Binding Peptides during Endolysosomal Degradation. RSC Advances 2016, 6 (91), 88216–88228. https://doi.org/10.1039/c6ra17261j. in RSC Advances. 2016;.
https://hdl.handle.net/21.15107/rcub_cherry_3528 .

Stanić-Vučinić, Dragana, Stojadinović, Marija M., Mirkov, Ivana, Apostolović, Danijela, Burazer, Lidija M., Atanasković-Marković, Marina, Kataranovski, Milena, Ćirković-Veličković, Tanja, "Supplementary data for the article: Stanic-Vucinic, D.; Stojadinovic, M.; Mirkov, I.; Apostolovic, D.; Burazer, L.; Atanaskovic-Markovic, M.; Kataranovski, M.; Cirkovic Velickovic, T. Hypoallergenic Acid-Sensitive Modification Preserves Major Mugwort Allergen Fold and Delivers Full Repertoire of MHC Class II-Binding Peptides during Endolysosomal Degradation. RSC Advances 2016, 6 (91), 88216–88228. https://doi.org/10.1039/c6ra17261j" in RSC Advances (2016),
https://hdl.handle.net/21.15107/rcub_cherry_3528 .

TY  - JOUR
AU  - Stanić-Vučinić, Dragana
AU  - Stojadinović, Marija M.
AU  - Mirkov, Ivana
AU  - Apostolović, Danijela
AU  - Burazer, Lidija M.
AU  - Atanasković-Marković, Marina
AU  - Kataranovski, Milena
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2321
AB  - Modified allergens are a safer and more efficient alternative to natural allergens for specific immunotherapy. As the modification of an allergen can diminish its immunogenicity due to the alteration of T-cell epitopes, in this paper we study the effects of a reversible chemical modification of Art v 1, the main allergen of mugwort pollen, on its allergenicity and immunogenicity. Modification of Art v 1 by cis-aconitylation into a polyanionic derivative (CAA) did not result in any significant structural alteration. However, IgE-binding epitopes on CAA were blocked, resulting in a reduced IgE-binding and basophil activation. Both proteins induced proliferation of CD3(+)CD4(+) T-cells in mugwort-allergic patients, but only unmodified allergens increased IL-4, IL-5 and IL-10 production. Rabbit and mouse anti-CAA antibodies exhibited cross-reactivity with native allergens and blocked human IgE-binding to Art v 1. Degradation of CAA by lysosomal fraction enzymes resulted in a similar set of peptides, harboring MHC class II-binding peptides, as unmodified proteins. Thus, cis-aconitylation modified Art v 1 had a significantly reduced allergenicity, whereas its immunogenicity was completely preserved. Acid-environment-responsive modification, which releases a full repertoire of native allergen epitopes within a particular site, can be considered a smart drug delivery system, which is able to deliver a therapeutically-effective dose in a controlled manner, and minimizes adverse side effects.
PB  - Royal Soc Chemistry, Cambridge
T2  - RSC Advances
T1  - Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation
VL  - 6
IS  - 91
SP  - 88216
EP  - 88228
DO  - 10.1039/c6ra17261j
ER  - 

@article{
author = "Stanić-Vučinić, Dragana and Stojadinović, Marija M. and Mirkov, Ivana and Apostolović, Danijela and Burazer, Lidija M. and Atanasković-Marković, Marina and Kataranovski, Milena and Ćirković-Veličković, Tanja",
year = "2016",
abstract = "Modified allergens are a safer and more efficient alternative to natural allergens for specific immunotherapy. As the modification of an allergen can diminish its immunogenicity due to the alteration of T-cell epitopes, in this paper we study the effects of a reversible chemical modification of Art v 1, the main allergen of mugwort pollen, on its allergenicity and immunogenicity. Modification of Art v 1 by cis-aconitylation into a polyanionic derivative (CAA) did not result in any significant structural alteration. However, IgE-binding epitopes on CAA were blocked, resulting in a reduced IgE-binding and basophil activation. Both proteins induced proliferation of CD3(+)CD4(+) T-cells in mugwort-allergic patients, but only unmodified allergens increased IL-4, IL-5 and IL-10 production. Rabbit and mouse anti-CAA antibodies exhibited cross-reactivity with native allergens and blocked human IgE-binding to Art v 1. Degradation of CAA by lysosomal fraction enzymes resulted in a similar set of peptides, harboring MHC class II-binding peptides, as unmodified proteins. Thus, cis-aconitylation modified Art v 1 had a significantly reduced allergenicity, whereas its immunogenicity was completely preserved. Acid-environment-responsive modification, which releases a full repertoire of native allergen epitopes within a particular site, can be considered a smart drug delivery system, which is able to deliver a therapeutically-effective dose in a controlled manner, and minimizes adverse side effects.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "RSC Advances",
title = "Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation",
volume = "6",
number = "91",
pages = "88216-88228",
doi = "10.1039/c6ra17261j"
}

Stanić-Vučinić, D., Stojadinović, M. M., Mirkov, I., Apostolović, D., Burazer, L. M., Atanasković-Marković, M., Kataranovski, M.,& Ćirković-Veličković, T.. (2016). Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation. in RSC Advances
Royal Soc Chemistry, Cambridge., 6(91), 88216-88228.
https://doi.org/10.1039/c6ra17261j

Stanić-Vučinić D, Stojadinović MM, Mirkov I, Apostolović D, Burazer LM, Atanasković-Marković M, Kataranovski M, Ćirković-Veličković T. Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation. in RSC Advances. 2016;6(91):88216-88228.
doi:10.1039/c6ra17261j .

Stanić-Vučinić, Dragana, Stojadinović, Marija M., Mirkov, Ivana, Apostolović, Danijela, Burazer, Lidija M., Atanasković-Marković, Marina, Kataranovski, Milena, Ćirković-Veličković, Tanja, "Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation" in RSC Advances, 6, no. 91 (2016):88216-88228,
https://doi.org/10.1039/c6ra17261j . .

TY  - JOUR
AU  - Atanasković-Marković, Marina
AU  - Gaeta, Francesco
AU  - Međo, Biljana
AU  - Gavrović-Jankulović, Marija
AU  - Ćirković-Veličković, Tanja
AU  - Tmušić, Vladimir
AU  - Romano, Antonino
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2278
AB  - BackgroundNon-immediate reactions to beta-lactam antibiotics (BL) occur more than one hour after drug administration, and the most common manifestations are maculopapular exanthemas and delayed-appearing urticaria and/or angioedema. Infections can lead to skin eruptions and mimic drug hypersensitivity reactions (DHR), if a drug is taken at the same time. The most of children are labeled as drug allergic' after considering only the clinical history. ObjectiveTo diagnose/detect a hypersensitivity or an infection which mimic DHR in children with non-immediate reactions to BL MethodsA prospective survey was conducted in a group of 1026 children with histories of non-immediate reactions to BL by performing patch tests, skin tests, and in case of negative results, drug provocation tests (DPTs). In 300 children, a study was performed to detect infections by viruses or Mycoplasma pneumoniae. ResultsUrticaria and maculopapular exanthemas were the most reported non-immediate reactions. Only 76 (7.4%) of 1026 children had confirmed non-immediate hypersensitivity reactions to BL. Fifty-seven children had positive delayed-reading intradermal tests (18 of these with a positive patch test). Nineteen children had positive DPT. Sixty-six of 300 children had positive tests for viruses or Mycoplasma pneumoniae and 2 of them had a positive allergy work-up. ConclusionsA diagnostic work-up should be performed in all children with non-immediate reactions to BL, to remove a false label of hypersensitivity. Even though only 57 (5.5%) of 1026 children displayed positive responses to delayed-reading intradermal tests to BL, such tests appear to be useful in order to reduce the risk for positive DPTs.
PB  - Wiley, Hoboken
T2  - Pediatric Allergy and Immunology
T1  - Non-immediate hypersensitivity reactions to beta-lactam antibiotics in children - our 10-year experience in allergy work-up
VL  - 27
IS  - 5
SP  - 533
EP  - 538
DO  - 10.1111/pai.12565
ER  - 

@article{
author = "Atanasković-Marković, Marina and Gaeta, Francesco and Međo, Biljana and Gavrović-Jankulović, Marija and Ćirković-Veličković, Tanja and Tmušić, Vladimir and Romano, Antonino",
year = "2016",
abstract = "BackgroundNon-immediate reactions to beta-lactam antibiotics (BL) occur more than one hour after drug administration, and the most common manifestations are maculopapular exanthemas and delayed-appearing urticaria and/or angioedema. Infections can lead to skin eruptions and mimic drug hypersensitivity reactions (DHR), if a drug is taken at the same time. The most of children are labeled as drug allergic' after considering only the clinical history. ObjectiveTo diagnose/detect a hypersensitivity or an infection which mimic DHR in children with non-immediate reactions to BL MethodsA prospective survey was conducted in a group of 1026 children with histories of non-immediate reactions to BL by performing patch tests, skin tests, and in case of negative results, drug provocation tests (DPTs). In 300 children, a study was performed to detect infections by viruses or Mycoplasma pneumoniae. ResultsUrticaria and maculopapular exanthemas were the most reported non-immediate reactions. Only 76 (7.4%) of 1026 children had confirmed non-immediate hypersensitivity reactions to BL. Fifty-seven children had positive delayed-reading intradermal tests (18 of these with a positive patch test). Nineteen children had positive DPT. Sixty-six of 300 children had positive tests for viruses or Mycoplasma pneumoniae and 2 of them had a positive allergy work-up. ConclusionsA diagnostic work-up should be performed in all children with non-immediate reactions to BL, to remove a false label of hypersensitivity. Even though only 57 (5.5%) of 1026 children displayed positive responses to delayed-reading intradermal tests to BL, such tests appear to be useful in order to reduce the risk for positive DPTs.",
publisher = "Wiley, Hoboken",
journal = "Pediatric Allergy and Immunology",
title = "Non-immediate hypersensitivity reactions to beta-lactam antibiotics in children - our 10-year experience in allergy work-up",
volume = "27",
number = "5",
pages = "533-538",
doi = "10.1111/pai.12565"
}

Atanasković-Marković, M., Gaeta, F., Međo, B., Gavrović-Jankulović, M., Ćirković-Veličković, T., Tmušić, V.,& Romano, A.. (2016). Non-immediate hypersensitivity reactions to beta-lactam antibiotics in children - our 10-year experience in allergy work-up. in Pediatric Allergy and Immunology
Wiley, Hoboken., 27(5), 533-538.
https://doi.org/10.1111/pai.12565

Atanasković-Marković M, Gaeta F, Međo B, Gavrović-Jankulović M, Ćirković-Veličković T, Tmušić V, Romano A. Non-immediate hypersensitivity reactions to beta-lactam antibiotics in children - our 10-year experience in allergy work-up. in Pediatric Allergy and Immunology. 2016;27(5):533-538.
doi:10.1111/pai.12565 .

Atanasković-Marković, Marina, Gaeta, Francesco, Međo, Biljana, Gavrović-Jankulović, Marija, Ćirković-Veličković, Tanja, Tmušić, Vladimir, Romano, Antonino, "Non-immediate hypersensitivity reactions to beta-lactam antibiotics in children - our 10-year experience in allergy work-up" in Pediatric Allergy and Immunology, 27, no. 5 (2016):533-538,
https://doi.org/10.1111/pai.12565 . .

TY  - JOUR
AU  - Ognjenović, Jana
AU  - Stojadinović, Marija M.
AU  - Milčić, Miloš K.
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Stambolić, Ivan
AU  - Atanasković-Marković, Marina
AU  - Simonovic, Miljan
AU  - Ćirković-Veličković, Tanja
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1820
AB  - Polyphenols, the potent plant secondary metabolites, have beneficial effects on human health, but the mechanism(s) by which these effects are exerted is not well understood. Here, we present the detailed analysis of the interactions between the major green tea catechin, epigallo-catechin 3-gallate (EGCG), and the major dietary protein and allergen, ovalbumin (OVA). We show that EGCG binds to the pocket that partly overlaps with the previously identified IgE-binding region in OVA, and that this interaction induces structural changes in the allergen. Moreover, our ex vivo studies reveal that OVA binds IgE and stimulates degranulation of basophils, and that its uptake by monocytes proceeds at a slower rate in the presence of EGCG. This study provides further evidence in support of the proposed mechanism by which EGCG interactions with the food allergens contribute to its diverse biological activities and may impair antigen uptake by antigen-presenting cells. (C) 2014 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Interactions of epigallo-catechin 3-gallate and ovalbumin, the major allergen of egg white
VL  - 164
SP  - 36
EP  - 43
DO  - 10.1016/j.foodchem.2014.05.005
ER  - 

@article{
author = "Ognjenović, Jana and Stojadinović, Marija M. and Milčić, Miloš K. and Apostolović, Danijela and Mihailović-Vesić, Jelena and Stambolić, Ivan and Atanasković-Marković, Marina and Simonovic, Miljan and Ćirković-Veličković, Tanja",
year = "2014",
abstract = "Polyphenols, the potent plant secondary metabolites, have beneficial effects on human health, but the mechanism(s) by which these effects are exerted is not well understood. Here, we present the detailed analysis of the interactions between the major green tea catechin, epigallo-catechin 3-gallate (EGCG), and the major dietary protein and allergen, ovalbumin (OVA). We show that EGCG binds to the pocket that partly overlaps with the previously identified IgE-binding region in OVA, and that this interaction induces structural changes in the allergen. Moreover, our ex vivo studies reveal that OVA binds IgE and stimulates degranulation of basophils, and that its uptake by monocytes proceeds at a slower rate in the presence of EGCG. This study provides further evidence in support of the proposed mechanism by which EGCG interactions with the food allergens contribute to its diverse biological activities and may impair antigen uptake by antigen-presenting cells. (C) 2014 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Interactions of epigallo-catechin 3-gallate and ovalbumin, the major allergen of egg white",
volume = "164",
pages = "36-43",
doi = "10.1016/j.foodchem.2014.05.005"
}

Ognjenović, J., Stojadinović, M. M., Milčić, M. K., Apostolović, D., Mihailović-Vesić, J., Stambolić, I., Atanasković-Marković, M., Simonovic, M.,& Ćirković-Veličković, T.. (2014). Interactions of epigallo-catechin 3-gallate and ovalbumin, the major allergen of egg white. in Food Chemistry
Elsevier Sci Ltd, Oxford., 164, 36-43.
https://doi.org/10.1016/j.foodchem.2014.05.005

Ognjenović J, Stojadinović MM, Milčić MK, Apostolović D, Mihailović-Vesić J, Stambolić I, Atanasković-Marković M, Simonovic M, Ćirković-Veličković T. Interactions of epigallo-catechin 3-gallate and ovalbumin, the major allergen of egg white. in Food Chemistry. 2014;164:36-43.
doi:10.1016/j.foodchem.2014.05.005 .

Ognjenović, Jana, Stojadinović, Marija M., Milčić, Miloš K., Apostolović, Danijela, Mihailović-Vesić, Jelena, Stambolić, Ivan, Atanasković-Marković, Marina, Simonovic, Miljan, Ćirković-Veličković, Tanja, "Interactions of epigallo-catechin 3-gallate and ovalbumin, the major allergen of egg white" in Food Chemistry, 164 (2014):36-43,
https://doi.org/10.1016/j.foodchem.2014.05.005 . .

TY  - JOUR
AU  - Atanasković-Marković, Marina
AU  - Međo, Biljana
AU  - Gavrović-Jankulović, Marija
AU  - Ćirković-Veličković, Tanja
AU  - Nikolić, Dimitrije
AU  - Nestorovic, Branimir
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1412
PB  - Wiley, Hoboken
T2  - Pediatric Allergy and Immunology
T1  - Stevens-Johnson syndrome and toxic epidermal necrolysis in children
VL  - 24
IS  - 7
SP  - 645
EP  - 649
DO  - 10.1111/pai.12121
ER  - 

@article{
author = "Atanasković-Marković, Marina and Međo, Biljana and Gavrović-Jankulović, Marija and Ćirković-Veličković, Tanja and Nikolić, Dimitrije and Nestorovic, Branimir",
year = "2013",
publisher = "Wiley, Hoboken",
journal = "Pediatric Allergy and Immunology",
title = "Stevens-Johnson syndrome and toxic epidermal necrolysis in children",
volume = "24",
number = "7",
pages = "645-649",
doi = "10.1111/pai.12121"
}

Atanasković-Marković, M., Međo, B., Gavrović-Jankulović, M., Ćirković-Veličković, T., Nikolić, D.,& Nestorovic, B.. (2013). Stevens-Johnson syndrome and toxic epidermal necrolysis in children. in Pediatric Allergy and Immunology
Wiley, Hoboken., 24(7), 645-649.
https://doi.org/10.1111/pai.12121

Atanasković-Marković M, Međo B, Gavrović-Jankulović M, Ćirković-Veličković T, Nikolić D, Nestorovic B. Stevens-Johnson syndrome and toxic epidermal necrolysis in children. in Pediatric Allergy and Immunology. 2013;24(7):645-649.
doi:10.1111/pai.12121 .

Atanasković-Marković, Marina, Međo, Biljana, Gavrović-Jankulović, Marija, Ćirković-Veličković, Tanja, Nikolić, Dimitrije, Nestorovic, Branimir, "Stevens-Johnson syndrome and toxic epidermal necrolysis in children" in Pediatric Allergy and Immunology, 24, no. 7 (2013):645-649,
https://doi.org/10.1111/pai.12121 . .

TY  - CONF
AU  - Ognjenović, J.
AU  - Mihajlovic, L.
AU  - Stanić-Vučinić, Dragana
AU  - Atanasković-Marković, Marina
AU  - Burazer, Lidija M.
AU  - Ćirković-Veličković, Tanja
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1544
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - Green tea catechins suppress antigen-specific proliferation and cytokine secretion but elevate intracellular oxidative stress in peripheral blood mononuclear cells of pollen allergic individuals
VL  - 67
SP  - 638
EP  - 639
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1544
ER  - 

@conference{
author = "Ognjenović, J. and Mihajlovic, L. and Stanić-Vučinić, Dragana and Atanasković-Marković, Marina and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2012",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Green tea catechins suppress antigen-specific proliferation and cytokine secretion but elevate intracellular oxidative stress in peripheral blood mononuclear cells of pollen allergic individuals",
volume = "67",
pages = "638-639",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1544"
}

Ognjenović, J., Mihajlovic, L., Stanić-Vučinić, D., Atanasković-Marković, M., Burazer, L. M.,& Ćirković-Veličković, T.. (2012). Green tea catechins suppress antigen-specific proliferation and cytokine secretion but elevate intracellular oxidative stress in peripheral blood mononuclear cells of pollen allergic individuals. in Allergy
Wiley-Blackwell, Hoboken., 67, 638-639.
https://hdl.handle.net/21.15107/rcub_cherry_1544

Ognjenović J, Mihajlovic L, Stanić-Vučinić D, Atanasković-Marković M, Burazer LM, Ćirković-Veličković T. Green tea catechins suppress antigen-specific proliferation and cytokine secretion but elevate intracellular oxidative stress in peripheral blood mononuclear cells of pollen allergic individuals. in Allergy. 2012;67:638-639.
https://hdl.handle.net/21.15107/rcub_cherry_1544 .

Ognjenović, J., Mihajlovic, L., Stanić-Vučinić, Dragana, Atanasković-Marković, Marina, Burazer, Lidija M., Ćirković-Veličković, Tanja, "Green tea catechins suppress antigen-specific proliferation and cytokine secretion but elevate intracellular oxidative stress in peripheral blood mononuclear cells of pollen allergic individuals" in Allergy, 67 (2012):638-639,
https://hdl.handle.net/21.15107/rcub_cherry_1544 .

TY  - JOUR
AU  - Stanić-Vučinić, Dragana
AU  - Stojadinović, Marija M.
AU  - Atanasković-Marković, Marina
AU  - Ognjenović, Jana
AU  - Gronlund, Hans
AU  - van Hage, Marianne
AU  - Lantto, Raija
AU  - Sancho, Ana I.
AU  - Ćirković-Veličković, Tanja
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1561
AB  - Scope The aim of this work was to investigate the effects of high-intensity ultrasound (sonication), on the structure and allergenicity of the major cow's milk allergen, beta-lactoglobulin (BLG). Methods and results Structural changes upon sonication of BLG were monitored by circular dichroism spectroscopy, tryptophan emission fluorescence, hydrophobic dye and retinol binding, as well as digestibility and phenol-oxidase cross-linking capacity. Allergenicity was monitored in individual patients sera, basophil activation test, and skin prick testing in 41 cow's milk allergy patients. Uncontrolled local temperature changes induced modifications in BLG secondary structure accompanied by formation of dimers, trimers, and oligomers of BLG that were more digestible by pepsin and had reduced retinol binding. Controlled temperature conditions induced changes in secondary structure of BLG without causing formation of oligomers, or changing protein's capacity to bind retinol. Both sonicated forms of BLG had more exposed hydrophobic surfaces than native BLG and underwent facilitated cross-linking reaction with phenol-oxidase. Sonication had a minor effect on IgE-binding properties of BLG. Conclusion Sonication-induced structural changes in major whey allergen were not clinically significant in cow's milk allergy patients. Ultrasound can be a safe procedure for dairy processing as it maintains the nutritional value and does not increase allergenic potential of BLG.
PB  - Wiley-Blackwell, Hoboken
T2  - Molecular Nutrition and Food Research
T1  - Structural changes and allergenic properties of beta-lactoglobulin upon exposure to high-intensity ultrasound
VL  - 56
IS  - 12
SP  - 1894
EP  - 1905
DO  - 10.1002/mnfr.201200179
ER  - 

@article{
author = "Stanić-Vučinić, Dragana and Stojadinović, Marija M. and Atanasković-Marković, Marina and Ognjenović, Jana and Gronlund, Hans and van Hage, Marianne and Lantto, Raija and Sancho, Ana I. and Ćirković-Veličković, Tanja",
year = "2012",
abstract = "Scope The aim of this work was to investigate the effects of high-intensity ultrasound (sonication), on the structure and allergenicity of the major cow's milk allergen, beta-lactoglobulin (BLG). Methods and results Structural changes upon sonication of BLG were monitored by circular dichroism spectroscopy, tryptophan emission fluorescence, hydrophobic dye and retinol binding, as well as digestibility and phenol-oxidase cross-linking capacity. Allergenicity was monitored in individual patients sera, basophil activation test, and skin prick testing in 41 cow's milk allergy patients. Uncontrolled local temperature changes induced modifications in BLG secondary structure accompanied by formation of dimers, trimers, and oligomers of BLG that were more digestible by pepsin and had reduced retinol binding. Controlled temperature conditions induced changes in secondary structure of BLG without causing formation of oligomers, or changing protein's capacity to bind retinol. Both sonicated forms of BLG had more exposed hydrophobic surfaces than native BLG and underwent facilitated cross-linking reaction with phenol-oxidase. Sonication had a minor effect on IgE-binding properties of BLG. Conclusion Sonication-induced structural changes in major whey allergen were not clinically significant in cow's milk allergy patients. Ultrasound can be a safe procedure for dairy processing as it maintains the nutritional value and does not increase allergenic potential of BLG.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Molecular Nutrition and Food Research",
title = "Structural changes and allergenic properties of beta-lactoglobulin upon exposure to high-intensity ultrasound",
volume = "56",
number = "12",
pages = "1894-1905",
doi = "10.1002/mnfr.201200179"
}

Stanić-Vučinić, D., Stojadinović, M. M., Atanasković-Marković, M., Ognjenović, J., Gronlund, H., van Hage, M., Lantto, R., Sancho, A. I.,& Ćirković-Veličković, T.. (2012). Structural changes and allergenic properties of beta-lactoglobulin upon exposure to high-intensity ultrasound. in Molecular Nutrition and Food Research
Wiley-Blackwell, Hoboken., 56(12), 1894-1905.
https://doi.org/10.1002/mnfr.201200179

Stanić-Vučinić D, Stojadinović MM, Atanasković-Marković M, Ognjenović J, Gronlund H, van Hage M, Lantto R, Sancho AI, Ćirković-Veličković T. Structural changes and allergenic properties of beta-lactoglobulin upon exposure to high-intensity ultrasound. in Molecular Nutrition and Food Research. 2012;56(12):1894-1905.
doi:10.1002/mnfr.201200179 .

Stanić-Vučinić, Dragana, Stojadinović, Marija M., Atanasković-Marković, Marina, Ognjenović, Jana, Gronlund, Hans, van Hage, Marianne, Lantto, Raija, Sancho, Ana I., Ćirković-Veličković, Tanja, "Structural changes and allergenic properties of beta-lactoglobulin upon exposure to high-intensity ultrasound" in Molecular Nutrition and Food Research, 56, no. 12 (2012):1894-1905,
https://doi.org/10.1002/mnfr.201200179 . .

TY  - JOUR
AU  - Abughren, Mohamed
AU  - Popović, Milica M.
AU  - Dimitrijevic, Rajna
AU  - Burazer, Lidija M.
AU  - Grozdanović, Milica
AU  - Atanasković-Marković, Marina
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1246
AB  - For the heterologous production of a banana glucanase in Escherichia coli, its gene (GenBank GQ268963) was cloned into a pGEX-4T expression vector as a fusion protein with glutathione-S-transferase (GST). BL21 cells transformed with the GST-Mus a 5 construct were employed for production of the protein induced by 1 mM isopropyl-beta-D-thiogalactopyranoside (IPTG). The conditions for protein expression were optimized by varying the temperature (25, 30 and 37 C) and duration of protein expression (3, 6 and 12 h). The level of protein production was analyzed by densitometry of the sodium dodecyl sulfate-polyacrylamide gel (SDS-PAG) after electrophoretic resolution of the respective cell lysates. The optimal protein expression for downstream processing was obtained after 12 h of cell growth at 25 degrees C upon addition of IPTG. Recombinant GST-Mus a 5 purified by glutathione affinity chromatography revealed a molecular mass of about 60 kDa. The IgE and IgG reactivity of the rGST-Mus a 5 was confirmed by dot blot analysis with sera of individual patients from subjects with banana allergy and polyclonal rabbit antibodies against banana extract, respectively. The purified recombinant glucanase is a potential candidate for banana allergy diagnosis.
AB  - Za potrebe proizvodnje u Escherichia coli gen glukanaze iz banane (GenBank GQ268963) je ukloniran u ekspresioni vektor pGEX-4T sa glutation-S-transferazom (GST). Proizvodnja ovog proteina u ćelijama je indukovana 1 mM izopropil-β-D-tiogalaktopiranozidom (IPTG). Uslovi za ekspresiju proteina su optimizovani variranjem temperature (25, 30 i 37°C) i dužine trajanja proteinske sinteze (3, 6 i 12 h). Nivo proizvodnje proteina je analiziran denzitometrijom SDS-PA gela nakon elektroforetskog razdvajanja ćelijskih lizata. Optimalna proizvodnja proteina za njegovo dalje procesovanje je dobijena gajenjem ćelija nakon dodatka IPTG na 25°C tokom 12 h. Rekombinantni GST-Mus a 5 prečišćen afinitetnom hromatografijom sa glutationom pokazuje molekulsku masu od 60 kDa. IgE i IgG reaktivnost izolovane glukanaze potvrđena je u 'dot blot' sa pojedinačnim serumima osoba alergičnih na bananu, i sa poliklonskim zečijim antitelima na ekstrakt banane, redom. Prečišćena rekombinantna glukanaza je potencijalan kandidat za dijagnozu alergije na bananu.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Optimization of the heterologous expression of banana glucanase in Escherichia coli
T1  - Optimizacija heterologe proizvodnje glukanaze iz banane u E. coli
VL  - 77
IS  - 1
SP  - 43
EP  - 52
DO  - 10.2298/JSC110309158A
ER  - 

@article{
author = "Abughren, Mohamed and Popović, Milica M. and Dimitrijevic, Rajna and Burazer, Lidija M. and Grozdanović, Milica and Atanasković-Marković, Marina and Gavrović-Jankulović, Marija",
year = "2012",
abstract = "For the heterologous production of a banana glucanase in Escherichia coli, its gene (GenBank GQ268963) was cloned into a pGEX-4T expression vector as a fusion protein with glutathione-S-transferase (GST). BL21 cells transformed with the GST-Mus a 5 construct were employed for production of the protein induced by 1 mM isopropyl-beta-D-thiogalactopyranoside (IPTG). The conditions for protein expression were optimized by varying the temperature (25, 30 and 37 C) and duration of protein expression (3, 6 and 12 h). The level of protein production was analyzed by densitometry of the sodium dodecyl sulfate-polyacrylamide gel (SDS-PAG) after electrophoretic resolution of the respective cell lysates. The optimal protein expression for downstream processing was obtained after 12 h of cell growth at 25 degrees C upon addition of IPTG. Recombinant GST-Mus a 5 purified by glutathione affinity chromatography revealed a molecular mass of about 60 kDa. The IgE and IgG reactivity of the rGST-Mus a 5 was confirmed by dot blot analysis with sera of individual patients from subjects with banana allergy and polyclonal rabbit antibodies against banana extract, respectively. The purified recombinant glucanase is a potential candidate for banana allergy diagnosis., Za potrebe proizvodnje u Escherichia coli gen glukanaze iz banane (GenBank GQ268963) je ukloniran u ekspresioni vektor pGEX-4T sa glutation-S-transferazom (GST). Proizvodnja ovog proteina u ćelijama je indukovana 1 mM izopropil-β-D-tiogalaktopiranozidom (IPTG). Uslovi za ekspresiju proteina su optimizovani variranjem temperature (25, 30 i 37°C) i dužine trajanja proteinske sinteze (3, 6 i 12 h). Nivo proizvodnje proteina je analiziran denzitometrijom SDS-PA gela nakon elektroforetskog razdvajanja ćelijskih lizata. Optimalna proizvodnja proteina za njegovo dalje procesovanje je dobijena gajenjem ćelija nakon dodatka IPTG na 25°C tokom 12 h. Rekombinantni GST-Mus a 5 prečišćen afinitetnom hromatografijom sa glutationom pokazuje molekulsku masu od 60 kDa. IgE i IgG reaktivnost izolovane glukanaze potvrđena je u 'dot blot' sa pojedinačnim serumima osoba alergičnih na bananu, i sa poliklonskim zečijim antitelima na ekstrakt banane, redom. Prečišćena rekombinantna glukanaza je potencijalan kandidat za dijagnozu alergije na bananu.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Optimization of the heterologous expression of banana glucanase in Escherichia coli, Optimizacija heterologe proizvodnje glukanaze iz banane u E. coli",
volume = "77",
number = "1",
pages = "43-52",
doi = "10.2298/JSC110309158A"
}

Abughren, M., Popović, M. M., Dimitrijevic, R., Burazer, L. M., Grozdanović, M., Atanasković-Marković, M.,& Gavrović-Jankulović, M.. (2012). Optimization of the heterologous expression of banana glucanase in Escherichia coli. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 77(1), 43-52.
https://doi.org/10.2298/JSC110309158A

Abughren M, Popović MM, Dimitrijevic R, Burazer LM, Grozdanović M, Atanasković-Marković M, Gavrović-Jankulović M. Optimization of the heterologous expression of banana glucanase in Escherichia coli. in Journal of the Serbian Chemical Society. 2012;77(1):43-52.
doi:10.2298/JSC110309158A .

Abughren, Mohamed, Popović, Milica M., Dimitrijevic, Rajna, Burazer, Lidija M., Grozdanović, Milica, Atanasković-Marković, Marina, Gavrović-Jankulović, Marija, "Optimization of the heterologous expression of banana glucanase in Escherichia coli" in Journal of the Serbian Chemical Society, 77, no. 1 (2012):43-52,
https://doi.org/10.2298/JSC110309158A . .

TY  - JOUR
AU  - Abughren, Mohamed
AU  - Popović, Milica M.
AU  - Dimitrijevic, Rajna
AU  - Burazer, Lidija M.
AU  - Grozdanović, Milica
AU  - Atanasković-Marković, Marina
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1259
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Optimization of the heterologous expression of banana glucanase in Escherichia coli (vol 77, pg 43, 2012)
VL  - 77
IS  - 2
SP  - 257
EP  - 258
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1259
ER  - 

@article{
author = "Abughren, Mohamed and Popović, Milica M. and Dimitrijevic, Rajna and Burazer, Lidija M. and Grozdanović, Milica and Atanasković-Marković, Marina and Gavrović-Jankulović, Marija",
year = "2012",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Optimization of the heterologous expression of banana glucanase in Escherichia coli (vol 77, pg 43, 2012)",
volume = "77",
number = "2",
pages = "257-258",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1259"
}

Abughren, M., Popović, M. M., Dimitrijevic, R., Burazer, L. M., Grozdanović, M., Atanasković-Marković, M.,& Gavrović-Jankulović, M.. (2012). Optimization of the heterologous expression of banana glucanase in Escherichia coli (vol 77, pg 43, 2012). in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 77(2), 257-258.
https://hdl.handle.net/21.15107/rcub_cherry_1259

Abughren M, Popović MM, Dimitrijevic R, Burazer LM, Grozdanović M, Atanasković-Marković M, Gavrović-Jankulović M. Optimization of the heterologous expression of banana glucanase in Escherichia coli (vol 77, pg 43, 2012). in Journal of the Serbian Chemical Society. 2012;77(2):257-258.
https://hdl.handle.net/21.15107/rcub_cherry_1259 .

Abughren, Mohamed, Popović, Milica M., Dimitrijevic, Rajna, Burazer, Lidija M., Grozdanović, Milica, Atanasković-Marković, Marina, Gavrović-Jankulović, Marija, "Optimization of the heterologous expression of banana glucanase in Escherichia coli (vol 77, pg 43, 2012)" in Journal of the Serbian Chemical Society, 77, no. 2 (2012):257-258,
https://hdl.handle.net/21.15107/rcub_cherry_1259 .

TY  - JOUR
AU  - Aleksić, Ivana
AU  - Popović, Milica M.
AU  - Dimitrijevic, Rajna
AU  - Anđelković, Uroš
AU  - Vassilopoulou, Emilia
AU  - Sinaniotis, Athanassios
AU  - Atanasković-Marković, Marina
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Papadopoulos, Nikolaos G.
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1268
AB  - Scope Banana fruit has become an important cause of fruit allergy in the recent years. Among the five registered IUIS allergens, Mus a 1 and Mus a 2 have been characterized in detail. In this study, molecular characterization and evaluation of the allergenic properties of beta-1,3-glucanase from banana (Musa acuminata), denoted as Mus a 5, were performed Methods and results: The gene of Mus a 5 was cloned and sequenced. The obtained cDNA revealed a novel Mus a 5 isoform with an open reading frame encoding a protein of 340 amino acids comprising a putative signal peptide of 28 amino acid residues. By MALDI-TOF analysis Mus a 5 isolated from banana fruit revealed a molecular mass of 33 451 +/- 67 Da. Two Mus a 5 isoforms (pI 7.7 and 8.0) were detected by 2D immunoblot with an identical N-terminal sequence. By mass fingerprint, 76 and 83% of the primary structure was confirmed for the two mature Mus a 5 isoforms, respectively. IgE reactivity to Mus a 5 was found in 74% of patients sensitized to banana fruit. Upregulation of basophil activation markers CD63 and CD203c was achieved with Mus a 5 in a concentration-dependent manner. Conclusion: Mus a 5 is a functional allergen and a candidate for the component-resolved allergy diagnosis of banana allergy.
PB  - Wiley-Blackwell, Malden
T2  - Molecular Nutrition and Food Research
T1  - Molecular and immunological characterization of Mus a 5 allergen from banana fruit
VL  - 56
IS  - 3
SP  - 446
EP  - 453
DO  - 10.1002/mnfr.201100541
ER  - 

@article{
author = "Aleksić, Ivana and Popović, Milica M. and Dimitrijevic, Rajna and Anđelković, Uroš and Vassilopoulou, Emilia and Sinaniotis, Athanassios and Atanasković-Marković, Marina and Lindner, Buko and Petersen, Arnd and Papadopoulos, Nikolaos G. and Gavrović-Jankulović, Marija",
year = "2012",
abstract = "Scope Banana fruit has become an important cause of fruit allergy in the recent years. Among the five registered IUIS allergens, Mus a 1 and Mus a 2 have been characterized in detail. In this study, molecular characterization and evaluation of the allergenic properties of beta-1,3-glucanase from banana (Musa acuminata), denoted as Mus a 5, were performed Methods and results: The gene of Mus a 5 was cloned and sequenced. The obtained cDNA revealed a novel Mus a 5 isoform with an open reading frame encoding a protein of 340 amino acids comprising a putative signal peptide of 28 amino acid residues. By MALDI-TOF analysis Mus a 5 isolated from banana fruit revealed a molecular mass of 33 451 +/- 67 Da. Two Mus a 5 isoforms (pI 7.7 and 8.0) were detected by 2D immunoblot with an identical N-terminal sequence. By mass fingerprint, 76 and 83% of the primary structure was confirmed for the two mature Mus a 5 isoforms, respectively. IgE reactivity to Mus a 5 was found in 74% of patients sensitized to banana fruit. Upregulation of basophil activation markers CD63 and CD203c was achieved with Mus a 5 in a concentration-dependent manner. Conclusion: Mus a 5 is a functional allergen and a candidate for the component-resolved allergy diagnosis of banana allergy.",
publisher = "Wiley-Blackwell, Malden",
journal = "Molecular Nutrition and Food Research",
title = "Molecular and immunological characterization of Mus a 5 allergen from banana fruit",
volume = "56",
number = "3",
pages = "446-453",
doi = "10.1002/mnfr.201100541"
}

Aleksić, I., Popović, M. M., Dimitrijevic, R., Anđelković, U., Vassilopoulou, E., Sinaniotis, A., Atanasković-Marković, M., Lindner, B., Petersen, A., Papadopoulos, N. G.,& Gavrović-Jankulović, M.. (2012). Molecular and immunological characterization of Mus a 5 allergen from banana fruit. in Molecular Nutrition and Food Research
Wiley-Blackwell, Malden., 56(3), 446-453.
https://doi.org/10.1002/mnfr.201100541

Aleksić I, Popović MM, Dimitrijevic R, Anđelković U, Vassilopoulou E, Sinaniotis A, Atanasković-Marković M, Lindner B, Petersen A, Papadopoulos NG, Gavrović-Jankulović M. Molecular and immunological characterization of Mus a 5 allergen from banana fruit. in Molecular Nutrition and Food Research. 2012;56(3):446-453.
doi:10.1002/mnfr.201100541 .

Aleksić, Ivana, Popović, Milica M., Dimitrijevic, Rajna, Anđelković, Uroš, Vassilopoulou, Emilia, Sinaniotis, Athanassios, Atanasković-Marković, Marina, Lindner, Buko, Petersen, Arnd, Papadopoulos, Nikolaos G., Gavrović-Jankulović, Marija, "Molecular and immunological characterization of Mus a 5 allergen from banana fruit" in Molecular Nutrition and Food Research, 56, no. 3 (2012):446-453,
https://doi.org/10.1002/mnfr.201100541 . .

TY  - JOUR
AU  - Grozdanović, Milica
AU  - Popović, Milica M.
AU  - Polović, Natalija
AU  - Burazer, Lidija M.
AU  - Vučković, Olga
AU  - Atanasković-Marković, Marina
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1286
AB  - Actinidin, an abundant cysteine protease from kiwifruit, is a specific biomarker of isolated allergy to kiwifruit. This study evaluates the IgE-binding properties of biologically active and thermally inactivated actinidin. Employing two different activity assays (caseinolytic assay and zymogram with gelatin) we showed that actinidin obtained from kiwifruit extract under native conditions represents a mixture of inactive and active enzyme. The structural integrity of actinidin was confirmed by SDS-PAGE. Edman degradation, mass fingerprint and Western blot with polyclonal antibodies. Although it was capable of inducing positive skin prick test reactions, we failed to detect IgE reactivity of active actinidin in Western blot with patient sera. Thermally inactivated actinidin exhibited IgE reactivity both in vivo and in vitro, indicating that heat processed kiwifruit products may induce clinical reactivity. These findings imply that apart from the allergenic epitopes on its surface, actinidin also contains hidden epitopes inside the protein which become accessible to IgE upon thermal treatment. (C) 2011 Elsevier Ltd. All rights reserved.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Food and Chemical Toxicology
T1  - Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy
VL  - 50
IS  - 3-4
SP  - 1013
EP  - 1018
DO  - 10.1016/j.fct.2011.12.030
ER  - 

@article{
author = "Grozdanović, Milica and Popović, Milica M. and Polović, Natalija and Burazer, Lidija M. and Vučković, Olga and Atanasković-Marković, Marina and Lindner, Buko and Petersen, Arnd and Gavrović-Jankulović, Marija",
year = "2012",
abstract = "Actinidin, an abundant cysteine protease from kiwifruit, is a specific biomarker of isolated allergy to kiwifruit. This study evaluates the IgE-binding properties of biologically active and thermally inactivated actinidin. Employing two different activity assays (caseinolytic assay and zymogram with gelatin) we showed that actinidin obtained from kiwifruit extract under native conditions represents a mixture of inactive and active enzyme. The structural integrity of actinidin was confirmed by SDS-PAGE. Edman degradation, mass fingerprint and Western blot with polyclonal antibodies. Although it was capable of inducing positive skin prick test reactions, we failed to detect IgE reactivity of active actinidin in Western blot with patient sera. Thermally inactivated actinidin exhibited IgE reactivity both in vivo and in vitro, indicating that heat processed kiwifruit products may induce clinical reactivity. These findings imply that apart from the allergenic epitopes on its surface, actinidin also contains hidden epitopes inside the protein which become accessible to IgE upon thermal treatment. (C) 2011 Elsevier Ltd. All rights reserved.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Food and Chemical Toxicology",
title = "Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy",
volume = "50",
number = "3-4",
pages = "1013-1018",
doi = "10.1016/j.fct.2011.12.030"
}

Grozdanović, M., Popović, M. M., Polović, N., Burazer, L. M., Vučković, O., Atanasković-Marković, M., Lindner, B., Petersen, A.,& Gavrović-Jankulović, M.. (2012). Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy. in Food and Chemical Toxicology
Pergamon-Elsevier Science Ltd, Oxford., 50(3-4), 1013-1018.
https://doi.org/10.1016/j.fct.2011.12.030

Grozdanović M, Popović MM, Polović N, Burazer LM, Vučković O, Atanasković-Marković M, Lindner B, Petersen A, Gavrović-Jankulović M. Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy. in Food and Chemical Toxicology. 2012;50(3-4):1013-1018.
doi:10.1016/j.fct.2011.12.030 .

Grozdanović, Milica, Popović, Milica M., Polović, Natalija, Burazer, Lidija M., Vučković, Olga, Atanasković-Marković, Marina, Lindner, Buko, Petersen, Arnd, Gavrović-Jankulović, Marija, "Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy" in Food and Chemical Toxicology, 50, no. 3-4 (2012):1013-1018,
https://doi.org/10.1016/j.fct.2011.12.030 . .

TY  - JOUR
AU  - Atanasković-Marković, Marina
AU  - Gaeta, Francesco
AU  - Gavrović-Jankulović, Marija
AU  - Ćirković-Veličković, Tanja
AU  - Valluzzi, Rocco Luigi
AU  - Romano, Antonino
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1560
AB  - Background Multiple drug hypersensitivity (MDH) has been defined as a hypersensitivity to two or more chemically different drugs. Two types of MDH have been reported: the first one, which develops to different drugs administered simultaneously and the second type, in which sensitizations develop sequentially. In children, studies which diagnose MDH on the basis of positive allergologic tests to 2 or more chemically different drugs are lacking. Methods We conducted a prospective study evaluating children with histories of MDH by skin tests, patch tests, serum-specific IgE assays, and drug provocation tests. Results A MDH was diagnosed in 7 (2.5%) of the 279 children evaluated who completed the study. The responsible drugs were beta-lactams (penicillins and cephalosporins) in 5 episodes, ibuprofen and anticonvulsants in 3, and erythromycin, fentanyl, methylprednisolone, and cotrimoxazole in 1. Sensitivity to 2 chemically different drugs was diagnosed in 6 children and to 3 drugs in 1 child. Two of the 7 children presented the first type of MDH, whereas 5 displayed the second one. Conclusions MDH can occur in children, even to drugs other than antibiotics. It is crucial to evaluate children with histories of MDH using both in vivo and in vitro allergologic tests, including challenges. In fact, such approach allows the physician to confirm the diagnosis of MDH in a small percentage of children with histories of MDH, as well as to rule it out in the great majority of them.
PB  - Wiley-Blackwell, Hoboken
T2  - Pediatric Allergy and Immunology
T1  - Diagnosing multiple drug hypersensitivity in children
VL  - 23
IS  - 8
SP  - 785
EP  - 791
DO  - 10.1111/pai.12020
ER  - 

@article{
author = "Atanasković-Marković, Marina and Gaeta, Francesco and Gavrović-Jankulović, Marija and Ćirković-Veličković, Tanja and Valluzzi, Rocco Luigi and Romano, Antonino",
year = "2012",
abstract = "Background Multiple drug hypersensitivity (MDH) has been defined as a hypersensitivity to two or more chemically different drugs. Two types of MDH have been reported: the first one, which develops to different drugs administered simultaneously and the second type, in which sensitizations develop sequentially. In children, studies which diagnose MDH on the basis of positive allergologic tests to 2 or more chemically different drugs are lacking. Methods We conducted a prospective study evaluating children with histories of MDH by skin tests, patch tests, serum-specific IgE assays, and drug provocation tests. Results A MDH was diagnosed in 7 (2.5%) of the 279 children evaluated who completed the study. The responsible drugs were beta-lactams (penicillins and cephalosporins) in 5 episodes, ibuprofen and anticonvulsants in 3, and erythromycin, fentanyl, methylprednisolone, and cotrimoxazole in 1. Sensitivity to 2 chemically different drugs was diagnosed in 6 children and to 3 drugs in 1 child. Two of the 7 children presented the first type of MDH, whereas 5 displayed the second one. Conclusions MDH can occur in children, even to drugs other than antibiotics. It is crucial to evaluate children with histories of MDH using both in vivo and in vitro allergologic tests, including challenges. In fact, such approach allows the physician to confirm the diagnosis of MDH in a small percentage of children with histories of MDH, as well as to rule it out in the great majority of them.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Pediatric Allergy and Immunology",
title = "Diagnosing multiple drug hypersensitivity in children",
volume = "23",
number = "8",
pages = "785-791",
doi = "10.1111/pai.12020"
}

Atanasković-Marković, M., Gaeta, F., Gavrović-Jankulović, M., Ćirković-Veličković, T., Valluzzi, R. L.,& Romano, A.. (2012). Diagnosing multiple drug hypersensitivity in children. in Pediatric Allergy and Immunology
Wiley-Blackwell, Hoboken., 23(8), 785-791.
https://doi.org/10.1111/pai.12020

Atanasković-Marković M, Gaeta F, Gavrović-Jankulović M, Ćirković-Veličković T, Valluzzi RL, Romano A. Diagnosing multiple drug hypersensitivity in children. in Pediatric Allergy and Immunology. 2012;23(8):785-791.
doi:10.1111/pai.12020 .

Atanasković-Marković, Marina, Gaeta, Francesco, Gavrović-Jankulović, Marija, Ćirković-Veličković, Tanja, Valluzzi, Rocco Luigi, Romano, Antonino, "Diagnosing multiple drug hypersensitivity in children" in Pediatric Allergy and Immunology, 23, no. 8 (2012):785-791,
https://doi.org/10.1111/pai.12020 . .

TY  - JOUR
AU  - Atanasković-Marković, Marina
AU  - Gavrović-Jankulović, Marija
AU  - Jankovic, Srdja
AU  - Blagojević, Gordan
AU  - Ćirković-Veličković, Tanja
AU  - Milojevic, Irina
AU  - Simic, Dusica
AU  - Nestorovic, Branimir
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1299
AB  - Introduction In spite of the wide usage of corticosteroids for the treatment of a plethora of diseases, sometimes they can induce immediate hypersensitivity reactions, which are however uncommon. Case Outline We report a case of immediate allergic reaction induced by intravenous methylprednisolone given before operation for surgical repair of an arm contracture as a sequel of burns, which the child had tolerated a month before. Six weeks later the patient repeated the anaphylactic reaction during skin testing to methylprednisolone. In addition, basophile activation test with methylprednisolone (BAT) was positive. Conclusion This case report describes a patient who experienced intraoperative anaphylaxis and anaphylactic reaction induced by skin testing. This is the first report on induction of both anaphylactic reactions by methylprednisolone in the same child. Clinical findings, positive BAT and positive skin tests with methylprednisolone imply that the child developed type-I hypersensitivity. The lack of cross-reactivity with other corticosteroids emphasizes that the reactions were caused by the steroid molecule.
AB  - Uvod. Uprkos širokoj primeni kortikosteroida u lečenju od različitih bolesti, oni ponekad mogu izazvati ranu alergijsku reakciju. Prikaz bolesnika. Kod dvanaestogodišnjeg dečaka došlo je do rane alergijske reakcije izazvane intravenskom primenom metilprednizolona neposredno pre hirurške intervencije, tačnije, korekcije kontrakture šake koja se javila kao komplikacija opekotine. Mesec dana pre pojave alergijske reakcije dete je primalo metilprednizolon i dobro ga podnosilo. Šest nedelja posle operacije ponovo se javila anafilaktička reakcija tokom kožnog testiranja metilprednizolonom. Primenjen je i test aktivacije bazofila (BAT) ovim lekom, čiji je nalaz bio pozitivan. Zaključak. Ovo je prvi prikaz dve vrste anafilaktičke reakcije izazvane metilprednizolonom kod iste osobe. Klinička slika, pozitivni nalaz BAT i pozitivne kožne probe na metilprednizolon pokazuju da se kod deteta razvio prvi tip hipersenzitivne reakcije. Nedostatak unakrsne reaktivnosti s ostalim kortikosteroidima ukazuje na to da je alergijska reakcija izazvana steroidnim molekulom.
PB  - Srpsko Lekarsko Drustvo, Beograd
T2  - Srpski arhiv za celokupno lekarstvo
T1  - Immediate Allergic Reaction to Methylprednisolone with Tolerance of Other Corticosteroids
T1  - Rana alergijska reakcija na metilprednizolon sa tolerancijom drugih kortikosteroida
VL  - 140
IS  - 3-4
SP  - 233
EP  - 235
DO  - 10.2298/SARH1204233A
ER  - 

@article{
author = "Atanasković-Marković, Marina and Gavrović-Jankulović, Marija and Jankovic, Srdja and Blagojević, Gordan and Ćirković-Veličković, Tanja and Milojevic, Irina and Simic, Dusica and Nestorovic, Branimir",
year = "2012",
abstract = "Introduction In spite of the wide usage of corticosteroids for the treatment of a plethora of diseases, sometimes they can induce immediate hypersensitivity reactions, which are however uncommon. Case Outline We report a case of immediate allergic reaction induced by intravenous methylprednisolone given before operation for surgical repair of an arm contracture as a sequel of burns, which the child had tolerated a month before. Six weeks later the patient repeated the anaphylactic reaction during skin testing to methylprednisolone. In addition, basophile activation test with methylprednisolone (BAT) was positive. Conclusion This case report describes a patient who experienced intraoperative anaphylaxis and anaphylactic reaction induced by skin testing. This is the first report on induction of both anaphylactic reactions by methylprednisolone in the same child. Clinical findings, positive BAT and positive skin tests with methylprednisolone imply that the child developed type-I hypersensitivity. The lack of cross-reactivity with other corticosteroids emphasizes that the reactions were caused by the steroid molecule., Uvod. Uprkos širokoj primeni kortikosteroida u lečenju od različitih bolesti, oni ponekad mogu izazvati ranu alergijsku reakciju. Prikaz bolesnika. Kod dvanaestogodišnjeg dečaka došlo je do rane alergijske reakcije izazvane intravenskom primenom metilprednizolona neposredno pre hirurške intervencije, tačnije, korekcije kontrakture šake koja se javila kao komplikacija opekotine. Mesec dana pre pojave alergijske reakcije dete je primalo metilprednizolon i dobro ga podnosilo. Šest nedelja posle operacije ponovo se javila anafilaktička reakcija tokom kožnog testiranja metilprednizolonom. Primenjen je i test aktivacije bazofila (BAT) ovim lekom, čiji je nalaz bio pozitivan. Zaključak. Ovo je prvi prikaz dve vrste anafilaktičke reakcije izazvane metilprednizolonom kod iste osobe. Klinička slika, pozitivni nalaz BAT i pozitivne kožne probe na metilprednizolon pokazuju da se kod deteta razvio prvi tip hipersenzitivne reakcije. Nedostatak unakrsne reaktivnosti s ostalim kortikosteroidima ukazuje na to da je alergijska reakcija izazvana steroidnim molekulom.",
publisher = "Srpsko Lekarsko Drustvo, Beograd",
journal = "Srpski arhiv za celokupno lekarstvo",
title = "Immediate Allergic Reaction to Methylprednisolone with Tolerance of Other Corticosteroids, Rana alergijska reakcija na metilprednizolon sa tolerancijom drugih kortikosteroida",
volume = "140",
number = "3-4",
pages = "233-235",
doi = "10.2298/SARH1204233A"
}

Atanasković-Marković, M., Gavrović-Jankulović, M., Jankovic, S., Blagojević, G., Ćirković-Veličković, T., Milojevic, I., Simic, D.,& Nestorovic, B.. (2012). Immediate Allergic Reaction to Methylprednisolone with Tolerance of Other Corticosteroids. in Srpski arhiv za celokupno lekarstvo
Srpsko Lekarsko Drustvo, Beograd., 140(3-4), 233-235.
https://doi.org/10.2298/SARH1204233A

Atanasković-Marković M, Gavrović-Jankulović M, Jankovic S, Blagojević G, Ćirković-Veličković T, Milojevic I, Simic D, Nestorovic B. Immediate Allergic Reaction to Methylprednisolone with Tolerance of Other Corticosteroids. in Srpski arhiv za celokupno lekarstvo. 2012;140(3-4):233-235.
doi:10.2298/SARH1204233A .

Atanasković-Marković, Marina, Gavrović-Jankulović, Marija, Jankovic, Srdja, Blagojević, Gordan, Ćirković-Veličković, Tanja, Milojevic, Irina, Simic, Dusica, Nestorovic, Branimir, "Immediate Allergic Reaction to Methylprednisolone with Tolerance of Other Corticosteroids" in Srpski arhiv za celokupno lekarstvo, 140, no. 3-4 (2012):233-235,
https://doi.org/10.2298/SARH1204233A . .

TY  - CONF
AU  - Abughren, Salem Alzwam M.
AU  - Dimitrijevic, R.
AU  - Popović, Milica M.
AU  - Atanasković-Marković, Marina
AU  - Gavrović-Jankulović, Marija
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1471
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - Production and characterisation of recombinant banana glucanase
VL  - 66
SP  - 391
EP  - 391
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1471
ER  - 

@conference{
author = "Abughren, Salem Alzwam M. and Dimitrijevic, R. and Popović, Milica M. and Atanasković-Marković, Marina and Gavrović-Jankulović, Marija",
year = "2011",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Production and characterisation of recombinant banana glucanase",
volume = "66",
pages = "391-391",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1471"
}

Abughren, S. A. M., Dimitrijevic, R., Popović, M. M., Atanasković-Marković, M.,& Gavrović-Jankulović, M.. (2011). Production and characterisation of recombinant banana glucanase. in Allergy
Wiley-Blackwell, Hoboken., 66, 391-391.
https://hdl.handle.net/21.15107/rcub_cherry_1471

Abughren SAM, Dimitrijevic R, Popović MM, Atanasković-Marković M, Gavrović-Jankulović M. Production and characterisation of recombinant banana glucanase. in Allergy. 2011;66:391-391.
https://hdl.handle.net/21.15107/rcub_cherry_1471 .

Abughren, Salem Alzwam M., Dimitrijevic, R., Popović, Milica M., Atanasković-Marković, Marina, Gavrović-Jankulović, Marija, "Production and characterisation of recombinant banana glucanase" in Allergy, 66 (2011):391-391,
https://hdl.handle.net/21.15107/rcub_cherry_1471 .

TY  - JOUR
AU  - Tantoush, Ziyad
AU  - Stanić, Dragana
AU  - Stojadinović, Marija M.
AU  - Ognjenović, Jana
AU  - Mihajlovic, Luka
AU  - Atanasković-Marković, Marina
AU  - Ćirković-Veličković, Tanja
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1137
AB  - beta-Lactoglobulin (BLG) is an important nutrient of dairy products, but it represents a serious health risk in patients allergic to milk. Sour cherry (Prunus cerasus L) extract (SCE) is frequently added as a natural food colour in composite foods, such as fruit yogurt, ice creams, frappes and milkshakes. The aim of this study was to investigate the potential of laccase to cross-link BLG in the presence of an SCE and to characterise the obtained products for their bioactivity. Laccase cross-linked BLG in the presence of sour cherry phenolics. In a basophil-activation assay, the allergenicity of the cross-linked protein was shown to decrease in all nine cow's milk-allergic patients, while digestibility of the remaining monomeric BLG in simulated conditions of the gastrointestinal tract increased. Tryptic peptides became immediately available in BLG treated by laccase and laccase/SCE. The hydrolysates obtained by trypsin digestion of BLG/laccase/SCE showed an increase of 57% in radical-scavenging activity, compared to the control BLG. Enzymatic processing and usage of natural phenolic extracts as mediators of enzymatic reaction may improve BLG safety and the availability of peptides following digestion, while conserving its bioactivity.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Digestibility and allergenicity of beta-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics
VL  - 125
IS  - 1
SP  - 84
EP  - 91
DO  - 10.1016/j.foodchem.2010.08.040
ER  - 

@article{
author = "Tantoush, Ziyad and Stanić, Dragana and Stojadinović, Marija M. and Ognjenović, Jana and Mihajlovic, Luka and Atanasković-Marković, Marina and Ćirković-Veličković, Tanja",
year = "2011",
abstract = "beta-Lactoglobulin (BLG) is an important nutrient of dairy products, but it represents a serious health risk in patients allergic to milk. Sour cherry (Prunus cerasus L) extract (SCE) is frequently added as a natural food colour in composite foods, such as fruit yogurt, ice creams, frappes and milkshakes. The aim of this study was to investigate the potential of laccase to cross-link BLG in the presence of an SCE and to characterise the obtained products for their bioactivity. Laccase cross-linked BLG in the presence of sour cherry phenolics. In a basophil-activation assay, the allergenicity of the cross-linked protein was shown to decrease in all nine cow's milk-allergic patients, while digestibility of the remaining monomeric BLG in simulated conditions of the gastrointestinal tract increased. Tryptic peptides became immediately available in BLG treated by laccase and laccase/SCE. The hydrolysates obtained by trypsin digestion of BLG/laccase/SCE showed an increase of 57% in radical-scavenging activity, compared to the control BLG. Enzymatic processing and usage of natural phenolic extracts as mediators of enzymatic reaction may improve BLG safety and the availability of peptides following digestion, while conserving its bioactivity.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Digestibility and allergenicity of beta-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics",
volume = "125",
number = "1",
pages = "84-91",
doi = "10.1016/j.foodchem.2010.08.040"
}

Tantoush, Z., Stanić, D., Stojadinović, M. M., Ognjenović, J., Mihajlovic, L., Atanasković-Marković, M.,& Ćirković-Veličković, T.. (2011). Digestibility and allergenicity of beta-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics. in Food Chemistry
Elsevier Sci Ltd, Oxford., 125(1), 84-91.
https://doi.org/10.1016/j.foodchem.2010.08.040

Tantoush Z, Stanić D, Stojadinović MM, Ognjenović J, Mihajlovic L, Atanasković-Marković M, Ćirković-Veličković T. Digestibility and allergenicity of beta-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics. in Food Chemistry. 2011;125(1):84-91.
doi:10.1016/j.foodchem.2010.08.040 .

Tantoush, Ziyad, Stanić, Dragana, Stojadinović, Marija M., Ognjenović, Jana, Mihajlovic, Luka, Atanasković-Marković, Marina, Ćirković-Veličković, Tanja, "Digestibility and allergenicity of beta-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics" in Food Chemistry, 125, no. 1 (2011):84-91,
https://doi.org/10.1016/j.foodchem.2010.08.040 . .

TY  - CONF
AU  - Grozdanović, M.
AU  - Petersen, A.
AU  - Lindner, B.
AU  - Atanasković-Marković, Marina
AU  - Polović, Natalija
AU  - Gavrović-Jankulović, Marija
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1591
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - Proenzyme and active actinidin from kiwifruit differs in IgE reactivity
VL  - 66
SP  - 531
EP  - 531
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1591
ER  - 

@conference{
author = "Grozdanović, M. and Petersen, A. and Lindner, B. and Atanasković-Marković, Marina and Polović, Natalija and Gavrović-Jankulović, Marija",
year = "2011",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Proenzyme and active actinidin from kiwifruit differs in IgE reactivity",
volume = "66",
pages = "531-531",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1591"
}

Grozdanović, M., Petersen, A., Lindner, B., Atanasković-Marković, M., Polović, N.,& Gavrović-Jankulović, M.. (2011). Proenzyme and active actinidin from kiwifruit differs in IgE reactivity. in Allergy
Wiley-Blackwell, Hoboken., 66, 531-531.
https://hdl.handle.net/21.15107/rcub_cherry_1591

Grozdanović M, Petersen A, Lindner B, Atanasković-Marković M, Polović N, Gavrović-Jankulović M. Proenzyme and active actinidin from kiwifruit differs in IgE reactivity. in Allergy. 2011;66:531-531.
https://hdl.handle.net/21.15107/rcub_cherry_1591 .

Grozdanović, M., Petersen, A., Lindner, B., Atanasković-Marković, Marina, Polović, Natalija, Gavrović-Jankulović, Marija, "Proenzyme and active actinidin from kiwifruit differs in IgE reactivity" in Allergy, 66 (2011):531-531,
https://hdl.handle.net/21.15107/rcub_cherry_1591 .

TY  - CONF
AU  - Atanasković-Marković, Marina
AU  - Međo, Biljana
AU  - Gavrović-Jankulović, Marija
AU  - Ćirković-Veličković, Tanja
AU  - Nestorović, B.
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1465
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - Multiple drug hypersensitivity in children
VL  - 65
SP  - 177
EP  - 177
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1465
ER  - 

@conference{
author = "Atanasković-Marković, Marina and Međo, Biljana and Gavrović-Jankulović, Marija and Ćirković-Veličković, Tanja and Nestorović, B.",
year = "2010",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Multiple drug hypersensitivity in children",
volume = "65",
pages = "177-177",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1465"
}

Atanasković-Marković, M., Međo, B., Gavrović-Jankulović, M., Ćirković-Veličković, T.,& Nestorović, B.. (2010). Multiple drug hypersensitivity in children. in Allergy
Wiley-Blackwell, Hoboken., 65, 177-177.
https://hdl.handle.net/21.15107/rcub_cherry_1465

Atanasković-Marković M, Međo B, Gavrović-Jankulović M, Ćirković-Veličković T, Nestorović B. Multiple drug hypersensitivity in children. in Allergy. 2010;65:177-177.
https://hdl.handle.net/21.15107/rcub_cherry_1465 .

Atanasković-Marković, Marina, Međo, Biljana, Gavrović-Jankulović, Marija, Ćirković-Veličković, Tanja, Nestorović, B., "Multiple drug hypersensitivity in children" in Allergy, 65 (2010):177-177,
https://hdl.handle.net/21.15107/rcub_cherry_1465 .

TY  - JOUR
AU  - Stanić, Dragana
AU  - Monogioudi, Evanthia
AU  - Dilek, Ercili
AU  - Radosavljević, Jelena
AU  - Atanasković-Marković, Marina
AU  - Vučković, Olga
AU  - Raija, Lantto
AU  - Mattinen, Maija
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1126
AB  - Crosslinking enzymes are frequently used in bioprocessing of dairy products. The aim of this study was to examine the effects of enzymatic crosslinking on IgE binding, allergenicity and digestion stability of beta-casein (CN). beta-CN was crosslinked by transglutaminase, tyrosinase, mushroom tyrosinase/caffeic acid and laccase/caffeic acid. The IgE binding to beta-CN was compared in vitro by CAP inhibition assay, ELISA inhibition as well as ex vivo by basophil activation assay. Crosslinked CNs were digested by simulated gastric fluid for 15 and 60 min and obtained digests analyzed for their ability to inhibit IgE binding by CAP inhibition assay and SDS-PAGE. The ability of crosslinked CNs to activate basophils was significantly reduced in seven patients in the case of CN crosslinked by laccase and moderately reduced in the case of tyrosinase/caffeic acid crosslinked CN (in two cow's milk allergy patients tested with different allergen concentrations). The response to various crosslinked CNs differed individually among patients' sera tested by ELISA inhibition assay. The presence of caffeic acid hampered digestion by pepsin, and this effect was most pronounced for the tyrosinase/caffeic acid crosslinked CN. The laccase/caffeic acid and mushroom tyrosinase/caffeic acid had the highest potential in mitigating IgE binding and allergenicity of the beta-CN out of all investigated enzymes. The presence of a small phenolic compound also increased digestion stability of beta-CN.
PB  - Wiley-V C H Verlag Gmbh, Weinheim
T2  - Molecular Nutrition and Food Research
T1  - Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein
VL  - 54
IS  - 9
SP  - 1273
EP  - 1284
DO  - 10.1002/mnfr.200900184
ER  - 

@article{
author = "Stanić, Dragana and Monogioudi, Evanthia and Dilek, Ercili and Radosavljević, Jelena and Atanasković-Marković, Marina and Vučković, Olga and Raija, Lantto and Mattinen, Maija and Buchert, Johanna and Ćirković-Veličković, Tanja",
year = "2010",
abstract = "Crosslinking enzymes are frequently used in bioprocessing of dairy products. The aim of this study was to examine the effects of enzymatic crosslinking on IgE binding, allergenicity and digestion stability of beta-casein (CN). beta-CN was crosslinked by transglutaminase, tyrosinase, mushroom tyrosinase/caffeic acid and laccase/caffeic acid. The IgE binding to beta-CN was compared in vitro by CAP inhibition assay, ELISA inhibition as well as ex vivo by basophil activation assay. Crosslinked CNs were digested by simulated gastric fluid for 15 and 60 min and obtained digests analyzed for their ability to inhibit IgE binding by CAP inhibition assay and SDS-PAGE. The ability of crosslinked CNs to activate basophils was significantly reduced in seven patients in the case of CN crosslinked by laccase and moderately reduced in the case of tyrosinase/caffeic acid crosslinked CN (in two cow's milk allergy patients tested with different allergen concentrations). The response to various crosslinked CNs differed individually among patients' sera tested by ELISA inhibition assay. The presence of caffeic acid hampered digestion by pepsin, and this effect was most pronounced for the tyrosinase/caffeic acid crosslinked CN. The laccase/caffeic acid and mushroom tyrosinase/caffeic acid had the highest potential in mitigating IgE binding and allergenicity of the beta-CN out of all investigated enzymes. The presence of a small phenolic compound also increased digestion stability of beta-CN.",
publisher = "Wiley-V C H Verlag Gmbh, Weinheim",
journal = "Molecular Nutrition and Food Research",
title = "Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein",
volume = "54",
number = "9",
pages = "1273-1284",
doi = "10.1002/mnfr.200900184"
}

Stanić, D., Monogioudi, E., Dilek, E., Radosavljević, J., Atanasković-Marković, M., Vučković, O., Raija, L., Mattinen, M., Buchert, J.,& Ćirković-Veličković, T.. (2010). Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein. in Molecular Nutrition and Food Research
Wiley-V C H Verlag Gmbh, Weinheim., 54(9), 1273-1284.
https://doi.org/10.1002/mnfr.200900184

Stanić D, Monogioudi E, Dilek E, Radosavljević J, Atanasković-Marković M, Vučković O, Raija L, Mattinen M, Buchert J, Ćirković-Veličković T. Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein. in Molecular Nutrition and Food Research. 2010;54(9):1273-1284.
doi:10.1002/mnfr.200900184 .

Stanić, Dragana, Monogioudi, Evanthia, Dilek, Ercili, Radosavljević, Jelena, Atanasković-Marković, Marina, Vučković, Olga, Raija, Lantto, Mattinen, Maija, Buchert, Johanna, Ćirković-Veličković, Tanja, "Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein" in Molecular Nutrition and Food Research, 54, no. 9 (2010):1273-1284,
https://doi.org/10.1002/mnfr.200900184 . .