FoodEnTwin-Twinning of research activities for the frontier research in the fields of food, nutrition and environmental omics

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FoodEnTwin-Twinning of research activities for the frontier research in the fields of food, nutrition and environmental omics (en)
Authors

Publications

Supplementary data for the article: Perusko, M.; Apostolovic, D.; Kiewiet, M. B. G.; Grundström, J.; Hamsten, C.; Starkhammar, M.; Velickovic, T. C.; Hage, M. van. Bovine γ-Globulin, Lactoferrin, and Lactoperoxidase Are Relevant Bovine Milk Allergens in Patients with α-Gal Syndrome. Allergy n/a (n/a). https://doi.org/10.1111/all.14889.

Peruško, Marija; Apostolović, Danijela; Kiewiet, Mensiena Berentje Geertje; Grundström, Jeanette; Hamsten, Carl; Starkhammar, Maria; Ćirković-Veličković, Tanja; Hage, Marianne van

TY  - BOOK
AU  - Peruško, Marija
AU  - Apostolović, Danijela
AU  - Kiewiet, Mensiena Berentje Geertje
AU  - Grundström, Jeanette
AU  - Hamsten, Carl
AU  - Starkhammar, Maria
AU  - Ćirković-Veličković, Tanja
AU  - Hage, Marianne van
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4447
PB  - Blackwell Publishing Ltd
T2  - Allergy
T2  - Allergy
T1  - Supplementary data for the article: Perusko, M.; Apostolovic, D.; Kiewiet, M. B. G.; Grundström, J.; Hamsten, C.; Starkhammar, M.; Velickovic, T. C.; Hage, M. van. Bovine γ-Globulin, Lactoferrin, and Lactoperoxidase Are Relevant Bovine Milk Allergens in Patients with α-Gal Syndrome. Allergy n/a (n/a). https://doi.org/10.1111/all.14889.
ER  - 
@book{
author = "Peruško, Marija and Apostolović, Danijela and Kiewiet, Mensiena Berentje Geertje and Grundström, Jeanette and Hamsten, Carl and Starkhammar, Maria and Ćirković-Veličković, Tanja and Hage, Marianne van",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4447",
publisher = "Blackwell Publishing Ltd",
journal = "Allergy, Allergy",
title = "Supplementary data for the article: Perusko, M.; Apostolovic, D.; Kiewiet, M. B. G.; Grundström, J.; Hamsten, C.; Starkhammar, M.; Velickovic, T. C.; Hage, M. van. Bovine γ-Globulin, Lactoferrin, and Lactoperoxidase Are Relevant Bovine Milk Allergens in Patients with α-Gal Syndrome. Allergy n/a (n/a). https://doi.org/10.1111/all.14889."
}
Peruško, M., Apostolović, D., Kiewiet, M. B. G., Grundström, J., Hamsten, C., Starkhammar, M., Ćirković-Veličković, T.,& Hage, M. v.Supplementary data for the article: Perusko, M.; Apostolovic, D.; Kiewiet, M. B. G.; Grundström, J.; Hamsten, C.; Starkhammar, M.; Velickovic, T. C.; Hage, M. van. Bovine γ-Globulin, Lactoferrin, and Lactoperoxidase Are Relevant Bovine Milk Allergens in Patients with α-Gal Syndrome. Allergy n/a (n/a). https://doi.org/10.1111/all.14889..
Allergy
Blackwell Publishing Ltd..
Peruško M, Apostolović D, Kiewiet MBG, Grundström J, Hamsten C, Starkhammar M, Ćirković-Veličković T, Hage MV. Supplementary data for the article: Perusko, M.; Apostolovic, D.; Kiewiet, M. B. G.; Grundström, J.; Hamsten, C.; Starkhammar, M.; Velickovic, T. C.; Hage, M. van. Bovine γ-Globulin, Lactoferrin, and Lactoperoxidase Are Relevant Bovine Milk Allergens in Patients with α-Gal Syndrome. Allergy n/a (n/a). https://doi.org/10.1111/all.14889.. Allergy.
Peruško Marija, Apostolović Danijela, Kiewiet Mensiena Berentje Geertje, Grundström Jeanette, Hamsten Carl, Starkhammar Maria, Ćirković-Veličković Tanja, Hage Marianne van, "Supplementary data for the article: Perusko, M.; Apostolovic, D.; Kiewiet, M. B. G.; Grundström, J.; Hamsten, C.; Starkhammar, M.; Velickovic, T. C.; Hage, M. van. Bovine γ-Globulin, Lactoferrin, and Lactoperoxidase Are Relevant Bovine Milk Allergens in Patients with α-Gal Syndrome. Allergy n/a (n/a). https://doi.org/10.1111/all.14889." Allergy

Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome

Peruško, Marija; Apostolović, Danijela; Kiewiet, Mensiena Berentje Geertje; Grundström, Jeanette; Hamsten, Carl; Starkhammar, Maria; Ćirković-Veličković, Tanja; Hage, Marianne van

TY  - JOUR
AU  - Peruško, Marija
AU  - Apostolović, Danijela
AU  - Kiewiet, Mensiena Berentje Geertje
AU  - Grundström, Jeanette
AU  - Hamsten, Carl
AU  - Starkhammar, Maria
AU  - Ćirković-Veličković, Tanja
AU  - Hage, Marianne van
UR  - https://onlinelibrary.wiley.com/doi/abs/10.1111/all.14889
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4446
AB  - Background Mammalian meat is the most common trigger of the allergic reactions in patients with α-Gal syndrome (AGS). Milk and dairy, although less often, also cause a significant number of allergic manifestations. The aim of this study was to identify α-Gal-containing bovine milk proteins with allergenic properties among AGS patients. Methods Thirty-eight AGS patients with IgE to milk were included in the study. Milk proteins were analyzed for the presence of α-Gal and for binding by patients’ IgE using immunoblot, ImmunoCAP, and inhibition ELISA. Allergenicity of milk and milk proteins was assessed by basophil activation test. Results More than half of the AGS patients reported allergic reactions to milk or dairy products. Bovine γ-globulin (BGG), lactoferrin (LF), and lactoperoxidase (LPO) were identified as α-Gal carrying proteins which were recognized by AGS patients’ IgE. Whey mirrored the anti-α-Gal and IgE reactivity of BGG, LF, and LPO. Eighty-nine percent of the patients displayed IgE to BGG, 91% to LF, and 57% to LPO. Inhibition of α-Gal-specific IgE binding was achieved by BGG, LF, LPO, and whey. These proteins also activated AGS patients’ basophils. Interestingly, at lower concentrations, LF was the most potent inhibitor of IgE binding, and the most potent activator of basophils. Conclusion BGG, LF, and LPO were all found to be relevant milk α-Gal-containing glycoproteins that bound AGS patients’ IgE antibodies and activated their basophils. These proteins are probably involved in the allergic reactions to milk in AGS patients. LPO was for the first time shown to be an allergen.
PB  - Blackwell Publishing Ltd
T2  - Allergy
T2  - Allergy
T1  - Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome
DO  - 10.1111/all.14889
ER  - 
@article{
author = "Peruško, Marija and Apostolović, Danijela and Kiewiet, Mensiena Berentje Geertje and Grundström, Jeanette and Hamsten, Carl and Starkhammar, Maria and Ćirković-Veličković, Tanja and Hage, Marianne van",
url = "https://onlinelibrary.wiley.com/doi/abs/10.1111/all.14889, http://cherry.chem.bg.ac.rs/handle/123456789/4446",
abstract = "Background Mammalian meat is the most common trigger of the allergic reactions in patients with α-Gal syndrome (AGS). Milk and dairy, although less often, also cause a significant number of allergic manifestations. The aim of this study was to identify α-Gal-containing bovine milk proteins with allergenic properties among AGS patients. Methods Thirty-eight AGS patients with IgE to milk were included in the study. Milk proteins were analyzed for the presence of α-Gal and for binding by patients’ IgE using immunoblot, ImmunoCAP, and inhibition ELISA. Allergenicity of milk and milk proteins was assessed by basophil activation test. Results More than half of the AGS patients reported allergic reactions to milk or dairy products. Bovine γ-globulin (BGG), lactoferrin (LF), and lactoperoxidase (LPO) were identified as α-Gal carrying proteins which were recognized by AGS patients’ IgE. Whey mirrored the anti-α-Gal and IgE reactivity of BGG, LF, and LPO. Eighty-nine percent of the patients displayed IgE to BGG, 91% to LF, and 57% to LPO. Inhibition of α-Gal-specific IgE binding was achieved by BGG, LF, LPO, and whey. These proteins also activated AGS patients’ basophils. Interestingly, at lower concentrations, LF was the most potent inhibitor of IgE binding, and the most potent activator of basophils. Conclusion BGG, LF, and LPO were all found to be relevant milk α-Gal-containing glycoproteins that bound AGS patients’ IgE antibodies and activated their basophils. These proteins are probably involved in the allergic reactions to milk in AGS patients. LPO was for the first time shown to be an allergen.",
publisher = "Blackwell Publishing Ltd",
journal = "Allergy, Allergy",
title = "Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome",
doi = "10.1111/all.14889"
}
Peruško, M., Apostolović, D., Kiewiet, M. B. G., Grundström, J., Hamsten, C., Starkhammar, M., Ćirković-Veličković, T.,& Hage, M. v.Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome.
Allergy
Blackwell Publishing Ltd..
https://doi.org/10.1111/all.14889
Peruško M, Apostolović D, Kiewiet MBG, Grundström J, Hamsten C, Starkhammar M, Ćirković-Veličković T, Hage MV. Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome. Allergy.
Peruško Marija, Apostolović Danijela, Kiewiet Mensiena Berentje Geertje, Grundström Jeanette, Hamsten Carl, Starkhammar Maria, Ćirković-Veličković Tanja, Hage Marianne van, "Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome" Allergy,
https://doi.org/10.1111/all.14889 .
4

Interaction, binding capacity and anticancer properties of N,N′-bis(acetylacetone)-propylenediimine-copper(II) on colorectal cancer cell line Caco-2

Stevanović, Nikola R.; Apostolović, Danijela; Milčić, Miloš K.; Lolić, Aleksandar; Hage, Marianne van; Ćirković-Veličković, Tanja; Baošić, Rada

(2021)

TY  - JOUR
AU  - Stevanović, Nikola R.
AU  - Apostolović, Danijela
AU  - Milčić, Miloš K.
AU  - Lolić, Aleksandar
AU  - Hage, Marianne van
AU  - Ćirković-Veličković, Tanja
AU  - Baošić, Rada
PY  - 2021
UR  - https://pubs.rsc.org/en/content/articlelanding/2021/nj/d1nj00040c
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4399
AB  - Different Schiff base complexes have biological activities that make them suitable for drug design. The biological properties of tetradentate Schiff base copper(II) complexed with N,N′-bis(acetylacetone)propylenediimine have been studied. The cytotoxic activity towards Caco-2 cells were determined by MTT, Anexin V and PI apoptosis assays. N,N′-bis(acetylacetone)propylenediimine-copper(II) showed the anti-cancer and anti-proliferative properties by inducing apoptosis in Caco-2 cells. A comparison of the cytotoxic activity of this compound with cisplatin shows that it is more effective on the colorectal cancer cell line Caco-2. The binding capacity and interaction of N,N′-bis(acetylacetone)propylenediimine-copper(II) with HSA were systemically investigated by in vitro fluorescence spectroscopy, CD spectroscopy, and in silico molecular docking study. Furthermore, in vitro and in silico interaction studies indicated that the complex binds to HSA through a static quenching mechanism without changes in protein conformation. The calculated number of binding sites was in line with molecular docking studies. The obtained Ka value suggests that the compound can be released from the protein in target cells. The tetradentate Schiff base copper(II) complex exhibited in vitro biological activities against cancer epithelial cells, which depend on the molecular structure of the complex, causing apoptosis, and the complex can bind to the protein drug carrier in circulation to the target tissue.
T2  - New Journal of Chemistry
T1  - Interaction, binding capacity and anticancer properties of N,N′-bis(acetylacetone)-propylenediimine-copper(II) on colorectal cancer cell line Caco-2
VL  - 45
IS  - 14
SP  - 6231
EP  - 6237
DO  - 10.1039/D1NJ00040C
ER  - 
@article{
author = "Stevanović, Nikola R. and Apostolović, Danijela and Milčić, Miloš K. and Lolić, Aleksandar and Hage, Marianne van and Ćirković-Veličković, Tanja and Baošić, Rada",
year = "2021",
url = "https://pubs.rsc.org/en/content/articlelanding/2021/nj/d1nj00040c, http://cherry.chem.bg.ac.rs/handle/123456789/4399",
abstract = "Different Schiff base complexes have biological activities that make them suitable for drug design. The biological properties of tetradentate Schiff base copper(II) complexed with N,N′-bis(acetylacetone)propylenediimine have been studied. The cytotoxic activity towards Caco-2 cells were determined by MTT, Anexin V and PI apoptosis assays. N,N′-bis(acetylacetone)propylenediimine-copper(II) showed the anti-cancer and anti-proliferative properties by inducing apoptosis in Caco-2 cells. A comparison of the cytotoxic activity of this compound with cisplatin shows that it is more effective on the colorectal cancer cell line Caco-2. The binding capacity and interaction of N,N′-bis(acetylacetone)propylenediimine-copper(II) with HSA were systemically investigated by in vitro fluorescence spectroscopy, CD spectroscopy, and in silico molecular docking study. Furthermore, in vitro and in silico interaction studies indicated that the complex binds to HSA through a static quenching mechanism without changes in protein conformation. The calculated number of binding sites was in line with molecular docking studies. The obtained Ka value suggests that the compound can be released from the protein in target cells. The tetradentate Schiff base copper(II) complex exhibited in vitro biological activities against cancer epithelial cells, which depend on the molecular structure of the complex, causing apoptosis, and the complex can bind to the protein drug carrier in circulation to the target tissue.",
journal = "New Journal of Chemistry",
title = "Interaction, binding capacity and anticancer properties of N,N′-bis(acetylacetone)-propylenediimine-copper(II) on colorectal cancer cell line Caco-2",
volume = "45",
number = "14",
pages = "6231-6237",
doi = "10.1039/D1NJ00040C"
}
Stevanović, N. R., Apostolović, D., Milčić, M. K., Lolić, A., Hage, M. v., Ćirković-Veličković, T.,& Baošić, R. (2021). Interaction, binding capacity and anticancer properties of N,N′-bis(acetylacetone)-propylenediimine-copper(II) on colorectal cancer cell line Caco-2.
New Journal of Chemistry, 45(14), 6231-6237.
https://doi.org/10.1039/D1NJ00040C
Stevanović NR, Apostolović D, Milčić MK, Lolić A, Hage MV, Ćirković-Veličković T, Baošić R. Interaction, binding capacity and anticancer properties of N,N′-bis(acetylacetone)-propylenediimine-copper(II) on colorectal cancer cell line Caco-2. New Journal of Chemistry. 2021;45(14):6231-6237
Stevanović Nikola R., Apostolović Danijela, Milčić Miloš K., Lolić Aleksandar, Hage Marianne van, Ćirković-Veličković Tanja, Baošić Rada, "Interaction, binding capacity and anticancer properties of N,N′-bis(acetylacetone)-propylenediimine-copper(II) on colorectal cancer cell line Caco-2" New Journal of Chemistry, 45, no. 14 (2021):6231-6237,
https://doi.org/10.1039/D1NJ00040C .

Supplementary data for the article: Stevanović, N.; Apostolović, D.; Milčić, M.; Lolić, A.; Hage, M. van; Veličković, T. Ć.; Baošić, R. Interaction, Binding Capacity and Anticancer Properties of N,N′-Bis(Acetylacetone)-Propylenediimine-Copper(II) on Colorectal Cancer Cell Line Caco-2. New J. Chem. 2021, 45 (14), 6231–6237. https://doi.org/10.1039/D1NJ00040C.

Stevanović, Nikola R.; Apostolović, Danijela; Milčić, Miloš K.; Lolić, Aleksandar; Hage, Marianne van; Ćirković-Veličković, Tanja; Baošić, Rada

(2021)

TY  - BOOK
AU  - Stevanović, Nikola R.
AU  - Apostolović, Danijela
AU  - Milčić, Miloš K.
AU  - Lolić, Aleksandar
AU  - Hage, Marianne van
AU  - Ćirković-Veličković, Tanja
AU  - Baošić, Rada
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4400
T2  - New Journal of Chemistry
T1  - Supplementary data for the article: Stevanović, N.; Apostolović, D.; Milčić, M.; Lolić, A.; Hage, M. van; Veličković, T. Ć.; Baošić, R. Interaction, Binding Capacity and Anticancer Properties of N,N′-Bis(Acetylacetone)-Propylenediimine-Copper(II) on Colorectal Cancer Cell Line Caco-2. New J. Chem. 2021, 45 (14), 6231–6237. https://doi.org/10.1039/D1NJ00040C.
ER  - 
@book{
author = "Stevanović, Nikola R. and Apostolović, Danijela and Milčić, Miloš K. and Lolić, Aleksandar and Hage, Marianne van and Ćirković-Veličković, Tanja and Baošić, Rada",
year = "2021",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4400",
journal = "New Journal of Chemistry",
title = "Supplementary data for the article: Stevanović, N.; Apostolović, D.; Milčić, M.; Lolić, A.; Hage, M. van; Veličković, T. Ć.; Baošić, R. Interaction, Binding Capacity and Anticancer Properties of N,N′-Bis(Acetylacetone)-Propylenediimine-Copper(II) on Colorectal Cancer Cell Line Caco-2. New J. Chem. 2021, 45 (14), 6231–6237. https://doi.org/10.1039/D1NJ00040C."
}
Stevanović, N. R., Apostolović, D., Milčić, M. K., Lolić, A., Hage, M. v., Ćirković-Veličković, T.,& Baošić, R. (2021). Supplementary data for the article: Stevanović, N.; Apostolović, D.; Milčić, M.; Lolić, A.; Hage, M. van; Veličković, T. Ć.; Baošić, R. Interaction, Binding Capacity and Anticancer Properties of N,N′-Bis(Acetylacetone)-Propylenediimine-Copper(II) on Colorectal Cancer Cell Line Caco-2. New J. Chem. 2021, 45 (14), 6231–6237. https://doi.org/10.1039/D1NJ00040C..
New Journal of Chemistry.
Stevanović NR, Apostolović D, Milčić MK, Lolić A, Hage MV, Ćirković-Veličković T, Baošić R. Supplementary data for the article: Stevanović, N.; Apostolović, D.; Milčić, M.; Lolić, A.; Hage, M. van; Veličković, T. Ć.; Baošić, R. Interaction, Binding Capacity and Anticancer Properties of N,N′-Bis(Acetylacetone)-Propylenediimine-Copper(II) on Colorectal Cancer Cell Line Caco-2. New J. Chem. 2021, 45 (14), 6231–6237. https://doi.org/10.1039/D1NJ00040C.. New Journal of Chemistry. 2021;
Stevanović Nikola R., Apostolović Danijela, Milčić Miloš K., Lolić Aleksandar, Hage Marianne van, Ćirković-Veličković Tanja, Baošić Rada, "Supplementary data for the article: Stevanović, N.; Apostolović, D.; Milčić, M.; Lolić, A.; Hage, M. van; Veličković, T. Ć.; Baošić, R. Interaction, Binding Capacity and Anticancer Properties of N,N′-Bis(Acetylacetone)-Propylenediimine-Copper(II) on Colorectal Cancer Cell Line Caco-2. New J. Chem. 2021, 45 (14), 6231–6237. https://doi.org/10.1039/D1NJ00040C." New Journal of Chemistry (2021)

Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying

Peruško, Marija; Ghnimi, Sami; Simović, Ana; Stevanović, Nikola R.; Radomirović, Mirjana Ž.; Gharsallaoui, Adem; Smiljanić, Katarina; Van Haute, Sam; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier, 2021)

TY  - JOUR
AU  - Peruško, Marija
AU  - Ghnimi, Sami
AU  - Simović, Ana
AU  - Stevanović, Nikola R.
AU  - Radomirović, Mirjana Ž.
AU  - Gharsallaoui, Adem
AU  - Smiljanić, Katarina
AU  - Van Haute, Sam
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4332
AB  - Demand for camel milk (CM) is increasing worldwide, due to its high nutritious value and health benefits. In this study, whole CM powders were produced by spray drying (SD) at six inlet temperatures (190 °C–250 °C) and by freeze drying (FD). Physicochemical and functional properties of CM powder proteins were investigated. SD at higher inlet temperatures (230 °C–250 °C) resulted in higher extent of Maillard reaction (MR), in comparison to lower temperatures (190 °C–200 °C) and FD treatment. Both treatments had negative effect on casein solubility, while whey proteins remained soluble and slightly increased its solubility with the extent of MR. The CM powders obtained at higher inlet temperatures demonstrated improved antioxidant activity. Secondary structure of whey proteins did not differ among the samples, while surface hydrophobicity of whey proteins was higher in all SD than in FD samples, suggesting only limited denaturation of camel whey proteins at higher inlet temperatures of drying. Thus, the effects of SD under the conditions applied in our study did not decrease camel whey protein solubility, while drying procedure itself regardless of temperature decreased solubility of camel milk caseins. MR generated during CM processing could be an important means of compensating for the lack of antioxidant protection normally associated with β-lactoglobulin but happens to be absent from this milk.
PB  - Elsevier
T2  - LWT
T1  - Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying
VL  - 143
SP  - 111091
DO  - 10.1016/j.lwt.2021.111091
ER  - 
@article{
author = "Peruško, Marija and Ghnimi, Sami and Simović, Ana and Stevanović, Nikola R. and Radomirović, Mirjana Ž. and Gharsallaoui, Adem and Smiljanić, Katarina and Van Haute, Sam and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2021",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4332",
abstract = "Demand for camel milk (CM) is increasing worldwide, due to its high nutritious value and health benefits. In this study, whole CM powders were produced by spray drying (SD) at six inlet temperatures (190 °C–250 °C) and by freeze drying (FD). Physicochemical and functional properties of CM powder proteins were investigated. SD at higher inlet temperatures (230 °C–250 °C) resulted in higher extent of Maillard reaction (MR), in comparison to lower temperatures (190 °C–200 °C) and FD treatment. Both treatments had negative effect on casein solubility, while whey proteins remained soluble and slightly increased its solubility with the extent of MR. The CM powders obtained at higher inlet temperatures demonstrated improved antioxidant activity. Secondary structure of whey proteins did not differ among the samples, while surface hydrophobicity of whey proteins was higher in all SD than in FD samples, suggesting only limited denaturation of camel whey proteins at higher inlet temperatures of drying. Thus, the effects of SD under the conditions applied in our study did not decrease camel whey protein solubility, while drying procedure itself regardless of temperature decreased solubility of camel milk caseins. MR generated during CM processing could be an important means of compensating for the lack of antioxidant protection normally associated with β-lactoglobulin but happens to be absent from this milk.",
publisher = "Elsevier",
journal = "LWT",
title = "Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying",
volume = "143",
pages = "111091",
doi = "10.1016/j.lwt.2021.111091"
}
Peruško, M., Ghnimi, S., Simović, A., Stevanović, N. R., Radomirović, M. Ž., Gharsallaoui, A., Smiljanić, K., Van Haute, S., Stanić-Vučinić, D.,& Ćirković-Veličković, T. (2021). Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying.
LWT
Elsevier., 143, 111091.
https://doi.org/10.1016/j.lwt.2021.111091
Peruško M, Ghnimi S, Simović A, Stevanović NR, Radomirović MŽ, Gharsallaoui A, Smiljanić K, Van Haute S, Stanić-Vučinić D, Ćirković-Veličković T. Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying. LWT. 2021;143:111091
Peruško Marija, Ghnimi Sami, Simović Ana, Stevanović Nikola R., Radomirović Mirjana Ž., Gharsallaoui Adem, Smiljanić Katarina, Van Haute Sam, Stanić-Vučinić Dragana, Ćirković-Veličković Tanja, "Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying" LWT, 143 (2021):111091,
https://doi.org/10.1016/j.lwt.2021.111091 .
1
1
1

Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying

Peruško, Marija; Ghnimi, Sami; Simović, Ana; Stevanović, Nikola R.; Radomirović, Mirjana Ž.; Gharsallaoui, Adem; Smiljanić, Katarina; Van Haute, Sam; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier, 2021)

TY  - JOUR
AU  - Peruško, Marija
AU  - Ghnimi, Sami
AU  - Simović, Ana
AU  - Stevanović, Nikola R.
AU  - Radomirović, Mirjana Ž.
AU  - Gharsallaoui, Adem
AU  - Smiljanić, Katarina
AU  - Van Haute, Sam
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4333
AB  - Demand for camel milk (CM) is increasing worldwide, due to its high nutritious value and health benefits. In this study, whole CM powders were produced by spray drying (SD) at six inlet temperatures (190 °C–250 °C) and by freeze drying (FD). Physicochemical and functional properties of CM powder proteins were investigated. SD at higher inlet temperatures (230 °C–250 °C) resulted in higher extent of Maillard reaction (MR), in comparison to lower temperatures (190 °C–200 °C) and FD treatment. Both treatments had negative effect on casein solubility, while whey proteins remained soluble and slightly increased its solubility with the extent of MR. The CM powders obtained at higher inlet temperatures demonstrated improved antioxidant activity. Secondary structure of whey proteins did not differ among the samples, while surface hydrophobicity of whey proteins was higher in all SD than in FD samples, suggesting only limited denaturation of camel whey proteins at higher inlet temperatures of drying. Thus, the effects of SD under the conditions applied in our study did not decrease camel whey protein solubility, while drying procedure itself regardless of temperature decreased solubility of camel milk caseins. MR generated during CM processing could be an important means of compensating for the lack of antioxidant protection normally associated with β-lactoglobulin but happens to be absent from this milk.
PB  - Elsevier
T2  - LWT
T1  - Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying
VL  - 143
SP  - 111091
DO  - 10.1016/j.lwt.2021.111091
ER  - 
@article{
author = "Peruško, Marija and Ghnimi, Sami and Simović, Ana and Stevanović, Nikola R. and Radomirović, Mirjana Ž. and Gharsallaoui, Adem and Smiljanić, Katarina and Van Haute, Sam and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2021",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4333",
abstract = "Demand for camel milk (CM) is increasing worldwide, due to its high nutritious value and health benefits. In this study, whole CM powders were produced by spray drying (SD) at six inlet temperatures (190 °C–250 °C) and by freeze drying (FD). Physicochemical and functional properties of CM powder proteins were investigated. SD at higher inlet temperatures (230 °C–250 °C) resulted in higher extent of Maillard reaction (MR), in comparison to lower temperatures (190 °C–200 °C) and FD treatment. Both treatments had negative effect on casein solubility, while whey proteins remained soluble and slightly increased its solubility with the extent of MR. The CM powders obtained at higher inlet temperatures demonstrated improved antioxidant activity. Secondary structure of whey proteins did not differ among the samples, while surface hydrophobicity of whey proteins was higher in all SD than in FD samples, suggesting only limited denaturation of camel whey proteins at higher inlet temperatures of drying. Thus, the effects of SD under the conditions applied in our study did not decrease camel whey protein solubility, while drying procedure itself regardless of temperature decreased solubility of camel milk caseins. MR generated during CM processing could be an important means of compensating for the lack of antioxidant protection normally associated with β-lactoglobulin but happens to be absent from this milk.",
publisher = "Elsevier",
journal = "LWT",
title = "Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying",
volume = "143",
pages = "111091",
doi = "10.1016/j.lwt.2021.111091"
}
Peruško, M., Ghnimi, S., Simović, A., Stevanović, N. R., Radomirović, M. Ž., Gharsallaoui, A., Smiljanić, K., Van Haute, S., Stanić-Vučinić, D.,& Ćirković-Veličković, T. (2021). Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying.
LWT
Elsevier., 143, 111091.
https://doi.org/10.1016/j.lwt.2021.111091
Peruško M, Ghnimi S, Simović A, Stevanović NR, Radomirović MŽ, Gharsallaoui A, Smiljanić K, Van Haute S, Stanić-Vučinić D, Ćirković-Veličković T. Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying. LWT. 2021;143:111091
Peruško Marija, Ghnimi Sami, Simović Ana, Stevanović Nikola R., Radomirović Mirjana Ž., Gharsallaoui Adem, Smiljanić Katarina, Van Haute Sam, Stanić-Vučinić Dragana, Ćirković-Veličković Tanja, "Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying" LWT, 143 (2021):111091,
https://doi.org/10.1016/j.lwt.2021.111091 .
1
1
1

Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091.

Peruško, Marija; Ghnimi, Sami; Simović, Ana; Stevanović, Nikola R.; Radomirović, Mirjana Ž.; Gharsallaoui, Adem; Smiljanić, Katarina; Van Haute, Sam; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier, 2021)

TY  - BOOK
AU  - Peruško, Marija
AU  - Ghnimi, Sami
AU  - Simović, Ana
AU  - Stevanović, Nikola R.
AU  - Radomirović, Mirjana Ž.
AU  - Gharsallaoui, Adem
AU  - Smiljanić, Katarina
AU  - Van Haute, Sam
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4334
PB  - Elsevier
T2  - LWT
T1  - Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091.
ER  - 
@book{
author = "Peruško, Marija and Ghnimi, Sami and Simović, Ana and Stevanović, Nikola R. and Radomirović, Mirjana Ž. and Gharsallaoui, Adem and Smiljanić, Katarina and Van Haute, Sam and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2021",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4334",
publisher = "Elsevier",
journal = "LWT",
title = "Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091."
}
Peruško, M., Ghnimi, S., Simović, A., Stevanović, N. R., Radomirović, M. Ž., Gharsallaoui, A., Smiljanić, K., Van Haute, S., Stanić-Vučinić, D.,& Ćirković-Veličković, T. (2021). Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091..
LWT
Elsevier..
Peruško M, Ghnimi S, Simović A, Stevanović NR, Radomirović MŽ, Gharsallaoui A, Smiljanić K, Van Haute S, Stanić-Vučinić D, Ćirković-Veličković T. Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091.. LWT. 2021;
Peruško Marija, Ghnimi Sami, Simović Ana, Stevanović Nikola R., Radomirović Mirjana Ž., Gharsallaoui Adem, Smiljanić Katarina, Van Haute Sam, Stanić-Vučinić Dragana, Ćirković-Veličković Tanja, "Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091." LWT (2021)

The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c

Stanić-Vučinić, Dragana; Nikolić, Stefan; Vlajić, Katarina; Radomirović, Mirjana Ž.; Mihailović, Jelena; Ćirković-Veličković, Tanja; Grgurić-Šipka, Sanja

(Springer, 2020)

TY  - JOUR
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Stefan
AU  - Vlajić, Katarina
AU  - Radomirović, Mirjana Ž.
AU  - Mihailović, Jelena
AU  - Ćirković-Veličković, Tanja
AU  - Grgurić-Šipka, Sanja
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3859
AB  - The reactions of four cymene-capped ruthenium(II) compounds with pro-apaptotic protein, cytochrome c (Cyt), and anti-proliferating protein lysozyme (Ly) in carbonate buffer were investigated by ESI-MS, UV–Vis absorption and CD spectroscopy. The complexes with two chloride ligands (C2 and C3) were more reactive toward proteins than those with only one (C1 and C4), and the complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). Dehalogenated complexes are most likely species initially coordinating proteins for all tested complexes. During the time, protein adducts vividly exchanged non-arene organic ligand L with CO32- and OH-, while cymene moiety was retained. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could generate different intermediate protein species. Although all complexes reduced Cyt, the reduction was not dependent on their reactivity to protein, implying that initially noncovalent binding to Cyt occures, causing its reduction, followed by coordination to protein. Cyt reduction was accompanied with rupture of ferro-Met 80 and occupation of this hem coordination site by a histidine His-33/26. Therefore, in Cyt with C2 and C3 less intensive reduction of hem iron leave more unoccupied target residues for Ru coordination, leading to more efficient formation of covalent adducts, in comparison to C1 and C4. This study contribute to development of new protein-targeted Ru(II) cymene complexes, and to design of new cancer therapies based on targeted delivery of Ru(II) arene complexes bound on pro-apoptotic/anti-proliferating proteins as vehicles.
PB  - Springer
T2  - Journal of Biological Inorganic Chemistry
T1  - The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c
VL  - 25
IS  - 2
SP  - 253
EP  - 265
DO  - 10.1007/s00775-020-01758-3
ER  - 
@article{
author = "Stanić-Vučinić, Dragana and Nikolić, Stefan and Vlajić, Katarina and Radomirović, Mirjana Ž. and Mihailović, Jelena and Ćirković-Veličković, Tanja and Grgurić-Šipka, Sanja",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3859",
abstract = "The reactions of four cymene-capped ruthenium(II) compounds with pro-apaptotic protein, cytochrome c (Cyt), and anti-proliferating protein lysozyme (Ly) in carbonate buffer were investigated by ESI-MS, UV–Vis absorption and CD spectroscopy. The complexes with two chloride ligands (C2 and C3) were more reactive toward proteins than those with only one (C1 and C4), and the complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). Dehalogenated complexes are most likely species initially coordinating proteins for all tested complexes. During the time, protein adducts vividly exchanged non-arene organic ligand L with CO32- and OH-, while cymene moiety was retained. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could generate different intermediate protein species. Although all complexes reduced Cyt, the reduction was not dependent on their reactivity to protein, implying that initially noncovalent binding to Cyt occures, causing its reduction, followed by coordination to protein. Cyt reduction was accompanied with rupture of ferro-Met 80 and occupation of this hem coordination site by a histidine His-33/26. Therefore, in Cyt with C2 and C3 less intensive reduction of hem iron leave more unoccupied target residues for Ru coordination, leading to more efficient formation of covalent adducts, in comparison to C1 and C4. This study contribute to development of new protein-targeted Ru(II) cymene complexes, and to design of new cancer therapies based on targeted delivery of Ru(II) arene complexes bound on pro-apoptotic/anti-proliferating proteins as vehicles.",
publisher = "Springer",
journal = "Journal of Biological Inorganic Chemistry",
title = "The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c",
volume = "25",
number = "2",
pages = "253-265",
doi = "10.1007/s00775-020-01758-3"
}
Stanić-Vučinić, D., Nikolić, S., Vlajić, K., Radomirović, M. Ž., Mihailović, J., Ćirković-Veličković, T.,& Grgurić-Šipka, S. (2020). The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c.
Journal of Biological Inorganic Chemistry
Springer., 25(2), 253-265.
https://doi.org/10.1007/s00775-020-01758-3
Stanić-Vučinić D, Nikolić S, Vlajić K, Radomirović MŽ, Mihailović J, Ćirković-Veličković T, Grgurić-Šipka S. The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c. Journal of Biological Inorganic Chemistry. 2020;25(2):253-265
Stanić-Vučinić Dragana, Nikolić Stefan, Vlajić Katarina, Radomirović Mirjana Ž., Mihailović Jelena, Ćirković-Veličković Tanja, Grgurić-Šipka Sanja, "The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c" Journal of Biological Inorganic Chemistry, 25, no. 2 (2020):253-265,
https://doi.org/10.1007/s00775-020-01758-3 .
2
1

Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3

Stanić-Vučinić, Dragana; Nikolić, Stefan; Vlajić, Katarina; Radomirović, Mirjana Ž.; Mihailović, Jelena; Ćirković-Veličković, Tanja; Grgurić-Šipka, Sanja

(Springer, 2020)

TY  - BOOK
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Stefan
AU  - Vlajić, Katarina
AU  - Radomirović, Mirjana Ž.
AU  - Mihailović, Jelena
AU  - Ćirković-Veličković, Tanja
AU  - Grgurić-Šipka, Sanja
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3863
PB  - Springer
T2  - Journal of Biological Inorganic Chemistry
T1  - Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3
ER  - 
@book{
author = "Stanić-Vučinić, Dragana and Nikolić, Stefan and Vlajić, Katarina and Radomirović, Mirjana Ž. and Mihailović, Jelena and Ćirković-Veličković, Tanja and Grgurić-Šipka, Sanja",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3863",
publisher = "Springer",
journal = "Journal of Biological Inorganic Chemistry",
title = "Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3"
}
Stanić-Vučinić, D., Nikolić, S., Vlajić, K., Radomirović, M. Ž., Mihailović, J., Ćirković-Veličković, T.,& Grgurić-Šipka, S. (2020). Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3.
Journal of Biological Inorganic Chemistry
Springer..
Stanić-Vučinić D, Nikolić S, Vlajić K, Radomirović MŽ, Mihailović J, Ćirković-Veličković T, Grgurić-Šipka S. Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3. Journal of Biological Inorganic Chemistry. 2020;
Stanić-Vučinić Dragana, Nikolić Stefan, Vlajić Katarina, Radomirović Mirjana Ž., Mihailović Jelena, Ćirković-Veličković Tanja, Grgurić-Šipka Sanja, "Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3" Journal of Biological Inorganic Chemistry (2020)

The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c

Stanić-Vučinić, Dragana; Nikolić, Stefan; Vlajić, Katarina; Radomirović, Mirjana Ž.; Mihailović, Jelena; Ćirković-Veličković, Tanja; Grgurić-Šipka, Sanja

(Springer, 2020)

TY  - JOUR
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Stefan
AU  - Vlajić, Katarina
AU  - Radomirović, Mirjana Ž.
AU  - Mihailović, Jelena
AU  - Ćirković-Veličković, Tanja
AU  - Grgurić-Šipka, Sanja
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3942
AB  - The reactions of four cymene-capped ruthenium(II) compounds with pro-apaptotic protein, cytochrome c (Cyt), and anti-proliferating protein lysozyme (Ly) in carbonate buffer were investigated by ESI-MS, UV–Vis absorption and CD spectroscopy. The complexes with two chloride ligands (C2 and C3) were more reactive toward proteins than those with only one (C1 and C4), and the complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). Dehalogenated complexes are most likely species initially coordinating proteins for all tested complexes. During the time, protein adducts vividly exchanged non-arene organic ligand L with CO32- and OH-, while cymene moiety was retained. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could generate different intermediate protein species. Although all complexes reduced Cyt, the reduction was not dependent on their reactivity to protein, implying that initially noncovalent binding to Cyt occures, causing its reduction, followed by coordination to protein. Cyt reduction was accompanied with rupture of ferro-Met 80 and occupation of this hem coordination site by a histidine His-33/26. Therefore, in Cyt with C2 and C3 less intensive reduction of hem iron leave more unoccupied target residues for Ru coordination, leading to more efficient formation of covalent adducts, in comparison to C1 and C4. This study contribute to development of new protein-targeted Ru(II) cymene complexes, and to design of new cancer therapies based on targeted delivery of Ru(II) arene complexes bound on pro-apoptotic/anti-proliferating proteins as vehicles.
PB  - Springer
T2  - Journal of Biological Inorganic Chemistry
T1  - The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c
VL  - 25
IS  - 2
SP  - 253
EP  - 265
DO  - 10.1007/s00775-020-01758-3
ER  - 
@article{
author = "Stanić-Vučinić, Dragana and Nikolić, Stefan and Vlajić, Katarina and Radomirović, Mirjana Ž. and Mihailović, Jelena and Ćirković-Veličković, Tanja and Grgurić-Šipka, Sanja",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3942",
abstract = "The reactions of four cymene-capped ruthenium(II) compounds with pro-apaptotic protein, cytochrome c (Cyt), and anti-proliferating protein lysozyme (Ly) in carbonate buffer were investigated by ESI-MS, UV–Vis absorption and CD spectroscopy. The complexes with two chloride ligands (C2 and C3) were more reactive toward proteins than those with only one (C1 and C4), and the complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). Dehalogenated complexes are most likely species initially coordinating proteins for all tested complexes. During the time, protein adducts vividly exchanged non-arene organic ligand L with CO32- and OH-, while cymene moiety was retained. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could generate different intermediate protein species. Although all complexes reduced Cyt, the reduction was not dependent on their reactivity to protein, implying that initially noncovalent binding to Cyt occures, causing its reduction, followed by coordination to protein. Cyt reduction was accompanied with rupture of ferro-Met 80 and occupation of this hem coordination site by a histidine His-33/26. Therefore, in Cyt with C2 and C3 less intensive reduction of hem iron leave more unoccupied target residues for Ru coordination, leading to more efficient formation of covalent adducts, in comparison to C1 and C4. This study contribute to development of new protein-targeted Ru(II) cymene complexes, and to design of new cancer therapies based on targeted delivery of Ru(II) arene complexes bound on pro-apoptotic/anti-proliferating proteins as vehicles.",
publisher = "Springer",
journal = "Journal of Biological Inorganic Chemistry",
title = "The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c",
volume = "25",
number = "2",
pages = "253-265",
doi = "10.1007/s00775-020-01758-3"
}
Stanić-Vučinić, D., Nikolić, S., Vlajić, K., Radomirović, M. Ž., Mihailović, J., Ćirković-Veličković, T.,& Grgurić-Šipka, S. (2020). The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c.
Journal of Biological Inorganic Chemistry
Springer., 25(2), 253-265.
https://doi.org/10.1007/s00775-020-01758-3
Stanić-Vučinić D, Nikolić S, Vlajić K, Radomirović MŽ, Mihailović J, Ćirković-Veličković T, Grgurić-Šipka S. The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c. Journal of Biological Inorganic Chemistry. 2020;25(2):253-265
Stanić-Vučinić Dragana, Nikolić Stefan, Vlajić Katarina, Radomirović Mirjana Ž., Mihailović Jelena, Ćirković-Veličković Tanja, Grgurić-Šipka Sanja, "The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c" Journal of Biological Inorganic Chemistry, 25, no. 2 (2020):253-265,
https://doi.org/10.1007/s00775-020-01758-3 .
2
1

Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy

Apostolović, Danijela; Mihailović, Jelena; Commins, Scott P.; Wijnveld, Michiel; Kazimirova, Maria; Starkhammar, Maria; Stockinger, Hannes; Platts-Mills, Thomas A. E.; Ćirković-Veličković, Tanja; Hamsten, Carl; van Hage, Marianne

(Wiley, 2020)

TY  - JOUR
AU  - Apostolović, Danijela
AU  - Mihailović, Jelena
AU  - Commins, Scott P.
AU  - Wijnveld, Michiel
AU  - Kazimirova, Maria
AU  - Starkhammar, Maria
AU  - Stockinger, Hannes
AU  - Platts-Mills, Thomas A. E.
AU  - Ćirković-Veličković, Tanja
AU  - Hamsten, Carl
AU  - van Hage, Marianne
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3860
PB  - Wiley
T2  - Allergy: European Journal of Allergy and Clinical Immunology
T1  - Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy
VL  - 75
IS  - 1
SP  - 217
EP  - 220
DO  - 10.1111/ALL.13978
ER  - 
@article{
author = "Apostolović, Danijela and Mihailović, Jelena and Commins, Scott P. and Wijnveld, Michiel and Kazimirova, Maria and Starkhammar, Maria and Stockinger, Hannes and Platts-Mills, Thomas A. E. and Ćirković-Veličković, Tanja and Hamsten, Carl and van Hage, Marianne",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3860",
publisher = "Wiley",
journal = "Allergy: European Journal of Allergy and Clinical Immunology",
title = "Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy",
volume = "75",
number = "1",
pages = "217-220",
doi = "10.1111/ALL.13978"
}
Apostolović, D., Mihailović, J., Commins, S. P., Wijnveld, M., Kazimirova, M., Starkhammar, M., Stockinger, H., Platts-Mills, T. A. E., Ćirković-Veličković, T., Hamsten, C.,& van Hage, M. (2020). Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy.
Allergy: European Journal of Allergy and Clinical Immunology
Wiley., 75(1), 217-220.
https://doi.org/10.1111/ALL.13978
Apostolović D, Mihailović J, Commins SP, Wijnveld M, Kazimirova M, Starkhammar M, Stockinger H, Platts-Mills TAE, Ćirković-Veličković T, Hamsten C, van Hage M. Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy. Allergy: European Journal of Allergy and Clinical Immunology. 2020;75(1):217-220
Apostolović Danijela, Mihailović Jelena, Commins Scott P., Wijnveld Michiel, Kazimirova Maria, Starkhammar Maria, Stockinger Hannes, Platts-Mills Thomas A. E., Ćirković-Veličković Tanja, Hamsten Carl, van Hage Marianne, "Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy" Allergy: European Journal of Allergy and Clinical Immunology, 75, no. 1 (2020):217-220,
https://doi.org/10.1111/ALL.13978 .
10
20
11
17

Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy

Apostolović, Danijela; Mihailović, Jelena; Commins, Scott P.; Wijnveld, Michiel; Kazimirova, Maria; Starkhammar, Maria; Stockinger, Hannes; Platts-Mills, Thomas A. E.; Ćirković-Veličković, Tanja; Hamsten, Carl; van Hage, Marianne

(Wiley, 2020)

TY  - JOUR
AU  - Apostolović, Danijela
AU  - Mihailović, Jelena
AU  - Commins, Scott P.
AU  - Wijnveld, Michiel
AU  - Kazimirova, Maria
AU  - Starkhammar, Maria
AU  - Stockinger, Hannes
AU  - Platts-Mills, Thomas A. E.
AU  - Ćirković-Veličković, Tanja
AU  - Hamsten, Carl
AU  - van Hage, Marianne
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3853
PB  - Wiley
T2  - Allergy: European Journal of Allergy and Clinical Immunology
T1  - Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy
VL  - 75
IS  - 1
SP  - 217
EP  - 220
DO  - 10.1111/all.13978
ER  - 
@article{
author = "Apostolović, Danijela and Mihailović, Jelena and Commins, Scott P. and Wijnveld, Michiel and Kazimirova, Maria and Starkhammar, Maria and Stockinger, Hannes and Platts-Mills, Thomas A. E. and Ćirković-Veličković, Tanja and Hamsten, Carl and van Hage, Marianne",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3853",
publisher = "Wiley",
journal = "Allergy: European Journal of Allergy and Clinical Immunology",
title = "Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy",
volume = "75",
number = "1",
pages = "217-220",
doi = "10.1111/all.13978"
}
Apostolović, D., Mihailović, J., Commins, S. P., Wijnveld, M., Kazimirova, M., Starkhammar, M., Stockinger, H., Platts-Mills, T. A. E., Ćirković-Veličković, T., Hamsten, C.,& van Hage, M. (2020). Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy.
Allergy: European Journal of Allergy and Clinical Immunology
Wiley., 75(1), 217-220.
https://doi.org/10.1111/all.13978
Apostolović D, Mihailović J, Commins SP, Wijnveld M, Kazimirova M, Starkhammar M, Stockinger H, Platts-Mills TAE, Ćirković-Veličković T, Hamsten C, van Hage M. Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy. Allergy: European Journal of Allergy and Clinical Immunology. 2020;75(1):217-220
Apostolović Danijela, Mihailović Jelena, Commins Scott P., Wijnveld Michiel, Kazimirova Maria, Starkhammar Maria, Stockinger Hannes, Platts-Mills Thomas A. E., Ćirković-Veličković Tanja, Hamsten Carl, van Hage Marianne, "Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy" Allergy: European Journal of Allergy and Clinical Immunology, 75, no. 1 (2020):217-220,
https://doi.org/10.1111/all.13978 .
10
20
11
17

Supplementary data for the article: Apostolovic, D.; Mihailovic, J.; Commins, S. P.; Wijnveld, M.; Kazimirova, M.; Starkhammar, M.; Stockinger, H.; Platts-Mills, T. A. E.; Cirkovic Velickovic, T.; Hamsten, C.; et al. Allergenomics of the Tick Ixodes Ricinus Reveals Important α-Gal–Carrying IgE-Binding Proteins in Red Meat Allergy. Allergy: European Journal of Allergy and Clinical Immunology 2020, 75 (1), 217–220. https://doi.org/10.1111/all.13978

Apostolović, Danijela; Mihailović, Jelena; Commins, Scott P.; Wijnveld, Michiel; Kazimirova, Maria; Starkhammar, Maria; Stockinger, Hannes; Platts-Mills, Thomas A. E.; Ćirković-Veličković, Tanja; Hamsten, Carl; van Hage, Marianne

(Wiley, 2020)

TY  - BOOK
AU  - Apostolović, Danijela
AU  - Mihailović, Jelena
AU  - Commins, Scott P.
AU  - Wijnveld, Michiel
AU  - Kazimirova, Maria
AU  - Starkhammar, Maria
AU  - Stockinger, Hannes
AU  - Platts-Mills, Thomas A. E.
AU  - Ćirković-Veličković, Tanja
AU  - Hamsten, Carl
AU  - van Hage, Marianne
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3864
PB  - Wiley
T2  - Allergy: European Journal of Allergy and Clinical Immunology
T1  - Supplementary data for the article: Apostolovic, D.; Mihailovic, J.; Commins, S. P.; Wijnveld, M.; Kazimirova, M.; Starkhammar, M.; Stockinger, H.; Platts-Mills, T. A. E.; Cirkovic Velickovic, T.; Hamsten, C.; et al. Allergenomics of the Tick Ixodes Ricinus Reveals Important α-Gal–Carrying IgE-Binding Proteins in Red Meat Allergy. Allergy: European Journal of Allergy and Clinical Immunology 2020, 75 (1), 217–220. https://doi.org/10.1111/all.13978
ER  - 
@book{
author = "Apostolović, Danijela and Mihailović, Jelena and Commins, Scott P. and Wijnveld, Michiel and Kazimirova, Maria and Starkhammar, Maria and Stockinger, Hannes and Platts-Mills, Thomas A. E. and Ćirković-Veličković, Tanja and Hamsten, Carl and van Hage, Marianne",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3864",
publisher = "Wiley",
journal = "Allergy: European Journal of Allergy and Clinical Immunology",
title = "Supplementary data for the article: Apostolovic, D.; Mihailovic, J.; Commins, S. P.; Wijnveld, M.; Kazimirova, M.; Starkhammar, M.; Stockinger, H.; Platts-Mills, T. A. E.; Cirkovic Velickovic, T.; Hamsten, C.; et al. Allergenomics of the Tick Ixodes Ricinus Reveals Important α-Gal–Carrying IgE-Binding Proteins in Red Meat Allergy. Allergy: European Journal of Allergy and Clinical Immunology 2020, 75 (1), 217–220. https://doi.org/10.1111/all.13978"
}
Apostolović, D., Mihailović, J., Commins, S. P., Wijnveld, M., Kazimirova, M., Starkhammar, M., Stockinger, H., Platts-Mills, T. A. E., Ćirković-Veličković, T., Hamsten, C.,& van Hage, M. (2020). Supplementary data for the article: Apostolovic, D.; Mihailovic, J.; Commins, S. P.; Wijnveld, M.; Kazimirova, M.; Starkhammar, M.; Stockinger, H.; Platts-Mills, T. A. E.; Cirkovic Velickovic, T.; Hamsten, C.; et al. Allergenomics of the Tick Ixodes Ricinus Reveals Important α-Gal–Carrying IgE-Binding Proteins in Red Meat Allergy. Allergy: European Journal of Allergy and Clinical Immunology 2020, 75 (1), 217–220. https://doi.org/10.1111/all.13978.
Allergy: European Journal of Allergy and Clinical Immunology
Wiley..
Apostolović D, Mihailović J, Commins SP, Wijnveld M, Kazimirova M, Starkhammar M, Stockinger H, Platts-Mills TAE, Ćirković-Veličković T, Hamsten C, van Hage M. Supplementary data for the article: Apostolovic, D.; Mihailovic, J.; Commins, S. P.; Wijnveld, M.; Kazimirova, M.; Starkhammar, M.; Stockinger, H.; Platts-Mills, T. A. E.; Cirkovic Velickovic, T.; Hamsten, C.; et al. Allergenomics of the Tick Ixodes Ricinus Reveals Important α-Gal–Carrying IgE-Binding Proteins in Red Meat Allergy. Allergy: European Journal of Allergy and Clinical Immunology 2020, 75 (1), 217–220. https://doi.org/10.1111/all.13978. Allergy: European Journal of Allergy and Clinical Immunology. 2020;
Apostolović Danijela, Mihailović Jelena, Commins Scott P., Wijnveld Michiel, Kazimirova Maria, Starkhammar Maria, Stockinger Hannes, Platts-Mills Thomas A. E., Ćirković-Veličković Tanja, Hamsten Carl, van Hage Marianne, "Supplementary data for the article: Apostolovic, D.; Mihailovic, J.; Commins, S. P.; Wijnveld, M.; Kazimirova, M.; Starkhammar, M.; Stockinger, H.; Platts-Mills, T. A. E.; Cirkovic Velickovic, T.; Hamsten, C.; et al. Allergenomics of the Tick Ixodes Ricinus Reveals Important α-Gal–Carrying IgE-Binding Proteins in Red Meat Allergy. Allergy: European Journal of Allergy and Clinical Immunology 2020, 75 (1), 217–220. https://doi.org/10.1111/all.13978" Allergy: European Journal of Allergy and Clinical Immunology (2020)

Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis

Moons, Jens; de Azambuja, Francisco; Mihailović, Jelena; Kozma, Karoly; Smiljanić, Katarina; Amiri, Mehran; Ćirković-Veličković, Tanja; Nyman, May; Parac-Vogt, Tatjana

(Wiley, 2020)

TY  - JOUR
AU  - Moons, Jens
AU  - de Azambuja, Francisco
AU  - Mihailović, Jelena
AU  - Kozma, Karoly
AU  - Smiljanić, Katarina
AU  - Amiri, Mehran
AU  - Ćirković-Veličković, Tanja
AU  - Nyman, May
AU  - Parac-Vogt, Tatjana
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3917
AB  - The selective hydrolysis of proteins by non‐enzymatic catalysis is difficult to achieve, yet it is crucial for applications in biotechnology and proteomics. Herein, we report that discrete hafnium metal‐oxo cluster [Hf18O10(OH)26(SO4)13⋅(H2O)33] (Hf18), which is centred by the same hexamer motif found in many MOFs, acts as a heterogeneous catalyst for the efficient hydrolysis of horse heart myoglobin (HHM) in low buffer concentrations. Among 154 amino acids present in the sequence of HHM, strictly selective cleavage at only 6 solvent accessible aspartate residues was observed. Mechanistic experiments suggest that the hydrolytic activity is likely derived from the actuation of HfIV Lewis acidic sites and the Brønsted acidic surface of Hf18. X‐ray scattering and ESI‐MS revealed that Hf18 is completely insoluble in these conditions, confirming the HHM hydrolysis is caused by a heterogeneous reaction of the solid Hf18 cluster, and not from smaller, soluble Hf species that could leach into solution.
PB  - Wiley
T2  - Angewandte Chemie (International Edition)
T1  - Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis
VL  - 59
IS  - 17
SP  - 1
EP  - 9
DO  - 10.1002/anie.202001036
ER  - 
@article{
author = "Moons, Jens and de Azambuja, Francisco and Mihailović, Jelena and Kozma, Karoly and Smiljanić, Katarina and Amiri, Mehran and Ćirković-Veličković, Tanja and Nyman, May and Parac-Vogt, Tatjana",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3917",
abstract = "The selective hydrolysis of proteins by non‐enzymatic catalysis is difficult to achieve, yet it is crucial for applications in biotechnology and proteomics. Herein, we report that discrete hafnium metal‐oxo cluster [Hf18O10(OH)26(SO4)13⋅(H2O)33] (Hf18), which is centred by the same hexamer motif found in many MOFs, acts as a heterogeneous catalyst for the efficient hydrolysis of horse heart myoglobin (HHM) in low buffer concentrations. Among 154 amino acids present in the sequence of HHM, strictly selective cleavage at only 6 solvent accessible aspartate residues was observed. Mechanistic experiments suggest that the hydrolytic activity is likely derived from the actuation of HfIV Lewis acidic sites and the Brønsted acidic surface of Hf18. X‐ray scattering and ESI‐MS revealed that Hf18 is completely insoluble in these conditions, confirming the HHM hydrolysis is caused by a heterogeneous reaction of the solid Hf18 cluster, and not from smaller, soluble Hf species that could leach into solution.",
publisher = "Wiley",
journal = "Angewandte Chemie (International Edition)",
title = "Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis",
volume = "59",
number = "17",
pages = "1-9",
doi = "10.1002/anie.202001036"
}
Moons, J., de Azambuja, F., Mihailović, J., Kozma, K., Smiljanić, K., Amiri, M., Ćirković-Veličković, T., Nyman, M.,& Parac-Vogt, T. (2020). Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis.
Angewandte Chemie (International Edition)
Wiley., 59(17), 1-9.
https://doi.org/10.1002/anie.202001036
Moons J, de Azambuja F, Mihailović J, Kozma K, Smiljanić K, Amiri M, Ćirković-Veličković T, Nyman M, Parac-Vogt T. Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis. Angewandte Chemie (International Edition). 2020;59(17):1-9
Moons Jens, de Azambuja Francisco, Mihailović Jelena, Kozma Karoly, Smiljanić Katarina, Amiri Mehran, Ćirković-Veličković Tanja, Nyman May, Parac-Vogt Tatjana, "Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis" Angewandte Chemie (International Edition), 59, no. 17 (2020):1-9,
https://doi.org/10.1002/anie.202001036 .
22
11
5
11

Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation

Gligorijević, Nikola; Radomirović, Mirjana Ž.; Rajković, Andreja; Nedić, Olgica; Ćirković-Veličković, Tanja

(Multidisciplinary Digital Publishing Institute (MDPI), 2020)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Radomirović, Mirjana Ž.
AU  - Rajković, Andreja
AU  - Nedić, Olgica
AU  - Ćirković-Veličković, Tanja
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4235
AB  - The French paradox describes a lower incidence of cardiovascular problems despite a high intake of saturated fats. This phenomenon was associated with higher consumption of red wine, as it was later discovered that the presence of antioxidants, including resveratrol, have beneficial effects. We hypothesized that resveratrol may have a more direct role in protection from harmful oxidation, presumably through binding to important proteins of the blood coagulation process. Spectrofluorimetry demonstrated that resveratrol is capable of binding to fibrinogen, the main protein in the coagulation process, which is also important as a food additive. Various spectroscopic methods determined that binding does not cause fibrinogen unfolding or destabilization since protein melting temperature remains unchanged. A mutually protective effect against the free radical-induced oxidation of polyphenol and fibrinogen was found. The presence of fibrinogen caused only a negligible masking effect of the antioxidative abilities of resveratrol, measured by a reduction of hexacyanoferrate (III), while greatly increasing its solubility in an aqueous environment, thus increasing its potential bioavailability. Due to its interaction with fibrinogen, resveratrol may serve as an antioxidant at the site of injury. The antioxidative effect of resveratrol may also protect and thus keep the desired characteristics of fibrinogen during the application of this protein as a food additive.
PB  - Multidisciplinary Digital Publishing Institute (MDPI)
T2  - Foods
T1  - Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation
VL  - 9
IS  - 6
SP  - 780
DO  - 10.3390/foods9060780
ER  - 
@article{
author = "Gligorijević, Nikola and Radomirović, Mirjana Ž. and Rajković, Andreja and Nedić, Olgica and Ćirković-Veličković, Tanja",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4235",
abstract = "The French paradox describes a lower incidence of cardiovascular problems despite a high intake of saturated fats. This phenomenon was associated with higher consumption of red wine, as it was later discovered that the presence of antioxidants, including resveratrol, have beneficial effects. We hypothesized that resveratrol may have a more direct role in protection from harmful oxidation, presumably through binding to important proteins of the blood coagulation process. Spectrofluorimetry demonstrated that resveratrol is capable of binding to fibrinogen, the main protein in the coagulation process, which is also important as a food additive. Various spectroscopic methods determined that binding does not cause fibrinogen unfolding or destabilization since protein melting temperature remains unchanged. A mutually protective effect against the free radical-induced oxidation of polyphenol and fibrinogen was found. The presence of fibrinogen caused only a negligible masking effect of the antioxidative abilities of resveratrol, measured by a reduction of hexacyanoferrate (III), while greatly increasing its solubility in an aqueous environment, thus increasing its potential bioavailability. Due to its interaction with fibrinogen, resveratrol may serve as an antioxidant at the site of injury. The antioxidative effect of resveratrol may also protect and thus keep the desired characteristics of fibrinogen during the application of this protein as a food additive.",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
journal = "Foods",
title = "Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation",
volume = "9",
number = "6",
pages = "780",
doi = "10.3390/foods9060780"
}
Gligorijević, N., Radomirović, M. Ž., Rajković, A., Nedić, O.,& Ćirković-Veličković, T. (2020). Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation.
Foods
Multidisciplinary Digital Publishing Institute (MDPI)., 9(6), 780.
https://doi.org/10.3390/foods9060780
Gligorijević N, Radomirović MŽ, Rajković A, Nedić O, Ćirković-Veličković T. Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation. Foods. 2020;9(6):780
Gligorijević Nikola, Radomirović Mirjana Ž., Rajković Andreja, Nedić Olgica, Ćirković-Veličković Tanja, "Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation" Foods, 9, no. 6 (2020):780,
https://doi.org/10.3390/foods9060780 .
2
1
1

Accumulation of U, Th, Pb, V, Rb, and Ag in wild Mushrooms macrolepiota procera (Scop.) Singer from Goc, Serbia

Vukojević, Vesna; Đurđić, Slađana Z.; Mutić, Jelena

(2019)

TY  - JOUR
AU  - Vukojević, Vesna
AU  - Đurđić, Slađana Z.
AU  - Mutić, Jelena
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3283
AB  - Cellobiose dehydrogenase (CDH) from Phanerochaete chrysosporium can be used in lactobionic acid production, biosensor for lactose, biofuel cells, lignocellulose degradation, and wound-healing applications. To make it a better biocatalyst, CDH with higher activity in an immobilized form is desirable. For this purpose, CDH was expressed for the first time on the surface of S. cerevisiae EBY100 cells in an active form as a triple mutant tmCDH (D20N, A64T, V592M) and evolved further for higher activity using resazurin-based fluorescent assay. In order to decrease blank reaction of resazurin with yeast cells and to have linear correlation between enzyme activity on the cell surface and fluorescence signal, the assay was optimized with respect to resazurin concentration (0.1 mM), substrate concentration (10mMlactose and 0.08mMcellobiose), and pH (6.0). Using optimized assay an error prone PCR gene library of tmCDH was screened. Two mutants with 5 (H5) and 7 mutations (H9) were found having two times higher activity than the parent tmCDH enzyme that already had improved activity compared to wild type CDH whose activity could not be detected on the surface of yeast cells.
T2  - Environmental Science and Pollution Research
T1  - Accumulation of U, Th, Pb, V, Rb, and Ag in wild Mushrooms macrolepiota procera (Scop.) Singer from Goc, Serbia
VL  - 26
IS  - 13
SP  - 13147
EP  - 13158
DO  - 10.1007/s11356-019-04723-z
ER  - 
@article{
author = "Vukojević, Vesna and Đurđić, Slađana Z. and Mutić, Jelena",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3283",
abstract = "Cellobiose dehydrogenase (CDH) from Phanerochaete chrysosporium can be used in lactobionic acid production, biosensor for lactose, biofuel cells, lignocellulose degradation, and wound-healing applications. To make it a better biocatalyst, CDH with higher activity in an immobilized form is desirable. For this purpose, CDH was expressed for the first time on the surface of S. cerevisiae EBY100 cells in an active form as a triple mutant tmCDH (D20N, A64T, V592M) and evolved further for higher activity using resazurin-based fluorescent assay. In order to decrease blank reaction of resazurin with yeast cells and to have linear correlation between enzyme activity on the cell surface and fluorescence signal, the assay was optimized with respect to resazurin concentration (0.1 mM), substrate concentration (10mMlactose and 0.08mMcellobiose), and pH (6.0). Using optimized assay an error prone PCR gene library of tmCDH was screened. Two mutants with 5 (H5) and 7 mutations (H9) were found having two times higher activity than the parent tmCDH enzyme that already had improved activity compared to wild type CDH whose activity could not be detected on the surface of yeast cells.",
journal = "Environmental Science and Pollution Research",
title = "Accumulation of U, Th, Pb, V, Rb, and Ag in wild Mushrooms macrolepiota procera (Scop.) Singer from Goc, Serbia",
volume = "26",
number = "13",
pages = "13147-13158",
doi = "10.1007/s11356-019-04723-z"
}
Vukojević, V., Đurđić, S. Z.,& Mutić, J. (2019). Accumulation of U, Th, Pb, V, Rb, and Ag in wild Mushrooms macrolepiota procera (Scop.) Singer from Goc, Serbia.
Environmental Science and Pollution Research, 26(13), 13147-13158.
https://doi.org/10.1007/s11356-019-04723-z
Vukojević V, Đurđić SZ, Mutić J. Accumulation of U, Th, Pb, V, Rb, and Ag in wild Mushrooms macrolepiota procera (Scop.) Singer from Goc, Serbia. Environmental Science and Pollution Research. 2019;26(13):13147-13158
Vukojević Vesna, Đurđić Slađana Z., Mutić Jelena, "Accumulation of U, Th, Pb, V, Rb, and Ag in wild Mushrooms macrolepiota procera (Scop.) Singer from Goc, Serbia" Environmental Science and Pollution Research, 26, no. 13 (2019):13147-13158,
https://doi.org/10.1007/s11356-019-04723-z .
9
8
9

Supplementary data for the article: Vukojević, V.; Durđić, S.; Mutić, J. Accumulation of U, Th, Pb, V, Rb, and Ag in Wild Mushrooms Macrolepiota Procera (Scop.) Singer from Goc, Serbia. Environ. Sci. Pollut. Res. 2019, 26 (13), 13147–13158. https://doi.org/10.1007/s11356-019-04723-z

Vukojević, Vesna; Đurđić, Slađana Z.; Mutić, Jelena

(2019)

TY  - BOOK
AU  - Vukojević, Vesna
AU  - Đurđić, Slađana Z.
AU  - Mutić, Jelena
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3284
T2  - Environmental Science and Pollution Research
T1  - Supplementary data for the article: Vukojević, V.; Durđić, S.; Mutić, J. Accumulation of U, Th, Pb, V, Rb, and Ag in Wild Mushrooms Macrolepiota Procera (Scop.) Singer from Goc, Serbia. Environ. Sci. Pollut. Res. 2019, 26 (13), 13147–13158. https://doi.org/10.1007/s11356-019-04723-z
ER  - 
@book{
author = "Vukojević, Vesna and Đurđić, Slađana Z. and Mutić, Jelena",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3284",
journal = "Environmental Science and Pollution Research",
title = "Supplementary data for the article: Vukojević, V.; Durđić, S.; Mutić, J. Accumulation of U, Th, Pb, V, Rb, and Ag in Wild Mushrooms Macrolepiota Procera (Scop.) Singer from Goc, Serbia. Environ. Sci. Pollut. Res. 2019, 26 (13), 13147–13158. https://doi.org/10.1007/s11356-019-04723-z"
}
Vukojević, V., Đurđić, S. Z.,& Mutić, J. (2019). Supplementary data for the article: Vukojević, V.; Durđić, S.; Mutić, J. Accumulation of U, Th, Pb, V, Rb, and Ag in Wild Mushrooms Macrolepiota Procera (Scop.) Singer from Goc, Serbia. Environ. Sci. Pollut. Res. 2019, 26 (13), 13147–13158. https://doi.org/10.1007/s11356-019-04723-z.
Environmental Science and Pollution Research.
Vukojević V, Đurđić SZ, Mutić J. Supplementary data for the article: Vukojević, V.; Durđić, S.; Mutić, J. Accumulation of U, Th, Pb, V, Rb, and Ag in Wild Mushrooms Macrolepiota Procera (Scop.) Singer from Goc, Serbia. Environ. Sci. Pollut. Res. 2019, 26 (13), 13147–13158. https://doi.org/10.1007/s11356-019-04723-z. Environmental Science and Pollution Research. 2019;
Vukojević Vesna, Đurđić Slađana Z., Mutić Jelena, "Supplementary data for the article: Vukojević, V.; Durđić, S.; Mutić, J. Accumulation of U, Th, Pb, V, Rb, and Ag in Wild Mushrooms Macrolepiota Procera (Scop.) Singer from Goc, Serbia. Environ. Sci. Pollut. Res. 2019, 26 (13), 13147–13158. https://doi.org/10.1007/s11356-019-04723-z" Environmental Science and Pollution Research (2019)

Klasifikacija školjki na osnovu sadržaja esencijalnih elemenata i hemometrije

Mutić, Jelena; Jovanović, Vesna; Ristivojević, Petar; Milojković-Opsenica, Dušanka; Đurđić, Slađana Z.; Ćirković-Veličković, Tanja

(Beograd : Srpsko hemijsko društvo, 2019)

TY  - CONF
AU  - Mutić, Jelena
AU  - Jovanović, Vesna
AU  - Ristivojević, Petar
AU  - Milojković-Opsenica, Dušanka
AU  - Đurđić, Slađana Z.
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3760
AB  - Cilj ove studije je klasifikacija biološki različitih vrsta školjki na osnovu sadržaja esencijalnih elemenata primenom hemometrije. Sadržaj esencijalnih elemenata kao što su Co, Cr, Cu, Mn, Ni, Se, Zn, i Fe je određen u četiri biološki različite vrste školjki Ruditapes philippinarum (Manila clam, MC), Yesso scallop (YS), Tegillarca granosa (TG) i Anadara brоughtonii (AB). Analizitani uzorci su kupljeni u Incheonu, Koreja. Sadržaj esenicjalnih elemenata je određen primenom induktivno spregnute plazme kuplovane sa masenom spektrometrijom (ICP-MS) nakon mikrotalasne digestije. Hemometrijske tehnike pokazuju grupisanje ispitivanih uzoraka školjki prema sadržaju esencijalnih elemenata i identifikuju elemente najvažnije za klasifikaciju.
AB  - The main aim of current study was classification of four biologically different sellfish species such as bivalve molluscs Ruditapes philippinarum (Manila clam, MC), Yesso scallop (YS), Tegillarca granosa (TG) and Anadara broughtonii (AB) bought in the Incheon, South Korea. Content of essencial ellements such as Co, Cr, Cu, Mn, Ni, Se, Zn, and Fe were determined by using inductively coupled plasma mass spectrometry (ICP-MS) after closed-vessel microwave digestion. Chemometrics techniques showed classification of sellfish smaples based on biological species and identified elements most important for classification.
PB  - Beograd : Srpsko hemijsko društvo
C3  - Kratki izvodi radova / 56. savetovanje Srpskog hemijskog društva , Niš 7. i 8. juni 2019.
T1  - Klasifikacija školjki na osnovu sadržaja esencijalnih elemenata i hemometrije
T1  - Chemometric characterization of sellfish according to their element composition
ER  - 
@conference{
author = "Mutić, Jelena and Jovanović, Vesna and Ristivojević, Petar and Milojković-Opsenica, Dušanka and Đurđić, Slađana Z. and Ćirković-Veličković, Tanja",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3760",
abstract = "Cilj ove studije je klasifikacija biološki različitih vrsta školjki na osnovu sadržaja esencijalnih elemenata primenom hemometrije. Sadržaj esencijalnih elemenata kao što su Co, Cr, Cu, Mn, Ni, Se, Zn, i Fe je određen u četiri biološki različite vrste školjki Ruditapes philippinarum (Manila clam, MC), Yesso scallop (YS), Tegillarca granosa (TG) i Anadara brоughtonii (AB). Analizitani uzorci su kupljeni u Incheonu, Koreja. Sadržaj esenicjalnih elemenata je određen primenom induktivno spregnute plazme kuplovane sa masenom spektrometrijom (ICP-MS) nakon mikrotalasne digestije. Hemometrijske tehnike pokazuju grupisanje ispitivanih uzoraka školjki prema sadržaju esencijalnih elemenata i identifikuju elemente najvažnije za klasifikaciju., The main aim of current study was classification of four biologically different sellfish species such as bivalve molluscs Ruditapes philippinarum (Manila clam, MC), Yesso scallop (YS), Tegillarca granosa (TG) and Anadara broughtonii (AB) bought in the Incheon, South Korea. Content of essencial ellements such as Co, Cr, Cu, Mn, Ni, Se, Zn, and Fe were determined by using inductively coupled plasma mass spectrometry (ICP-MS) after closed-vessel microwave digestion. Chemometrics techniques showed classification of sellfish smaples based on biological species and identified elements most important for classification.",
publisher = "Beograd : Srpsko hemijsko društvo",
journal = "Kratki izvodi radova / 56. savetovanje Srpskog hemijskog društva , Niš 7. i 8. juni 2019.",
title = "Klasifikacija školjki na osnovu sadržaja esencijalnih elemenata i hemometrije, Chemometric characterization of sellfish according to their element composition"
}
Mutić, J., Jovanović, V., Ristivojević, P., Milojković-Opsenica, D., Đurđić, S. Z.,& Ćirković-Veličković, T. (2019). Chemometric characterization of sellfish according to their element composition.
Kratki izvodi radova / 56. savetovanje Srpskog hemijskog društva , Niš 7. i 8. juni 2019.
Beograd : Srpsko hemijsko društvo..
Mutić J, Jovanović V, Ristivojević P, Milojković-Opsenica D, Đurđić SZ, Ćirković-Veličković T. Chemometric characterization of sellfish according to their element composition. Kratki izvodi radova / 56. savetovanje Srpskog hemijskog društva , Niš 7. i 8. juni 2019.. 2019;
Mutić Jelena, Jovanović Vesna, Ristivojević Petar, Milojković-Opsenica Dušanka, Đurđić Slađana Z., Ćirković-Veličković Tanja, "Chemometric characterization of sellfish according to their element composition" Kratki izvodi radova / 56. savetovanje Srpskog hemijskog društva , Niš 7. i 8. juni 2019. (2019)

Određivanje toksičnih elemenata (žive, kadmijuma, olova i arsena) u uzorcima školjki

Đurđić, Slađana Z.; Jovanović, Vesna; Tomić, Sofija; Ćirković-Veličković, Tanja; Mutić, Jelena

(Beograd : Srpsko hemijsko društvo, 2019)

TY  - CONF
AU  - Đurđić, Slađana Z.
AU  - Jovanović, Vesna
AU  - Tomić, Sofija
AU  - Ćirković-Veličković, Tanja
AU  - Mutić, Jelena
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3762
AB  - Morski plodovi imaju visoku nutritivnu vrednost, ali sa druge strane postoji rizik od kontaminacije toksičnim elementima. Sadržaj As, Cd, Hg i Pb je određen u četiri vrste školjki Ruditapes philippinarum (Manila clam, MC), Yesso scallop (YS), Tegillarca granosa (TG) i Anadara broughtonii (AB) kupljene u Incheonu, Koreja. Uzorci su analizirani induktivno spregnutom plazmom - masenom spektrometrijom (ICP-MS) nakon mikrotalasne digestije. Izračunati su dnevni/nedeljni unosi za ove elemente u mg/300 g uzorka. Ukupan sadržaj As (neoganski i organski) u svim vrstama je bio veći od dozvoljenog limita preporučenog od Svetske zdravstvene organizacije (WHO). Procenjeni dnevni unosi ostalih elemenata (Hg, Cd i Pb) su niži od maksimalnih podnošljivih granica (MDI) koje je odredila Evropska agencija za bezbednost hrane (EFSA) što ukazuje da nema rizika za konzumente.
AB  - Bivalve molluscs, which include mussels, oysters and clams, have high nutritional value. On the other hand, seafood may also contain harmful contaminants and other undesirable substances such as mercury and persistent halogenated compounds. Four species of bivalve molluscs Ruditapes philippinarum (Manila clam, MC), Yesso scallop (YS), Tegillarca granosa (TG) and Anadara broughtonii (AB) were bought in Incheon, Korea, in order to determine content of As, Cd, Hg, and Pb and consequently, to estimate the health hazards associated to dietary intake. The samples were analyzed by inductively coupled plasma mass spectrometry (ICP-MS) after microwave digestion. All species showed As content higher than the maximum tolerable limit specified by EFSA. Estimated daily intake of Hg, Cd and Pb from consumption of 300 g was very low and hence poses no toxicological risk.
PB  - Beograd : Srpsko hemijsko društvo
C3  - Kratki izvodi radova / 56. savetovanje Srpskog hemijskog društva , Niš 7. i 8. juni 2019.
T1  - Određivanje toksičnih elemenata (žive, kadmijuma, olova i arsena) u uzorcima školjki
T1  - Determination of toxic elements (mercury, cadmium, lead and arsenic) in shellfish samples
ER  - 
@conference{
author = "Đurđić, Slađana Z. and Jovanović, Vesna and Tomić, Sofija and Ćirković-Veličković, Tanja and Mutić, Jelena",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3762",
abstract = "Morski plodovi imaju visoku nutritivnu vrednost, ali sa druge strane postoji rizik od kontaminacije toksičnim elementima. Sadržaj As, Cd, Hg i Pb je određen u četiri vrste školjki Ruditapes philippinarum (Manila clam, MC), Yesso scallop (YS), Tegillarca granosa (TG) i Anadara broughtonii (AB) kupljene u Incheonu, Koreja. Uzorci su analizirani induktivno spregnutom plazmom - masenom spektrometrijom (ICP-MS) nakon mikrotalasne digestije. Izračunati su dnevni/nedeljni unosi za ove elemente u mg/300 g uzorka. Ukupan sadržaj As (neoganski i organski) u svim vrstama je bio veći od dozvoljenog limita preporučenog od Svetske zdravstvene organizacije (WHO). Procenjeni dnevni unosi ostalih elemenata (Hg, Cd i Pb) su niži od maksimalnih podnošljivih granica (MDI) koje je odredila Evropska agencija za bezbednost hrane (EFSA) što ukazuje da nema rizika za konzumente., Bivalve molluscs, which include mussels, oysters and clams, have high nutritional value. On the other hand, seafood may also contain harmful contaminants and other undesirable substances such as mercury and persistent halogenated compounds. Four species of bivalve molluscs Ruditapes philippinarum (Manila clam, MC), Yesso scallop (YS), Tegillarca granosa (TG) and Anadara broughtonii (AB) were bought in Incheon, Korea, in order to determine content of As, Cd, Hg, and Pb and consequently, to estimate the health hazards associated to dietary intake. The samples were analyzed by inductively coupled plasma mass spectrometry (ICP-MS) after microwave digestion. All species showed As content higher than the maximum tolerable limit specified by EFSA. Estimated daily intake of Hg, Cd and Pb from consumption of 300 g was very low and hence poses no toxicological risk.",
publisher = "Beograd : Srpsko hemijsko društvo",
journal = "Kratki izvodi radova / 56. savetovanje Srpskog hemijskog društva , Niš 7. i 8. juni 2019.",
title = "Određivanje toksičnih elemenata (žive, kadmijuma, olova i arsena) u uzorcima školjki, Determination of toxic elements (mercury, cadmium, lead and arsenic) in shellfish samples"
}
Đurđić, S. Z., Jovanović, V., Tomić, S., Ćirković-Veličković, T.,& Mutić, J. (2019). Determination of toxic elements (mercury, cadmium, lead and arsenic) in shellfish samples.
Kratki izvodi radova / 56. savetovanje Srpskog hemijskog društva , Niš 7. i 8. juni 2019.
Beograd : Srpsko hemijsko društvo..
Đurđić SZ, Jovanović V, Tomić S, Ćirković-Veličković T, Mutić J. Determination of toxic elements (mercury, cadmium, lead and arsenic) in shellfish samples. Kratki izvodi radova / 56. savetovanje Srpskog hemijskog društva , Niš 7. i 8. juni 2019.. 2019;
Đurđić Slađana Z., Jovanović Vesna, Tomić Sofija, Ćirković-Veličković Tanja, Mutić Jelena, "Determination of toxic elements (mercury, cadmium, lead and arsenic) in shellfish samples" Kratki izvodi radova / 56. savetovanje Srpskog hemijskog društva , Niš 7. i 8. juni 2019. (2019)

Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments

Smiljanić, Katarina; Prodić, Ivana; Apostolović, Danijela; Mutić, Jelena; van Hage, Marianne; Burazer, Lidija M.; Ćirković-Veličković, Tanja

(Belgrade : Faculty of Chemistry, 2019)

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Mutić, Jelena
AU  - van Hage, Marianne
AU  - Burazer, Lidija M.
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3742
AB  - Field-realistic exposure studies provide the most relevant assessment of the
effects of the intensity and diversity of urban and industrial contamination on
pollen structure and allergenicity. The significance of in-depth post-translational
modification (PTM) studies of pollen proteomes, when compared with studies on
other aspects of pollution and altered pollen allergenicity, has not yet been
determined; hence, little progress has been made within this field.
PB  - Belgrade : Faculty of Chemistry
C3  - 1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia
T1  - Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments
SP  - 6
EP  - 7
ER  - 
@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3742",
abstract = "Field-realistic exposure studies provide the most relevant assessment of the
effects of the intensity and diversity of urban and industrial contamination on
pollen structure and allergenicity. The significance of in-depth post-translational
modification (PTM) studies of pollen proteomes, when compared with studies on
other aspects of pollution and altered pollen allergenicity, has not yet been
determined; hence, little progress has been made within this field.",
publisher = "Belgrade : Faculty of Chemistry",
journal = "1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia",
title = "Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments",
pages = "6-7"
}
Smiljanić, K., Prodić, I., Apostolović, D., Mutić, J., van Hage, M., Burazer, L. M.,& Ćirković-Veličković, T. (2019). Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments.
1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia
Belgrade : Faculty of Chemistry., 6-7.
Smiljanić K, Prodić I, Apostolović D, Mutić J, van Hage M, Burazer LM, Ćirković-Veličković T. Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments. 1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia. 2019;:6-7
Smiljanić Katarina, Prodić Ivana, Apostolović Danijela, Mutić Jelena, van Hage Marianne, Burazer Lidija M., Ćirković-Veličković Tanja, "Highly improved method for in-depth post-translational modification profiling: example of Timothy grass (Phleum pratense) pollen proteomes from polluted and preserved environments" 1st FoodEnTwin Workshop "Food and Environmental - Omics", June 20-21, 2019 Belgrade, Serbia (2019):6-7

Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution

Smiljanić, Katarina; Prodić, Ivana; Apostolović, Danijela; Mutić, Jelena; van Hage, Marianne; Burazer, Lidija M.; Ćirković-Veličković, Tanja

(2019)

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Mutić, Jelena
AU  - van Hage, Marianne
AU  - Burazer, Lidija M.
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3763
AB  - The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. 
Therefore, we created a comprehensive approach for the comparison of pollen from polluted and environmentally preserved areas. To examine the effects of long-term, in vivo pollen exposure to multiple source pollutants, Phleum pratense (Timothy grass) pollen samples were collected along a regional road in Kruševac, central Serbia and were compared with pollen samples from rural, environmentally preserved area over two consecutive pollination seasons. We combined the quantitative comparison of proteome expression profiles from in-solution and 2D-gels with unrestrictive in-depth quantitative PTM profiling using high resolution tandem mass spectrometry and the PEAKS 8.5 Suite platform.
An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, and significantly higher content of mercury, cadmium, and manganese. Antioxidative defense-related enzymes were significantly upregulated. Seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected pollen allergens, especially Phl p 6, with several different oxidative modifications. 
Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach was used for the first time to map extensive modifications in the pollen proteome, reflecting increased environmental oxidative stress, primarily caused by increased content of heavy metals in pollen.
C3  - XIV Italian Proteomics Association Annual Meeting with HPS, 2019.
T1  - Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution
SP  - 38
EP  - 38
ER  - 
@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3763",
abstract = "The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. 
Therefore, we created a comprehensive approach for the comparison of pollen from polluted and environmentally preserved areas. To examine the effects of long-term, in vivo pollen exposure to multiple source pollutants, Phleum pratense (Timothy grass) pollen samples were collected along a regional road in Kruševac, central Serbia and were compared with pollen samples from rural, environmentally preserved area over two consecutive pollination seasons. We combined the quantitative comparison of proteome expression profiles from in-solution and 2D-gels with unrestrictive in-depth quantitative PTM profiling using high resolution tandem mass spectrometry and the PEAKS 8.5 Suite platform.
An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, and significantly higher content of mercury, cadmium, and manganese. Antioxidative defense-related enzymes were significantly upregulated. Seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected pollen allergens, especially Phl p 6, with several different oxidative modifications. 
Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach was used for the first time to map extensive modifications in the pollen proteome, reflecting increased environmental oxidative stress, primarily caused by increased content of heavy metals in pollen.",
journal = "XIV Italian Proteomics Association Annual Meeting with HPS, 2019.",
title = "Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution",
pages = "38-38"
}
Smiljanić, K., Prodić, I., Apostolović, D., Mutić, J., van Hage, M., Burazer, L. M.,& Ćirković-Veličković, T. (2019). Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution.
XIV Italian Proteomics Association Annual Meeting with HPS, 2019., 38-38.
Smiljanić K, Prodić I, Apostolović D, Mutić J, van Hage M, Burazer LM, Ćirković-Veličković T. Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution. XIV Italian Proteomics Association Annual Meeting with HPS, 2019.. 2019;:38-38
Smiljanić Katarina, Prodić Ivana, Apostolović Danijela, Mutić Jelena, van Hage Marianne, Burazer Lidija M., Ćirković-Veličković Tanja, "Unrestricted and quantitative method of post translational modifications profiling: Timothy grass pollen proteome in relation to increased oxidative stress caused by enviromental pollution" XIV Italian Proteomics Association Annual Meeting with HPS, 2019. (2019):38-38

Study of element contents in bivalve molluscs: health benefit and risk

Tomić, Sofija; Jovanović, Vesna B.; Ristivojević, Petar; Milojković-Opsenica, Dušanka; Đurić, Slađana; Mutić, Jelena; Ćirković-Veličković, Tanja

(Portugal : Sociedade Portuguesa de Química, 2019)

TY  - CONF
AU  - Tomić, Sofija
AU  - Jovanović, Vesna B.
AU  - Ristivojević, Petar
AU  - Milojković-Opsenica, Dušanka
AU  - Đurić, Slađana
AU  - Mutić, Jelena
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3778
AB  - Bivalve molluscs, which include mussels, oysters and clams, have high nutritional value. They are regarded as a good source for proteins, lipids, carbohydrates and minerals [1]. On the other hand, seafood may also contain harmful contaminants and other undesirable substances such as mercury and persistent halogenated compounds, which has resulted in a number of risk-benefit assessments during the last decade [2].
Four species of bivalve molluscs Ruditapes philippinarum (Manila clam, MC), Yesso scallop (YS), Tegillarca granosa (TG) and Anadara broughtonii (AB) were bought in two fish markets in Incheon, Korea, in order to determine content of As, Cd, Co, Cr, Cu, Hg, Mn, Ni, Pb, Se, Zn, and Fe and consequently, to estimate the health hazards associated to dietary intake. The samples were analyzed by inductively coupled plasma mass spectrometry (ICP-MS) after closed-vessel microwave digestion. The analytical accuracy of the method was evaluated by using the SRM (TORT-2, lobster hepatopancreas). Application of principal component analysis (PCA) and hierarchical cluster analysis (HCA) showed a tendency to form three groups between samples belonging to different genus of samples.
European food safety authority (EFSA) has established recommended daily intake (RDI) values for Cu, Fe, Mn and Zn of 3, 14, 5 and 10 mg/day, respectively. We calculated the RDI for daily consumption in milligrams per 300 g of sample. Our results showed that these species could serve as a good dietary source of essential elements, especially Fe, Mn and Zn. However, all species showed As content higher than the maximum tolerable limit specified by EFSA. Seafood is the major contributor to As in the diet though As in seafood mostly occurs as organic As species [3]. In addition, content of Mn in Yesso scallop is few times higher than in other species.
PB  - Portugal : Sociedade Portuguesa de Química
C3  - Book of Abstracts of the XX EuroFoodChem Congress EDITORS
T1  - Study of element contents in bivalve molluscs: health benefit and risk
ER  - 
@conference{
author = "Tomić, Sofija and Jovanović, Vesna B. and Ristivojević, Petar and Milojković-Opsenica, Dušanka and Đurić, Slađana and Mutić, Jelena and Ćirković-Veličković, Tanja",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3778",
abstract = "Bivalve molluscs, which include mussels, oysters and clams, have high nutritional value. They are regarded as a good source for proteins, lipids, carbohydrates and minerals [1]. On the other hand, seafood may also contain harmful contaminants and other undesirable substances such as mercury and persistent halogenated compounds, which has resulted in a number of risk-benefit assessments during the last decade [2].
Four species of bivalve molluscs Ruditapes philippinarum (Manila clam, MC), Yesso scallop (YS), Tegillarca granosa (TG) and Anadara broughtonii (AB) were bought in two fish markets in Incheon, Korea, in order to determine content of As, Cd, Co, Cr, Cu, Hg, Mn, Ni, Pb, Se, Zn, and Fe and consequently, to estimate the health hazards associated to dietary intake. The samples were analyzed by inductively coupled plasma mass spectrometry (ICP-MS) after closed-vessel microwave digestion. The analytical accuracy of the method was evaluated by using the SRM (TORT-2, lobster hepatopancreas). Application of principal component analysis (PCA) and hierarchical cluster analysis (HCA) showed a tendency to form three groups between samples belonging to different genus of samples.
European food safety authority (EFSA) has established recommended daily intake (RDI) values for Cu, Fe, Mn and Zn of 3, 14, 5 and 10 mg/day, respectively. We calculated the RDI for daily consumption in milligrams per 300 g of sample. Our results showed that these species could serve as a good dietary source of essential elements, especially Fe, Mn and Zn. However, all species showed As content higher than the maximum tolerable limit specified by EFSA. Seafood is the major contributor to As in the diet though As in seafood mostly occurs as organic As species [3]. In addition, content of Mn in Yesso scallop is few times higher than in other species.",
publisher = "Portugal : Sociedade Portuguesa de Química",
journal = "Book of Abstracts of the XX EuroFoodChem Congress EDITORS",
title = "Study of element contents in bivalve molluscs: health benefit and risk"
}
Tomić, S., Jovanović, V. B., Ristivojević, P., Milojković-Opsenica, D., Đurić, S., Mutić, J.,& Ćirković-Veličković, T. (2019). Study of element contents in bivalve molluscs: health benefit and risk.
Book of Abstracts of the XX EuroFoodChem Congress EDITORS
Portugal : Sociedade Portuguesa de Química..
Tomić S, Jovanović VB, Ristivojević P, Milojković-Opsenica D, Đurić S, Mutić J, Ćirković-Veličković T. Study of element contents in bivalve molluscs: health benefit and risk. Book of Abstracts of the XX EuroFoodChem Congress EDITORS. 2019;
Tomić Sofija, Jovanović Vesna B., Ristivojević Petar, Milojković-Opsenica Dušanka, Đurić Slađana, Mutić Jelena, Ćirković-Veličković Tanja, "Study of element contents in bivalve molluscs: health benefit and risk" Book of Abstracts of the XX EuroFoodChem Congress EDITORS (2019)

In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress

Smiljanić, Katarina; Prodić, Ivana; Apostolović, Danijela; Cvetković, Anka; Veljović, Đorđe; Mutić, Jelena; van Hage, Marianne; Burazer, Lidija M.; Ćirković-Veličković, Tanja

(Elsevier, 2019)

TY  - JOUR
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Cvetković, Anka
AU  - Veljović, Đorđe
AU  - Mutić, Jelena
AU  - van Hage, Marianne
AU  - Burazer, Lidija M.
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2857
AB  - An association between pollution (e.g., from traffic emissions) and the increased prevalence of respiratory allergies has been observed. Field-realistic exposure studies provide the most relevant assessment of the effects of the intensity and diversity of urban and industrial contamination on pollen structure and allergenicity. The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. We undertook a comprehensive comparative analysis of multiple polluted and environmentally preserved Phleum pratense (Timothy grass) pollen samples using scanning electron microscopy, in-depth PTM profiling, determination of organic and inorganic pollutants, analysis of the release of sub-pollen particles and phenols/proteins, and analysis of proteome expression using high resolution tandem mass spectrometry. In addition, we used quantitative enzyme-linked immunosorbent assays (ELISA) and immunoglobulin E (IgE) immunoblotting. An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, including a significantly higher content of mercury, cadmium, and manganese, with irregular long spines on pollen grain surface structures. Antioxidative defense-related enzymes were significantly upregulated and seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected several Timothy pollen allergens; Phl p 6, in particular, exhibited several different oxidative modifications. The expression of Phl p 6, 12, and 13 allergens were downregulated in polluted pollen, and IgE binding to pollen extract was substantially lower in the 18 patients studied, as measured by quantitative ELISA. Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed to modification of Timothy pollen allergens and suggested that heavy metals are primarily responsible for oxidative stress effects observed in pollen proteins.
PB  - Elsevier
T2  - Environment International
T1  - In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress
VL  - 126
SP  - 644
EP  - 658
DO  - 10.1016/j.envint.2019.03.001
ER  - 
@article{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Cvetković, Anka and Veljović, Đorđe and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2857",
abstract = "An association between pollution (e.g., from traffic emissions) and the increased prevalence of respiratory allergies has been observed. Field-realistic exposure studies provide the most relevant assessment of the effects of the intensity and diversity of urban and industrial contamination on pollen structure and allergenicity. The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. We undertook a comprehensive comparative analysis of multiple polluted and environmentally preserved Phleum pratense (Timothy grass) pollen samples using scanning electron microscopy, in-depth PTM profiling, determination of organic and inorganic pollutants, analysis of the release of sub-pollen particles and phenols/proteins, and analysis of proteome expression using high resolution tandem mass spectrometry. In addition, we used quantitative enzyme-linked immunosorbent assays (ELISA) and immunoglobulin E (IgE) immunoblotting. An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, including a significantly higher content of mercury, cadmium, and manganese, with irregular long spines on pollen grain surface structures. Antioxidative defense-related enzymes were significantly upregulated and seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected several Timothy pollen allergens; Phl p 6, in particular, exhibited several different oxidative modifications. The expression of Phl p 6, 12, and 13 allergens were downregulated in polluted pollen, and IgE binding to pollen extract was substantially lower in the 18 patients studied, as measured by quantitative ELISA. Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed to modification of Timothy pollen allergens and suggested that heavy metals are primarily responsible for oxidative stress effects observed in pollen proteins.",
publisher = "Elsevier",
journal = "Environment International",
title = "In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress",
volume = "126",
pages = "644-658",
doi = "10.1016/j.envint.2019.03.001"
}
Smiljanić, K., Prodić, I., Apostolović, D., Cvetković, A., Veljović, Đ., Mutić, J., van Hage, M., Burazer, L. M.,& Ćirković-Veličković, T. (2019). In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress.
Environment International
Elsevier., 126, 644-658.
https://doi.org/10.1016/j.envint.2019.03.001
Smiljanić K, Prodić I, Apostolović D, Cvetković A, Veljović Đ, Mutić J, van Hage M, Burazer LM, Ćirković-Veličković T. In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress. Environment International. 2019;126:644-658
Smiljanić Katarina, Prodić Ivana, Apostolović Danijela, Cvetković Anka, Veljović Đorđe, Mutić Jelena, van Hage Marianne, Burazer Lidija M., Ćirković-Veličković Tanja, "In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress" Environment International, 126 (2019):644-658,
https://doi.org/10.1016/j.envint.2019.03.001 .
2
5
2
5

Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study

Radibratović, Milica; Al-Hanish, Ayah; Minić, Simeon L.; Radomirović, Mirjana Ž.; Milčić, Miloš K.; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier, 2019)

TY  - JOUR
AU  - Radibratović, Milica
AU  - Al-Hanish, Ayah
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3733
AB  - α-Lactalbumin (ALA) is a Ca2+-binding protein which constitutes up to 20% of whey protein. At acidic pH, and in the apo-state at elevated temperatures, ALA is the classic 'molten globule' (MG). This study examined epigallo-catechin-3-gallate (EGCG) binding to ALA in its apo form (apoALA) and stabilizing effect on protein structure thereof. 

EGCG binds to apoALA in both native and MG state. The complex of EGCG and ALA is more stable to thermal denaturation. The docking analysis and molecular dynamic simulation (MDS) showed that Ca2+ removal decreased conformational stability of ALA, because of the local destabilization of Ca2+-binding region. EGCG binding to apoALA increases its stability by reverting of conformation and stability of Ca2+-binding region. Therefore, EGCG-induced thermal stability of apoALA is based on increased apoALA conformational rigidity. This study implies that during gastric digestion of tea with milk EGCG would remain bound to ALA, albeit in the Ca2+-free form.
PB  - Elsevier
T2  - Food Chemistry
T1  - Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study
VL  - 278
SP  - 388
EP  - 395
DO  - 10.1016/j.foodchem.2018.11.038
ER  - 
@article{
author = "Radibratović, Milica and Al-Hanish, Ayah and Minić, Simeon L. and Radomirović, Mirjana Ž. and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3733",
abstract = "α-Lactalbumin (ALA) is a Ca2+-binding protein which constitutes up to 20% of whey protein. At acidic pH, and in the apo-state at elevated temperatures, ALA is the classic 'molten globule' (MG). This study examined epigallo-catechin-3-gallate (EGCG) binding to ALA in its apo form (apoALA) and stabilizing effect on protein structure thereof. 

EGCG binds to apoALA in both native and MG state. The complex of EGCG and ALA is more stable to thermal denaturation. The docking analysis and molecular dynamic simulation (MDS) showed that Ca2+ removal decreased conformational stability of ALA, because of the local destabilization of Ca2+-binding region. EGCG binding to apoALA increases its stability by reverting of conformation and stability of Ca2+-binding region. Therefore, EGCG-induced thermal stability of apoALA is based on increased apoALA conformational rigidity. This study implies that during gastric digestion of tea with milk EGCG would remain bound to ALA, albeit in the Ca2+-free form.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study",
volume = "278",
pages = "388-395",
doi = "10.1016/j.foodchem.2018.11.038"
}
Radibratović, M., Al-Hanish, A., Minić, S. L., Radomirović, M. Ž., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T. (2019). Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study.
Food Chemistry
Elsevier., 278, 388-395.
https://doi.org/10.1016/j.foodchem.2018.11.038
Radibratović M, Al-Hanish A, Minić SL, Radomirović MŽ, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study. Food Chemistry. 2019;278:388-395
Radibratović Milica, Al-Hanish Ayah, Minić Simeon L., Radomirović Mirjana Ž., Milčić Miloš K., Stanić-Vučinić Dragana, Ćirković-Veličković Tanja, "Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study" Food Chemistry, 278 (2019):388-395,
https://doi.org/10.1016/j.foodchem.2018.11.038 .
4
3
4

Impact of oxidative stress on plant proteins modifications: relevance for plant allergens

Smiljanić, Katarina; Mihailović, Jelena; Đukić, Teodora; Ćirković-Veličković, Tanja

(2019)

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Mihailović, Jelena
AU  - Đukić, Teodora
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3745
C3  - Book of Abstracts,4th Edition of Global Conference on Plant Science and Molecular Biology
T1  - Impact of oxidative stress on plant proteins modifications: relevance for plant allergens
SP  - 130
EP  - 130
ER  - 
@conference{
author = "Smiljanić, Katarina and Mihailović, Jelena and Đukić, Teodora and Ćirković-Veličković, Tanja",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3745",
journal = "Book of Abstracts,4th Edition of Global Conference on Plant Science and Molecular Biology",
title = "Impact of oxidative stress on plant proteins modifications: relevance for plant allergens",
pages = "130-130"
}
Smiljanić, K., Mihailović, J., Đukić, T.,& Ćirković-Veličković, T. (2019). Impact of oxidative stress on plant proteins modifications: relevance for plant allergens.
Book of Abstracts,4th Edition of Global Conference on Plant Science and Molecular Biology, 130-130.
Smiljanić K, Mihailović J, Đukić T, Ćirković-Veličković T. Impact of oxidative stress on plant proteins modifications: relevance for plant allergens. Book of Abstracts,4th Edition of Global Conference on Plant Science and Molecular Biology. 2019;:130-130
Smiljanić Katarina, Mihailović Jelena, Đukić Teodora, Ćirković-Veličković Tanja, "Impact of oxidative stress on plant proteins modifications: relevance for plant allergens" Book of Abstracts,4th Edition of Global Conference on Plant Science and Molecular Biology (2019):130-130