Apostolović, Danijela

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orcid::0000-0001-8388-6916
  • Apostolović, Danijela (52)
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Author's Bibliography

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)

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)

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
17
11
15

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
17
11
15

Novel insights into the allergenic relationship between red meat and bovine milk

Peruško, Marija; Apostolović, Danijela; Starkhammar, Maria; Ćirković-Veličković, Tanja; van Hage, Marianne

(Wiley, 2019)

TY  - CONF
AU  - Peruško, Marija
AU  - Apostolović, Danijela
AU  - Starkhammar, Maria
AU  - Ćirković-Veličković, Tanja
AU  - van Hage, Marianne
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3735
AB  - Novel insights into the allergenic relationship between red meat and bovine milk
Marija Perusko1, Danijela Apostolovic2, Maria Starkhammar3, Tanja Cirkovic Velickovic4,5,6,7, Marianne van Hage2
1Innovation Center of the Faculty of Chemistry, Belgrade, Serbia
2Department of Medicine, Solna, Immunology and Allergy Unit, Karolinska Institutet and University Hospital, Stockholm, Sweden
3Department of Internal Medicine, Sodersjukhuset, Stockholm, Sweden
4Serbian Academy of Sciences and Arts, Belgrade, Serbia
5Center of Excellence for Molecular Food Sciences & Department of Biochemistry, University of Belgrade - Faculty of Chemistry, Belgrade, Serbia
6Ghent University Global Campus, Yeonsu-gu, Incheon, South Korea
7Faculty of Bioscience Engineering, Ghent University, Ghent, Belgium
 
Background
Red meat allergy is a severe form of food allergy with delayed symptoms including anaphylaxis where the IgE antibodies are directed against a carbohydrate epitope, galactose-α-1,3-galactose (α-Gal). Many red meat allergic patients report allergic symptoms upon consumption of milk or dairy products. The aim of the project was to investigate the allergenic relationship between bovine milk and red meat at a molecular level.
Methods
Adults with diagnosed red meat allergy (n = 27) were recruited and their specific IgE levels to α-Gal, beef and milk were analyzed by ImmunoCAP. Milk proteins were assayed by immunoblot and inhibition ELISA for the presence of the α-Gal epitope and for the binding to red meat allergic patients’ IgE. The involvement of the carbohydrate epitope in the IgE binding to milk proteins was assessed by an inhibition assay with thyroglobulin. Basophil activation test was performed with milk and milk proteins in samples from 11 red meat allergic patients and 2 controls.
Results
All patients were IgE positive to milk, but the IgE levels to milk were lower than those to α-Gal or beef. Significant correlations between IgE levels to milk and α-Gal (rs=0.64, P < 0.01), as well as between milk and beef (rs=0.90, P < 0.01) were observed. Immunoblot analysis of milk proteins revealed bovine γ-globulin (BGG) as α-Gal carrier. Other milk proteins, α-lactalbumin, β-lactoglobulin, α-casein, β-casein and κ-casein were negative for the presence of α-Gal epitope. BGG was also shown to bind IgE antibodies of red meat allergic patients. Inhibition immunoblot with thyroglobulin resulted in the loss of IgE binding to BGG. Additionally, ELISA experiments showed that BGG, as well as whey proteins exert a dose-dependent inhibition of red meat allergic patients’ IgE binding to -Gal. Inhibition with raw milk and commercially available milk preparations showed that raw milk exerted a slightly higher inhibition of the IgE binding to the α-Gal epitope than the commercially available milks. Importantly, activation of red meat allergic patient’s basophils by BGG and milk was demonstrated.
Conclusion
BGG was identified as a major milk carrier of the -Gal epitope that bound IgE antibodies and furthermore activated basophils of red meat allergic patients. This study highlights the importance of milk as allergenic food source among the meat allergic population.
PB  - Wiley
C3  - Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI)
T1  - Novel insights into the allergenic relationship between red meat and bovine milk
VL  - 74
VL  - supp. 106
SP  - 596
EP  - 596
ER  - 
@conference{
author = "Peruško, Marija and Apostolović, Danijela and Starkhammar, Maria and Ćirković-Veličković, Tanja and van Hage, Marianne",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3735",
abstract = "Novel insights into the allergenic relationship between red meat and bovine milk
Marija Perusko1, Danijela Apostolovic2, Maria Starkhammar3, Tanja Cirkovic Velickovic4,5,6,7, Marianne van Hage2
1Innovation Center of the Faculty of Chemistry, Belgrade, Serbia
2Department of Medicine, Solna, Immunology and Allergy Unit, Karolinska Institutet and University Hospital, Stockholm, Sweden
3Department of Internal Medicine, Sodersjukhuset, Stockholm, Sweden
4Serbian Academy of Sciences and Arts, Belgrade, Serbia
5Center of Excellence for Molecular Food Sciences & Department of Biochemistry, University of Belgrade - Faculty of Chemistry, Belgrade, Serbia
6Ghent University Global Campus, Yeonsu-gu, Incheon, South Korea
7Faculty of Bioscience Engineering, Ghent University, Ghent, Belgium
 
Background
Red meat allergy is a severe form of food allergy with delayed symptoms including anaphylaxis where the IgE antibodies are directed against a carbohydrate epitope, galactose-α-1,3-galactose (α-Gal). Many red meat allergic patients report allergic symptoms upon consumption of milk or dairy products. The aim of the project was to investigate the allergenic relationship between bovine milk and red meat at a molecular level.
Methods
Adults with diagnosed red meat allergy (n = 27) were recruited and their specific IgE levels to α-Gal, beef and milk were analyzed by ImmunoCAP. Milk proteins were assayed by immunoblot and inhibition ELISA for the presence of the α-Gal epitope and for the binding to red meat allergic patients’ IgE. The involvement of the carbohydrate epitope in the IgE binding to milk proteins was assessed by an inhibition assay with thyroglobulin. Basophil activation test was performed with milk and milk proteins in samples from 11 red meat allergic patients and 2 controls.
Results
All patients were IgE positive to milk, but the IgE levels to milk were lower than those to α-Gal or beef. Significant correlations between IgE levels to milk and α-Gal (rs=0.64, P < 0.01), as well as between milk and beef (rs=0.90, P < 0.01) were observed. Immunoblot analysis of milk proteins revealed bovine γ-globulin (BGG) as α-Gal carrier. Other milk proteins, α-lactalbumin, β-lactoglobulin, α-casein, β-casein and κ-casein were negative for the presence of α-Gal epitope. BGG was also shown to bind IgE antibodies of red meat allergic patients. Inhibition immunoblot with thyroglobulin resulted in the loss of IgE binding to BGG. Additionally, ELISA experiments showed that BGG, as well as whey proteins exert a dose-dependent inhibition of red meat allergic patients’ IgE binding to -Gal. Inhibition with raw milk and commercially available milk preparations showed that raw milk exerted a slightly higher inhibition of the IgE binding to the α-Gal epitope than the commercially available milks. Importantly, activation of red meat allergic patient’s basophils by BGG and milk was demonstrated.
Conclusion
BGG was identified as a major milk carrier of the -Gal epitope that bound IgE antibodies and furthermore activated basophils of red meat allergic patients. This study highlights the importance of milk as allergenic food source among the meat allergic population.",
publisher = "Wiley",
journal = "Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI)",
title = "Novel insights into the allergenic relationship between red meat and bovine milk",
volume = "74, supp. 106",
pages = "596-596"
}
Peruško, M., Apostolović, D., Starkhammar, M., Ćirković-Veličković, T.,& van Hage, M. (2019). Novel insights into the allergenic relationship between red meat and bovine milk.
Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI)
Wiley., supp. 106, 596-596.
Peruško M, Apostolović D, Starkhammar M, Ćirković-Veličković T, van Hage M. Novel insights into the allergenic relationship between red meat and bovine milk. Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI). 2019;supp. 106:596-596
Peruško Marija, Apostolović Danijela, Starkhammar Maria, Ćirković-Veličković Tanja, van Hage Marianne, "Novel insights into the allergenic relationship between red meat and bovine milk" Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI), supp. 106 (2019):596-596

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

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

(Wiley, 2019)

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Cvetković, Anka
AU  - Veljković, 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/123456789/3737
PB  - Wiley
C3  - Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI)
T1  - In- depth quantitative profiling of post- translational modifications of Timothy grass pollen allergome in relation to environmental pollution and oxidative stress
VL  - 74
IS  - supp. 106
SP  - 878
EP  - 878
ER  - 
@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Cvetković, Anka and Veljković, 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/123456789/3737",
publisher = "Wiley",
journal = "Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI)",
title = "In- depth quantitative profiling of post- translational modifications of Timothy grass pollen allergome in relation to environmental pollution and oxidative stress",
volume = "74",
number = "supp. 106",
pages = "878-878"
}
Smiljanić, K., Prodić, I., Apostolović, D., Cvetković, A., Veljković, 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 pollution and oxidative stress.
Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI)
Wiley., 74(supp. 106), 878-878.
Smiljanić K, Prodić I, Apostolović D, Cvetković A, Veljković 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 pollution and oxidative stress. Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI). 2019;74(supp. 106):878-878
Smiljanić Katarina, Prodić Ivana, Apostolović Danijela, Cvetković Anka, Veljković 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 pollution and oxidative stress" Allergy; Congress of the European-Academy-of-Allergy-and-Clinical-Immunology (EAACI), 74, no. supp. 106 (2019):878-878

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

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
4

Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides

Prodić, Ivana; Stanić-Vučinić, Dragana; Apostolović, Danijela; Mihailović-Vesić, Jelena; Radibratović, Milica; Radosavljević, Jelena; Burazer, Lidija M.; Milčić, Miloš K.; Smiljanić, Katarina; van Hage, Marianne; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2018)

TY  - JOUR
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Radibratović, Milica
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija M.
AU  - Milčić, Miloš K.
AU  - Smiljanić, Katarina
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3224
AB  - BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides
VL  - 48
IS  - 6
SP  - 731
EP  - 740
DO  - 10.1111/cea.13113
ER  - 
@article{
author = "Prodić, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Mihailović-Vesić, Jelena and Radibratović, Milica and Radosavljević, Jelena and Burazer, Lidija M. and Milčić, Miloš K. and Smiljanić, Katarina and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3224",
abstract = "BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides",
volume = "48",
number = "6",
pages = "731-740",
doi = "10.1111/cea.13113"
}
Prodić, I., Stanić-Vučinić, D., Apostolović, D., Mihailović-Vesić, J., Radibratović, M., Radosavljević, J., Burazer, L. M., Milčić, M. K., Smiljanić, K., van Hage, M.,& Ćirković-Veličković, T. (2018). Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides.
Clinical and Experimental Allergy
Wiley, Hoboken., 48(6), 731-740.
https://doi.org/10.1111/cea.13113
Prodić I, Stanić-Vučinić D, Apostolović D, Mihailović-Vesić J, Radibratović M, Radosavljević J, Burazer LM, Milčić MK, Smiljanić K, van Hage M, Ćirković-Veličković T. Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. Clinical and Experimental Allergy. 2018;48(6):731-740
Prodić Ivana, Stanić-Vučinić Dragana, Apostolović Danijela, Mihailović-Vesić Jelena, Radibratović Milica, Radosavljević Jelena, Burazer Lidija M., Milčić Miloš K., Smiljanić Katarina, van Hage Marianne, Ćirković-Veličković Tanja, "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides" Clinical and Experimental Allergy, 48, no. 6 (2018):731-740,
https://doi.org/10.1111/cea.13113 .
3
21
18
19

Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. Influence of Peanut Matrix on Stability of Allergens in Gastric-Simulated Digesta: 2S Albumins Are Main Contributors to the IgE Reactivity of Short Digestion-Resistant Peptides. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113

Prodić, Ivana; Stanić-Vučinić, Dragana; Apostolović, Danijela; Mihailović-Vesić, Jelena; Radibratović, Milica; Radosavljević, Jelena; Burazer, Lidija M.; Milčić, Miloš K.; Smiljanić, Katarina; van Hage, Marianne; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2018)

TY  - BOOK
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Radibratović, Milica
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija M.
AU  - Milčić, Miloš K.
AU  - Smiljanić, Katarina
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3225
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. Influence of Peanut Matrix on Stability of Allergens in Gastric-Simulated Digesta: 2S Albumins Are Main Contributors to the IgE Reactivity of Short Digestion-Resistant Peptides. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113
ER  - 
@book{
author = "Prodić, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Mihailović-Vesić, Jelena and Radibratović, Milica and Radosavljević, Jelena and Burazer, Lidija M. and Milčić, Miloš K. and Smiljanić, Katarina and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3225",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. Influence of Peanut Matrix on Stability of Allergens in Gastric-Simulated Digesta: 2S Albumins Are Main Contributors to the IgE Reactivity of Short Digestion-Resistant Peptides. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113"
}
Prodić, I., Stanić-Vučinić, D., Apostolović, D., Mihailović-Vesić, J., Radibratović, M., Radosavljević, J., Burazer, L. M., Milčić, M. K., Smiljanić, K., van Hage, M.,& Ćirković-Veličković, T. (2018). Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. Influence of Peanut Matrix on Stability of Allergens in Gastric-Simulated Digesta: 2S Albumins Are Main Contributors to the IgE Reactivity of Short Digestion-Resistant Peptides. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113.
Clinical and Experimental Allergy
Wiley, Hoboken..
Prodić I, Stanić-Vučinić D, Apostolović D, Mihailović-Vesić J, Radibratović M, Radosavljević J, Burazer LM, Milčić MK, Smiljanić K, van Hage M, Ćirković-Veličković T. Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. Influence of Peanut Matrix on Stability of Allergens in Gastric-Simulated Digesta: 2S Albumins Are Main Contributors to the IgE Reactivity of Short Digestion-Resistant Peptides. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113. Clinical and Experimental Allergy. 2018;
Prodić Ivana, Stanić-Vučinić Dragana, Apostolović Danijela, Mihailović-Vesić Jelena, Radibratović Milica, Radosavljević Jelena, Burazer Lidija M., Milčić Miloš K., Smiljanić Katarina, van Hage Marianne, Ćirković-Veličković Tanja, "Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. Influence of Peanut Matrix on Stability of Allergens in Gastric-Simulated Digesta: 2S Albumins Are Main Contributors to the IgE Reactivity of Short Digestion-Resistant Peptides. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113" Clinical and Experimental Allergy (2018)

New insights into allergenic relationship between red meat and cow's milk

Peruško, Marija; Apostolović, Danijela; Ćirković-Veličković, Tanja; van Hage, Marianne

(Wiley, Hoboken, 2018)

TY  - CONF
AU  - Peruško, Marija
AU  - Apostolović, Danijela
AU  - Ćirković-Veličković, Tanja
AU  - van Hage, Marianne
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2177
PB  - Wiley, Hoboken
C3  - FEBS OPEN BIO
T1  - New insights into allergenic relationship between red meat and cow's milk
VL  - 8
SP  - 279
EP  - 279
ER  - 
@conference{
author = "Peruško, Marija and Apostolović, Danijela and Ćirković-Veličković, Tanja and van Hage, Marianne",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2177",
publisher = "Wiley, Hoboken",
journal = "FEBS OPEN BIO",
title = "New insights into allergenic relationship between red meat and cow's milk",
volume = "8",
pages = "279-279"
}
Peruško, M., Apostolović, D., Ćirković-Veličković, T.,& van Hage, M. (2018). New insights into allergenic relationship between red meat and cow's milk.
FEBS OPEN BIO
Wiley, Hoboken., 8, 279-279.
Peruško M, Apostolović D, Ćirković-Veličković T, van Hage M. New insights into allergenic relationship between red meat and cow's milk. FEBS OPEN BIO. 2018;8:279-279
Peruško Marija, Apostolović Danijela, Ćirković-Veličković Tanja, van Hage Marianne, "New insights into allergenic relationship between red meat and cow's milk" FEBS OPEN BIO, 8 (2018):279-279

Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides

Prodić, Ivana; Stanić-Vučinić, Dragana; Apostolović, Danijela; Mihailović-Vesić, Jelena; Radibratović, Milica; Radosavljević, Jelena; Burazer, Lidija M.; Milčić, Miloš K.; Smiljanić, Katarina; van Hage, Marianne; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2018)

TY  - JOUR
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Radibratović, Milica
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija M.
AU  - Milčić, Miloš K.
AU  - Smiljanić, Katarina
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2155
AB  - BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides
VL  - 48
IS  - 6
SP  - 731
EP  - 740
DO  - 10.1111/cea.13113
ER  - 
@article{
author = "Prodić, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Mihailović-Vesić, Jelena and Radibratović, Milica and Radosavljević, Jelena and Burazer, Lidija M. and Milčić, Miloš K. and Smiljanić, Katarina and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2155",
abstract = "BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides",
volume = "48",
number = "6",
pages = "731-740",
doi = "10.1111/cea.13113"
}
Prodić, I., Stanić-Vučinić, D., Apostolović, D., Mihailović-Vesić, J., Radibratović, M., Radosavljević, J., Burazer, L. M., Milčić, M. K., Smiljanić, K., van Hage, M.,& Ćirković-Veličković, T. (2018). Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides.
Clinical and Experimental Allergy
Wiley, Hoboken., 48(6), 731-740.
https://doi.org/10.1111/cea.13113
Prodić I, Stanić-Vučinić D, Apostolović D, Mihailović-Vesić J, Radibratović M, Radosavljević J, Burazer LM, Milčić MK, Smiljanić K, van Hage M, Ćirković-Veličković T. Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. Clinical and Experimental Allergy. 2018;48(6):731-740
Prodić Ivana, Stanić-Vučinić Dragana, Apostolović Danijela, Mihailović-Vesić Jelena, Radibratović Milica, Radosavljević Jelena, Burazer Lidija M., Milčić Miloš K., Smiljanić Katarina, van Hage Marianne, Ćirković-Veličković Tanja, "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides" Clinical and Experimental Allergy, 48, no. 6 (2018):731-740,
https://doi.org/10.1111/cea.13113 .
3
21
18
19

Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes

Radosavljević, Jelena; Apostolović, Danijela; Mihailović-Vesić, Jelena; Atanasković-Marković, Marina; Burazer, Lidija M.; van Hage, Marianne; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2018)

TY  - CONF
AU  - Radosavljević, Jelena
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Atanasković-Marković, Marina
AU  - Burazer, Lidija M.
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2176
PB  - Wiley, Hoboken
C3  - FEBS OPEN BIO
T1  - Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes
VL  - 8
SP  - 257
EP  - 257
ER  - 
@conference{
author = "Radosavljević, Jelena and Apostolović, Danijela and Mihailović-Vesić, Jelena and Atanasković-Marković, Marina and Burazer, Lidija M. and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2176",
publisher = "Wiley, Hoboken",
journal = "FEBS OPEN BIO",
title = "Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes",
volume = "8",
pages = "257-257"
}
Radosavljević, J., Apostolović, D., Mihailović-Vesić, J., Atanasković-Marković, M., Burazer, L. M., van Hage, M.,& Ćirković-Veličković, T. (2018). Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes.
FEBS OPEN BIO
Wiley, Hoboken., 8, 257-257.
Radosavljević J, Apostolović D, Mihailović-Vesić J, Atanasković-Marković M, Burazer LM, van Hage M, Ćirković-Veličković T. Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes. FEBS OPEN BIO. 2018;8:257-257
Radosavljević Jelena, Apostolović Danijela, Mihailović-Vesić Jelena, Atanasković-Marković Marina, Burazer Lidija M., van Hage Marianne, Ćirković-Veličković Tanja, "Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes" FEBS OPEN BIO, 8 (2018):257-257

alpha-Gal on the protein surface affects uptake and degradation in immature monocyte derived dendritic cells

Krstić-Ristivojević, Maja; Grundström, Jeanette; Tran, Thi Anh Thu; Apostolović, Danijela; Radoi, Vlad; Starkhammar, Maria; Vukojević, Vesna; Ćirković-Veličković, Tanja; Hamsten, Carl; van Hage, Marianne

(Nature Publishing Group, London, 2018)

TY  - JOUR
AU  - Krstić-Ristivojević, Maja
AU  - Grundström, Jeanette
AU  - Tran, Thi Anh Thu
AU  - Apostolović, Danijela
AU  - Radoi, Vlad
AU  - Starkhammar, Maria
AU  - Vukojević, Vesna
AU  - Ćirković-Veličković, Tanja
AU  - Hamsten, Carl
AU  - van Hage, Marianne
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2207
AB  - Red meat allergy is characterized by an IgE response against the carbohydrate galactose-alpha-1,3-galactose (alpha-Gal), which is abundantly expressed on glycoproteins from non-primate mammals. The mechanisms of how alpha-Gal is processed and presented to the immune system to initiate an allergic reaction are still unknown. The aim of this study was to reveal whether the presence of alpha-Gal epitopes on the protein surface influence antigen uptake and processing in immature monocyte-derived dendritic cells (iMDDCs). Immature MDDCs were prepared from healthy blood donors and red meat allergic patients. We found an increased internalization of alpha-Gal carrying proteins over time in iMDDCs by flow cytometric analysis, which was independent of the donor allergic status. The uptake of alpha-Gal carrying proteins was significantly higher than the uptake of non-alpha-Gal carrying proteins. Confocal microscopy revealed alpha-Gal carrying proteins scattered around the cytoplasm in most iMDDCs while detection of proteins not carrying alpha-Gal was negligible. Fluorescent detection of protein on SDS-PAGE showed that degradation of alpha-Gal carrying proteins was slower than degradation of non-alpha-Gal carrying proteins. Thus, the presence of alpha-Gal on the protein surface affects both uptake and degradation of the protein, and the results add new knowledge of alpha-Gal as a clinically relevant food allergen.
PB  - Nature Publishing Group, London
T2  - Scientific Reports
T1  - alpha-Gal on the protein surface affects uptake and degradation in immature monocyte derived dendritic cells
VL  - 8
DO  - 10.1038/s41598-018-30887-8
ER  - 
@article{
author = "Krstić-Ristivojević, Maja and Grundström, Jeanette and Tran, Thi Anh Thu and Apostolović, Danijela and Radoi, Vlad and Starkhammar, Maria and Vukojević, Vesna and Ćirković-Veličković, Tanja and Hamsten, Carl and van Hage, Marianne",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2207",
abstract = "Red meat allergy is characterized by an IgE response against the carbohydrate galactose-alpha-1,3-galactose (alpha-Gal), which is abundantly expressed on glycoproteins from non-primate mammals. The mechanisms of how alpha-Gal is processed and presented to the immune system to initiate an allergic reaction are still unknown. The aim of this study was to reveal whether the presence of alpha-Gal epitopes on the protein surface influence antigen uptake and processing in immature monocyte-derived dendritic cells (iMDDCs). Immature MDDCs were prepared from healthy blood donors and red meat allergic patients. We found an increased internalization of alpha-Gal carrying proteins over time in iMDDCs by flow cytometric analysis, which was independent of the donor allergic status. The uptake of alpha-Gal carrying proteins was significantly higher than the uptake of non-alpha-Gal carrying proteins. Confocal microscopy revealed alpha-Gal carrying proteins scattered around the cytoplasm in most iMDDCs while detection of proteins not carrying alpha-Gal was negligible. Fluorescent detection of protein on SDS-PAGE showed that degradation of alpha-Gal carrying proteins was slower than degradation of non-alpha-Gal carrying proteins. Thus, the presence of alpha-Gal on the protein surface affects both uptake and degradation of the protein, and the results add new knowledge of alpha-Gal as a clinically relevant food allergen.",
publisher = "Nature Publishing Group, London",
journal = "Scientific Reports",
title = "alpha-Gal on the protein surface affects uptake and degradation in immature monocyte derived dendritic cells",
volume = "8",
doi = "10.1038/s41598-018-30887-8"
}
Krstić-Ristivojević, M., Grundström, J., Tran, T. A. T., Apostolović, D., Radoi, V., Starkhammar, M., Vukojević, V., Ćirković-Veličković, T., Hamsten, C.,& van Hage, M. (2018). alpha-Gal on the protein surface affects uptake and degradation in immature monocyte derived dendritic cells.
Scientific Reports
Nature Publishing Group, London., 8.
https://doi.org/10.1038/s41598-018-30887-8
Krstić-Ristivojević M, Grundström J, Tran TAT, Apostolović D, Radoi V, Starkhammar M, Vukojević V, Ćirković-Veličković T, Hamsten C, van Hage M. alpha-Gal on the protein surface affects uptake and degradation in immature monocyte derived dendritic cells. Scientific Reports. 2018;8
Krstić-Ristivojević Maja, Grundström Jeanette, Tran Thi Anh Thu, Apostolović Danijela, Radoi Vlad, Starkhammar Maria, Vukojević Vesna, Ćirković-Veličković Tanja, Hamsten Carl, van Hage Marianne, "alpha-Gal on the protein surface affects uptake and degradation in immature monocyte derived dendritic cells" Scientific Reports, 8 (2018),
https://doi.org/10.1038/s41598-018-30887-8 .
4
7
5
6

Supplementary data for the article: Ristivojević, M. K.; Grundström, J.; Tran, T. A. T.; Apostolovic, D.; Radoi, V.; Starkhammar, M.; Vukojević, V.; Ćirković Veličković, T.; Hamsten, C.; van Hage, M. α-Gal on the Protein Surface Affects Uptake and Degradation in Immature Monocyte Derived Dendritic Cells. Scientific Reports 2018, 8 (1). https://doi.org/10.1038/s41598-018-30887-8

Krstić-Ristivojević, Maja; Grundström, Jeanette; Tran, Thi Anh Thu; Apostolović, Danijela; Radoi, Vlad; Starkhammar, Maria; Vukojević, Vesna; Ćirković-Veličković, Tanja; Hamsten, Carl; van Hage, Marianne

(Nature Publishing Group, London, 2018)

TY  - BOOK
AU  - Krstić-Ristivojević, Maja
AU  - Grundström, Jeanette
AU  - Tran, Thi Anh Thu
AU  - Apostolović, Danijela
AU  - Radoi, Vlad
AU  - Starkhammar, Maria
AU  - Vukojević, Vesna
AU  - Ćirković-Veličković, Tanja
AU  - Hamsten, Carl
AU  - van Hage, Marianne
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3073
PB  - Nature Publishing Group, London
T2  - Scientific Reports
T1  - Supplementary data for the article: Ristivojević, M. K.; Grundström, J.; Tran, T. A. T.; Apostolovic, D.; Radoi, V.; Starkhammar, M.; Vukojević, V.; Ćirković Veličković, T.; Hamsten, C.; van Hage, M. α-Gal on the Protein Surface Affects Uptake and Degradation in Immature Monocyte Derived Dendritic Cells. Scientific Reports 2018, 8 (1). https://doi.org/10.1038/s41598-018-30887-8
ER  - 
@book{
author = "Krstić-Ristivojević, Maja and Grundström, Jeanette and Tran, Thi Anh Thu and Apostolović, Danijela and Radoi, Vlad and Starkhammar, Maria and Vukojević, Vesna and Ćirković-Veličković, Tanja and Hamsten, Carl and van Hage, Marianne",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3073",
publisher = "Nature Publishing Group, London",
journal = "Scientific Reports",
title = "Supplementary data for the article: Ristivojević, M. K.; Grundström, J.; Tran, T. A. T.; Apostolovic, D.; Radoi, V.; Starkhammar, M.; Vukojević, V.; Ćirković Veličković, T.; Hamsten, C.; van Hage, M. α-Gal on the Protein Surface Affects Uptake and Degradation in Immature Monocyte Derived Dendritic Cells. Scientific Reports 2018, 8 (1). https://doi.org/10.1038/s41598-018-30887-8"
}
Krstić-Ristivojević, M., Grundström, J., Tran, T. A. T., Apostolović, D., Radoi, V., Starkhammar, M., Vukojević, V., Ćirković-Veličković, T., Hamsten, C.,& van Hage, M. (2018). Supplementary data for the article: Ristivojević, M. K.; Grundström, J.; Tran, T. A. T.; Apostolovic, D.; Radoi, V.; Starkhammar, M.; Vukojević, V.; Ćirković Veličković, T.; Hamsten, C.; van Hage, M. α-Gal on the Protein Surface Affects Uptake and Degradation in Immature Monocyte Derived Dendritic Cells. Scientific Reports 2018, 8 (1). https://doi.org/10.1038/s41598-018-30887-8.
Scientific Reports
Nature Publishing Group, London..
Krstić-Ristivojević M, Grundström J, Tran TAT, Apostolović D, Radoi V, Starkhammar M, Vukojević V, Ćirković-Veličković T, Hamsten C, van Hage M. Supplementary data for the article: Ristivojević, M. K.; Grundström, J.; Tran, T. A. T.; Apostolovic, D.; Radoi, V.; Starkhammar, M.; Vukojević, V.; Ćirković Veličković, T.; Hamsten, C.; van Hage, M. α-Gal on the Protein Surface Affects Uptake and Degradation in Immature Monocyte Derived Dendritic Cells. Scientific Reports 2018, 8 (1). https://doi.org/10.1038/s41598-018-30887-8. Scientific Reports. 2018;
Krstić-Ristivojević Maja, Grundström Jeanette, Tran Thi Anh Thu, Apostolović Danijela, Radoi Vlad, Starkhammar Maria, Vukojević Vesna, Ćirković-Veličković Tanja, Hamsten Carl, van Hage Marianne, "Supplementary data for the article: Ristivojević, M. K.; Grundström, J.; Tran, T. A. T.; Apostolovic, D.; Radoi, V.; Starkhammar, M.; Vukojević, V.; Ćirković Veličković, T.; Hamsten, C.; van Hage, M. α-Gal on the Protein Surface Affects Uptake and Degradation in Immature Monocyte Derived Dendritic Cells. Scientific Reports 2018, 8 (1). https://doi.org/10.1038/s41598-018-30887-8" Scientific Reports (2018)

Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study

Smiljanić, Katarina; Apostolović, Danijela; Trifunović, Snežana S.; Ognjenović, J.; Peruško, Marija; Mihajlović-Lalić, Ljiljana; Burazer, Lidija M.; van Hage, Marianne; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2017)

TY  - JOUR
AU  - Smiljanić, Katarina
AU  - Apostolović, Danijela
AU  - Trifunović, Snežana S.
AU  - Ognjenović, J.
AU  - Peruško, Marija
AU  - Mihajlović-Lalić, Ljiljana
AU  - Burazer, Lidija M.
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3126
AB  - Background Short ragweed (Ambrosia artemisiifolia) allergies affect more than 36 million people annually. Ragweed pollen grains release subpollen particles (SPP) of respirable size upon hydration or a change in air electrical conditions. The aim of this study was to characterize the proteomes and allergomes of short ragweed SPP and total pollen protein extract (TOT), and compare their effects with those of standard aqueous pollen protein extract (APE) using sera from short ragweed pollen-sensitized patients. Methods Quantitative 2D gel-based and shotgun proteomics, 1D and 2D immunoblotting, and quantitative ELISA were applied. Novel SPP extraction and preparation protocols enabled appropriate sample preparation and further downstream analysis by quantitative proteomics. Results The SPP fraction contained the highest proportion (94%) of the allergome, with the largest quantities of the minor Amb a 4 and major Amb a 1 allergens, and as unique, NADH dehydrogenases. APE was the richest in Amb a 6, Amb a 5 and Amb a 3, and TOT fraction was the richest in the Amb a 8 allergens (89% and 83% of allergome, respectively). Allergenic potency correlated well among the three fractions tested, with 1D immunoblots demonstrating a slight predominance of IgE reactivity to SPP compared to TOT and APE. However, the strongest IgE binding in ELISA was noted against APE. New allergenic candidates, phosphoglycerate mutase and phosphoglucomutase, were identified in all the three pollen fractions. Enolase, UTP-glucose-1-phosphate uridylyltransferase and polygalacturonase were observed in SPP and TOT fractions as novel allergens of the short ragweed pollen, as previously described. Conclusion and Clinical Relevance We demonstrated that the complete major (Amb a 1 and 11) and almost all minor (Amb a 3, 4, 5, 6, 8 and 9) short ragweed pollen allergen repertoire as well as NADH oxidases are present in SPP, highlighting an important role for SPP in allergic sensitization to short ragweed.
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study
VL  - 47
IS  - 6
SP  - 815
EP  - 828
DO  - 10.1111/cea.12874
ER  - 
@article{
author = "Smiljanić, Katarina and Apostolović, Danijela and Trifunović, Snežana S. and Ognjenović, J. and Peruško, Marija and Mihajlović-Lalić, Ljiljana and Burazer, Lidija M. and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3126",
abstract = "Background Short ragweed (Ambrosia artemisiifolia) allergies affect more than 36 million people annually. Ragweed pollen grains release subpollen particles (SPP) of respirable size upon hydration or a change in air electrical conditions. The aim of this study was to characterize the proteomes and allergomes of short ragweed SPP and total pollen protein extract (TOT), and compare their effects with those of standard aqueous pollen protein extract (APE) using sera from short ragweed pollen-sensitized patients. Methods Quantitative 2D gel-based and shotgun proteomics, 1D and 2D immunoblotting, and quantitative ELISA were applied. Novel SPP extraction and preparation protocols enabled appropriate sample preparation and further downstream analysis by quantitative proteomics. Results The SPP fraction contained the highest proportion (94%) of the allergome, with the largest quantities of the minor Amb a 4 and major Amb a 1 allergens, and as unique, NADH dehydrogenases. APE was the richest in Amb a 6, Amb a 5 and Amb a 3, and TOT fraction was the richest in the Amb a 8 allergens (89% and 83% of allergome, respectively). Allergenic potency correlated well among the three fractions tested, with 1D immunoblots demonstrating a slight predominance of IgE reactivity to SPP compared to TOT and APE. However, the strongest IgE binding in ELISA was noted against APE. New allergenic candidates, phosphoglycerate mutase and phosphoglucomutase, were identified in all the three pollen fractions. Enolase, UTP-glucose-1-phosphate uridylyltransferase and polygalacturonase were observed in SPP and TOT fractions as novel allergens of the short ragweed pollen, as previously described. Conclusion and Clinical Relevance We demonstrated that the complete major (Amb a 1 and 11) and almost all minor (Amb a 3, 4, 5, 6, 8 and 9) short ragweed pollen allergen repertoire as well as NADH oxidases are present in SPP, highlighting an important role for SPP in allergic sensitization to short ragweed.",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study",
volume = "47",
number = "6",
pages = "815-828",
doi = "10.1111/cea.12874"
}
Smiljanić, K., Apostolović, D., Trifunović, S. S., Ognjenović, J., Peruško, M., Mihajlović-Lalić, L., Burazer, L. M., van Hage, M.,& Ćirković-Veličković, T. (2017). Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study.
Clinical and Experimental Allergy
Wiley, Hoboken., 47(6), 815-828.
https://doi.org/10.1111/cea.12874
Smiljanić K, Apostolović D, Trifunović SS, Ognjenović J, Peruško M, Mihajlović-Lalić L, Burazer LM, van Hage M, Ćirković-Veličković T. Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study. Clinical and Experimental Allergy. 2017;47(6):815-828
Smiljanić Katarina, Apostolović Danijela, Trifunović Snežana S., Ognjenović J., Peruško Marija, Mihajlović-Lalić Ljiljana, Burazer Lidija M., van Hage Marianne, Ćirković-Veličković Tanja, "Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study" Clinical and Experimental Allergy, 47, no. 6 (2017):815-828,
https://doi.org/10.1111/cea.12874 .
2
14
12
14

Supplementary data for article: Smiljanic, K.; Apostolovic, D.; Trifunovic, S.; Ognjenovic, J.; Perusko, M.; Mihajlovic, L.; Burazer, L.; van Hage, M.; Cirkovic Velickovic, T. Subpollen Particles Are Rich Carriers of Major Short Ragweed Allergens and NADH Dehydrogenases: Quantitative Proteomic and Allergomic Study. Clinical and Experimental Allergy 2017, 47 (6), 815–828. https://doi.org/10.1111/cea.12874

Smiljanić, Katarina; Apostolović, Danijela; Trifunović, Snežana S.; Ognjenović, J.; Peruško, Marija; Mihajlović-Lalić, Ljiljana; Burazer, Lidija M.; van Hage, Marianne; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2017)

TY  - BOOK
AU  - Smiljanić, Katarina
AU  - Apostolović, Danijela
AU  - Trifunović, Snežana S.
AU  - Ognjenović, J.
AU  - Peruško, Marija
AU  - Mihajlović-Lalić, Ljiljana
AU  - Burazer, Lidija M.
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3127
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Supplementary data for article:            Smiljanic, K.; Apostolovic, D.; Trifunovic, S.; Ognjenovic, J.; Perusko, M.; Mihajlovic, L.; Burazer, L.; van Hage, M.; Cirkovic Velickovic, T. Subpollen Particles Are Rich Carriers of Major Short Ragweed Allergens and NADH Dehydrogenases: Quantitative Proteomic and Allergomic Study. Clinical and Experimental Allergy 2017, 47 (6), 815–828. https://doi.org/10.1111/cea.12874
ER  - 
@book{
author = "Smiljanić, Katarina and Apostolović, Danijela and Trifunović, Snežana S. and Ognjenović, J. and Peruško, Marija and Mihajlović-Lalić, Ljiljana and Burazer, Lidija M. and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3127",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Supplementary data for article:            Smiljanic, K.; Apostolovic, D.; Trifunovic, S.; Ognjenovic, J.; Perusko, M.; Mihajlovic, L.; Burazer, L.; van Hage, M.; Cirkovic Velickovic, T. Subpollen Particles Are Rich Carriers of Major Short Ragweed Allergens and NADH Dehydrogenases: Quantitative Proteomic and Allergomic Study. Clinical and Experimental Allergy 2017, 47 (6), 815–828. https://doi.org/10.1111/cea.12874"
}
Smiljanić, K., Apostolović, D., Trifunović, S. S., Ognjenović, J., Peruško, M., Mihajlović-Lalić, L., Burazer, L. M., van Hage, M.,& Ćirković-Veličković, T. (2017). Supplementary data for article:            Smiljanic, K.; Apostolovic, D.; Trifunovic, S.; Ognjenovic, J.; Perusko, M.; Mihajlovic, L.; Burazer, L.; van Hage, M.; Cirkovic Velickovic, T. Subpollen Particles Are Rich Carriers of Major Short Ragweed Allergens and NADH Dehydrogenases: Quantitative Proteomic and Allergomic Study. Clinical and Experimental Allergy 2017, 47 (6), 815–828. https://doi.org/10.1111/cea.12874.
Clinical and Experimental Allergy
Wiley, Hoboken..
Smiljanić K, Apostolović D, Trifunović SS, Ognjenović J, Peruško M, Mihajlović-Lalić L, Burazer LM, van Hage M, Ćirković-Veličković T. Supplementary data for article:            Smiljanic, K.; Apostolovic, D.; Trifunovic, S.; Ognjenovic, J.; Perusko, M.; Mihajlovic, L.; Burazer, L.; van Hage, M.; Cirkovic Velickovic, T. Subpollen Particles Are Rich Carriers of Major Short Ragweed Allergens and NADH Dehydrogenases: Quantitative Proteomic and Allergomic Study. Clinical and Experimental Allergy 2017, 47 (6), 815–828. https://doi.org/10.1111/cea.12874. Clinical and Experimental Allergy. 2017;
Smiljanić Katarina, Apostolović Danijela, Trifunović Snežana S., Ognjenović J., Peruško Marija, Mihajlović-Lalić Ljiljana, Burazer Lidija M., van Hage Marianne, Ćirković-Veličković Tanja, "Supplementary data for article:            Smiljanic, K.; Apostolovic, D.; Trifunovic, S.; Ognjenovic, J.; Perusko, M.; Mihajlovic, L.; Burazer, L.; van Hage, M.; Cirkovic Velickovic, T. Subpollen Particles Are Rich Carriers of Major Short Ragweed Allergens and NADH Dehydrogenases: Quantitative Proteomic and Allergomic Study. Clinical and Experimental Allergy 2017, 47 (6), 815–828. https://doi.org/10.1111/cea.12874" Clinical and Experimental Allergy (2017)

Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study

Smiljanić, Katarina; Apostolović, Danijela; Trifunović, Snežana S.; Ognjenović, J.; Peruško, Marija; Mihajlović-Lalić, Ljiljana; Burazer, Lidija M.; van Hage, Marianne; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2017)

TY  - JOUR
AU  - Smiljanić, Katarina
AU  - Apostolović, Danijela
AU  - Trifunović, Snežana S.
AU  - Ognjenović, J.
AU  - Peruško, Marija
AU  - Mihajlović-Lalić, Ljiljana
AU  - Burazer, Lidija M.
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2468
AB  - Background Short ragweed (Ambrosia artemisiifolia) allergies affect more than 36 million people annually. Ragweed pollen grains release subpollen particles (SPP) of respirable size upon hydration or a change in air electrical conditions. The aim of this study was to characterize the proteomes and allergomes of short ragweed SPP and total pollen protein extract (TOT), and compare their effects with those of standard aqueous pollen protein extract (APE) using sera from short ragweed pollen-sensitized patients. Methods Quantitative 2D gel-based and shotgun proteomics, 1D and 2D immunoblotting, and quantitative ELISA were applied. Novel SPP extraction and preparation protocols enabled appropriate sample preparation and further downstream analysis by quantitative proteomics. Results The SPP fraction contained the highest proportion (94%) of the allergome, with the largest quantities of the minor Amb a 4 and major Amb a 1 allergens, and as unique, NADH dehydrogenases. APE was the richest in Amb a 6, Amb a 5 and Amb a 3, and TOT fraction was the richest in the Amb a 8 allergens (89% and 83% of allergome, respectively). Allergenic potency correlated well among the three fractions tested, with 1D immunoblots demonstrating a slight predominance of IgE reactivity to SPP compared to TOT and APE. However, the strongest IgE binding in ELISA was noted against APE. New allergenic candidates, phosphoglycerate mutase and phosphoglucomutase, were identified in all the three pollen fractions. Enolase, UTP-glucose-1-phosphate uridylyltransferase and polygalacturonase were observed in SPP and TOT fractions as novel allergens of the short ragweed pollen, as previously described. Conclusion and Clinical Relevance We demonstrated that the complete major (Amb a 1 and 11) and almost all minor (Amb a 3, 4, 5, 6, 8 and 9) short ragweed pollen allergen repertoire as well as NADH oxidases are present in SPP, highlighting an important role for SPP in allergic sensitization to short ragweed.
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study
VL  - 47
IS  - 6
SP  - 815
EP  - 828
DO  - 10.1111/cea.12874
ER  - 
@article{
author = "Smiljanić, Katarina and Apostolović, Danijela and Trifunović, Snežana S. and Ognjenović, J. and Peruško, Marija and Mihajlović-Lalić, Ljiljana and Burazer, Lidija M. and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2468",
abstract = "Background Short ragweed (Ambrosia artemisiifolia) allergies affect more than 36 million people annually. Ragweed pollen grains release subpollen particles (SPP) of respirable size upon hydration or a change in air electrical conditions. The aim of this study was to characterize the proteomes and allergomes of short ragweed SPP and total pollen protein extract (TOT), and compare their effects with those of standard aqueous pollen protein extract (APE) using sera from short ragweed pollen-sensitized patients. Methods Quantitative 2D gel-based and shotgun proteomics, 1D and 2D immunoblotting, and quantitative ELISA were applied. Novel SPP extraction and preparation protocols enabled appropriate sample preparation and further downstream analysis by quantitative proteomics. Results The SPP fraction contained the highest proportion (94%) of the allergome, with the largest quantities of the minor Amb a 4 and major Amb a 1 allergens, and as unique, NADH dehydrogenases. APE was the richest in Amb a 6, Amb a 5 and Amb a 3, and TOT fraction was the richest in the Amb a 8 allergens (89% and 83% of allergome, respectively). Allergenic potency correlated well among the three fractions tested, with 1D immunoblots demonstrating a slight predominance of IgE reactivity to SPP compared to TOT and APE. However, the strongest IgE binding in ELISA was noted against APE. New allergenic candidates, phosphoglycerate mutase and phosphoglucomutase, were identified in all the three pollen fractions. Enolase, UTP-glucose-1-phosphate uridylyltransferase and polygalacturonase were observed in SPP and TOT fractions as novel allergens of the short ragweed pollen, as previously described. Conclusion and Clinical Relevance We demonstrated that the complete major (Amb a 1 and 11) and almost all minor (Amb a 3, 4, 5, 6, 8 and 9) short ragweed pollen allergen repertoire as well as NADH oxidases are present in SPP, highlighting an important role for SPP in allergic sensitization to short ragweed.",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study",
volume = "47",
number = "6",
pages = "815-828",
doi = "10.1111/cea.12874"
}
Smiljanić, K., Apostolović, D., Trifunović, S. S., Ognjenović, J., Peruško, M., Mihajlović-Lalić, L., Burazer, L. M., van Hage, M.,& Ćirković-Veličković, T. (2017). Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study.
Clinical and Experimental Allergy
Wiley, Hoboken., 47(6), 815-828.
https://doi.org/10.1111/cea.12874
Smiljanić K, Apostolović D, Trifunović SS, Ognjenović J, Peruško M, Mihajlović-Lalić L, Burazer LM, van Hage M, Ćirković-Veličković T. Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study. Clinical and Experimental Allergy. 2017;47(6):815-828
Smiljanić Katarina, Apostolović Danijela, Trifunović Snežana S., Ognjenović J., Peruško Marija, Mihajlović-Lalić Ljiljana, Burazer Lidija M., van Hage Marianne, Ćirković-Veličković Tanja, "Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study" Clinical and Experimental Allergy, 47, no. 6 (2017):815-828,
https://doi.org/10.1111/cea.12874 .
2
14
12
14

Supplementary data for article: Apostolovic, D.; Krstic, M.; Mihailovic, J.; Starkhammar, M.; Cirkovic Velickovic, T.; Hamsten, C.; Van Hage, M. Peptidomics of an in Vitro Digested α-Gal Carrying Protein Revealed IgE-Reactive Peptides. Scientific Reports 2017, 7 (1). https://doi.org/10.1038/s41598-017-05355-4

Apostolović, Danijela; Krstić-Ristivojević, Maja; Mihailović-Vesić, Jelena; Starkhammar, Maria; Ćirković-Veličković, Tanja; Hamsten, Carl; van Hage, Marianne

(Nature Publishing Group, London, 2017)

TY  - BOOK
AU  - Apostolović, Danijela
AU  - Krstić-Ristivojević, Maja
AU  - Mihailović-Vesić, Jelena
AU  - Starkhammar, Maria
AU  - Ćirković-Veličković, Tanja
AU  - Hamsten, Carl
AU  - van Hage, Marianne
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3020
PB  - Nature Publishing Group, London
T2  - Scientific Reports
T1  - Supplementary data for article: Apostolovic, D.; Krstic, M.; Mihailovic, J.; Starkhammar, M.; Cirkovic Velickovic, T.; Hamsten, C.; Van Hage, M. Peptidomics of an in Vitro Digested α-Gal Carrying Protein Revealed IgE-Reactive Peptides. Scientific Reports 2017, 7 (1). https://doi.org/10.1038/s41598-017-05355-4
VL  - 7
IS  - 1
ER  - 
@book{
author = "Apostolović, Danijela and Krstić-Ristivojević, Maja and Mihailović-Vesić, Jelena and Starkhammar, Maria and Ćirković-Veličković, Tanja and Hamsten, Carl and van Hage, Marianne",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3020",
publisher = "Nature Publishing Group, London",
journal = "Scientific Reports",
title = "Supplementary data for article: Apostolovic, D.; Krstic, M.; Mihailovic, J.; Starkhammar, M.; Cirkovic Velickovic, T.; Hamsten, C.; Van Hage, M. Peptidomics of an in Vitro Digested α-Gal Carrying Protein Revealed IgE-Reactive Peptides. Scientific Reports 2017, 7 (1). https://doi.org/10.1038/s41598-017-05355-4",
volume = "7",
number = "1"
}
Apostolović, D., Krstić-Ristivojević, M., Mihailović-Vesić, J., Starkhammar, M., Ćirković-Veličković, T., Hamsten, C.,& van Hage, M. (2017). Supplementary data for article: Apostolovic, D.; Krstic, M.; Mihailovic, J.; Starkhammar, M.; Cirkovic Velickovic, T.; Hamsten, C.; Van Hage, M. Peptidomics of an in Vitro Digested α-Gal Carrying Protein Revealed IgE-Reactive Peptides. Scientific Reports 2017, 7 (1). https://doi.org/10.1038/s41598-017-05355-4.
Scientific Reports
Nature Publishing Group, London., 7(1).
Apostolović D, Krstić-Ristivojević M, Mihailović-Vesić J, Starkhammar M, Ćirković-Veličković T, Hamsten C, van Hage M. Supplementary data for article: Apostolovic, D.; Krstic, M.; Mihailovic, J.; Starkhammar, M.; Cirkovic Velickovic, T.; Hamsten, C.; Van Hage, M. Peptidomics of an in Vitro Digested α-Gal Carrying Protein Revealed IgE-Reactive Peptides. Scientific Reports 2017, 7 (1). https://doi.org/10.1038/s41598-017-05355-4. Scientific Reports. 2017;7(1)
Apostolović Danijela, Krstić-Ristivojević Maja, Mihailović-Vesić Jelena, Starkhammar Maria, Ćirković-Veličković Tanja, Hamsten Carl, van Hage Marianne, "Supplementary data for article: Apostolovic, D.; Krstic, M.; Mihailovic, J.; Starkhammar, M.; Cirkovic Velickovic, T.; Hamsten, C.; Van Hage, M. Peptidomics of an in Vitro Digested α-Gal Carrying Protein Revealed IgE-Reactive Peptides. Scientific Reports 2017, 7 (1). https://doi.org/10.1038/s41598-017-05355-4" Scientific Reports, 7, no. 1 (2017)

Peptidomics of an in vitro digested alpha-Gal carrying protein revealed IgE-reactive peptides

Apostolović, Danijela; Krstić-Ristivojević, Maja; Mihailović-Vesić, Jelena; Starkhammar, Maria; Ćirković-Veličković, Tanja; Hamsten, Carl; van Hage, Marianne

(Nature Publishing Group, London, 2017)

TY  - JOUR
AU  - Apostolović, Danijela
AU  - Krstić-Ristivojević, Maja
AU  - Mihailović-Vesić, Jelena
AU  - Starkhammar, Maria
AU  - Ćirković-Veličković, Tanja
AU  - Hamsten, Carl
AU  - van Hage, Marianne
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2486
AB  - The mammalian carbohydrate galactose-alpha 1,3-galactose (alpha-Gal) causes a novel form of food allergy, red meat allergy, where patients experience severe allergic reactions several hours after red meat consumption. Here we explored gastric digestion of alpha-Gal glycoproteins using an in vitro model. Bovine thyroglobulin (BTG), a typical alpha-Gal carrying glycoprotein, was digested with pepsin. The resulting peptides were characterised by SDS PAGE, immunoblot and ImmunoCAP using sera from 20 red meat allergic patients. During pepsinolysis of BTG, a wide range of peptide bands was observed of which 14 to 17 kDa peptides remained stable throughout the gastric phase. The presence of the alpha-Gal epitope on the obtained peptides was demonstrated by an anti-alpha-Gal antibody and IgE from red meat allergic patients. The alpha-Gal digests were able to inhibit up to 86% of IgE reactivity to BTG. Importantly, basophil activation test demonstrated that the allergenic activity of BTG was retained after digestion in all four tested patients. Mass spectrometry-based peptidomics revealed that these peptides represent mostly internal and C-terminal parts of the protein, where the most potent IgE-binding alpha-Gal residues were identified at Asn(1756), Asn(1850) and Asn(2231). Thus allergenic a-Gal epitopes are stable to pepsinolysis, reinforcing their role as clinically relevant food allergens.
PB  - Nature Publishing Group, London
T2  - Scientific Reports
T1  - Peptidomics of an in vitro digested alpha-Gal carrying protein revealed IgE-reactive peptides
VL  - 7
DO  - 10.1038/s41598-017-05355-4
ER  - 
@article{
author = "Apostolović, Danijela and Krstić-Ristivojević, Maja and Mihailović-Vesić, Jelena and Starkhammar, Maria and Ćirković-Veličković, Tanja and Hamsten, Carl and van Hage, Marianne",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2486",
abstract = "The mammalian carbohydrate galactose-alpha 1,3-galactose (alpha-Gal) causes a novel form of food allergy, red meat allergy, where patients experience severe allergic reactions several hours after red meat consumption. Here we explored gastric digestion of alpha-Gal glycoproteins using an in vitro model. Bovine thyroglobulin (BTG), a typical alpha-Gal carrying glycoprotein, was digested with pepsin. The resulting peptides were characterised by SDS PAGE, immunoblot and ImmunoCAP using sera from 20 red meat allergic patients. During pepsinolysis of BTG, a wide range of peptide bands was observed of which 14 to 17 kDa peptides remained stable throughout the gastric phase. The presence of the alpha-Gal epitope on the obtained peptides was demonstrated by an anti-alpha-Gal antibody and IgE from red meat allergic patients. The alpha-Gal digests were able to inhibit up to 86% of IgE reactivity to BTG. Importantly, basophil activation test demonstrated that the allergenic activity of BTG was retained after digestion in all four tested patients. Mass spectrometry-based peptidomics revealed that these peptides represent mostly internal and C-terminal parts of the protein, where the most potent IgE-binding alpha-Gal residues were identified at Asn(1756), Asn(1850) and Asn(2231). Thus allergenic a-Gal epitopes are stable to pepsinolysis, reinforcing their role as clinically relevant food allergens.",
publisher = "Nature Publishing Group, London",
journal = "Scientific Reports",
title = "Peptidomics of an in vitro digested alpha-Gal carrying protein revealed IgE-reactive peptides",
volume = "7",
doi = "10.1038/s41598-017-05355-4"
}
Apostolović, D., Krstić-Ristivojević, M., Mihailović-Vesić, J., Starkhammar, M., Ćirković-Veličković, T., Hamsten, C.,& van Hage, M. (2017). Peptidomics of an in vitro digested alpha-Gal carrying protein revealed IgE-reactive peptides.
Scientific Reports
Nature Publishing Group, London., 7.
https://doi.org/10.1038/s41598-017-05355-4
Apostolović D, Krstić-Ristivojević M, Mihailović-Vesić J, Starkhammar M, Ćirković-Veličković T, Hamsten C, van Hage M. Peptidomics of an in vitro digested alpha-Gal carrying protein revealed IgE-reactive peptides. Scientific Reports. 2017;7
Apostolović Danijela, Krstić-Ristivojević Maja, Mihailović-Vesić Jelena, Starkhammar Maria, Ćirković-Veličković Tanja, Hamsten Carl, van Hage Marianne, "Peptidomics of an in vitro digested alpha-Gal carrying protein revealed IgE-reactive peptides" Scientific Reports, 7 (2017),
https://doi.org/10.1038/s41598-017-05355-4 .
9
11
11

Alpha-gal epitope on protein surface affects uptake and degradation in immature monocyte-derived dendritic cells

Krstić-Ristivojević, Maja; Apostolović, Danijela; Tran, T.; Grundström, Jeanette; Radoi, Vlad; Vukojević, Vesna; Ćirković-Veličković, Tanja; Hamsten, Carl; van Hage, Marianne

(Wiley, Hoboken, 2017)

TY  - CONF
AU  - Krstić-Ristivojević, Maja
AU  - Apostolović, Danijela
AU  - Tran, T.
AU  - Grundström, Jeanette
AU  - Radoi, Vlad
AU  - Vukojević, Vesna
AU  - Ćirković-Veličković, Tanja
AU  - Hamsten, Carl
AU  - van Hage, Marianne
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2516
PB  - Wiley, Hoboken
C3  - Allergy
T1  - Alpha-gal epitope on protein surface affects uptake and degradation in immature monocyte-derived dendritic cells
VL  - 72
SP  - 796
EP  - 796
ER  - 
@conference{
author = "Krstić-Ristivojević, Maja and Apostolović, Danijela and Tran, T. and Grundström, Jeanette and Radoi, Vlad and Vukojević, Vesna and Ćirković-Veličković, Tanja and Hamsten, Carl and van Hage, Marianne",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2516",
publisher = "Wiley, Hoboken",
journal = "Allergy",
title = "Alpha-gal epitope on protein surface affects uptake and degradation in immature monocyte-derived dendritic cells",
volume = "72",
pages = "796-796"
}
Krstić-Ristivojević, M., Apostolović, D., Tran, T., Grundström, J., Radoi, V., Vukojević, V., Ćirković-Veličković, T., Hamsten, C.,& van Hage, M. (2017). Alpha-gal epitope on protein surface affects uptake and degradation in immature monocyte-derived dendritic cells.
Allergy
Wiley, Hoboken., 72, 796-796.
Krstić-Ristivojević M, Apostolović D, Tran T, Grundström J, Radoi V, Vukojević V, Ćirković-Veličković T, Hamsten C, van Hage M. Alpha-gal epitope on protein surface affects uptake and degradation in immature monocyte-derived dendritic cells. Allergy. 2017;72:796-796
Krstić-Ristivojević Maja, Apostolović Danijela, Tran T., Grundström Jeanette, Radoi Vlad, Vukojević Vesna, Ćirković-Veličković Tanja, Hamsten Carl, van Hage Marianne, "Alpha-gal epitope on protein surface affects uptake and degradation in immature monocyte-derived dendritic cells" Allergy, 72 (2017):796-796

Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249

Apostolović, Danijela; Stanić-Vučinić, Dragana; de Jongh, Harmen H. J.; de Jong, Govardus A. H.; Mihailović-Vesić, Jelena; Radosavljević, Jelena; Radibratović, Milica; Nordlee, Julie A.; Baumert, Joseph L.; Milčić, Miloš K.; Taylor, Steve L.; Clua, Nuria Garrido; Ćirković-Veličković, Tanja; Koppelman, Stef J.

(Nature Publishing Group, London, 2016)

TY  - BOOK
AU  - Apostolović, Danijela
AU  - Stanić-Vučinić, Dragana
AU  - de Jongh, Harmen H. J.
AU  - de Jong, Govardus A. H.
AU  - Mihailović-Vesić, Jelena
AU  - Radosavljević, Jelena
AU  - Radibratović, Milica
AU  - Nordlee, Julie A.
AU  - Baumert, Joseph L.
AU  - Milčić, Miloš K.
AU  - Taylor, Steve L.
AU  - Clua, Nuria Garrido
AU  - Ćirković-Veličković, Tanja
AU  - Koppelman, Stef J.
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3415
PB  - Nature Publishing Group, London
T2  - Scientific Reports
T1  - Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249
ER  - 
@book{
author = "Apostolović, Danijela and Stanić-Vučinić, Dragana and de Jongh, Harmen H. J. and de Jong, Govardus A. H. and Mihailović-Vesić, Jelena and Radosavljević, Jelena and Radibratović, Milica and Nordlee, Julie A. and Baumert, Joseph L. and Milčić, Miloš K. and Taylor, Steve L. and Clua, Nuria Garrido and Ćirković-Veličković, Tanja and Koppelman, Stef J.",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3415",
publisher = "Nature Publishing Group, London",
journal = "Scientific Reports",
title = "Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249"
}
Apostolović, D., Stanić-Vučinić, D., de Jongh, H. H. J., de Jong, G. A. H., Mihailović-Vesić, J., Radosavljević, J., Radibratović, M., Nordlee, J. A., Baumert, J. L., Milčić, M. K., Taylor, S. L., Clua, N. G., Ćirković-Veličković, T.,& Koppelman, S. J. (2016). Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249.
Scientific Reports
Nature Publishing Group, London..
Apostolović D, Stanić-Vučinić D, de Jongh HHJ, de Jong GAH, Mihailović-Vesić J, Radosavljević J, Radibratović M, Nordlee JA, Baumert JL, Milčić MK, Taylor SL, Clua NG, Ćirković-Veličković T, Koppelman SJ. Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249. Scientific Reports. 2016;
Apostolović Danijela, Stanić-Vučinić Dragana, de Jongh Harmen H. J., de Jong Govardus A. H., Mihailović-Vesić Jelena, Radosavljević Jelena, Radibratović Milica, Nordlee Julie A., Baumert Joseph L., Milčić Miloš K., Taylor Steve L., Clua Nuria Garrido, Ćirković-Veličković Tanja, Koppelman Stef J., "Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249" Scientific Reports (2016)

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

Stanić-Vučinić, Dragana; Stojadinović, Marija M.; Mirkov, Ivana; Apostolović, Danijela; Burazer, Lidija M.; Atanasković-Marković, Marina; Kataranovski, Milena; Ćirković-Veličković, Tanja

(Royal Soc Chemistry, Cambridge, 2016)

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