Mihailović, Jelena

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3b3b6d2d-a907-49f8-b2db-12a6d76a05c4
  • Mihailović, Jelena (9)
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Author's Bibliography

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",
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. in 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. in Allergy: European Journal of Allergy and Clinical Immunology. 2020;75(1):217-220.
doi: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, "Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy" in Allergy: European Journal of Allergy and Clinical Immunology, 75, no. 1 (2020):217-220,
https://doi.org/10.1111/ALL.13978 . .
10
21
20
20

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",
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. in 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. in Allergy: European Journal of Allergy and Clinical Immunology. 2020;75(1):217-220.
doi: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, "Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy" in Allergy: European Journal of Allergy and Clinical Immunology, 75, no. 1 (2020):217-220,
https://doi.org/10.1111/all.13978 . .
10
21
20
20

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

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

(Springer, 2020)

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

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

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

(Springer, 2020)

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

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  - DATA
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  - 
@misc{
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",
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. in 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. in 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" in Allergy: European Journal of Allergy and Clinical Immunology (2020).

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

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

(Wiley, 2020)

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

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

(Springer, 2020)

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

Proteomika posttranslacionih i hemijskih modifikacija proteina i interakcije proteina od značaja u alergiji na hranu

Mihailović, Jelena

(Универзитет у Београду, Хемијски факултет, 2019)

TY  - THES
AU  - Mihailović, Jelena
PY  - 2019
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=7675
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:22858/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=24146185
UR  - https://nardus.mpn.gov.rs/handle/123456789/17611
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4381
AB  - Alergija na hranu je reakcija preosetljivosti imunskog sistema na hranu koja dovodi dostvaranja IgE antitela. Ne postoji efikasan tretman i izbegavanje namirnica koje izazivajusimptome je jedini način za sprečavanje ozbiljnih posledica. Cilj ove teze je izučavanjeposttranslacionih i hemijskih modifikacija (PTM i HM) i interakcija alergena hrane sabiološki aktivnim polifenolom biljnog porekla.Alergija na crveno meso je novootkriveni tip odložene reakcije, sa PTM galaktozil-α-1,3-galaktozom (α-Gal) kao epitopom. Ispitani su podložnost model proteina - tiroglobulina(TG) digestiji pepsinom, prisustvo α-Gal na rezultujućim peptidima i pretpostavljenomesto vezivanja α-Gal za TG. Pokazano je da je α-Gal celim tokom simulirane želudačnedigestije vezan za nastale peptide TG, koji zadržavaju sposobnost da vežu IgE.Alergija na kikiriki je među najopasnijim zbog učestalosti, postojanosti i ozbiljnostisimptoma. Postoje razlike u alergenosti između sirovog i pečenog kikirikija, koje mogupoticati od razlika u modifikacijama alergena. U ovoj disertaciji je proučena razlika umodifikacijama glavnih alergena iz sirovog i pečenog kikirikija. Detektovano je 27modifikacija, od kojih 4 isključivo na proteinima pečenog kikirikija. Pokazane su razlikeu profilima modifikacija proteina između ekstrakata, koje mogu uticati na alergenost.2S albumini kikirikija su zbog kompaktne strukture otporni na delovanje digestivnihenzima, što se povezuje sa njihovom alergenošću. Ispitane su interakcije između njih iepigalokatehin-3-galata (EGCG), katehina zelenog čaja sa imunomodulatornimsvojstvima koji pospešuje digestiju proteina pepsinom. Vezivanje EGCG-a za alergeneizaziva promene u njihovoj strukturi (entalpijski povoljan proces), sa konstantamavezivanja reda veličine 104 M-1.
AB  - Food allergy is an immune system reaction to certain foods that results in IgE antibodygeneration. Efficient treatment does not exist, so avoidance of trigger foods is the onlyway to prevent serious consequences. The aim of this thesis was to study posttranslationaland chemical modifications (PTM and CM) of food allergens and their interactions withbiologically active plant polyphenol.Red meat allergy is a newly discovered type of allergy with delayed symptoms and aPTM - galactose-α-1,3-galactose (α-Gal) as an epitope. Digestibility of a model protein -thyroglobulin (TG) by pepsin and presence of α-Gal on resulting peptides was studied,and the position of α-Gal containing glycan on TG was proposed. It was shown thatthroughout simulated gastric digestion α-Gal remains bound to IgE reactive TG peptides.Peanut allergy is among most dangerous types of food allergies due to prevalence,persistence and symptom severity. Differences in allergenicity between raw and roastedpeanuts were previously shown and might stem from differences in protein modifications.Differences in major allergen modifications between raw and roasted peanut werestudied. Twenty-seven modifications were detected, 4 of which exclusively on allergensfrom roasted peanuts. Differences in modification profiling were found between the twoprotein preparations that can affect their allergenicity.Peanut 2S albumins are compact digestion-resistant proteins, which attributes to theirallergenicity. Their interactions with epigallocatechin-3-gallate (EGCG), animmunomodulatory green tea catechin that facilitates pepsin digestion of proteins werestudied. The results show that binding of EGCG to these allergens induces conformationalchanges, and is enthalpy favorable with binding constants of 104 M-1.
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Proteomika posttranslacionih i hemijskih modifikacija proteina i interakcije proteina od značaja u alergiji na hranu
ER  - 
@phdthesis{
author = "Mihailović, Jelena",
year = "2019",
abstract = "Alergija na hranu je reakcija preosetljivosti imunskog sistema na hranu koja dovodi dostvaranja IgE antitela. Ne postoji efikasan tretman i izbegavanje namirnica koje izazivajusimptome je jedini način za sprečavanje ozbiljnih posledica. Cilj ove teze je izučavanjeposttranslacionih i hemijskih modifikacija (PTM i HM) i interakcija alergena hrane sabiološki aktivnim polifenolom biljnog porekla.Alergija na crveno meso je novootkriveni tip odložene reakcije, sa PTM galaktozil-α-1,3-galaktozom (α-Gal) kao epitopom. Ispitani su podložnost model proteina - tiroglobulina(TG) digestiji pepsinom, prisustvo α-Gal na rezultujućim peptidima i pretpostavljenomesto vezivanja α-Gal za TG. Pokazano je da je α-Gal celim tokom simulirane želudačnedigestije vezan za nastale peptide TG, koji zadržavaju sposobnost da vežu IgE.Alergija na kikiriki je među najopasnijim zbog učestalosti, postojanosti i ozbiljnostisimptoma. Postoje razlike u alergenosti između sirovog i pečenog kikirikija, koje mogupoticati od razlika u modifikacijama alergena. U ovoj disertaciji je proučena razlika umodifikacijama glavnih alergena iz sirovog i pečenog kikirikija. Detektovano je 27modifikacija, od kojih 4 isključivo na proteinima pečenog kikirikija. Pokazane su razlikeu profilima modifikacija proteina između ekstrakata, koje mogu uticati na alergenost.2S albumini kikirikija su zbog kompaktne strukture otporni na delovanje digestivnihenzima, što se povezuje sa njihovom alergenošću. Ispitane su interakcije između njih iepigalokatehin-3-galata (EGCG), katehina zelenog čaja sa imunomodulatornimsvojstvima koji pospešuje digestiju proteina pepsinom. Vezivanje EGCG-a za alergeneizaziva promene u njihovoj strukturi (entalpijski povoljan proces), sa konstantamavezivanja reda veličine 104 M-1., Food allergy is an immune system reaction to certain foods that results in IgE antibodygeneration. Efficient treatment does not exist, so avoidance of trigger foods is the onlyway to prevent serious consequences. The aim of this thesis was to study posttranslationaland chemical modifications (PTM and CM) of food allergens and their interactions withbiologically active plant polyphenol.Red meat allergy is a newly discovered type of allergy with delayed symptoms and aPTM - galactose-α-1,3-galactose (α-Gal) as an epitope. Digestibility of a model protein -thyroglobulin (TG) by pepsin and presence of α-Gal on resulting peptides was studied,and the position of α-Gal containing glycan on TG was proposed. It was shown thatthroughout simulated gastric digestion α-Gal remains bound to IgE reactive TG peptides.Peanut allergy is among most dangerous types of food allergies due to prevalence,persistence and symptom severity. Differences in allergenicity between raw and roastedpeanuts were previously shown and might stem from differences in protein modifications.Differences in major allergen modifications between raw and roasted peanut werestudied. Twenty-seven modifications were detected, 4 of which exclusively on allergensfrom roasted peanuts. Differences in modification profiling were found between the twoprotein preparations that can affect their allergenicity.Peanut 2S albumins are compact digestion-resistant proteins, which attributes to theirallergenicity. Their interactions with epigallocatechin-3-gallate (EGCG), animmunomodulatory green tea catechin that facilitates pepsin digestion of proteins werestudied. The results show that binding of EGCG to these allergens induces conformationalchanges, and is enthalpy favorable with binding constants of 104 M-1.",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Proteomika posttranslacionih i hemijskih modifikacija proteina i interakcije proteina od značaja u alergiji na hranu"
}
Mihailović, J.. (2019). Proteomika posttranslacionih i hemijskih modifikacija proteina i interakcije proteina od značaja u alergiji na hranu. in Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
Mihailović J. Proteomika posttranslacionih i hemijskih modifikacija proteina i interakcije proteina od značaja u alergiji na hranu. in Универзитет у Београду. 2019;..
Mihailović, Jelena, "Proteomika posttranslacionih i hemijskih modifikacija proteina i interakcije proteina od značaja u alergiji na hranu" in Универзитет у Београду (2019).

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

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

(2019)

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