TY  - JOUR
AU  - Smiljanić, Katarina
AU  - Apostolović, Danijela
AU  - Trifunović, Snežana S.
AU  - Ognjenović, J.
AU  - Peruško, Marija
AU  - Mihajlović, Luka
AU  - Burazer, Lidija M.
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - https://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, Luka and Burazer, Lidija M. and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2017",
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, 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. in 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 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. in Clinical and Experimental Allergy. 2017;47(6):815-828.
doi:10.1111/cea.12874 .

Smiljanić, Katarina, Apostolović, Danijela, Trifunović, Snežana S., Ognjenović, J., Peruško, Marija, Mihajlović, Luka, 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" in Clinical and Experimental Allergy, 47, no. 6 (2017):815-828,
https://doi.org/10.1111/cea.12874 . .

TY  - DATA
AU  - Smiljanić, Katarina
AU  - Apostolović, Danijela
AU  - Trifunović, Snežana S.
AU  - Ognjenović, J.
AU  - Peruško, Marija
AU  - Mihajlović, Luka
AU  - Burazer, Lidija M.
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - https://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
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3127
ER  - 

@misc{
author = "Smiljanić, Katarina and Apostolović, Danijela and Trifunović, Snežana S. and Ognjenović, J. and Peruško, Marija and Mihajlović, Luka and Burazer, Lidija M. and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2017",
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",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3127"
}

Smiljanić, K., Apostolović, D., Trifunović, S. S., Ognjenović, J., Peruško, M., Mihajlović, 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. in Clinical and Experimental Allergy
Wiley, Hoboken..
https://hdl.handle.net/21.15107/rcub_cherry_3127

Smiljanić K, Apostolović D, Trifunović SS, Ognjenović J, Peruško M, Mihajlović 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. in Clinical and Experimental Allergy. 2017;.
https://hdl.handle.net/21.15107/rcub_cherry_3127 .

Smiljanić, Katarina, Apostolović, Danijela, Trifunović, Snežana S., Ognjenović, J., Peruško, Marija, Mihajlović, Luka, 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" in Clinical and Experimental Allergy (2017),
https://hdl.handle.net/21.15107/rcub_cherry_3127 .

TY  - JOUR
AU  - Smiljanić, Katarina
AU  - Apostolović, Danijela
AU  - Trifunović, Snežana S.
AU  - Ognjenović, J.
AU  - Peruško, Marija
AU  - Mihajlović, Luka
AU  - Burazer, Lidija M.
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - https://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, Luka and Burazer, Lidija M. and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2017",
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, 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. in 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 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. in Clinical and Experimental Allergy. 2017;47(6):815-828.
doi:10.1111/cea.12874 .

Smiljanić, Katarina, Apostolović, Danijela, Trifunović, Snežana S., Ognjenović, J., Peruško, Marija, Mihajlović, Luka, 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" in Clinical and Experimental Allergy, 47, no. 6 (2017):815-828,
https://doi.org/10.1111/cea.12874 . .

TY  - CHAP
AU  - Ćirković-Veličković, Tanja
AU  - Ognjenović, J.
AU  - Mihajlović, L.
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/290
AB  - Separation of amino acids, peptides, and proteins (bioanalytes) via ion exchange (IE) has widespread usage because it is usually very simple to design and it has high capacity and easily achievable control of the separation process. Amino acids, as principal constituents of proteins and having a plethora of biological functions of their own, are always in focus when developing novel methods. Separation and quantification of amino acids is essential in food science, medicine, agricultural science, etc. Peptides exist in nature and have diverse functions. Digestion of proteins by enzymes also gives complex mixtures of peptides and IE finds its application in peptide separation. There are lots of reasons for the popularity of IE in protein isolation and purification. It is used in research, analysis, and large-scale purification of proteins. Ion exchange is ideal for the initial capture of proteins because of its high capacity, relatively low cost, and its ability to survive rigorous cleaning regimes. This chapter covers basic principles and modern applications of IE in separation of amino acids, peptides, and proteins. © 2012 Springer Science+Business Media B.V. All rights are reserved.
T2  - Ion Exchange Technology II: Applications
T1  - Separation of amino acids, peptides, and proteins by ion exchange chromatography
SP  - 1
EP  - 34
DO  - 10.1007/978-94-007-4026-6_1
ER  - 

@inbook{
author = "Ćirković-Veličković, Tanja and Ognjenović, J. and Mihajlović, L.",
year = "2012",
abstract = "Separation of amino acids, peptides, and proteins (bioanalytes) via ion exchange (IE) has widespread usage because it is usually very simple to design and it has high capacity and easily achievable control of the separation process. Amino acids, as principal constituents of proteins and having a plethora of biological functions of their own, are always in focus when developing novel methods. Separation and quantification of amino acids is essential in food science, medicine, agricultural science, etc. Peptides exist in nature and have diverse functions. Digestion of proteins by enzymes also gives complex mixtures of peptides and IE finds its application in peptide separation. There are lots of reasons for the popularity of IE in protein isolation and purification. It is used in research, analysis, and large-scale purification of proteins. Ion exchange is ideal for the initial capture of proteins because of its high capacity, relatively low cost, and its ability to survive rigorous cleaning regimes. This chapter covers basic principles and modern applications of IE in separation of amino acids, peptides, and proteins. © 2012 Springer Science+Business Media B.V. All rights are reserved.",
journal = "Ion Exchange Technology II: Applications",
booktitle = "Separation of amino acids, peptides, and proteins by ion exchange chromatography",
pages = "1-34",
doi = "10.1007/978-94-007-4026-6_1"
}

Ćirković-Veličković, T., Ognjenović, J.,& Mihajlović, L.. (2012). Separation of amino acids, peptides, and proteins by ion exchange chromatography. in Ion Exchange Technology II: Applications, 1-34.
https://doi.org/10.1007/978-94-007-4026-6_1

Ćirković-Veličković T, Ognjenović J, Mihajlović L. Separation of amino acids, peptides, and proteins by ion exchange chromatography. in Ion Exchange Technology II: Applications. 2012;:1-34.
doi:10.1007/978-94-007-4026-6_1 .

Ćirković-Veličković, Tanja, Ognjenović, J., Mihajlović, L., "Separation of amino acids, peptides, and proteins by ion exchange chromatography" in Ion Exchange Technology II: Applications (2012):1-34,
https://doi.org/10.1007/978-94-007-4026-6_1 . .

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

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

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

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

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

TY  - CONF
AU  - Stojadinović, Marija M.
AU  - Ognjenović, J.
AU  - Radosavljević, Jelena
AU  - Mihailović-Vesić, Jelena
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1527
PB  - Wiley-Blackwell, Hoboken
C3  - FEBS Journal / Federation of European of Biochemical Societies
T1  - Non-covalent interactions between dietary polyphenols and bovine beta-lactoglobulin: Effect on the protein structure, digestibility and total antioxidant capacity
VL  - 279
SP  - 400
EP  - 400
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1527
ER  - 

@conference{
author = "Stojadinović, Marija M. and Ognjenović, J. and Radosavljević, Jelena and Mihailović-Vesić, Jelena and Prodić, Ivana and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2012",
publisher = "Wiley-Blackwell, Hoboken",
journal = "FEBS Journal / Federation of European of Biochemical Societies",
title = "Non-covalent interactions between dietary polyphenols and bovine beta-lactoglobulin: Effect on the protein structure, digestibility and total antioxidant capacity",
volume = "279",
pages = "400-400",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1527"
}

Stojadinović, M. M., Ognjenović, J., Radosavljević, J., Mihailović-Vesić, J., Prodić, I., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2012). Non-covalent interactions between dietary polyphenols and bovine beta-lactoglobulin: Effect on the protein structure, digestibility and total antioxidant capacity. in FEBS Journal / Federation of European of Biochemical Societies
Wiley-Blackwell, Hoboken., 279, 400-400.
https://hdl.handle.net/21.15107/rcub_cherry_1527

Stojadinović MM, Ognjenović J, Radosavljević J, Mihailović-Vesić J, Prodić I, Stanić-Vučinić D, Ćirković-Veličković T. Non-covalent interactions between dietary polyphenols and bovine beta-lactoglobulin: Effect on the protein structure, digestibility and total antioxidant capacity. in FEBS Journal / Federation of European of Biochemical Societies. 2012;279:400-400.
https://hdl.handle.net/21.15107/rcub_cherry_1527 .

Stojadinović, Marija M., Ognjenović, J., Radosavljević, Jelena, Mihailović-Vesić, Jelena, Prodić, Ivana, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Non-covalent interactions between dietary polyphenols and bovine beta-lactoglobulin: Effect on the protein structure, digestibility and total antioxidant capacity" in FEBS Journal / Federation of European of Biochemical Societies, 279 (2012):400-400,
https://hdl.handle.net/21.15107/rcub_cherry_1527 .

TY  - CONF
AU  - Ognjenović, J.
AU  - Tantoush, Z.
AU  - Janko, R.
AU  - Ćirković-Veličković, Tanja
AU  - Vukmirica, J.
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1472
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - Optimisation of high-quality nucleic acid isolation from linden tree (Tilia cordata) leaves and pollen
VL  - 66
SP  - 485
EP  - 485
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1472
ER  - 

@conference{
author = "Ognjenović, J. and Tantoush, Z. and Janko, R. and Ćirković-Veličković, Tanja and Vukmirica, J.",
year = "2011",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Optimisation of high-quality nucleic acid isolation from linden tree (Tilia cordata) leaves and pollen",
volume = "66",
pages = "485-485",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1472"
}

Ognjenović, J., Tantoush, Z., Janko, R., Ćirković-Veličković, T.,& Vukmirica, J.. (2011). Optimisation of high-quality nucleic acid isolation from linden tree (Tilia cordata) leaves and pollen. in Allergy
Wiley-Blackwell, Hoboken., 66, 485-485.
https://hdl.handle.net/21.15107/rcub_cherry_1472

Ognjenović J, Tantoush Z, Janko R, Ćirković-Veličković T, Vukmirica J. Optimisation of high-quality nucleic acid isolation from linden tree (Tilia cordata) leaves and pollen. in Allergy. 2011;66:485-485.
https://hdl.handle.net/21.15107/rcub_cherry_1472 .

Ognjenović, J., Tantoush, Z., Janko, R., Ćirković-Veličković, Tanja, Vukmirica, J., "Optimisation of high-quality nucleic acid isolation from linden tree (Tilia cordata) leaves and pollen" in Allergy, 66 (2011):485-485,
https://hdl.handle.net/21.15107/rcub_cherry_1472 .