TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
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/123456789/5724
AB  - Background: 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 appreciated; hence, little progress has been made within this field. Our aim was to show that in-depth PTM profiling has a great importance and deserves to be explored with renewed and simple method with advanced algorithm.
Method: 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.
Results: 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.
Conclusion: Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed that heavy metals are primarily responsible for oxidative stress effects observed in Timothy grass pollen proteome, rather than gaseous pollutants formed during road traffics such as ozone, nitric dioxide or Sulphur di- and/or trioxide.
PB  - Serbian Proteomic Association - SePA
C3  - Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, envirinmental protection and medical research, Novi Sad 2019
T1  - In-depth quantitative profiling of post-translational modifications of Timothy grass pollen proteome in relation to environmental pollution and causal oxidative stress
IS  - L7
SP  - 13
EP  - 13
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5724
ER  - 

@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Veljović, Đorđe and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Background: 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 appreciated; hence, little progress has been made within this field. Our aim was to show that in-depth PTM profiling has a great importance and deserves to be explored with renewed and simple method with advanced algorithm.
Method: 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.
Results: 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.
Conclusion: Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed that heavy metals are primarily responsible for oxidative stress effects observed in Timothy grass pollen proteome, rather than gaseous pollutants formed during road traffics such as ozone, nitric dioxide or Sulphur di- and/or trioxide.",
publisher = "Serbian Proteomic Association - SePA",
journal = "Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, envirinmental protection and medical research, Novi Sad 2019",
title = "In-depth quantitative profiling of post-translational modifications of Timothy grass pollen proteome in relation to environmental pollution and causal oxidative stress",
number = "L7",
pages = "13-13",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5724"
}

Smiljanić, K., Prodić, I., Apostolović, D., 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 proteome in relation to environmental pollution and causal oxidative stress. in Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, envirinmental protection and medical research, Novi Sad 2019
Serbian Proteomic Association - SePA.(L7), 13-13.
https://hdl.handle.net/21.15107/rcub_cherry_5724

Smiljanić K, Prodić I, Apostolović D, Veljović Đ, Mutić J, van Hage M, Burazer LM, Ćirković-Veličković T. In-depth quantitative profiling of post-translational modifications of Timothy grass pollen proteome in relation to environmental pollution and causal oxidative stress. in Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, envirinmental protection and medical research, Novi Sad 2019. 2019;(L7):13-13.
https://hdl.handle.net/21.15107/rcub_cherry_5724 .

Smiljanić, Katarina, Prodić, Ivana, Apostolović, Danijela, 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 proteome in relation to environmental pollution and causal oxidative stress" in Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, envirinmental protection and medical research, Novi Sad 2019, no. L7 (2019):13-13,
https://hdl.handle.net/21.15107/rcub_cherry_5724 .

TY  - DATA
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  - https://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
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3225
ER  - 

@misc{
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",
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",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3225"
}

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. in Clinical and Experimental Allergy
Wiley, Hoboken..
https://hdl.handle.net/21.15107/rcub_cherry_3225

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. in Clinical and Experimental Allergy. 2018;.
https://hdl.handle.net/21.15107/rcub_cherry_3225 .

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" in Clinical and Experimental Allergy (2018),
https://hdl.handle.net/21.15107/rcub_cherry_3225 .

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Aleksić, Ivana
AU  - Veljović, Đorđe
AU  - Ćirković-Veličković, Tanja
AU  - Mutić, Jelena
AU  - Burazer, Lidija M.
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5709
AB  - Objective: to create method for unrestrictive deep, relative quantification of post translational
modifications (PTMs) within different proteomes. Pollution field studies of bio indicators such as
pollen are valuable because of realistic situation of target contamination, however they carry the
great extent of uncertainty in attributing and delineating the polluting effect from multiple sources.
Holistic research platform focusing on comprehensively characterized and quantified PTMs of
comparable bio-indicator proteomes could help and overcome these obstacles of field pollution
studies.
Material and Methods: Scanning electron and light microscopy assessed surface and sub pollen
particle (SPP) releasing features of timothy grass (TG) pollen. Inductively coupled atomic emission
spectrometry revealed metal elemental content in pollen while in solution trypsin digested pollen
proteomes analysed with high resolution Orbitrap mass tandem spectrometry and PEAKS Suite 8.5
brought quantitative information on protein expression level and its PTM profiling.
Results: TG polluted pollen samples (P2) collected along regional road and chemical plant,
exposed to air contaminants from road traffics and chemical plants showed 4.5 times higher SPP
releasing capacity, with notable surface changes, as well as significantly higher contents of Mn, Hg
and Cd. Antioxidative enzymes (oxidoreductases, superoxide dismutases and peroxidases),
including actin, were upregulated several times in polluted sample compared to ecologically
preserved pollen (P1). While the level of spontaneous and physiological PTMs including
methylation, acetylation, deamidation and formylation, was similar without significant changes in
P1 and P2 pollens, oxidative PTMs including oxidation of Met, Lys, His, Pro and HNE and hexose
adducts showed several times higher and significant increase in abundancy of P2 compared to P1.
PTMs connected to road traffic such as tyrosine nitration were very rare and low abundant.
Conclusion: Results suggest prominent role of chemical pollution compared to effect of road traffic
pollution, with primary consequences from oxidative properties of mercury (Hg) and cadmium
(Cd).
PB  - Srpsko Udruženje za Proteomiku, SePA; IBISS
C3  - IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija
T1  - Deep and quantitative profiling of PTMs in ecologically preserved and polluted pollen proteomes of timothy grass reveals predominant source of contamination
SP  - 13
EP  - 13
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5709
ER  - 

@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Aleksić, Ivana and Veljović, Đorđe and Ćirković-Veličković, Tanja and Mutić, Jelena and Burazer, Lidija M.",
year = "2018",
abstract = "Objective: to create method for unrestrictive deep, relative quantification of post translational
modifications (PTMs) within different proteomes. Pollution field studies of bio indicators such as
pollen are valuable because of realistic situation of target contamination, however they carry the
great extent of uncertainty in attributing and delineating the polluting effect from multiple sources.
Holistic research platform focusing on comprehensively characterized and quantified PTMs of
comparable bio-indicator proteomes could help and overcome these obstacles of field pollution
studies.
Material and Methods: Scanning electron and light microscopy assessed surface and sub pollen
particle (SPP) releasing features of timothy grass (TG) pollen. Inductively coupled atomic emission
spectrometry revealed metal elemental content in pollen while in solution trypsin digested pollen
proteomes analysed with high resolution Orbitrap mass tandem spectrometry and PEAKS Suite 8.5
brought quantitative information on protein expression level and its PTM profiling.
Results: TG polluted pollen samples (P2) collected along regional road and chemical plant,
exposed to air contaminants from road traffics and chemical plants showed 4.5 times higher SPP
releasing capacity, with notable surface changes, as well as significantly higher contents of Mn, Hg
and Cd. Antioxidative enzymes (oxidoreductases, superoxide dismutases and peroxidases),
including actin, were upregulated several times in polluted sample compared to ecologically
preserved pollen (P1). While the level of spontaneous and physiological PTMs including
methylation, acetylation, deamidation and formylation, was similar without significant changes in
P1 and P2 pollens, oxidative PTMs including oxidation of Met, Lys, His, Pro and HNE and hexose
adducts showed several times higher and significant increase in abundancy of P2 compared to P1.
PTMs connected to road traffic such as tyrosine nitration were very rare and low abundant.
Conclusion: Results suggest prominent role of chemical pollution compared to effect of road traffic
pollution, with primary consequences from oxidative properties of mercury (Hg) and cadmium
(Cd).",
publisher = "Srpsko Udruženje za Proteomiku, SePA; IBISS",
journal = "IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija",
title = "Deep and quantitative profiling of PTMs in ecologically preserved and polluted pollen proteomes of timothy grass reveals predominant source of contamination",
pages = "13-13",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5709"
}

Smiljanić, K., Prodić, I., Aleksić, I., Veljović, Đ., Ćirković-Veličković, T., Mutić, J.,& Burazer, L. M.. (2018). Deep and quantitative profiling of PTMs in ecologically preserved and polluted pollen proteomes of timothy grass reveals predominant source of contamination. in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija
Srpsko Udruženje za Proteomiku, SePA; IBISS., 13-13.
https://hdl.handle.net/21.15107/rcub_cherry_5709

Smiljanić K, Prodić I, Aleksić I, Veljović Đ, Ćirković-Veličković T, Mutić J, Burazer LM. Deep and quantitative profiling of PTMs in ecologically preserved and polluted pollen proteomes of timothy grass reveals predominant source of contamination. in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija. 2018;:13-13.
https://hdl.handle.net/21.15107/rcub_cherry_5709 .

Smiljanić, Katarina, Prodić, Ivana, Aleksić, Ivana, Veljović, Đorđe, Ćirković-Veličković, Tanja, Mutić, Jelena, Burazer, Lidija M., "Deep and quantitative profiling of PTMs in ecologically preserved and polluted pollen proteomes of timothy grass reveals predominant source of contamination" in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija (2018):13-13,
https://hdl.handle.net/21.15107/rcub_cherry_5709 .

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  - Stojadinović, Marija M.
AU  - Burazer, Lidija M.
AU  - Ercili-Cura, Dilek
AU  - Sancho, Ana
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
AU  - Stanić-Vučinić, Dragana
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1275
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5261
AB  - BACKGROUND: The major whey protein beta-lactoglobulin (BLG) has been widely studied for its functional properties. The aim of this study was to develop an efficient, inexpensive and rapid one-step method for the isolation and purification of BLG while preserving its native structure. RESULTS: BLGwas purified fromdefattedwheyobtainedfromrawcow's milkbyanionexchangechromatography. Protein purity and identitywere determined using reverse phase high-performance liquid chromatography andmass spectrometry. Total BLG yield was 80% with protein purity from 97 to 99%. BLG isoforms A and B were separated into fractions of 91 and 99% purity respectively. The structure and native conformation of the isolated BLGwere compared with those of standard commercial BLG by circular dichroism spectrometry, susceptibility to various crosslinking enzymes and enzyme-linked immunosorbent assay inhibition. CONCLUSION: Theproposedmethodis veryuseful for the rapid preparationofBLGsuitable for studying antigenicandmolecular characteristics of this protein, aswell as the effect of food processing on these properties. The procedure requires only 1 day for the purification of about 300 mgof BLG from a single run using a small column (2.5 cmx20 cm) of diethylaminoethyl Sephadex and has potential for scaling up. (C) 2011 Society of Chemical Industry
PB  - Wiley-Blackwell, Malden
T2  - Journal of the Science of Food and Agriculture
T1  - One-step method for isolation and purification of native beta-lactoglobulin from bovine whey
VL  - 92
IS  - 7
SP  - 1432
EP  - 1440
DO  - 10.1002/jsfa.4722
ER  - 

@article{
author = "Stojadinović, Marija M. and Burazer, Lidija M. and Ercili-Cura, Dilek and Sancho, Ana and Buchert, Johanna and Ćirković-Veličković, Tanja and Stanić-Vučinić, Dragana",
year = "2012",
abstract = "BACKGROUND: The major whey protein beta-lactoglobulin (BLG) has been widely studied for its functional properties. The aim of this study was to develop an efficient, inexpensive and rapid one-step method for the isolation and purification of BLG while preserving its native structure. RESULTS: BLGwas purified fromdefattedwheyobtainedfromrawcow's milkbyanionexchangechromatography. Protein purity and identitywere determined using reverse phase high-performance liquid chromatography andmass spectrometry. Total BLG yield was 80% with protein purity from 97 to 99%. BLG isoforms A and B were separated into fractions of 91 and 99% purity respectively. The structure and native conformation of the isolated BLGwere compared with those of standard commercial BLG by circular dichroism spectrometry, susceptibility to various crosslinking enzymes and enzyme-linked immunosorbent assay inhibition. CONCLUSION: Theproposedmethodis veryuseful for the rapid preparationofBLGsuitable for studying antigenicandmolecular characteristics of this protein, aswell as the effect of food processing on these properties. The procedure requires only 1 day for the purification of about 300 mgof BLG from a single run using a small column (2.5 cmx20 cm) of diethylaminoethyl Sephadex and has potential for scaling up. (C) 2011 Society of Chemical Industry",
publisher = "Wiley-Blackwell, Malden",
journal = "Journal of the Science of Food and Agriculture",
title = "One-step method for isolation and purification of native beta-lactoglobulin from bovine whey",
volume = "92",
number = "7",
pages = "1432-1440",
doi = "10.1002/jsfa.4722"
}

Stojadinović, M. M., Burazer, L. M., Ercili-Cura, D., Sancho, A., Buchert, J., Ćirković-Veličković, T.,& Stanić-Vučinić, D.. (2012). One-step method for isolation and purification of native beta-lactoglobulin from bovine whey. in Journal of the Science of Food and Agriculture
Wiley-Blackwell, Malden., 92(7), 1432-1440.
https://doi.org/10.1002/jsfa.4722

Stojadinović MM, Burazer LM, Ercili-Cura D, Sancho A, Buchert J, Ćirković-Veličković T, Stanić-Vučinić D. One-step method for isolation and purification of native beta-lactoglobulin from bovine whey. in Journal of the Science of Food and Agriculture. 2012;92(7):1432-1440.
doi:10.1002/jsfa.4722 .

Stojadinović, Marija M., Burazer, Lidija M., Ercili-Cura, Dilek, Sancho, Ana, Buchert, Johanna, Ćirković-Veličković, Tanja, Stanić-Vučinić, Dragana, "One-step method for isolation and purification of native beta-lactoglobulin from bovine whey" in Journal of the Science of Food and Agriculture, 92, no. 7 (2012):1432-1440,
https://doi.org/10.1002/jsfa.4722 . .