Grozdanović, M.

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  • Grozdanović, M. (7)
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Author's Bibliography

Design and cloning strategies of recombinant allergens for diagnosis and specific immunotherapy

Grozdanović, M.; Popović, Milica M.; Gavrović-Jankulović, Marija

(2014)

TY  - CHAP
AU  - Grozdanović, M.
AU  - Popović, Milica M.
AU  - Gavrović-Jankulović, Marija
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/294
AB  - Persons suffering from allergy (Type I hypersensitivity) produce immunoglobulin E against innocuous environmental antigens such as pollen, house dust, animal dander, food proteins. Diagnosis of allergy is based on the measurement of allergen-specific IgE antibodies and on provocation with allergens in skin prick test. Diagnostic reagents based on allergen extracts obtained from natural biological material often reveal unbalanced allergen content, a presence of nonallergenic components, and are difficult to standardize. Replacement of allergen extracts with a set of individual allergens in component-resolved diagnostics is regarded as a tool for patient selection for specific immunotherapy. The concept of using single recombinant allergens to determine the patient's sensitization profile was coined "component-resolved diagnosis" and is regarded as a precondition for patient-tailored immunotherapy, i.e.,"component resolved immunotherapy"To provide reliable, more specific reagents for allergy diagnosis and therapy recombinant DNA technology has been widely applied. The majority of recombinant allergens by far, have been produced in the prokaryotic expression system; however eukaryotic cells (yeast, plant, insect and mammalian cells) were also exploited. To avoid side effects in the course of immunotherapy various approaches in design of hypoallergenic molecules have been performed. This chapter will give an overview of the concepts and approaches in producing recombinant allergens for component resolved diagnosis and component resolved immunotherapy. © 2014 by Nova Science Publishers, Inc. All rights reserved.
T2  - Advances in Genetics Research
T1  - Design and cloning strategies of recombinant allergens for diagnosis and specific immunotherapy
VL  - 11
SP  - 19
EP  - 46
UR  - https://hdl.handle.net/21.15107/rcub_cherry_294
ER  - 
@inbook{
author = "Grozdanović, M. and Popović, Milica M. and Gavrović-Jankulović, Marija",
year = "2014",
abstract = "Persons suffering from allergy (Type I hypersensitivity) produce immunoglobulin E against innocuous environmental antigens such as pollen, house dust, animal dander, food proteins. Diagnosis of allergy is based on the measurement of allergen-specific IgE antibodies and on provocation with allergens in skin prick test. Diagnostic reagents based on allergen extracts obtained from natural biological material often reveal unbalanced allergen content, a presence of nonallergenic components, and are difficult to standardize. Replacement of allergen extracts with a set of individual allergens in component-resolved diagnostics is regarded as a tool for patient selection for specific immunotherapy. The concept of using single recombinant allergens to determine the patient's sensitization profile was coined "component-resolved diagnosis" and is regarded as a precondition for patient-tailored immunotherapy, i.e.,"component resolved immunotherapy"To provide reliable, more specific reagents for allergy diagnosis and therapy recombinant DNA technology has been widely applied. The majority of recombinant allergens by far, have been produced in the prokaryotic expression system; however eukaryotic cells (yeast, plant, insect and mammalian cells) were also exploited. To avoid side effects in the course of immunotherapy various approaches in design of hypoallergenic molecules have been performed. This chapter will give an overview of the concepts and approaches in producing recombinant allergens for component resolved diagnosis and component resolved immunotherapy. © 2014 by Nova Science Publishers, Inc. All rights reserved.",
journal = "Advances in Genetics Research",
booktitle = "Design and cloning strategies of recombinant allergens for diagnosis and specific immunotherapy",
volume = "11",
pages = "19-46",
url = "https://hdl.handle.net/21.15107/rcub_cherry_294"
}
Grozdanović, M., Popović, M. M.,& Gavrović-Jankulović, M.. (2014). Design and cloning strategies of recombinant allergens for diagnosis and specific immunotherapy. in Advances in Genetics Research, 11, 19-46.
https://hdl.handle.net/21.15107/rcub_cherry_294
Grozdanović M, Popović MM, Gavrović-Jankulović M. Design and cloning strategies of recombinant allergens for diagnosis and specific immunotherapy. in Advances in Genetics Research. 2014;11:19-46.
https://hdl.handle.net/21.15107/rcub_cherry_294 .
Grozdanović, M., Popović, Milica M., Gavrović-Jankulović, Marija, "Design and cloning strategies of recombinant allergens for diagnosis and specific immunotherapy" in Advances in Genetics Research, 11 (2014):19-46,
https://hdl.handle.net/21.15107/rcub_cherry_294 .

Comparison of natural Bet v 1 with recombinant isoforms and mutants regarding allergenicity and biochemical structure

Petersen, A.; Grozdanović, M.; Pfuetzner, W.; Moebs, C.; Ernst, M.; Gavrović-Jankulović, Marija; Jappe, Uta

(Wiley-Blackwell, Hoboken, 2013)

TY  - CONF
AU  - Petersen, A.
AU  - Grozdanović, M.
AU  - Pfuetzner, W.
AU  - Moebs, C.
AU  - Ernst, M.
AU  - Gavrović-Jankulović, Marija
AU  - Jappe, Uta
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1410
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - Comparison of natural Bet v 1 with recombinant isoforms and mutants regarding allergenicity and biochemical structure
VL  - 68
SP  - 127
EP  - 128
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1410
ER  - 
@conference{
author = "Petersen, A. and Grozdanović, M. and Pfuetzner, W. and Moebs, C. and Ernst, M. and Gavrović-Jankulović, Marija and Jappe, Uta",
year = "2013",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Comparison of natural Bet v 1 with recombinant isoforms and mutants regarding allergenicity and biochemical structure",
volume = "68",
pages = "127-128",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1410"
}
Petersen, A., Grozdanović, M., Pfuetzner, W., Moebs, C., Ernst, M., Gavrović-Jankulović, M.,& Jappe, U.. (2013). Comparison of natural Bet v 1 with recombinant isoforms and mutants regarding allergenicity and biochemical structure. in Allergy
Wiley-Blackwell, Hoboken., 68, 127-128.
https://hdl.handle.net/21.15107/rcub_cherry_1410
Petersen A, Grozdanović M, Pfuetzner W, Moebs C, Ernst M, Gavrović-Jankulović M, Jappe U. Comparison of natural Bet v 1 with recombinant isoforms and mutants regarding allergenicity and biochemical structure. in Allergy. 2013;68:127-128.
https://hdl.handle.net/21.15107/rcub_cherry_1410 .
Petersen, A., Grozdanović, M., Pfuetzner, W., Moebs, C., Ernst, M., Gavrović-Jankulović, Marija, Jappe, Uta, "Comparison of natural Bet v 1 with recombinant isoforms and mutants regarding allergenicity and biochemical structure" in Allergy, 68 (2013):127-128,
https://hdl.handle.net/21.15107/rcub_cherry_1410 .

The effect of kiwifruit cysteine protease actinidin on the epithelial integrity and the expression of proinflammatory cytokines in T84 human colonic cells

Gavrović-Jankulović, Marija; Čavić, Milena; Grozdanović, M.; Cavic, D.; Jankovic, R.

(Wiley-Blackwell, Hoboken, 2012)

TY  - CONF
AU  - Gavrović-Jankulović, Marija
AU  - Čavić, Milena
AU  - Grozdanović, M.
AU  - Cavic, D.
AU  - Jankovic, R.
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1526
PB  - Wiley-Blackwell, Hoboken
C3  - FEBS Journal / Federation of European of Biochemical Societies
T1  - The effect of kiwifruit cysteine protease actinidin on the epithelial integrity and the expression of proinflammatory cytokines in T84 human colonic cells
VL  - 279
SP  - 304
EP  - 304
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1526
ER  - 
@conference{
author = "Gavrović-Jankulović, Marija and Čavić, Milena and Grozdanović, M. and Cavic, D. and Jankovic, R.",
year = "2012",
publisher = "Wiley-Blackwell, Hoboken",
journal = "FEBS Journal / Federation of European of Biochemical Societies",
title = "The effect of kiwifruit cysteine protease actinidin on the epithelial integrity and the expression of proinflammatory cytokines in T84 human colonic cells",
volume = "279",
pages = "304-304",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1526"
}
Gavrović-Jankulović, M., Čavić, M., Grozdanović, M., Cavic, D.,& Jankovic, R.. (2012). The effect of kiwifruit cysteine protease actinidin on the epithelial integrity and the expression of proinflammatory cytokines in T84 human colonic cells. in FEBS Journal / Federation of European of Biochemical Societies
Wiley-Blackwell, Hoboken., 279, 304-304.
https://hdl.handle.net/21.15107/rcub_cherry_1526
Gavrović-Jankulović M, Čavić M, Grozdanović M, Cavic D, Jankovic R. The effect of kiwifruit cysteine protease actinidin on the epithelial integrity and the expression of proinflammatory cytokines in T84 human colonic cells. in FEBS Journal / Federation of European of Biochemical Societies. 2012;279:304-304.
https://hdl.handle.net/21.15107/rcub_cherry_1526 .
Gavrović-Jankulović, Marija, Čavić, Milena, Grozdanović, M., Cavic, D., Jankovic, R., "The effect of kiwifruit cysteine protease actinidin on the epithelial integrity and the expression of proinflammatory cytokines in T84 human colonic cells" in FEBS Journal / Federation of European of Biochemical Societies, 279 (2012):304-304,
https://hdl.handle.net/21.15107/rcub_cherry_1526 .

Kiwifruit allergen actinidin disrupts the epithelial monolayer integrity of human intestinal T84 cells

Čavić, Milena; Bajić, A.; Grozdanović, M.; Cavic, D.; Jakovljević, Ksenija; Andjus, P.; Gavrović-Jankulović, Marija

(Wiley-Blackwell, Hoboken, 2012)

TY  - CONF
AU  - Čavić, Milena
AU  - Bajić, A.
AU  - Grozdanović, M.
AU  - Cavic, D.
AU  - Jakovljević, Ksenija
AU  - Andjus, P.
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1543
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - Kiwifruit allergen actinidin disrupts the epithelial monolayer integrity of human intestinal T84 cells
VL  - 67
SP  - 602
EP  - 603
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1543
ER  - 
@conference{
author = "Čavić, Milena and Bajić, A. and Grozdanović, M. and Cavic, D. and Jakovljević, Ksenija and Andjus, P. and Gavrović-Jankulović, Marija",
year = "2012",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Kiwifruit allergen actinidin disrupts the epithelial monolayer integrity of human intestinal T84 cells",
volume = "67",
pages = "602-603",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1543"
}
Čavić, M., Bajić, A., Grozdanović, M., Cavic, D., Jakovljević, K., Andjus, P.,& Gavrović-Jankulović, M.. (2012). Kiwifruit allergen actinidin disrupts the epithelial monolayer integrity of human intestinal T84 cells. in Allergy
Wiley-Blackwell, Hoboken., 67, 602-603.
https://hdl.handle.net/21.15107/rcub_cherry_1543
Čavić M, Bajić A, Grozdanović M, Cavic D, Jakovljević K, Andjus P, Gavrović-Jankulović M. Kiwifruit allergen actinidin disrupts the epithelial monolayer integrity of human intestinal T84 cells. in Allergy. 2012;67:602-603.
https://hdl.handle.net/21.15107/rcub_cherry_1543 .
Čavić, Milena, Bajić, A., Grozdanović, M., Cavic, D., Jakovljević, Ksenija, Andjus, P., Gavrović-Jankulović, Marija, "Kiwifruit allergen actinidin disrupts the epithelial monolayer integrity of human intestinal T84 cells" in Allergy, 67 (2012):602-603,
https://hdl.handle.net/21.15107/rcub_cherry_1543 .

Application of plant-derived food lectins in proteoglycomics and immunomodulation

Gavrović-Jankulović, Marija; Grozdanović, M.

(2011)

TY  - CHAP
AU  - Gavrović-Jankulović, Marija
AU  - Grozdanović, M.
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/124
AB  - Lectins are carbohydrate-binding proteins that discriminate sugars based on subtle difference in structure. The biological role of intracellular lectins has not been completely elucidated yet; however, it is known that lectins exposed on the cell membrane are involved in various biological processes: cell-to-cell communication, cell migration, and the lectin pathway of complement activation. The functional significance of carbohydrates, particularly those attached to proteins, has been determined in health investigations and imposed structural investigations on lectins, as well as by their application in research and medicine. Considerable knowledge gained on the structure and carbohydrate specificity of plant lectins established them as a good tool for profiling carbohydrate structures present on cell-surfaces. A lectin microarray approach rapidly evaluates the carbohydrate composition on the surface of intact cells, and provides means to elucidate the dynamic role of sugars in biological systems. The importance of protein glycosylation has been implicated in designing novel therapeutic approaches in certain diseases. Due to their unique carbohydrate specificity, besides being applicable in deciphering the structural diversity of carbohydrates, plant lectins exhibit modulatory potential on the immune system. Certain plant lectins are prone to induce immune response upon oral feeding. Therefore, a search for novel immunostimulatory molecules and adjuvants, in order to enhance or to direct an appropriate immune response against target immunogens, has been a major and recurrent issue in vaccine development.
T2  - Handbook of Nutritional Biochemistry: Genomics, Metabolomics, and Food Supply
T1  - Application of plant-derived food lectins in proteoglycomics and immunomodulation
SP  - 405
EP  - 423
UR  - https://hdl.handle.net/21.15107/rcub_cherry_124
ER  - 
@inbook{
author = "Gavrović-Jankulović, Marija and Grozdanović, M.",
year = "2011",
abstract = "Lectins are carbohydrate-binding proteins that discriminate sugars based on subtle difference in structure. The biological role of intracellular lectins has not been completely elucidated yet; however, it is known that lectins exposed on the cell membrane are involved in various biological processes: cell-to-cell communication, cell migration, and the lectin pathway of complement activation. The functional significance of carbohydrates, particularly those attached to proteins, has been determined in health investigations and imposed structural investigations on lectins, as well as by their application in research and medicine. Considerable knowledge gained on the structure and carbohydrate specificity of plant lectins established them as a good tool for profiling carbohydrate structures present on cell-surfaces. A lectin microarray approach rapidly evaluates the carbohydrate composition on the surface of intact cells, and provides means to elucidate the dynamic role of sugars in biological systems. The importance of protein glycosylation has been implicated in designing novel therapeutic approaches in certain diseases. Due to their unique carbohydrate specificity, besides being applicable in deciphering the structural diversity of carbohydrates, plant lectins exhibit modulatory potential on the immune system. Certain plant lectins are prone to induce immune response upon oral feeding. Therefore, a search for novel immunostimulatory molecules and adjuvants, in order to enhance or to direct an appropriate immune response against target immunogens, has been a major and recurrent issue in vaccine development.",
journal = "Handbook of Nutritional Biochemistry: Genomics, Metabolomics, and Food Supply",
booktitle = "Application of plant-derived food lectins in proteoglycomics and immunomodulation",
pages = "405-423",
url = "https://hdl.handle.net/21.15107/rcub_cherry_124"
}
Gavrović-Jankulović, M.,& Grozdanović, M.. (2011). Application of plant-derived food lectins in proteoglycomics and immunomodulation. in Handbook of Nutritional Biochemistry: Genomics, Metabolomics, and Food Supply, 405-423.
https://hdl.handle.net/21.15107/rcub_cherry_124
Gavrović-Jankulović M, Grozdanović M. Application of plant-derived food lectins in proteoglycomics and immunomodulation. in Handbook of Nutritional Biochemistry: Genomics, Metabolomics, and Food Supply. 2011;:405-423.
https://hdl.handle.net/21.15107/rcub_cherry_124 .
Gavrović-Jankulović, Marija, Grozdanović, M., "Application of plant-derived food lectins in proteoglycomics and immunomodulation" in Handbook of Nutritional Biochemistry: Genomics, Metabolomics, and Food Supply (2011):405-423,
https://hdl.handle.net/21.15107/rcub_cherry_124 .
1

Proenzyme and active actinidin from kiwifruit differs in IgE reactivity

Grozdanović, M.; Petersen, A.; Lindner, B.; Atanasković-Marković, Marina; Polović, Natalija; Gavrović-Jankulović, Marija

(Wiley-Blackwell, Hoboken, 2011)

TY  - CONF
AU  - Grozdanović, M.
AU  - Petersen, A.
AU  - Lindner, B.
AU  - Atanasković-Marković, Marina
AU  - Polović, Natalija
AU  - Gavrović-Jankulović, Marija
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1591
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - Proenzyme and active actinidin from kiwifruit differs in IgE reactivity
VL  - 66
SP  - 531
EP  - 531
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1591
ER  - 
@conference{
author = "Grozdanović, M. and Petersen, A. and Lindner, B. and Atanasković-Marković, Marina and Polović, Natalija and Gavrović-Jankulović, Marija",
year = "2011",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Proenzyme and active actinidin from kiwifruit differs in IgE reactivity",
volume = "66",
pages = "531-531",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1591"
}
Grozdanović, M., Petersen, A., Lindner, B., Atanasković-Marković, M., Polović, N.,& Gavrović-Jankulović, M.. (2011). Proenzyme and active actinidin from kiwifruit differs in IgE reactivity. in Allergy
Wiley-Blackwell, Hoboken., 66, 531-531.
https://hdl.handle.net/21.15107/rcub_cherry_1591
Grozdanović M, Petersen A, Lindner B, Atanasković-Marković M, Polović N, Gavrović-Jankulović M. Proenzyme and active actinidin from kiwifruit differs in IgE reactivity. in Allergy. 2011;66:531-531.
https://hdl.handle.net/21.15107/rcub_cherry_1591 .
Grozdanović, M., Petersen, A., Lindner, B., Atanasković-Marković, Marina, Polović, Natalija, Gavrović-Jankulović, Marija, "Proenzyme and active actinidin from kiwifruit differs in IgE reactivity" in Allergy, 66 (2011):531-531,
https://hdl.handle.net/21.15107/rcub_cherry_1591 .

Characterisation of a thaumatin-like homologue from birch (Betula verrucosa) pollen

Grozdanović, M.; Burazer, Lidija M.; Vučković, O.; Ćirković-Veličković, Tanja; Jankov, Ratko M.; Gavrović-Jankulović, Marija

(Wiley-Blackwell Publishing, Inc, Malden, 2009)

TY  - CONF
AU  - Grozdanović, M.
AU  - Burazer, Lidija M.
AU  - Vučković, O.
AU  - Ćirković-Veličković, Tanja
AU  - Jankov, Ratko M.
AU  - Gavrović-Jankulović, Marija
PY  - 2009
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/984
PB  - Wiley-Blackwell Publishing, Inc, Malden
C3  - Allergy
T1  - Characterisation of a thaumatin-like homologue from birch (Betula verrucosa) pollen
VL  - 64
SP  - 249
EP  - 249
UR  - https://hdl.handle.net/21.15107/rcub_cherry_984
ER  - 
@conference{
author = "Grozdanović, M. and Burazer, Lidija M. and Vučković, O. and Ćirković-Veličković, Tanja and Jankov, Ratko M. and Gavrović-Jankulović, Marija",
year = "2009",
publisher = "Wiley-Blackwell Publishing, Inc, Malden",
journal = "Allergy",
title = "Characterisation of a thaumatin-like homologue from birch (Betula verrucosa) pollen",
volume = "64",
pages = "249-249",
url = "https://hdl.handle.net/21.15107/rcub_cherry_984"
}
Grozdanović, M., Burazer, L. M., Vučković, O., Ćirković-Veličković, T., Jankov, R. M.,& Gavrović-Jankulović, M.. (2009). Characterisation of a thaumatin-like homologue from birch (Betula verrucosa) pollen. in Allergy
Wiley-Blackwell Publishing, Inc, Malden., 64, 249-249.
https://hdl.handle.net/21.15107/rcub_cherry_984
Grozdanović M, Burazer LM, Vučković O, Ćirković-Veličković T, Jankov RM, Gavrović-Jankulović M. Characterisation of a thaumatin-like homologue from birch (Betula verrucosa) pollen. in Allergy. 2009;64:249-249.
https://hdl.handle.net/21.15107/rcub_cherry_984 .
Grozdanović, M., Burazer, Lidija M., Vučković, O., Ćirković-Veličković, Tanja, Jankov, Ratko M., Gavrović-Jankulović, Marija, "Characterisation of a thaumatin-like homologue from birch (Betula verrucosa) pollen" in Allergy, 64 (2009):249-249,
https://hdl.handle.net/21.15107/rcub_cherry_984 .