Gligorijević, Nikola

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orcid::0000-0002-8691-2486
  • Gligorijević, Nikola (12)
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Author's Bibliography

Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation

Gligorijević, Nikola; Radomirović, Mirjana Ž.; Rajković, Andreja; Nedić, Olgica; Ćirković-Veličković, Tanja

(Multidisciplinary Digital Publishing Institute (MDPI), 2020)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Radomirović, Mirjana Ž.
AU  - Rajković, Andreja
AU  - Nedić, Olgica
AU  - Ćirković-Veličković, Tanja
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4235
AB  - The French paradox describes a lower incidence of cardiovascular problems despite a high intake of saturated fats. This phenomenon was associated with higher consumption of red wine, as it was later discovered that the presence of antioxidants, including resveratrol, have beneficial effects. We hypothesized that resveratrol may have a more direct role in protection from harmful oxidation, presumably through binding to important proteins of the blood coagulation process. Spectrofluorimetry demonstrated that resveratrol is capable of binding to fibrinogen, the main protein in the coagulation process, which is also important as a food additive. Various spectroscopic methods determined that binding does not cause fibrinogen unfolding or destabilization since protein melting temperature remains unchanged. A mutually protective effect against the free radical-induced oxidation of polyphenol and fibrinogen was found. The presence of fibrinogen caused only a negligible masking effect of the antioxidative abilities of resveratrol, measured by a reduction of hexacyanoferrate (III), while greatly increasing its solubility in an aqueous environment, thus increasing its potential bioavailability. Due to its interaction with fibrinogen, resveratrol may serve as an antioxidant at the site of injury. The antioxidative effect of resveratrol may also protect and thus keep the desired characteristics of fibrinogen during the application of this protein as a food additive.
PB  - Multidisciplinary Digital Publishing Institute (MDPI)
T2  - Foods
T1  - Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation
VL  - 9
IS  - 6
SP  - 780
DO  - 10.3390/foods9060780
ER  - 
@article{
author = "Gligorijević, Nikola and Radomirović, Mirjana Ž. and Rajković, Andreja and Nedić, Olgica and Ćirković-Veličković, Tanja",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/4235",
abstract = "The French paradox describes a lower incidence of cardiovascular problems despite a high intake of saturated fats. This phenomenon was associated with higher consumption of red wine, as it was later discovered that the presence of antioxidants, including resveratrol, have beneficial effects. We hypothesized that resveratrol may have a more direct role in protection from harmful oxidation, presumably through binding to important proteins of the blood coagulation process. Spectrofluorimetry demonstrated that resveratrol is capable of binding to fibrinogen, the main protein in the coagulation process, which is also important as a food additive. Various spectroscopic methods determined that binding does not cause fibrinogen unfolding or destabilization since protein melting temperature remains unchanged. A mutually protective effect against the free radical-induced oxidation of polyphenol and fibrinogen was found. The presence of fibrinogen caused only a negligible masking effect of the antioxidative abilities of resveratrol, measured by a reduction of hexacyanoferrate (III), while greatly increasing its solubility in an aqueous environment, thus increasing its potential bioavailability. Due to its interaction with fibrinogen, resveratrol may serve as an antioxidant at the site of injury. The antioxidative effect of resveratrol may also protect and thus keep the desired characteristics of fibrinogen during the application of this protein as a food additive.",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
journal = "Foods",
title = "Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation",
volume = "9",
number = "6",
pages = "780",
doi = "10.3390/foods9060780"
}
Gligorijević, N., Radomirović, M. Ž., Rajković, A., Nedić, O.,& Ćirković-Veličković, T. (2020). Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation.
Foods
Multidisciplinary Digital Publishing Institute (MDPI)., 9(6), 780.
https://doi.org/10.3390/foods9060780
Gligorijević N, Radomirović MŽ, Rajković A, Nedić O, Ćirković-Veličković T. Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation. Foods. 2020;9(6):780
Gligorijević Nikola, Radomirović Mirjana Ž., Rajković Andreja, Nedić Olgica, Ćirković-Veličković Tanja, "Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation" Foods, 9, no. 6 (2020):780,
https://doi.org/10.3390/foods9060780 .
2
1
1

Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation

Gligorijević, Nikola; Vasović, Tamara; Lević, Steva M.; Miljević, Čedo; Nedić, Olgica; Nikolić, Milan

(Elsevier, 2020)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Vasović, Tamara
AU  - Lević, Steva M.
AU  - Miljević, Čedo
AU  - Nedić, Olgica
AU  - Nikolić, Milan
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3896
AB  - Clozapine is an atypical antipsychotic used for the treatment of schizophrenia. The prescribed target daily doses may reach 900 mg. Literature studies report a connection between clozapine usage and thrombosis development. Our in vitro study aimed to provide insight into molecular bases of this observation, investigating clozapine binding to fibrinogen, the main plasma protein involved in hemostasis. Fibrinogen/clozapine interaction was confirmed by protein fluorescence quenching, with an affinity constant of 1.7 × 105 M−1. Direct interactions did not affect the structure of fibrinogen, nor fibrinogen melting temperature. Clozapine binding affected fibrin formation by reducing coagulation speed and thickness of fibrin fibers suggesting that in the presence of clozapine, fibrinogen may acquire thrombogenic characteristics. Although no difference in fibrin gel porosity was detected, other factors present in the blood may act synergistically with altered fibrin formation to modify fibrin clot, thus increasing the risk for development of thrombosis in patients on clozapine treatment. ORAC and HORAC assays showed that clozapine reduced free radical-induced oxidation of fibrinogen. All observed effects of clozapine on fibrinogen are dose-dependent, with the effect on fibrin formation being more pronounced.
PB  - Elsevier
T2  - International Journal of Biological Macromolecules
T1  - Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation
VL  - 154
SP  - 142
EP  - 149
DO  - 10.1016/j.ijbiomac.2020.03.119
ER  - 
@article{
author = "Gligorijević, Nikola and Vasović, Tamara and Lević, Steva M. and Miljević, Čedo and Nedić, Olgica and Nikolić, Milan",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3896",
abstract = "Clozapine is an atypical antipsychotic used for the treatment of schizophrenia. The prescribed target daily doses may reach 900 mg. Literature studies report a connection between clozapine usage and thrombosis development. Our in vitro study aimed to provide insight into molecular bases of this observation, investigating clozapine binding to fibrinogen, the main plasma protein involved in hemostasis. Fibrinogen/clozapine interaction was confirmed by protein fluorescence quenching, with an affinity constant of 1.7 × 105 M−1. Direct interactions did not affect the structure of fibrinogen, nor fibrinogen melting temperature. Clozapine binding affected fibrin formation by reducing coagulation speed and thickness of fibrin fibers suggesting that in the presence of clozapine, fibrinogen may acquire thrombogenic characteristics. Although no difference in fibrin gel porosity was detected, other factors present in the blood may act synergistically with altered fibrin formation to modify fibrin clot, thus increasing the risk for development of thrombosis in patients on clozapine treatment. ORAC and HORAC assays showed that clozapine reduced free radical-induced oxidation of fibrinogen. All observed effects of clozapine on fibrinogen are dose-dependent, with the effect on fibrin formation being more pronounced.",
publisher = "Elsevier",
journal = "International Journal of Biological Macromolecules",
title = "Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation",
volume = "154",
pages = "142-149",
doi = "10.1016/j.ijbiomac.2020.03.119"
}
Gligorijević, N., Vasović, T., Lević, S. M., Miljević, Č., Nedić, O.,& Nikolić, M. (2020). Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation.
International Journal of Biological Macromolecules
Elsevier., 154, 142-149.
https://doi.org/10.1016/j.ijbiomac.2020.03.119
Gligorijević N, Vasović T, Lević SM, Miljević Č, Nedić O, Nikolić M. Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation. International Journal of Biological Macromolecules. 2020;154:142-149
Gligorijević Nikola, Vasović Tamara, Lević Steva M., Miljević Čedo, Nedić Olgica, Nikolić Milan, "Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation" International Journal of Biological Macromolecules, 154 (2020):142-149,
https://doi.org/10.1016/j.ijbiomac.2020.03.119 .
2
1
3

Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation

Gligorijević, Nikola; Vasović, Tamara; Lević, Steva M.; Miljević, Čedo; Nedić, Olgica; Nikolić, Milan

(Elsevier, 2020)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Vasović, Tamara
AU  - Lević, Steva M.
AU  - Miljević, Čedo
AU  - Nedić, Olgica
AU  - Nikolić, Milan
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3886
AB  - Clozapine is an atypical antipsychotic used for the treatment of schizophrenia. The prescribed target daily doses may reach 900 mg. Literature studies report a connection between clozapine usage and thrombosis development. Our in vitro study aimed to provide insight into molecular bases of this observation, investigating clozapine binding to fibrinogen, the main plasma protein involved in hemostasis. Fibrinogen/clozapine interaction was confirmed by protein fluorescence quenching, with an affinity constant of 1.7 × 105 M−1. Direct interactions did not affect the structure of fibrinogen, nor fibrinogen melting temperature. Clozapine binding affected fibrin formation by reducing coagulation speed and thickness of fibrin fibers suggesting that in the presence of clozapine, fibrinogen may acquire thrombogenic characteristics. Although no difference in fibrin gel porosity was detected, other factors present in the blood may act synergistically with altered fibrin formation to modify fibrin clot, thus increasing the risk for development of thrombosis in patients on clozapine treatment. ORAC and HORAC assays showed that clozapine reduced free radical-induced oxidation of fibrinogen. All observed effects of clozapine on fibrinogen are dose-dependent, with the effect on fibrin formation being more pronounced.
PB  - Elsevier
T2  - International Journal of Biological Macromolecules
T1  - Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation
VL  - 154
SP  - 142
EP  - 149
DO  - 10.1016/j.ijbiomac.2020.03.119
ER  - 
@article{
author = "Gligorijević, Nikola and Vasović, Tamara and Lević, Steva M. and Miljević, Čedo and Nedić, Olgica and Nikolić, Milan",
year = "2020",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3886",
abstract = "Clozapine is an atypical antipsychotic used for the treatment of schizophrenia. The prescribed target daily doses may reach 900 mg. Literature studies report a connection between clozapine usage and thrombosis development. Our in vitro study aimed to provide insight into molecular bases of this observation, investigating clozapine binding to fibrinogen, the main plasma protein involved in hemostasis. Fibrinogen/clozapine interaction was confirmed by protein fluorescence quenching, with an affinity constant of 1.7 × 105 M−1. Direct interactions did not affect the structure of fibrinogen, nor fibrinogen melting temperature. Clozapine binding affected fibrin formation by reducing coagulation speed and thickness of fibrin fibers suggesting that in the presence of clozapine, fibrinogen may acquire thrombogenic characteristics. Although no difference in fibrin gel porosity was detected, other factors present in the blood may act synergistically with altered fibrin formation to modify fibrin clot, thus increasing the risk for development of thrombosis in patients on clozapine treatment. ORAC and HORAC assays showed that clozapine reduced free radical-induced oxidation of fibrinogen. All observed effects of clozapine on fibrinogen are dose-dependent, with the effect on fibrin formation being more pronounced.",
publisher = "Elsevier",
journal = "International Journal of Biological Macromolecules",
title = "Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation",
volume = "154",
pages = "142-149",
doi = "10.1016/j.ijbiomac.2020.03.119"
}
Gligorijević, N., Vasović, T., Lević, S. M., Miljević, Č., Nedić, O.,& Nikolić, M. (2020). Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation.
International Journal of Biological Macromolecules
Elsevier., 154, 142-149.
https://doi.org/10.1016/j.ijbiomac.2020.03.119
Gligorijević N, Vasović T, Lević SM, Miljević Č, Nedić O, Nikolić M. Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation. International Journal of Biological Macromolecules. 2020;154:142-149
Gligorijević Nikola, Vasović Tamara, Lević Steva M., Miljević Čedo, Nedić Olgica, Nikolić Milan, "Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation" International Journal of Biological Macromolecules, 154 (2020):142-149,
https://doi.org/10.1016/j.ijbiomac.2020.03.119 .
2
1
3

Characterisation and the effects of bilirubin binding to human fibrinogen

Gligorijević, Nikola; Minić, Simeon L.; Robajac, Dragana B.; Nikolić, Milan; Ćirković-Veličković, Tanja; Nedić, Olgica

(2019)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Minić, Simeon L.
AU  - Robajac, Dragana B.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
AU  - Nedić, Olgica
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2824
AB  - Fibrinogen, a protein involved in blood coagulation, is very susceptible to oxidation. Oxidation alters its function and usually makes it more thrombogenic. Bilirubin, an end-product of the haem degradation in vertebrates, is known for its antioxidant properties. The present paper describes interaction between fibrinogen and bilirubin, and the influence of bilirubin on the formation of fibrin and protection against oxidation. The binding constant of 4.5 × 104 M−1 was determined for the fibrinogen/bilirubin complex at 37 °C. There is no change in secondary and tertiary structure of fibrinogen or its thermal stability upon bilirubin binding. The binding site of fibrinogen is not stereospecific for bilirubin and is able to accommodate both bilirubin conformers. A change in absorption maximum of bilirubin occurs upon its interaction with fibrinogen, suggesting an alteration in the conformation of bilirubin to the more cyclic one. Bilirubin exerts antioxidant effect on fibrinogen, preventing its carbonylation and aggregation. The presence of bilirubin induces the formation of fibrin with thicker fibres, as assessed by the coagulation assay. Fibrinogen and bilirubin interact at physiological concentrations, bilirubin may act as an antioxidant for fibrinogen and may modulate an important event in haemostasis, which altogether suggests possible physiological relevance of this interaction.
T2  - International Journal of Biological Macromolecules
T1  - Characterisation and the effects of bilirubin binding to human fibrinogen
VL  - 128
SP  - 74
EP  - 79
DO  - 10.1016/j.ijbiomac.2019.01.124
ER  - 
@article{
author = "Gligorijević, Nikola and Minić, Simeon L. and Robajac, Dragana B. and Nikolić, Milan and Ćirković-Veličković, Tanja and Nedić, Olgica",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2824",
abstract = "Fibrinogen, a protein involved in blood coagulation, is very susceptible to oxidation. Oxidation alters its function and usually makes it more thrombogenic. Bilirubin, an end-product of the haem degradation in vertebrates, is known for its antioxidant properties. The present paper describes interaction between fibrinogen and bilirubin, and the influence of bilirubin on the formation of fibrin and protection against oxidation. The binding constant of 4.5 × 104 M−1 was determined for the fibrinogen/bilirubin complex at 37 °C. There is no change in secondary and tertiary structure of fibrinogen or its thermal stability upon bilirubin binding. The binding site of fibrinogen is not stereospecific for bilirubin and is able to accommodate both bilirubin conformers. A change in absorption maximum of bilirubin occurs upon its interaction with fibrinogen, suggesting an alteration in the conformation of bilirubin to the more cyclic one. Bilirubin exerts antioxidant effect on fibrinogen, preventing its carbonylation and aggregation. The presence of bilirubin induces the formation of fibrin with thicker fibres, as assessed by the coagulation assay. Fibrinogen and bilirubin interact at physiological concentrations, bilirubin may act as an antioxidant for fibrinogen and may modulate an important event in haemostasis, which altogether suggests possible physiological relevance of this interaction.",
journal = "International Journal of Biological Macromolecules",
title = "Characterisation and the effects of bilirubin binding to human fibrinogen",
volume = "128",
pages = "74-79",
doi = "10.1016/j.ijbiomac.2019.01.124"
}
Gligorijević, N., Minić, S. L., Robajac, D. B., Nikolić, M., Ćirković-Veličković, T.,& Nedić, O. (2019). Characterisation and the effects of bilirubin binding to human fibrinogen.
International Journal of Biological Macromolecules, 128, 74-79.
https://doi.org/10.1016/j.ijbiomac.2019.01.124
Gligorijević N, Minić SL, Robajac DB, Nikolić M, Ćirković-Veličković T, Nedić O. Characterisation and the effects of bilirubin binding to human fibrinogen. International Journal of Biological Macromolecules. 2019;128:74-79
Gligorijević Nikola, Minić Simeon L., Robajac Dragana B., Nikolić Milan, Ćirković-Veličković Tanja, Nedić Olgica, "Characterisation and the effects of bilirubin binding to human fibrinogen" International Journal of Biological Macromolecules, 128 (2019):74-79,
https://doi.org/10.1016/j.ijbiomac.2019.01.124 .
6
5
6

Characterisation and the effects of bilirubin binding to human fibrinogen

Gligorijević, Nikola; Minić, Simeon L.; Robajac, Dragana B.; Nikolić, Milan; Ćirković-Veličković, Tanja; Nedić, Olgica

(2019)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Minić, Simeon L.
AU  - Robajac, Dragana B.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
AU  - Nedić, Olgica
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2825
AB  - Fibrinogen, a protein involved in blood coagulation, is very susceptible to oxidation. Oxidation alters its function and usually makes it more thrombogenic. Bilirubin, an end-product of the haem degradation in vertebrates, is known for its antioxidant properties. The present paper describes interaction between fibrinogen and bilirubin, and the influence of bilirubin on the formation of fibrin and protection against oxidation. The binding constant of 4.5 × 104 M−1 was determined for the fibrinogen/bilirubin complex at 37 °C. There is no change in secondary and tertiary structure of fibrinogen or its thermal stability upon bilirubin binding. The binding site of fibrinogen is not stereospecific for bilirubin and is able to accommodate both bilirubin conformers. A change in absorption maximum of bilirubin occurs upon its interaction with fibrinogen, suggesting an alteration in the conformation of bilirubin to the more cyclic one. Bilirubin exerts antioxidant effect on fibrinogen, preventing its carbonylation and aggregation. The presence of bilirubin induces the formation of fibrin with thicker fibres, as assessed by the coagulation assay. Fibrinogen and bilirubin interact at physiological concentrations, bilirubin may act as an antioxidant for fibrinogen and may modulate an important event in haemostasis, which altogether suggests possible physiological relevance of this interaction.
T2  - International Journal of Biological Macromolecules
T1  - Characterisation and the effects of bilirubin binding to human fibrinogen
VL  - 128
SP  - 74
EP  - 79
DO  - 10.1016/j.ijbiomac.2019.01.124
ER  - 
@article{
author = "Gligorijević, Nikola and Minić, Simeon L. and Robajac, Dragana B. and Nikolić, Milan and Ćirković-Veličković, Tanja and Nedić, Olgica",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2825",
abstract = "Fibrinogen, a protein involved in blood coagulation, is very susceptible to oxidation. Oxidation alters its function and usually makes it more thrombogenic. Bilirubin, an end-product of the haem degradation in vertebrates, is known for its antioxidant properties. The present paper describes interaction between fibrinogen and bilirubin, and the influence of bilirubin on the formation of fibrin and protection against oxidation. The binding constant of 4.5 × 104 M−1 was determined for the fibrinogen/bilirubin complex at 37 °C. There is no change in secondary and tertiary structure of fibrinogen or its thermal stability upon bilirubin binding. The binding site of fibrinogen is not stereospecific for bilirubin and is able to accommodate both bilirubin conformers. A change in absorption maximum of bilirubin occurs upon its interaction with fibrinogen, suggesting an alteration in the conformation of bilirubin to the more cyclic one. Bilirubin exerts antioxidant effect on fibrinogen, preventing its carbonylation and aggregation. The presence of bilirubin induces the formation of fibrin with thicker fibres, as assessed by the coagulation assay. Fibrinogen and bilirubin interact at physiological concentrations, bilirubin may act as an antioxidant for fibrinogen and may modulate an important event in haemostasis, which altogether suggests possible physiological relevance of this interaction.",
journal = "International Journal of Biological Macromolecules",
title = "Characterisation and the effects of bilirubin binding to human fibrinogen",
volume = "128",
pages = "74-79",
doi = "10.1016/j.ijbiomac.2019.01.124"
}
Gligorijević, N., Minić, S. L., Robajac, D. B., Nikolić, M., Ćirković-Veličković, T.,& Nedić, O. (2019). Characterisation and the effects of bilirubin binding to human fibrinogen.
International Journal of Biological Macromolecules, 128, 74-79.
https://doi.org/10.1016/j.ijbiomac.2019.01.124
Gligorijević N, Minić SL, Robajac DB, Nikolić M, Ćirković-Veličković T, Nedić O. Characterisation and the effects of bilirubin binding to human fibrinogen. International Journal of Biological Macromolecules. 2019;128:74-79
Gligorijević Nikola, Minić Simeon L., Robajac Dragana B., Nikolić Milan, Ćirković-Veličković Tanja, Nedić Olgica, "Characterisation and the effects of bilirubin binding to human fibrinogen" International Journal of Biological Macromolecules, 128 (2019):74-79,
https://doi.org/10.1016/j.ijbiomac.2019.01.124 .
6
5
6

Supplementary data for the article: Gligorijević, N.; Minić, S. L.; Robajac, D. B.; Nikolić, M.; Ćirković-Veličković, T.; Nedić, O. Characterisation and the Effects of Bilirubin Binding to Human Fibrinogen. International Journal of Biological Macromolecules 2019, 128, 74–79. https://doi.org/10.1016/j.ijbiomac.2019.01.124

Gligorijević, Nikola; Minić, Simeon L.; Robajac, Dragana B.; Nikolić, Milan; Ćirković-Veličković, Tanja; Nedić, Olgica

(2019)

TY  - BOOK
AU  - Gligorijević, Nikola
AU  - Minić, Simeon L.
AU  - Robajac, Dragana B.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
AU  - Nedić, Olgica
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2937
T2  - International Journal of Biological Macromolecules
T1  - Supplementary data for the article: Gligorijević, N.; Minić, S. L.; Robajac, D. B.; Nikolić, M.; Ćirković-Veličković, T.; Nedić, O. Characterisation and the Effects of Bilirubin Binding to Human Fibrinogen. International Journal of Biological Macromolecules 2019, 128, 74–79. https://doi.org/10.1016/j.ijbiomac.2019.01.124
ER  - 
@book{
author = "Gligorijević, Nikola and Minić, Simeon L. and Robajac, Dragana B. and Nikolić, Milan and Ćirković-Veličković, Tanja and Nedić, Olgica",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2937",
journal = "International Journal of Biological Macromolecules",
title = "Supplementary data for the article: Gligorijević, N.; Minić, S. L.; Robajac, D. B.; Nikolić, M.; Ćirković-Veličković, T.; Nedić, O. Characterisation and the Effects of Bilirubin Binding to Human Fibrinogen. International Journal of Biological Macromolecules 2019, 128, 74–79. https://doi.org/10.1016/j.ijbiomac.2019.01.124"
}
Gligorijević, N., Minić, S. L., Robajac, D. B., Nikolić, M., Ćirković-Veličković, T.,& Nedić, O. (2019). Supplementary data for the article: Gligorijević, N.; Minić, S. L.; Robajac, D. B.; Nikolić, M.; Ćirković-Veličković, T.; Nedić, O. Characterisation and the Effects of Bilirubin Binding to Human Fibrinogen. International Journal of Biological Macromolecules 2019, 128, 74–79. https://doi.org/10.1016/j.ijbiomac.2019.01.124.
International Journal of Biological Macromolecules.
Gligorijević N, Minić SL, Robajac DB, Nikolić M, Ćirković-Veličković T, Nedić O. Supplementary data for the article: Gligorijević, N.; Minić, S. L.; Robajac, D. B.; Nikolić, M.; Ćirković-Veličković, T.; Nedić, O. Characterisation and the Effects of Bilirubin Binding to Human Fibrinogen. International Journal of Biological Macromolecules 2019, 128, 74–79. https://doi.org/10.1016/j.ijbiomac.2019.01.124. International Journal of Biological Macromolecules. 2019;
Gligorijević Nikola, Minić Simeon L., Robajac Dragana B., Nikolić Milan, Ćirković-Veličković Tanja, Nedić Olgica, "Supplementary data for the article: Gligorijević, N.; Minić, S. L.; Robajac, D. B.; Nikolić, M.; Ćirković-Veličković, T.; Nedić, O. Characterisation and the Effects of Bilirubin Binding to Human Fibrinogen. International Journal of Biological Macromolecules 2019, 128, 74–79. https://doi.org/10.1016/j.ijbiomac.2019.01.124" International Journal of Biological Macromolecules (2019)

Uticaj posttranslacionih modifikacija fibrinogena na njegovu reaktivnost i funkciju

Gligorijević, Nikola

(Универзитет у Београду, Хемијски факултет, 2018)

TY  - BOOK
AU  - Gligorijević, Nikola
PY  - 2018
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=6386
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:19076/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=50770447
UR  - http://nardus.mpn.gov.rs/123456789/10480
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3162
AB  - Fibrinogen je vaţan protein primarne i glavni protein sekundarne hemostaze. Nakon povrede, on se dejstvom trombina pretvara u nerastvorni fibrin koji se dalje umreţava, pri čemu nastaje fibrinska mreţa koja ojačava krvni ugrušak na mestu povrede. Da bi fibrinogen obavljao svoju biohemijsku ulogu, bitni su odreĎeni faktori, u koje spadaju njegove posttranslacione modifikacije i interakcije sa drugim proteinima. Posttranslacione modifikacije fibrinogena utiču na njegovu strukturu, strukturu fibrina i interakcije sa drugim proteinima. Fibrin nije pasivna mreţa koja samo daje potporu krvnom ugrušku, već je aktivna struktura koja reguliše svoju sintezu i razgradnju interakcijom sa brojnim proteinima. Zato je vaţno otkriti nove proteine koji sa njim interaguju, a koji imaju uticaj na proces zarastanja povreda.U okviru ove diseretacije, optimizovana je procedura za izolovanje i analizu fibrinogena. Upotrebom dvostrukog taloţenja etanolom dobijen je visoko prečišćen fibrinogen, pogodan za dalju karakterizaciju.Kako je poznato da fibrinogen interaguje sa IGFBP-3 proteinom, postavilo se pitanje da li još neki protein iz grupe vezujućih proteina za IGF, pri fiziološkim uslovima, ima tu sposobnost. Upotrebom većeg broja afinitetnih metoda je pokazano da IGFBP-1 interaguje sa fibrinogenom i da je to opšta fiziološka pojava. Značaj ove interakcije treba sagledavati imajući u vidu da i IGFBP-1 podstiče zarastanje tkivnih povreda, samostalno i kao transporter IGF molekula.Brojne patologije pri kojima se javljaju i koagulopatije, kao što su dijabetes melitus tipa 2 i ciroza jetre, karakteriše izmenjena koncentracija i struktura fibrinogena, što za posledicu ima stvaranje abnormalnog, trombogenog fibrina. Detaljno izučavanje pojedinačnih proteina uključenih u koagulopatiju moţe dati bliţu sliku mehanizma odgovornog za ovu pojavu. Sa druge strane, promene na nivou posttranslacionih modifikacija i strukture fibrinogena sa starenjem mogu doprineti boljem razumevanju prisustva ili odsustva odreĎenih patologija kod starijih ljudi.Struktura fibrinogena sa starenjem se menja. Primenom lektinskog eseja uočeno je povećanje visoko-manoznih i/ili hibridnih N-glikana, tri-/tertaantenarnih kompleksnih glikana sa većim sadrţajem Gal i GlcNAc. Spektrofluorimetrijska analiza je pokazala da kod zdravih ljudi preko 60 godina starosti, fibrinogen ima kompaktniju tercijarnustrukturu...
AB  - Fibrinogen is an important protein of primary and main protein of secondary hemostasis. Upon injury, fibrinogen is converted to insoluble fibrin by the action of thrombin. Fibrin further cross-links and creates fibrin network which reinforces blood clotting at the site of injury. There is a significant contribution of posttranslational modifications as well as interactions with other proteins necessary for fulfillment of fibrinogen biochemical role. Posttranslational modifications of fibrinogen influence its structure, fibrin structure and interactions with other proteins. Fibrin is not only a passive network that supports blood clot, but also an active structure that regulates its synthesis and degradation by interacting with many different proteins. For this reason, it is important to identify new proteins which interact with fibrinogen and may also have a role in wound healing.The procedure for isolation and analysis of fibrinogen was optimized in this dissertation. Application of double precipitation using ethanol resulted in highly purified fibrinogen, suitable for further characterisation.Since it is known that fibrinogen interacts with IGFBP-3 protein, the question was raised weather some other protein from the family of the IGF-binding proteins has this ability under physiological conditions. By using several affinity methods, it was shown that IGFBP-1 interacts with fibrinogen and this is a general physiological event. The significance of this interaction should be evaluated taking into consideration that IGFBP-1 itself may have beneficial effect on tissue wound healing, alone and as a transporter of the IGF molecule.Several pathologies accompanied by coagulopathies, such as diabetes mellitus type 2 and cirrhosis, are characterised by altered concentration and structure of fibrinogen, which in turn creates abnormal, thrombogenic fibrin. Detailed study of individual proteins included in coagulopathy may enable closer look at mechanisms responsible for this outcome. On the other hand, changes in posttranslational modifications and structure of fibrinogen with aging may lead to better understanding of presence or absence of certain pathologies associated with ageing.The structure of fibrinogen alteres with aging. An increase of high-mannose and/or hybrid N-glycans, tri-/tetraantennary complex glycans with greater amounts ofGal and GlcNAc was detected by lectin array...
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Uticaj posttranslacionih modifikacija fibrinogena na njegovu reaktivnost i funkciju
ER  - 
@phdthesis{
author = "Gligorijević, Nikola",
year = "2018",
url = "http://eteze.bg.ac.rs/application/showtheses?thesesId=6386, https://fedorabg.bg.ac.rs/fedora/get/o:19076/bdef:Content/download, http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=50770447, http://nardus.mpn.gov.rs/123456789/10480, http://cherry.chem.bg.ac.rs/handle/123456789/3162",
abstract = "Fibrinogen je vaţan protein primarne i glavni protein sekundarne hemostaze. Nakon povrede, on se dejstvom trombina pretvara u nerastvorni fibrin koji se dalje umreţava, pri čemu nastaje fibrinska mreţa koja ojačava krvni ugrušak na mestu povrede. Da bi fibrinogen obavljao svoju biohemijsku ulogu, bitni su odreĎeni faktori, u koje spadaju njegove posttranslacione modifikacije i interakcije sa drugim proteinima. Posttranslacione modifikacije fibrinogena utiču na njegovu strukturu, strukturu fibrina i interakcije sa drugim proteinima. Fibrin nije pasivna mreţa koja samo daje potporu krvnom ugrušku, već je aktivna struktura koja reguliše svoju sintezu i razgradnju interakcijom sa brojnim proteinima. Zato je vaţno otkriti nove proteine koji sa njim interaguju, a koji imaju uticaj na proces zarastanja povreda.U okviru ove diseretacije, optimizovana je procedura za izolovanje i analizu fibrinogena. Upotrebom dvostrukog taloţenja etanolom dobijen je visoko prečišćen fibrinogen, pogodan za dalju karakterizaciju.Kako je poznato da fibrinogen interaguje sa IGFBP-3 proteinom, postavilo se pitanje da li još neki protein iz grupe vezujućih proteina za IGF, pri fiziološkim uslovima, ima tu sposobnost. Upotrebom većeg broja afinitetnih metoda je pokazano da IGFBP-1 interaguje sa fibrinogenom i da je to opšta fiziološka pojava. Značaj ove interakcije treba sagledavati imajući u vidu da i IGFBP-1 podstiče zarastanje tkivnih povreda, samostalno i kao transporter IGF molekula.Brojne patologije pri kojima se javljaju i koagulopatije, kao što su dijabetes melitus tipa 2 i ciroza jetre, karakteriše izmenjena koncentracija i struktura fibrinogena, što za posledicu ima stvaranje abnormalnog, trombogenog fibrina. Detaljno izučavanje pojedinačnih proteina uključenih u koagulopatiju moţe dati bliţu sliku mehanizma odgovornog za ovu pojavu. Sa druge strane, promene na nivou posttranslacionih modifikacija i strukture fibrinogena sa starenjem mogu doprineti boljem razumevanju prisustva ili odsustva odreĎenih patologija kod starijih ljudi.Struktura fibrinogena sa starenjem se menja. Primenom lektinskog eseja uočeno je povećanje visoko-manoznih i/ili hibridnih N-glikana, tri-/tertaantenarnih kompleksnih glikana sa većim sadrţajem Gal i GlcNAc. Spektrofluorimetrijska analiza je pokazala da kod zdravih ljudi preko 60 godina starosti, fibrinogen ima kompaktniju tercijarnustrukturu..., Fibrinogen is an important protein of primary and main protein of secondary hemostasis. Upon injury, fibrinogen is converted to insoluble fibrin by the action of thrombin. Fibrin further cross-links and creates fibrin network which reinforces blood clotting at the site of injury. There is a significant contribution of posttranslational modifications as well as interactions with other proteins necessary for fulfillment of fibrinogen biochemical role. Posttranslational modifications of fibrinogen influence its structure, fibrin structure and interactions with other proteins. Fibrin is not only a passive network that supports blood clot, but also an active structure that regulates its synthesis and degradation by interacting with many different proteins. For this reason, it is important to identify new proteins which interact with fibrinogen and may also have a role in wound healing.The procedure for isolation and analysis of fibrinogen was optimized in this dissertation. Application of double precipitation using ethanol resulted in highly purified fibrinogen, suitable for further characterisation.Since it is known that fibrinogen interacts with IGFBP-3 protein, the question was raised weather some other protein from the family of the IGF-binding proteins has this ability under physiological conditions. By using several affinity methods, it was shown that IGFBP-1 interacts with fibrinogen and this is a general physiological event. The significance of this interaction should be evaluated taking into consideration that IGFBP-1 itself may have beneficial effect on tissue wound healing, alone and as a transporter of the IGF molecule.Several pathologies accompanied by coagulopathies, such as diabetes mellitus type 2 and cirrhosis, are characterised by altered concentration and structure of fibrinogen, which in turn creates abnormal, thrombogenic fibrin. Detailed study of individual proteins included in coagulopathy may enable closer look at mechanisms responsible for this outcome. On the other hand, changes in posttranslational modifications and structure of fibrinogen with aging may lead to better understanding of presence or absence of certain pathologies associated with ageing.The structure of fibrinogen alteres with aging. An increase of high-mannose and/or hybrid N-glycans, tri-/tetraantennary complex glycans with greater amounts ofGal and GlcNAc was detected by lectin array...",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Uticaj posttranslacionih modifikacija fibrinogena na njegovu reaktivnost i funkciju"
}
Gligorijević, N. (2018). Uticaj posttranslacionih modifikacija fibrinogena na njegovu reaktivnost i funkciju.
Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
Gligorijević N. Uticaj posttranslacionih modifikacija fibrinogena na njegovu reaktivnost i funkciju. Универзитет у Београду. 2018;
Gligorijević Nikola, "Uticaj posttranslacionih modifikacija fibrinogena na njegovu reaktivnost i funkciju" Универзитет у Београду (2018)

Structural changes of fibrinogen as a consequence of cirrhosis

Gligorijević, Nikola; Minić, Simeon L.; Krizakova, Martina; Katrlik, Jaroslav; Nedić, Olgica

(Pergamon-Elsevier Science Ltd, Oxford, 2018)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Minić, Simeon L.
AU  - Krizakova, Martina
AU  - Katrlik, Jaroslav
AU  - Nedić, Olgica
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2142
AB  - Cirrhosis is a disease which may develop as a consequence of various conditions. In advanced liver disease, blood coagulation can be seriously affected. Portal hypertension, vascular abnormalities and/or a dysbalance in coagulation factors may result in bleeding disorders or in the development of thrombosis. Fibrinogen is the main protein involved in clot formation and wound healing. The aim of this work was to analyse the glycosylation pattern of the isolated fibrinogen molecules by lectin-based protein microarray, together with the carbonylation pattern of the individual fibrinogen chains, possible changes in the molecular secondary and tertiary structure and reactivity with the insulin-like growth factor-binding protein 1 (IGFBP-1) in patients with cirrhosis. The results pointed to an increase in several carbohydrate moieties: tri/tetra-antennary structures, Gal beta-1,4 GlcNAc, terminal alpha-2,3 Sia and alpha-1,3 Man, and a decrease in core alpha-1,6 Fuc and bi-antennary galactosylated N-glycans with bisecting GlcNAc. Fibrinogen A alpha chain was the most susceptible to carbonylation, followed by the B beta chain. Cirrhosis induced additional protein carbonylation, mostly on the alpha chain. Spectrofluorimetry and CD spectrometry detected reduction in the alpha-helix content, protein unfolding and/or appearance of modified amino acid residues in cirrhosis. The amount of complexes which fibrinogen forms with IGFBP-1, another factor involved in wound healing was significantly greater in patients with cirrhosis than in healthy individuals. A more detailed knowledge of individual molecules in coagulation process may contribute to deeper understanding of coagulopathies and the results of this study offer additional information on the possible mechanisms involved in impaired coagulation due to cirrhosis.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Thrombosis Research
T1  - Structural changes of fibrinogen as a consequence of cirrhosis
VL  - 166
SP  - 43
EP  - 49
DO  - 10.1016/j.thromres.2018.04.005
ER  - 
@article{
author = "Gligorijević, Nikola and Minić, Simeon L. and Krizakova, Martina and Katrlik, Jaroslav and Nedić, Olgica",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2142",
abstract = "Cirrhosis is a disease which may develop as a consequence of various conditions. In advanced liver disease, blood coagulation can be seriously affected. Portal hypertension, vascular abnormalities and/or a dysbalance in coagulation factors may result in bleeding disorders or in the development of thrombosis. Fibrinogen is the main protein involved in clot formation and wound healing. The aim of this work was to analyse the glycosylation pattern of the isolated fibrinogen molecules by lectin-based protein microarray, together with the carbonylation pattern of the individual fibrinogen chains, possible changes in the molecular secondary and tertiary structure and reactivity with the insulin-like growth factor-binding protein 1 (IGFBP-1) in patients with cirrhosis. The results pointed to an increase in several carbohydrate moieties: tri/tetra-antennary structures, Gal beta-1,4 GlcNAc, terminal alpha-2,3 Sia and alpha-1,3 Man, and a decrease in core alpha-1,6 Fuc and bi-antennary galactosylated N-glycans with bisecting GlcNAc. Fibrinogen A alpha chain was the most susceptible to carbonylation, followed by the B beta chain. Cirrhosis induced additional protein carbonylation, mostly on the alpha chain. Spectrofluorimetry and CD spectrometry detected reduction in the alpha-helix content, protein unfolding and/or appearance of modified amino acid residues in cirrhosis. The amount of complexes which fibrinogen forms with IGFBP-1, another factor involved in wound healing was significantly greater in patients with cirrhosis than in healthy individuals. A more detailed knowledge of individual molecules in coagulation process may contribute to deeper understanding of coagulopathies and the results of this study offer additional information on the possible mechanisms involved in impaired coagulation due to cirrhosis.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Thrombosis Research",
title = "Structural changes of fibrinogen as a consequence of cirrhosis",
volume = "166",
pages = "43-49",
doi = "10.1016/j.thromres.2018.04.005"
}
Gligorijević, N., Minić, S. L., Krizakova, M., Katrlik, J.,& Nedić, O. (2018). Structural changes of fibrinogen as a consequence of cirrhosis.
Thrombosis Research
Pergamon-Elsevier Science Ltd, Oxford., 166, 43-49.
https://doi.org/10.1016/j.thromres.2018.04.005
Gligorijević N, Minić SL, Krizakova M, Katrlik J, Nedić O. Structural changes of fibrinogen as a consequence of cirrhosis. Thrombosis Research. 2018;166:43-49
Gligorijević Nikola, Minić Simeon L., Krizakova Martina, Katrlik Jaroslav, Nedić Olgica, "Structural changes of fibrinogen as a consequence of cirrhosis" Thrombosis Research, 166 (2018):43-49,
https://doi.org/10.1016/j.thromres.2018.04.005 .
4
4
4

Structural changes of fibrinogen as a consequence of cirrhosis

Gligorijević, Nikola; Minić, Simeon L.; Krizakova, Martina; Katrlik, Jaroslav; Nedić, Olgica

(Pergamon-Elsevier Science Ltd, Oxford, 2018)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Minić, Simeon L.
AU  - Krizakova, Martina
AU  - Katrlik, Jaroslav
AU  - Nedić, Olgica
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3265
AB  - Cirrhosis is a disease which may develop as a consequence of various conditions. In advanced liver disease, blood coagulation can be seriously affected. Portal hypertension, vascular abnormalities and/or a dysbalance in coagulation factors may result in bleeding disorders or in the development of thrombosis. Fibrinogen is the main protein involved in clot formation and wound healing. The aim of this work was to analyse the glycosylation pattern of the isolated fibrinogen molecules by lectin-based protein microarray, together with the carbonylation pattern of the individual fibrinogen chains, possible changes in the molecular secondary and tertiary structure and reactivity with the insulin-like growth factor-binding protein 1 (IGFBP-1) in patients with cirrhosis. The results pointed to an increase in several carbohydrate moieties: tri/tetra-antennary structures, Gal beta-1,4 GlcNAc, terminal alpha-2,3 Sia and alpha-1,3 Man, and a decrease in core alpha-1,6 Fuc and bi-antennary galactosylated N-glycans with bisecting GlcNAc. Fibrinogen A alpha chain was the most susceptible to carbonylation, followed by the B beta chain. Cirrhosis induced additional protein carbonylation, mostly on the alpha chain. Spectrofluorimetry and CD spectrometry detected reduction in the alpha-helix content, protein unfolding and/or appearance of modified amino acid residues in cirrhosis. The amount of complexes which fibrinogen forms with IGFBP-1, another factor involved in wound healing was significantly greater in patients with cirrhosis than in healthy individuals. A more detailed knowledge of individual molecules in coagulation process may contribute to deeper understanding of coagulopathies and the results of this study offer additional information on the possible mechanisms involved in impaired coagulation due to cirrhosis.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Thrombosis Research
T1  - Structural changes of fibrinogen as a consequence of cirrhosis
VL  - 166
SP  - 43
EP  - 49
DO  - 10.1016/j.thromres.2018.04.005
ER  - 
@article{
author = "Gligorijević, Nikola and Minić, Simeon L. and Krizakova, Martina and Katrlik, Jaroslav and Nedić, Olgica",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3265",
abstract = "Cirrhosis is a disease which may develop as a consequence of various conditions. In advanced liver disease, blood coagulation can be seriously affected. Portal hypertension, vascular abnormalities and/or a dysbalance in coagulation factors may result in bleeding disorders or in the development of thrombosis. Fibrinogen is the main protein involved in clot formation and wound healing. The aim of this work was to analyse the glycosylation pattern of the isolated fibrinogen molecules by lectin-based protein microarray, together with the carbonylation pattern of the individual fibrinogen chains, possible changes in the molecular secondary and tertiary structure and reactivity with the insulin-like growth factor-binding protein 1 (IGFBP-1) in patients with cirrhosis. The results pointed to an increase in several carbohydrate moieties: tri/tetra-antennary structures, Gal beta-1,4 GlcNAc, terminal alpha-2,3 Sia and alpha-1,3 Man, and a decrease in core alpha-1,6 Fuc and bi-antennary galactosylated N-glycans with bisecting GlcNAc. Fibrinogen A alpha chain was the most susceptible to carbonylation, followed by the B beta chain. Cirrhosis induced additional protein carbonylation, mostly on the alpha chain. Spectrofluorimetry and CD spectrometry detected reduction in the alpha-helix content, protein unfolding and/or appearance of modified amino acid residues in cirrhosis. The amount of complexes which fibrinogen forms with IGFBP-1, another factor involved in wound healing was significantly greater in patients with cirrhosis than in healthy individuals. A more detailed knowledge of individual molecules in coagulation process may contribute to deeper understanding of coagulopathies and the results of this study offer additional information on the possible mechanisms involved in impaired coagulation due to cirrhosis.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Thrombosis Research",
title = "Structural changes of fibrinogen as a consequence of cirrhosis",
volume = "166",
pages = "43-49",
doi = "10.1016/j.thromres.2018.04.005"
}
Gligorijević, N., Minić, S. L., Krizakova, M., Katrlik, J.,& Nedić, O. (2018). Structural changes of fibrinogen as a consequence of cirrhosis.
Thrombosis Research
Pergamon-Elsevier Science Ltd, Oxford., 166, 43-49.
https://doi.org/10.1016/j.thromres.2018.04.005
Gligorijević N, Minić SL, Krizakova M, Katrlik J, Nedić O. Structural changes of fibrinogen as a consequence of cirrhosis. Thrombosis Research. 2018;166:43-49
Gligorijević Nikola, Minić Simeon L., Krizakova Martina, Katrlik Jaroslav, Nedić Olgica, "Structural changes of fibrinogen as a consequence of cirrhosis" Thrombosis Research, 166 (2018):43-49,
https://doi.org/10.1016/j.thromres.2018.04.005 .
4
4
4

A thin layer chromatographic comparison of raw and soluble starch hydrolysis patterns of some alpha-amylases from Bacillus sp isolated in Serbia

Gligorijević, Nikola; Stevanović, Nikola R.; Lončar, Nikola L.; Baošić, Rada; Vujčić, Zoran; Božić, Nataša

(Serbian Chemical Soc, Belgrade, 2014)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Stevanović, Nikola R.
AU  - Lončar, Nikola L.
AU  - Baošić, Rada
AU  - Vujčić, Zoran
AU  - Božić, Nataša
PY  - 2014
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1771
AB  - Several natural isolates of Bacillus strains namely 5B, 12B, 16B, 18 and 24B were grown at two different temperatures in submerged fermentation for the production of raw-starch-digesting alpha-amylases. All strains except Bacillus sp. 18 produced more alpha-amylase at 37 degrees C. The hydrolysis of raw cornstarch followed the same pattern. Efficient hydrolysis was obtained with alpha-amylases from Bacillus sp. 5B, 12B, 16B and 24B grown at 37 degrees C and Bacillus sp. 18 grown at 50 degrees C. Zymography after isoelectric focusing showed that alpha-amylases were produced in multiple forms, from 2 to 6, depending on the strain when they were growing at 37 degrees C, while growth at 50 degrees C induced only 1 or 2 isoforms. Thin layer chromatography (TLC) analysis of the hydrolysis products of raw corn and soluble starch by alpha-amylases revealed the production of various mixtures of oligosaccharides. In most cases, G3 was the most dominant product from soluble starch while G2, G3 and G5 were the main products of raw starch hydrolysis. This indicates that the obtained alpha-amylases could be used for starch liquidification or short-chain-oligosaccharide formation, depending on the type of starch (raw or soluble) used for the hydrolysis.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - A thin layer chromatographic comparison of raw and soluble starch hydrolysis patterns of some alpha-amylases from Bacillus sp isolated in Serbia
VL  - 79
IS  - 4
SP  - 411
EP  - 420
DO  - 10.2298/JSC130909155G
ER  - 
@article{
author = "Gligorijević, Nikola and Stevanović, Nikola R. and Lončar, Nikola L. and Baošić, Rada and Vujčić, Zoran and Božić, Nataša",
year = "2014",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1771",
abstract = "Several natural isolates of Bacillus strains namely 5B, 12B, 16B, 18 and 24B were grown at two different temperatures in submerged fermentation for the production of raw-starch-digesting alpha-amylases. All strains except Bacillus sp. 18 produced more alpha-amylase at 37 degrees C. The hydrolysis of raw cornstarch followed the same pattern. Efficient hydrolysis was obtained with alpha-amylases from Bacillus sp. 5B, 12B, 16B and 24B grown at 37 degrees C and Bacillus sp. 18 grown at 50 degrees C. Zymography after isoelectric focusing showed that alpha-amylases were produced in multiple forms, from 2 to 6, depending on the strain when they were growing at 37 degrees C, while growth at 50 degrees C induced only 1 or 2 isoforms. Thin layer chromatography (TLC) analysis of the hydrolysis products of raw corn and soluble starch by alpha-amylases revealed the production of various mixtures of oligosaccharides. In most cases, G3 was the most dominant product from soluble starch while G2, G3 and G5 were the main products of raw starch hydrolysis. This indicates that the obtained alpha-amylases could be used for starch liquidification or short-chain-oligosaccharide formation, depending on the type of starch (raw or soluble) used for the hydrolysis.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "A thin layer chromatographic comparison of raw and soluble starch hydrolysis patterns of some alpha-amylases from Bacillus sp isolated in Serbia",
volume = "79",
number = "4",
pages = "411-420",
doi = "10.2298/JSC130909155G"
}
Gligorijević, N., Stevanović, N. R., Lončar, N. L., Baošić, R., Vujčić, Z.,& Božić, N. (2014). A thin layer chromatographic comparison of raw and soluble starch hydrolysis patterns of some alpha-amylases from Bacillus sp isolated in Serbia.
Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 79(4), 411-420.
https://doi.org/10.2298/JSC130909155G
Gligorijević N, Stevanović NR, Lončar NL, Baošić R, Vujčić Z, Božić N. A thin layer chromatographic comparison of raw and soluble starch hydrolysis patterns of some alpha-amylases from Bacillus sp isolated in Serbia. Journal of the Serbian Chemical Society. 2014;79(4):411-420
Gligorijević Nikola, Stevanović Nikola R., Lončar Nikola L., Baošić Rada, Vujčić Zoran, Božić Nataša, "A thin layer chromatographic comparison of raw and soluble starch hydrolysis patterns of some alpha-amylases from Bacillus sp isolated in Serbia" Journal of the Serbian Chemical Society, 79, no. 4 (2014):411-420,
https://doi.org/10.2298/JSC130909155G .
2
2
2

Congo red degrading laccases from Bacillus amyloliquefaciens strains isolated from salt spring in Serbia

Lončar, Nikola L.; Gligorijević, Nikola; Božić, Nataša; Vujčić, Zoran

(Elsevier Sci Ltd, Oxford, 2014)

TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Gligorijević, Nikola
AU  - Božić, Nataša
AU  - Vujčić, Zoran
PY  - 2014
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1791
AB  - Halotolerant strains of Bacillus amyloliquefaciens were isolated from salt spring in Ovca spa located in Republic of Serbia. Strains exhibit robust spore laccase with high temperature optimum of 65 degrees C while pH optimum is wide and substrate dependant. Ability to oxidize azo dyes was demonstrated. Under optimized conditions more than 85% removal of Congo red dye was achieved at pH 5.7. Substantial resistance to inhibition by high concentration of chloride ions was observed and tolerance of some commonly used cosolvents shows that applicability of these laccases goes beyond decolorization of textile effluents. (C) 2014 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - International Biodeterioration and Biodegradation
T1  - Congo red degrading laccases from Bacillus amyloliquefaciens strains isolated from salt spring in Serbia
VL  - 91
SP  - 18
EP  - 23
DO  - 10.1016/j.ibiod.2014.03.008
ER  - 
@article{
author = "Lončar, Nikola L. and Gligorijević, Nikola and Božić, Nataša and Vujčić, Zoran",
year = "2014",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1791",
abstract = "Halotolerant strains of Bacillus amyloliquefaciens were isolated from salt spring in Ovca spa located in Republic of Serbia. Strains exhibit robust spore laccase with high temperature optimum of 65 degrees C while pH optimum is wide and substrate dependant. Ability to oxidize azo dyes was demonstrated. Under optimized conditions more than 85% removal of Congo red dye was achieved at pH 5.7. Substantial resistance to inhibition by high concentration of chloride ions was observed and tolerance of some commonly used cosolvents shows that applicability of these laccases goes beyond decolorization of textile effluents. (C) 2014 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "International Biodeterioration and Biodegradation",
title = "Congo red degrading laccases from Bacillus amyloliquefaciens strains isolated from salt spring in Serbia",
volume = "91",
pages = "18-23",
doi = "10.1016/j.ibiod.2014.03.008"
}
Lončar, N. L., Gligorijević, N., Božić, N.,& Vujčić, Z. (2014). Congo red degrading laccases from Bacillus amyloliquefaciens strains isolated from salt spring in Serbia.
International Biodeterioration and Biodegradation
Elsevier Sci Ltd, Oxford., 91, 18-23.
https://doi.org/10.1016/j.ibiod.2014.03.008
Lončar NL, Gligorijević N, Božić N, Vujčić Z. Congo red degrading laccases from Bacillus amyloliquefaciens strains isolated from salt spring in Serbia. International Biodeterioration and Biodegradation. 2014;91:18-23
Lončar Nikola L., Gligorijević Nikola, Božić Nataša, Vujčić Zoran, "Congo red degrading laccases from Bacillus amyloliquefaciens strains isolated from salt spring in Serbia" International Biodeterioration and Biodegradation, 91 (2014):18-23,
https://doi.org/10.1016/j.ibiod.2014.03.008 .
16
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Sensitivity of Human Melanoma Cells on the Activity of Picolinate Ruthenium(Ii)-P-Cymene Complex Alone Or in Combination with Parp Inhibitor

Gligorijević, Nikola; Aranđelović, Sandra; Filipović, Lana; Krivokuca, A.; Jankovic, R.; Radulović, Siniša; Ivanović, I.; Grgurić-Šipka, Sanja; Tešić, Živoslav Lj.

(Oxford Univ Press, Oxford, 2012)

TY  - CONF
AU  - Gligorijević, Nikola
AU  - Aranđelović, Sandra
AU  - Filipović, Lana
AU  - Krivokuca, A.
AU  - Jankovic, R.
AU  - Radulović, Siniša
AU  - Ivanović, I.
AU  - Grgurić-Šipka, Sanja
AU  - Tešić, Živoslav Lj.
PY  - 2012
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1296
PB  - Oxford Univ Press, Oxford
C3  - Annals of Oncology
T1  - Sensitivity of Human Melanoma Cells on the Activity of Picolinate Ruthenium(Ii)-P-Cymene Complex Alone Or in Combination with Parp Inhibitor
VL  - 23
SP  - 30
EP  - 31
ER  - 
@conference{
author = "Gligorijević, Nikola and Aranđelović, Sandra and Filipović, Lana and Krivokuca, A. and Jankovic, R. and Radulović, Siniša and Ivanović, I. and Grgurić-Šipka, Sanja and Tešić, Živoslav Lj.",
year = "2012",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1296",
publisher = "Oxford Univ Press, Oxford",
journal = "Annals of Oncology",
title = "Sensitivity of Human Melanoma Cells on the Activity of Picolinate Ruthenium(Ii)-P-Cymene Complex Alone Or in Combination with Parp Inhibitor",
volume = "23",
pages = "30-31"
}
Gligorijević, N., Aranđelović, S., Filipović, L., Krivokuca, A., Jankovic, R., Radulović, S., Ivanović, I., Grgurić-Šipka, S.,& Tešić, Ž. Lj. (2012). Sensitivity of Human Melanoma Cells on the Activity of Picolinate Ruthenium(Ii)-P-Cymene Complex Alone Or in Combination with Parp Inhibitor.
Annals of Oncology
Oxford Univ Press, Oxford., 23, 30-31.
Gligorijević N, Aranđelović S, Filipović L, Krivokuca A, Jankovic R, Radulović S, Ivanović I, Grgurić-Šipka S, Tešić ŽL. Sensitivity of Human Melanoma Cells on the Activity of Picolinate Ruthenium(Ii)-P-Cymene Complex Alone Or in Combination with Parp Inhibitor. Annals of Oncology. 2012;23:30-31
Gligorijević Nikola, Aranđelović Sandra, Filipović Lana, Krivokuca A., Jankovic R., Radulović Siniša, Ivanović I., Grgurić-Šipka Sanja, Tešić Živoslav Lj., "Sensitivity of Human Melanoma Cells on the Activity of Picolinate Ruthenium(Ii)-P-Cymene Complex Alone Or in Combination with Parp Inhibitor" Annals of Oncology, 23 (2012):30-31