Ligand binding to fibrinogen influences its structure and function
Аутори
Gligorijević, NikolaMinić, Simeon
Radomirović, Mirjana
Lević, Steva
Ćirković Veličković, Tanja
Nikolić, Milan
Nedić, Olgica
Конференцијски прилог (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
Fibrinogen is a plasma protein most susceptible to oxidation. Through this chemical
modification, fibrinogen acquires thrombogenic characteristics in different
pathophysiological conditions. Increased carbonyl content and reduced porosity impair the
degradation of formed fibrin mediated by plasmin. Fibrinogen is capable of interacting
with many proteins, ions, and small molecules. These interactions can modify the
functions of this protein. The discovery of new binding partners that may protect
fibrinogen from harmful oxidation and, thus, preserve its normal function is essential.
Some of the newly detected interactions between fibrinogen and small, natural bioactive
molecules, together with the influence of these interactions on the structure and function of
fibrinogen, will be presented in this text.
Кључне речи:
bilirubin / dihydrolipoic acid / fibrinogen / protein function / protein-ligand interaction / protein structure / resveratrolИзвор:
Serbian Biochemical Society Tenth Conference with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia, 2021, 31-31Издавач:
- Serbian Biochemical Society
Финансирање / пројекти:
- Serbian Academy of Sciences and Arts, grant number F-26
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200168 (Универзитет у Београду, Хемијски факултет) (RS-MESTD-inst-2020-200168)
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200019 (Универзитет у Београду, Институт за примену нуклеарне енергије - ИНЕП) (RS-MESTD-inst-2020-200019)
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200116 (Универзитет у Београду, Пољопривредни факултет) (RS-MESTD-inst-2020-200116)
- FoodEnTwin-Twinning of research activities for the frontier research in the fields of food, nutrition and environmental omics (EU-H2020-810752)
Напомена:
- Full paper: http://dx.doi.org/10.5281/zenodo.5512285
- Full paper: https://cer.ihtm.bg.ac.rs/handle/123456789/7288
Повезане информације:
- Повезани садржај
http://dx.doi.org/10.5281/zenodo.5512285 - Повезани садржај
https://cer.ihtm.bg.ac.rs/handle/123456789/7288
Институција/група
IHTMTY - CONF AU - Gligorijević, Nikola AU - Minić, Simeon AU - Radomirović, Mirjana AU - Lević, Steva AU - Ćirković Veličković, Tanja AU - Nikolić, Milan AU - Nedić, Olgica PY - 2021 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/7287 AB - Fibrinogen is a plasma protein most susceptible to oxidation. Through this chemical modification, fibrinogen acquires thrombogenic characteristics in different pathophysiological conditions. Increased carbonyl content and reduced porosity impair the degradation of formed fibrin mediated by plasmin. Fibrinogen is capable of interacting with many proteins, ions, and small molecules. These interactions can modify the functions of this protein. The discovery of new binding partners that may protect fibrinogen from harmful oxidation and, thus, preserve its normal function is essential. Some of the newly detected interactions between fibrinogen and small, natural bioactive molecules, together with the influence of these interactions on the structure and function of fibrinogen, will be presented in this text. PB - Serbian Biochemical Society C3 - Serbian Biochemical Society Tenth Conference with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia T1 - Ligand binding to fibrinogen influences its structure and function SP - 31 EP - 31 UR - https://hdl.handle.net/21.15107/rcub_cer_7287 ER -
@conference{ author = "Gligorijević, Nikola and Minić, Simeon and Radomirović, Mirjana and Lević, Steva and Ćirković Veličković, Tanja and Nikolić, Milan and Nedić, Olgica", year = "2021", abstract = "Fibrinogen is a plasma protein most susceptible to oxidation. Through this chemical modification, fibrinogen acquires thrombogenic characteristics in different pathophysiological conditions. Increased carbonyl content and reduced porosity impair the degradation of formed fibrin mediated by plasmin. Fibrinogen is capable of interacting with many proteins, ions, and small molecules. These interactions can modify the functions of this protein. The discovery of new binding partners that may protect fibrinogen from harmful oxidation and, thus, preserve its normal function is essential. Some of the newly detected interactions between fibrinogen and small, natural bioactive molecules, together with the influence of these interactions on the structure and function of fibrinogen, will be presented in this text.", publisher = "Serbian Biochemical Society", journal = "Serbian Biochemical Society Tenth Conference with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia", title = "Ligand binding to fibrinogen influences its structure and function", pages = "31-31", url = "https://hdl.handle.net/21.15107/rcub_cer_7287" }
Gligorijević, N., Minić, S., Radomirović, M., Lević, S., Ćirković Veličković, T., Nikolić, M.,& Nedić, O.. (2021). Ligand binding to fibrinogen influences its structure and function. in Serbian Biochemical Society Tenth Conference with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia Serbian Biochemical Society., 31-31. https://hdl.handle.net/21.15107/rcub_cer_7287
Gligorijević N, Minić S, Radomirović M, Lević S, Ćirković Veličković T, Nikolić M, Nedić O. Ligand binding to fibrinogen influences its structure and function. in Serbian Biochemical Society Tenth Conference with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia. 2021;:31-31. https://hdl.handle.net/21.15107/rcub_cer_7287 .
Gligorijević, Nikola, Minić, Simeon, Radomirović, Mirjana, Lević, Steva, Ćirković Veličković, Tanja, Nikolić, Milan, Nedić, Olgica, "Ligand binding to fibrinogen influences its structure and function" in Serbian Biochemical Society Tenth Conference with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia (2021):31-31, https://hdl.handle.net/21.15107/rcub_cer_7287 .