Ligand binding to fibrinogen influences its structure and function
Autori
Gligorijević, NikolaMinić, Simeon
Radomirović, Mirjana
Lević, Steva
Ćirković Veličković, Tanja
Nikolić, Milan
Nedić, Olgica
Konferencijski prilog (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
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.
Ključne reči:
bilirubin / dihydrolipoic acid / fibrinogen / protein function / protein-ligand interaction / protein structure / resveratrolIzvor:
Serbian Biochemical Society Tenth Conference with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia, 2021, 31-31Izdavač:
- Serbian Biochemical Society
Finansiranje / projekti:
- Serbian Academy of Sciences and Arts, grant number F-26
- Ministarstvo nauke, tehnološkog razvoja i inovacija Republike Srbije, institucionalno finansiranje - 200168 (Univerzitet u Beogradu, Hemijski fakultet) (RS-MESTD-inst-2020-200168)
- Ministarstvo nauke, tehnološkog razvoja i inovacija Republike Srbije, institucionalno finansiranje - 200019 (Univerzitet u Beogradu, Institut za primenu nuklearne energije - INEP) (RS-MESTD-inst-2020-200019)
- Ministarstvo nauke, tehnološkog razvoja i inovacija Republike Srbije, institucionalno finansiranje - 200116 (Univerzitet u Beogradu, Poljoprivredni fakultet) (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)
Napomena:
- Full paper: http://dx.doi.org/10.5281/zenodo.5512285
- Full paper: https://cer.ihtm.bg.ac.rs/handle/123456789/7288
Povezane informacije:
- Povezani sadržaj
http://dx.doi.org/10.5281/zenodo.5512285 - Povezani sadržaj
https://cer.ihtm.bg.ac.rs/handle/123456789/7288
Institucija/grupa
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 .