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Ligand binding to fibrinogen influences its structure and function
dc.creator | Gligorijević, Nikola | |
dc.creator | Minić, Simeon | |
dc.creator | Radomirović, Mirjana | |
dc.creator | Lević, Steva | |
dc.creator | Ćirković Veličković, Tanja | |
dc.creator | Nikolić, Milan | |
dc.creator | Nedić, Olgica | |
dc.date.accessioned | 2024-01-04T17:46:07Z | |
dc.date.available | 2024-01-04T17:46:07Z | |
dc.date.issued | 2021 | |
dc.identifier.uri | https://cer.ihtm.bg.ac.rs/handle/123456789/7287 | |
dc.description.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. | sr |
dc.language.iso | en | sr |
dc.publisher | Serbian Biochemical Society | sr |
dc.relation | Serbian Academy of Sciences and Arts, grant number F-26 | sr |
dc.relation | info:eu-repo/grantAgreement/MESTD/inst-2020/200168/RS// | sr |
dc.relation | info:eu-repo/grantAgreement/MESTD/inst-2020/200019/RS// | sr |
dc.relation | info:eu-repo/grantAgreement/MESTD/inst-2020/200116/RS// | sr |
dc.relation | info:eu-repo/grantAgreement/EC/H2020/810752/EU// | sr |
dc.relation.isreferencedby | http://dx.doi.org/10.5281/zenodo.5512285 | |
dc.relation.isreferencedby | https://cer.ihtm.bg.ac.rs/handle/123456789/7288 | |
dc.rights | openAccess | sr |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | |
dc.source | Serbian Biochemical Society Tenth Conference with international participation, “Biochemical Insights into Molecular Mechanisms”, 24.09.2021. Kragujevac, Serbia | sr |
dc.subject | bilirubin | sr |
dc.subject | dihydrolipoic acid | sr |
dc.subject | fibrinogen | sr |
dc.subject | protein function | sr |
dc.subject | protein-ligand interaction | sr |
dc.subject | protein structure | sr |
dc.subject | resveratrol | sr |
dc.title | Ligand binding to fibrinogen influences its structure and function | sr |
dc.type | conferenceObject | sr |
dc.rights.license | BY | sr |
dc.citation.spage | 31 | |
dc.citation.epage | 31 | |
dc.description.other | Full paper: [http://dx.doi.org/10.5281/zenodo.5512285] | |
dc.description.other | Full paper: [https://cer.ihtm.bg.ac.rs/handle/123456789/7288] | |
dc.identifier.rcub | https://hdl.handle.net/21.15107/rcub_cer_7287 | |
dc.identifier.fulltext | http://cer.ihtm.bg.ac.rs/bitstream/id/29169/M61_1_5.pdf | |
dc.type.version | publishedVersion | sr |