{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zabrodskaya YA"],"funding":["Российский Фонд Фундаментальных Исследований"],"pagination":["1157-1168"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9375587"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["35(6)"],"pubmed_abstract":["The work is devoted to the study of the structural characteristics of the myeloperoxidase-ceruloplasmin-thrombin complex using small-angle neutron scattering methods in combination with computer modeling, as well as surface plasmon resonance and solid-phase enzyme assay. We have previously shown that the functioning of active myeloperoxidase during inflammation, despite the presence in the blood of an excess of ceruloplasmin which inhibits its activity, is possible due to the partial proteolysis of ceruloplasmin by thrombin. In this study, the myeloperoxidase-ceruloplasmin-thrombin heterohexamer was obtained in vitro. The building of a heterohexamer full-atomic model in silico, considering the glycosylation of the constituent proteins, confirmed the absence of steric barriers for the forma"],"journal":["Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine"],"pubmed_title":["Caught red handed: modeling and confirmation of the myeloperoxidase ceruloplasmin alpha-thrombin complex."],"pmcid":["PMC9375587"],"funding_grant_id":["18-015-00241"],"pubmed_authors":["Ramsay ES","Gorshkova YE","Ivankov OI","Sokolov AV","Gorbunov NP","Fedorova ND","Bondarenko AB","Kostevich VA","Zabrodskaya YA","Shvetsov AV","Vasilyev VB","Egorov VV"],"additional_accession":[]},"is_claimable":false,"name":"Caught red handed: modeling and confirmation of the myeloperoxidase ceruloplasmin alpha-thrombin complex.","description":"The work is devoted to the study of the structural characteristics of the myeloperoxidase-ceruloplasmin-thrombin complex using small-angle neutron scattering methods in combination with computer modeling, as well as surface plasmon resonance and solid-phase enzyme assay. We have previously shown that the functioning of active myeloperoxidase during inflammation, despite the presence in the blood of an excess of ceruloplasmin which inhibits its activity, is possible due to the partial proteolysis of ceruloplasmin by thrombin. In this study, the myeloperoxidase-ceruloplasmin-thrombin heterohexamer was obtained in vitro. The building of a heterohexamer full-atomic model in silico, considering the glycosylation of the constituent proteins, confirmed the absence of steric barriers for the forma","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Dec","modification":"2025-05-31T22:18:36.751Z","creation":"2024-11-09T20:27:27.432Z"},"accession":"S-EPMC9375587","cross_references":{"pubmed":["35962914"],"doi":["10.1007/s10534-022-00432-2"]}}