{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Harder MJ"],"funding":["NIAID NIH HHS","Biotechnology and Biological Sciences Research Council"],"pagination":["866-76"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4707092"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["196(2)"],"pubmed_abstract":["The serum proteins factor H (FH), consisting of 20 complement control protein modules (CCPs), and its splice product FH-like protein 1 (FHL-1; consisting of CCPs 1-7) are major regulators of the alternative pathway (AP) of complement activation. The engineered version of FH, miniFH, contains only the N- and C-terminal portions of FH linked by an optimized peptide and shows ∼ 10-fold higher ex vivo potency. We explored the hypothesis that regulatory potency is enhanced by unmasking of a ligand-binding site in the C-terminal CCPs 19-20 that is cryptic in full-length native FH. Therefore, we produced an FH variant lacking the central domains 10-15 (FHΔ10-15). To explore how avidity affects regulatory strength, we generated a duplicated version of miniFH, termed midiFH. We compared activities "],"journal":["Journal of immunology (Baltimore, Md. : 1950)"],"pubmed_title":["Comparative Analysis of Novel Complement-Targeted Inhibitors, MiniFH, and the Natural Regulators Factor H and Factor H-like Protein 1 Reveal Functional Determinants of Complement Regulation."],"pmcid":["PMC4707092"],"funding_grant_id":["R01 AI030040","AI068730","N01 AI030040","P01 AI068730","BB/L024403/1","BB/I007946/1"],"pubmed_authors":["Schmidt CQ","Huber-Lang M","Simmet T","Barlow PN","Anliker M","Harder MJ","Lambris JD","Schrezenmeier H","Hochsmann B","Ricklin D"],"additional_accession":[]},"is_claimable":false,"name":"Comparative Analysis of Novel Complement-Targeted Inhibitors, MiniFH, and the Natural Regulators Factor H and Factor H-like Protein 1 Reveal Functional Determinants of Complement Regulation.","description":"The serum proteins factor H (FH), consisting of 20 complement control protein modules (CCPs), and its splice product FH-like protein 1 (FHL-1; consisting of CCPs 1-7) are major regulators of the alternative pathway (AP) of complement activation. The engineered version of FH, miniFH, contains only the N- and C-terminal portions of FH linked by an optimized peptide and shows ∼ 10-fold higher ex vivo potency. We explored the hypothesis that regulatory potency is enhanced by unmasking of a ligand-binding site in the C-terminal CCPs 19-20 that is cryptic in full-length native FH. Therefore, we produced an FH variant lacking the central domains 10-15 (FHΔ10-15). To explore how avidity affects regulatory strength, we generated a duplicated version of miniFH, termed midiFH. We compared activities ","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Jan","modification":"2026-05-05T19:25:59.167Z","creation":"2019-03-27T02:06:37Z"},"accession":"S-EPMC4707092","cross_references":{"pubmed":["26643478"],"doi":["10.4049/jimmunol.1501919"]}}