{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Gray PE"],"funding":["Kidney Research UK","NIDDK NIH HHS","Medical Research Council"],"pagination":["2659"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6868084"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10"],"pubmed_abstract":["<b>Background:</b> Goodpasture's disease (GP) is mediated by autoantibodies that bind the glomerular and alveolar basement membrane, causing rapidly progressive glomerulonephritis with or without pulmonary hemorrhage. The autoantibodies bind neoepitopes formed upon disruption of the quaternary structure of α345NC1 hexamer, a critical structural domain of α345 collagen IV scaffolds. Hexamer disruption leads to a conformational changes that transitions α3 and α5NC1 subunits into immunogens, however, the trigger remains unknown. This contrasts with another anti-GBM disease, Alports' post-transplant nephritis (APTN), where the pathogenic alloantibody binds directly to native NC1 hexamer. The current report includes the first study of antigenic specificity and allo-incompatability in anti-GBM d"],"journal":["Frontiers in immunology"],"pubmed_title":["Molecular Analysis of Goodpasture's Disease Following Hematopoietic Stem Cell Transplant in a Pediatric Patient, Recalls the Conformeropathy of Wild-Type Anti-GBM Disease."],"pmcid":["PMC6868084"],"funding_grant_id":["MR/R003017/1","MR/P024297/1","R01 DK018381","ST2/2010","KKR/Paed2017/04","1006412","G0800571","RP45/2008","MR/L002418/1","G0800200","MR/R013942/1"],"pubmed_authors":["Siggs OM","Kitching AR","Gray PE","Pedchenko V","Frith K","Saleem MA","O' Brien T","Hudson BG","McCarthy H","Ziegler JB","Fogo AB"],"additional_accession":[]},"is_claimable":false,"name":"Molecular Analysis of Goodpasture's Disease Following Hematopoietic Stem Cell Transplant in a Pediatric Patient, Recalls the Conformeropathy of Wild-Type Anti-GBM Disease.","description":"<b>Background:</b> Goodpasture's disease (GP) is mediated by autoantibodies that bind the glomerular and alveolar basement membrane, causing rapidly progressive glomerulonephritis with or without pulmonary hemorrhage. The autoantibodies bind neoepitopes formed upon disruption of the quaternary structure of α345NC1 hexamer, a critical structural domain of α345 collagen IV scaffolds. Hexamer disruption leads to a conformational changes that transitions α3 and α5NC1 subunits into immunogens, however, the trigger remains unknown. This contrasts with another anti-GBM disease, Alports' post-transplant nephritis (APTN), where the pathogenic alloantibody binds directly to native NC1 hexamer. The current report includes the first study of antigenic specificity and allo-incompatability in anti-GBM d","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019","modification":"2025-04-04T13:27:10.675Z","creation":"2020-05-21T21:26:09Z"},"accession":"S-EPMC6868084","cross_references":{"pubmed":["31798588"],"doi":["10.3389/fimmu.2019.02659"]}}