{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Bapat RA"],"funding":["NIDCR NIH HHS"],"pagination":["622086"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7786100"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11"],"pubmed_abstract":["Macromolecular assembly of extracellular enamel matrix proteins (EMPs) is intimately associated with the nucleation, growth, and maturation of highly organized hydroxyapatite crystals giving rise to healthy dental enamel. Although the colocalization of two of the most abundant EMPs amelogenin (Amel) and ameloblastin (Ambn) in molar enamel has been established, the evidence toward their interaction is scarce. We used co-immunoprecipitation (co-IP) to show evidence of direct molecular interactions between recombinant and native Amel and Ambn. Ambn fragments containing Y/F-x-x-Y/L/F-x-Y/F self-assembly motif were isolated from the co-IP column and characterized by mass spectroscopy. We used recombinant Ambn (rAmbn) mutants with deletion of exons 5 and 6 as well as Ambn derived synthetic pepti"],"journal":["Frontiers in physiology"],"pubmed_title":["Co-Immunoprecipitation Reveals Interactions Between Amelogenin and Ameloblastin <i>via</i> Their Self-Assembly Domains."],"pmcid":["PMC7786100"],"funding_grant_id":["R01 DE013414","R01 DE027632"],"pubmed_authors":["Moradian-Oldak J","Su J","Bapat RA"],"additional_accession":[]},"is_claimable":false,"name":"Co-Immunoprecipitation Reveals Interactions Between Amelogenin and Ameloblastin <i>via</i> Their Self-Assembly Domains.","description":"Macromolecular assembly of extracellular enamel matrix proteins (EMPs) is intimately associated with the nucleation, growth, and maturation of highly organized hydroxyapatite crystals giving rise to healthy dental enamel. Although the colocalization of two of the most abundant EMPs amelogenin (Amel) and ameloblastin (Ambn) in molar enamel has been established, the evidence toward their interaction is scarce. We used co-immunoprecipitation (co-IP) to show evidence of direct molecular interactions between recombinant and native Amel and Ambn. Ambn fragments containing Y/F-x-x-Y/L/F-x-Y/F self-assembly motif were isolated from the co-IP column and characterized by mass spectroscopy. We used recombinant Ambn (rAmbn) mutants with deletion of exons 5 and 6 as well as Ambn derived synthetic pepti","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020","modification":"2026-07-16T10:17:59.43Z","creation":"2025-04-06T11:22:25.376Z"},"accession":"S-EPMC7786100","cross_references":{"pubmed":["33424645"],"doi":["10.3389/fphys.2020.622086"]}}