{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["103(11)"],"submitter":["Ivanova MI"],"pubmed_abstract":["Identifying sequence determinants of fibril-forming proteins is crucial for understanding the processes causing >20 proteins to form pathological amyloid depositions. Our approach to identifying which sequences form amyloid-like fibrils is to screen the amyloid-forming proteins human insulin and beta(2)-microglobulin for segments that form fibrils. Our screen is of 60 sequentially overlapping peptides, 59 being six residues in length and 1 being five residues, covering every noncysteine-containing segment in these two proteins. Each peptide was characterized as amyloid-like or nonfibril-forming. Amyloid-like peptides formed fibrils visible in electron micrographs or needle-like microcrystals showing a cross-beta diffraction pattern. Eight of the 60 peptides (three from insulin and five fro"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pagination":["4079-82"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC1449649"],"repository":["biostudies-literature"],"pubmed_title":["A systematic screen of beta(2)-microglobulin and insulin for amyloid-like segments."],"pmcid":["PMC1449649"],"pubmed_authors":["Eisenberg D","Thompson MJ","Ivanova MI"],"additional_accession":[]},"is_claimable":false,"name":"A systematic screen of beta(2)-microglobulin and insulin for amyloid-like segments.","description":"Identifying sequence determinants of fibril-forming proteins is crucial for understanding the processes causing >20 proteins to form pathological amyloid depositions. Our approach to identifying which sequences form amyloid-like fibrils is to screen the amyloid-forming proteins human insulin and beta(2)-microglobulin for segments that form fibrils. Our screen is of 60 sequentially overlapping peptides, 59 being six residues in length and 1 being five residues, covering every noncysteine-containing segment in these two proteins. Each peptide was characterized as amyloid-like or nonfibril-forming. Amyloid-like peptides formed fibrils visible in electron micrographs or needle-like microcrystals showing a cross-beta diffraction pattern. Eight of the 60 peptides (three from insulin and five fro","dates":{"release":"2006-01-01T00:00:00Z","publication":"2006 Mar","modification":"2026-05-02T17:25:06.614Z","creation":"2019-03-27T01:26:19Z"},"accession":"S-EPMC1449649","cross_references":{"pubmed":["16537488"],"doi":["10.1073/pnas.0511298103"]}}