{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Yang T"],"funding":["UKRI Medical Research Council","Medical Research Council","National Institutes of Health","Wellcome Trust","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["107168"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11223093"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["307"],"pubmed_abstract":["The polypeptide hormone Amylin (also known as islet amyloid polypeptide) plays a role in regulation of glucose metabolism, but forms pancreatic islet amyloid deposits in type 2 diabetes. The process of islet amyloid formation contributes to β-cell dysfunction and the development of the disease. Amylin is produced as a pro-from and undergoes processing prior to secretion. The mature hormone contains an amidated C-terminus. Analysis of an alignment of vertebrate amylin sequences reveals that the processing signal for amidation is strictly conserved. Furthermore, the enzyme responsible for C-terminal amidation is found in all of these organisms. Comparison of the physiologically relevant amidated form to a variant with a free C-terminus (Amylin-COO<sup>-</sup>) shows that replacement of the C"],"journal":["Biophysical chemistry"],"pubmed_title":["On the importance of being amidated: Analysis of the role of the conserved C-terminal amide of amylin in amyloid formation and cytotoxicity."],"pmcid":["PMC11223093"],"funding_grant_id":["R01 GM078114","GM078114","107927/Z/15/Z","MR/T032154/1"],"pubmed_authors":["Filippov I","Zhyvoloup A","Manathunga L","Raleigh DP","Yang T","Baghai A","Marechal A"],"additional_accession":[]},"is_claimable":false,"name":"On the importance of being amidated: Analysis of the role of the conserved C-terminal amide of amylin in amyloid formation and cytotoxicity.","description":"The polypeptide hormone Amylin (also known as islet amyloid polypeptide) plays a role in regulation of glucose metabolism, but forms pancreatic islet amyloid deposits in type 2 diabetes. The process of islet amyloid formation contributes to β-cell dysfunction and the development of the disease. Amylin is produced as a pro-from and undergoes processing prior to secretion. The mature hormone contains an amidated C-terminus. Analysis of an alignment of vertebrate amylin sequences reveals that the processing signal for amidation is strictly conserved. Furthermore, the enzyme responsible for C-terminal amidation is found in all of these organisms. Comparison of the physiologically relevant amidated form to a variant with a free C-terminus (Amylin-COO<sup>-</sup>) shows that replacement of the C","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Apr","modification":"2026-06-01T09:24:59.83Z","creation":"2025-04-04T12:21:46.296Z"},"accession":"S-EPMC11223093","cross_references":{"pubmed":["38367541"],"doi":["10.1016/j.bpc.2023.107168"]}}