{"_id":"xNRAk3ZtFwkPtgDse","bibbaseid":"anonymous-doesdeamidationofisletamyloidpolypeptideaccelerateamyloidfibrilformation-2018","authorIDs":[],"bibdata":{"bibtype":"article","type":"article","author":[{"propositions":[],"lastnames":["Lam"],"firstnames":["Y.P.Y."],"suffixes":[]},{"propositions":[],"lastnames":["Wootton"],"firstnames":["C.A."],"suffixes":[]},{"propositions":[],"lastnames":["Hands-Portman"],"firstnames":["I."],"suffixes":[]},{"propositions":[],"lastnames":["Wei"],"firstnames":["J."],"suffixes":[]},{"propositions":[],"lastnames":["Chiu"],"firstnames":["C.K.C."],"suffixes":[]},{"propositions":[],"lastnames":["Romero-Canelon"],"firstnames":["I."],"suffixes":[]},{"propositions":[],"lastnames":["Lermyte"],"firstnames":["F."],"suffixes":[]},{"propositions":[],"lastnames":["Barrow"],"firstnames":["M.P."],"suffixes":[]},{"propositions":[],"lastnames":["O'Connor"],"firstnames":["P.B."],"suffixes":[]}],"title":"Does deamidation of islet amyloid polypeptide accelerate amyloid fibril formation?","journal":"Chemical Communications","year":"2018","volume":"54","number":"98","pages":"13853-13856","doi":"10.1039/C8CC06675B","note":"cited By 0","url":"https://www.scopus.com/inward/record.uri?eid=2-s2.0-85058083325&doi=10.1039%2fC8CC06675B&partnerID=40&md5=699de904096a6aedf062aab4f4aef0d3","affiliation":"Department of Chemistry, University of Warwick, Coventry, United Kingdom; Department of Life Sciences, University of Warwick, Coventry, United Kingdom; School of Pharmacy, University of Birmingham, Birmingham, United Kingdom","abstract":"Mass spectrometry has been applied to determine the deamidation sites and the aggregation region of the deamidated human islet amyloid polypeptide (hIAPP). Mutant hIAPP with iso-aspartic residue mutations at possible deamidation sites showed very different fibril formation behaviour, which correlates with the observed deamidation-induced acceleration of hIAPP aggregation. © The Royal Society of Chemistry.","keywords":"amylin; aspartic acid; mutant protein; amide; amylin; amyloid; isoaspartic acid; protein aggregate, amino acid sequence; Article; binding site; controlled study; correlation analysis; deamidation; fibril; human; mass spectrometry; spectrofluorometry; chemistry; genetics; point mutation; ultrastructure, Amides; Amino Acid Sequence; Amyloid; Humans; Islet Amyloid Polypeptide; Isoaspartic Acid; Point Mutation; Protein Aggregates","chemicals_cas":"amylin, 106602-62-4; aspartic acid, 56-84-8, 6899-03-2; amide, 17655-31-1; amyloid, 11061-24-8; Amides; Amyloid; Islet Amyloid Polypeptide; Isoaspartic Acid; Protein Aggregates","funding_details":"Engineering and Physical Sciences Research CouncilEngineering and Physical Sciences Research Council, EP/N021630/1, EP/F034210/1, FfWG 167136, EP/J000302/1","key":"Lam201813853","id":"Lam201813853","bibbaseid":"anonymous-doesdeamidationofisletamyloidpolypeptideaccelerateamyloidfibrilformation-2018","role":"author","urls":{"Paper":"https://www.scopus.com/inward/record.uri?eid=2-s2.0-85058083325&doi=10.1039%2fC8CC06675B&partnerID=40&md5=699de904096a6aedf062aab4f4aef0d3"},"keyword":["amylin; aspartic acid; mutant protein; amide; amylin; amyloid; isoaspartic acid; protein aggregate","amino acid sequence; Article; binding site; controlled study; correlation analysis; deamidation; fibril; human; mass spectrometry; spectrofluorometry; chemistry; genetics; point mutation; ultrastructure","Amides; Amino Acid Sequence; Amyloid; Humans; Islet Amyloid Polypeptide; Isoaspartic Acid; Point Mutation; Protein Aggregates"],"metadata":{"authorlinks":{}},"downloads":0,"html":""},"bibtype":"article","biburl":"https://files.warwick.ac.uk/mpbarrow/files/Public/scopus.bib","creationDate":"2019-08-07T22:21:28.338Z","downloads":0,"keywords":["amylin; aspartic acid; mutant protein; amide; amylin; amyloid; isoaspartic acid; protein aggregate","amino acid sequence; article; binding site; controlled study; correlation analysis; deamidation; fibril; human; mass spectrometry; spectrofluorometry; chemistry; genetics; point mutation; ultrastructure","amides; amino acid sequence; amyloid; humans; islet amyloid polypeptide; isoaspartic acid; point mutation; protein aggregates"],"search_terms":["deamidation","islet","amyloid","polypeptide","accelerate","amyloid","fibril","formation"],"title":"Does deamidation of islet amyloid polypeptide accelerate amyloid fibril formation?","year":2018,"dataSources":["tFNp76Pk2Bi7BzABL"]}