{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T06:16:25Z","timestamp":1788416185346,"version":"build-2803163510"},"reference-count":31,"publisher":"American Chemical Society (ACS)","issue":"4","license":[{"start":{"date-parts":[[2015,12,26]],"date-time":"2015-12-26T00:00:00Z","timestamp":1451088000000},"content-version":"vor","delay-in-days":365,"URL":"https:\/\/pubs.acs.org\/page\/policy\/authorchoice_termsofuse.html"}],"funder":[{"DOI":"10.13039\/100000041","name":"American Diabetes Association","doi-asserted-by":"publisher","award":["7-12-MN-55"],"award-info":[{"award-number":["7-12-MN-55"]}],"id":[{"id":"10.13039\/100000041","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["GM102815"],"award-info":[{"award-number":["GM102815"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000078","name":"Division of Materials Research","doi-asserted-by":"publisher","award":["0907671"],"award-info":[{"award-number":["0907671"]}],"id":[{"id":"10.13039\/100000078","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2015,2,3]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Homomeric self-assembly of peptides into amyloid fibers is a feature of many diseases. A central role has been suggested for the lateral fiber surface affecting gains of toxic function. To investigate this, a protein scaffold that presents a discrete, parallel \u03b2-sheet surface for amyloid subdomains up to eight residues in length has been designed. Scaffolds that present the fiber surface of islet amyloid polypeptide (IAPP) were prepared. The designs show sequence-specific surface effects apparent in that they gain the capacity to attenuate rates of IAPP self-assembly in solution and affect IAPP-induced toxicity in insulin-secreting cells.<\/jats:p>","DOI":"10.1021\/bi5011442","type":"journal-article","created":{"date-parts":[[2014,12,26]],"date-time":"2014-12-26T12:24:12Z","timestamp":1419596652000},"page":"987-993","source":"Crossref","is-referenced-by-count":8,"title":["Peptide Amyloid Surface Display"],"prefix":"10.1021","volume":"54","author":[{"given":"Marisa A.","family":"Rubio","sequence":"first","affiliation":[{"name":"Yale University , , 260 Whitney Avenue , , ,","place":["New Haven, Connecticut, United States, 06520-8114"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Diana E.","family":"Schlamadinger","sequence":"additional","affiliation":[{"name":"Yale University , , 260 Whitney Avenue , , ,","place":["New Haven, Connecticut, United States, 06520-8114"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ellen M.","family":"White","sequence":"additional","affiliation":[{"name":"Yale University , , 260 Whitney Avenue , , ,","place":["New Haven, Connecticut, United States, 06520-8114"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrew D.","family":"Miranker","sequence":"additional","affiliation":[{"name":"Yale University , , 260 Whitney Avenue , , ,","place":["New Haven, Connecticut, United States, 06520-8114"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2014,12,26]]},"reference":[{"key":"2026090301475814700_cit1","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1146\/annurev.biochem.75.101304.123901","article-title":"Protein Misfolding,\nFunctional Amyloid, and Human Disease","volume":"75","author":"Chiti","year":"2006","journal-title":"Annu.\nRev. Biochem."},{"key":"2026090301475814700_cit2","doi-asserted-by":"crossref","first-page":"e6","DOI":"10.1371\/journal.pbio.0040006","article-title":"Functional amyloid\nformation within mammalian tissue","volume":"4","author":"Fowler","year":"2005","journal-title":"PLoS Biol."},{"key":"2026090301475814700_cit3","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1038\/nrn1007","article-title":"Unfolding\nthe role of protein misfolding in neurodegenerative diseases","volume":"4","author":"Soto","year":"2003","journal-title":"Nat. Rev. Neurosci."},{"key":"2026090301475814700_cit4","doi-asserted-by":"crossref","first-page":"1059","DOI":"10.1016\/j.cell.2007.10.014","article-title":"Semen-derived amyloid fibrils drastically\nenhance HIV infection","volume":"131","author":"Mu\u0308nch","year":"2007","journal-title":"Cell"},{"key":"2026090301475814700_cit5","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1038\/nchembio.546","article-title":"Gain of function of mutant p53 by coaggregation with\nmultiple tumor suppressors","volume":"7","author":"Xu","year":"2011","journal-title":"Nat. Chem. Biol."},{"key":"2026090301475814700_cit6","doi-asserted-by":"crossref","first-page":"1188","DOI":"10.1016\/j.cell.2012.02.022","article-title":"The amyloid state of\nproteins in human diseases","volume":"148","author":"Eisenberg","year":"2012","journal-title":"Cell"},{"key":"2026090301475814700_cit7","doi-asserted-by":"crossref","first-page":"12341","DOI":"10.1073\/pnas.0703306104","article-title":"Fiber-dependent\namyloid formation as catalysis of an existing reaction pathway","volume":"104","author":"Ruschak","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026090301475814700_cit8","doi-asserted-by":"crossref","first-page":"9758","DOI":"10.1073\/pnas.1218402110","article-title":"Proliferation of amyloid-\u03b242\naggregates occurs through a secondary nucleation mechanism","volume":"110","author":"Cohen","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026090301475814700_cit9","doi-asserted-by":"crossref","first-page":"2559","DOI":"10.1016\/j.bpj.2014.09.047","article-title":"Fiber-Dependent and -Independent Toxicity of Islet\nAmyloid Polypeptide","volume":"107","author":"Schlamadinger","year":"2014","journal-title":"Biophys. J."},{"key":"2026090301475814700_cit10","doi-asserted-by":"crossref","first-page":"2334","DOI":"10.1110\/ps.073164107","article-title":"Protein aggregation processes: In\nsearch of the mechanism","volume":"16","author":"Frieden","year":"2007","journal-title":"Protein Sci."},{"key":"2026090301475814700_cit11","doi-asserted-by":"crossref","first-page":"1228","DOI":"10.1096\/fj.11-194613","article-title":"Concentration-dependent\ntransitions govern the subcellular localization of islet amyloid polypeptide","volume":"26","author":"Magzoub","year":"2012","journal-title":"FASEB J."},{"key":"2026090301475814700_cit12","doi-asserted-by":"crossref","first-page":"2585","DOI":"10.1016\/j.bpj.2009.08.028","article-title":"Human serum albumin inhibits A\u03b2\nfibrillization through a \u201cmonomer-competitor\u201d mechanism","volume":"97","author":"Milojevic","year":"2009","journal-title":"Biophys. J."},{"key":"2026090301475814700_cit13","doi-asserted-by":"crossref","first-page":"753","DOI":"10.3233\/JAD-131169","article-title":"In vitro amyloid-\u03b2\nbinding and inhibition of amyloid-\u03b2 self-association by therapeutic\nalbumin","volume":"38","author":"Milojevic","year":"2014","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"2026090301475814700_cit14","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1021\/cn900015v","article-title":"Amyloid \u03b2-protein aggregation produces highly reproducible\nkinetic data and occurs by a two-phase process","volume":"1","author":"Hellstrand","year":"2010","journal-title":"ACS Chem. Neurosci."},{"key":"2026090301475814700_cit15","doi-asserted-by":"crossref","first-page":"14990","DOI":"10.1021\/ja802483d","article-title":"Structural insights into the polymorphism of amyloid-like\nfibrils formed by region 20\u201329 of amylin revealed by solid-state\nNMR and X-ray fiber diffraction","volume":"130","author":"Madine","year":"2008","journal-title":"J. Am. Chem.\nSoc."},{"key":"2026090301475814700_cit16","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1016\/j.jmb.2009.06.026","article-title":"The role\nof prefibrillar structures in the assembly of a peptide amyloid","volume":"393","author":"Ruschak","year":"2009","journal-title":"J. Mol. Biol."},{"key":"2026090301475814700_cit17","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1016\/S1074-5521(00)00034-X","article-title":"Amyloidogenicity\nof recombinant human pro-islet amyloid polypeptide (ProIAPP)","volume":"7","author":"Krampert","year":"2000","journal-title":"Chem. Biol."},{"key":"2026090301475814700_cit18","doi-asserted-by":"crossref","first-page":"1055","DOI":"10.1006\/jmbi.1999.3422","article-title":"Identification of a penta- and hexapeptide of islet\namyloid polypeptide (IAPP) with amyloidogenic and cytotoxic properties","volume":"295","author":"Tenidis","year":"2000","journal-title":"J. Mol. Biol."},{"key":"2026090301475814700_cit19","doi-asserted-by":"crossref","first-page":"34156","DOI":"10.1074\/jbc.M102883200","article-title":"Analysis of the minimal amyloid-forming fragment of the islet amyloid\npolypeptide. An experimental support for the key role of the phenylalanine\nresidue in amyloid formation","volume":"276","author":"Azriel","year":"2001","journal-title":"J. Biol. Chem."},{"key":"2026090301475814700_cit20","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1038\/415553a","article-title":"Structure\nof the cell-puncturing device of bacteriophage T4","volume":"415","author":"Kanamaru","year":"2002","journal-title":"Nature"},{"key":"2026090301475814700_cit21","doi-asserted-by":"crossref","first-page":"2739","DOI":"10.1128\/JB.181.9.2739-2744.1999","article-title":"The C-terminal\nfragment of the precursor tail lysozyme of bacteriophage T4 stays\nas a structural component of the baseplate after cleavage","volume":"181","author":"Kanamaru","year":"1999","journal-title":"J. Bacteriol."},{"key":"2026090301475814700_cit22","doi-asserted-by":"crossref","first-page":"1873","DOI":"10.1002\/smll.201000772","article-title":"Construction of Robust\nBio-nanotubes using the Controlled Self-Assembly of Component Proteins\nof Bacteriophage T4","volume":"6","author":"Yokoi","year":"2010","journal-title":"Small"},{"key":"2026090301475814700_cit23","doi-asserted-by":"crossref","first-page":"789","DOI":"10.1016\/S0969-2126(97)00233-5","article-title":"Structure of bacteriophage\nT4 fibritin: A segmented coiled coil and the role of the C-terminal\ndomain","volume":"5","author":"Tao","year":"1997","journal-title":"Structure"},{"key":"2026090301475814700_cit24","doi-asserted-by":"crossref","first-page":"2559","DOI":"10.1016\/j.bpj.2014.09.047","article-title":"Fiber-Dependent and -Independent\nToxicity of Islet Amyloid Polypeptide","volume":"107","author":"Schlamadinger","year":"2014","journal-title":"Biophys.\nJ."},{"key":"2026090301475814700_cit25","doi-asserted-by":"crossref","first-page":"13505","DOI":"10.1021\/bi701427q","article-title":"Peptide conformation and supramolecular organization in amylin fibrils:\nConstraints from solid-state NMR","volume":"46","author":"Luca","year":"2007","journal-title":"Biochemistry"},{"key":"2026090301475814700_cit26","doi-asserted-by":"crossref","first-page":"5235","DOI":"10.1074\/jbc.M111.327817","article-title":"Fibril structure\nof human islet amyloid polypeptide","volume":"287","author":"Bedrood","year":"2012","journal-title":"J. Biol.\nChem."},{"key":"2026090301475814700_cit27","doi-asserted-by":"crossref","first-page":"2016","DOI":"10.2337\/db07-0197","article-title":"High Expression\nRates of Human Islet Amyloid Polypeptide Induce Endoplasmic Reticulum\nStress-Mediated \u03b2-Cell Apoptosis, a Characteristic of Humans\nwith Type 2 but Not Type 1 Diabetes","volume":"56","author":"Huang","year":"2007","journal-title":"Diabetes"},{"key":"2026090301475814700_cit28","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1016\/j.jmb.2011.12.032","article-title":"Sensitivity of Amyloid Formation by Human Islet Amyloid\nPolypeptide to Mutations at Residue 20","volume":"421","author":"Cao","year":"2012","journal-title":"J. Mol.\nBiol."},{"key":"2026090301475814700_cit29","doi-asserted-by":"crossref","first-page":"3000","DOI":"10.1021\/ol901015a","article-title":"Use of\nDisulfide \u201cStaples\u201d To Stabilize \u03b2-Sheet Quaternary\nStructure","volume":"11","author":"Khakshoor","year":"2009","journal-title":"Org. Lett."},{"key":"2026090301475814700_cit30","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1038\/nsb0498-284","article-title":"Unusual \u03b2-sheet\nperiodicity in small cyclic peptides","volume":"5","author":"Gibbs","year":"1998","journal-title":"Nat. Struct.\nBiol."},{"key":"2026090301475814700_cit31","doi-asserted-by":"crossref","first-page":"3166","DOI":"10.1021\/jo102598n","article-title":"Giant Macrolactams\nBased on \u03b2-Sheet Peptides","volume":"76","author":"Cheng","year":"2011","journal-title":"J. Org. Chem."}],"container-title":["Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/bi5011442","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/bichaw\/article-pdf\/54\/4\/987\/7904527\/bi5011442.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/bichaw\/article-pdf\/54\/4\/987\/7904527\/bi5011442.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T05:48:06Z","timestamp":1788414486000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/bichaw\/article\/54\/4\/987\/775323\/Peptide-Amyloid-Surface-Display"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,12,26]]},"references-count":31,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2014,12,26]]},"published-print":{"date-parts":[[2015,2,3]]}},"URL":"https:\/\/doi.org\/10.1021\/bi5011442","relation":{},"ISSN":["0006-2960","1520-4995"],"issn-type":[{"value":"0006-2960","type":"print"},{"value":"1520-4995","type":"electronic"}],"subject":[],"published":{"date-parts":[[2014,12,26]]}}}